ALPHASUITEATLASTM
EGFR · P00533Homo sapiens
PROTEIN OVERVIEW

EGFREpidermal growth factor receptor

P00533Homo sapiensReviewed · UniProt

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses.

Sequence1210 aa
Source mass134.28 kDa
Recorded PDB entries388
Isoforms listed4

UniProt locations Cell membrane · Endoplasmic reticulum membrane · Golgi apparatus membrane · Nucleus membrane · Endosome · Endosome membrane · Nucleus · Secreted

01

Function

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses [42, 100, 101, 40, 102, 45, 50, 109, 74, 88, 24, 97, 34]. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF [99, 46, 52, 111, 88, 24, 26, 30, 33]. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues [36, 105, 106, 109, 62].

The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades [36, 105, 106, 109, 62]. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules [88]. May also activate the NF-kappa-B signaling cascade [43].

Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling [38]. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin [44]. Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration [70].

Acts as a positive regulator of cGAS-STING signaling by mediating tyrosine phosphorylation of STING1, promoting production of type I interferon (IFN-alpha and IFN-beta), while inhibiting STING1 ability to regulate autophagy [95]. Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity)

By similarityExperimental evidence 29 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "Q01279"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10026169"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10805725"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11116146"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11483589"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11602604"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12297049"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12297050"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12620237"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12873986"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15374980"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15590694"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15611079"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17115032"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17349580"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17909029"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18046415"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19560417"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19836242"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20462955"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20837704"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21258366"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "27153536"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "2790960"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32926474"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "35538033"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "7679104"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "8144591"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9419975"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9488479"
        }
      ],
      "value": "Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:12297050, PubMed:12620237, PubMed:12873986, PubMed:15374980, PubMed:15590694, PubMed:17115032, PubMed:19560417, PubMed:21258366, PubMed:27153536, PubMed:2790960, PubMed:35538033, PubMed:9488479). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:12297049, PubMed:15611079, PubMed:17909029, PubMed:20837704, PubMed:27153536, PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues (PubMed:10026169, PubMed:17349580, PubMed:18046415, PubMed:19560417, PubMed:19836242). The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades (PubMed:10026169, PubMed:17349580, PubMed:18046415, PubMed:19560417, PubMed:19836242). Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Acts as a positive regulator of cGAS-STING signaling by mediating tyrosine phosphorylation of STING1, promoting production of type I interferon (IFN-alpha and IFN-beta), while inhibiting STING1 ability to regulate autophagy (PubMed:32926474). Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity)"
    }
  ],
  "commentType": "FUNCTION"
}
Isoform 2

May act as an antagonist of EGF action

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "8918811"
        }
      ],
      "value": "May act as an antagonist of EGF action"
    }
  ],
  "commentType": "FUNCTION",
  "molecule": "Isoform 2"
}

(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21516087"
        }
      ],
      "value": "(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins"
    }
  ],
  "commentType": "FUNCTION"
}

Catalytic activity

L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)

Evidence
Complete source annotation
{
  "commentType": "CATALYTIC ACTIVITY",
  "reaction": {
    "name": "L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)",
    "reactionCrossReferences": [
      {
        "database": "Rhea",
        "id": "RHEA:10596"
      },
      {
        "database": "Rhea",
        "id": "RHEA-COMP:10136"
      },
      {
        "database": "Rhea",
        "id": "RHEA-COMP:20101"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:15378"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:30616"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:46858"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:61978"
      },
      {
        "database": "ChEBI",
        "id": "CHEBI:456216"
      }
    ],
    "ecNumber": "2.7.10.1",
    "evidences": [
      {
        "evidenceCode": "ECO:0000255",
        "source": "PROSITE-ProRule",
        "id": "PRU10028"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "15374980"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "17349580"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "18046415"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "18227510"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "19560417"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "19563760"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "32926474"
      }
    ]
  }
}

Activity regulation

Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling.

Up-regulated by NEU3-mediated desialylation of N-linked glycan at Asn-528

Experimental evidence 6 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15282549"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15590694"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17334392"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18046415"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19836242"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "25922362"
        }
      ],
      "value": "Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling. Up-regulated by NEU3-mediated desialylation of N-linked glycan at Asn-528"
    }
  ],
  "commentType": "ACTIVITY REGULATION"
}

GO functions & biological processes

positive regulation of G1/S transition of mitotic cell cycleacts upstream ofUniProtKB:P00533
GO
GO:1900087 · evidence & context
cell surface receptor signaling pathwayacts upstream of or withinUniProtKB:P00533
GO
GO:0007166 · evidence & context
  • ECO:0000314 PMID:7736574 ↗ IDA · MGI · 20101102
    qualifier: acts_upstream_of_or_within
epidermal growth factor receptor signaling pathwayacts upstream of or withinUniProtKB:P00533
GO
GO:0007173 · evidence & context
  • ECO:0000314 PMID:7736574 ↗ IDA · MGI · 20101102
    qualifier: acts_upstream_of_or_within
  • ECO:0000314 PMID:9890893 ↗ IDA · MGI · 20220304
    qualifier: acts_upstream_of_or_within
positive regulation of cell population proliferationacts upstream of or withinUniProtKB:P00533
GO
GO:0008284 · evidence & context
  • ECO:0000314 PMID:7736574 ↗ IDA · MGI · 20101102
    qualifier: acts_upstream_of_or_within
ERBB2-EGFR signaling pathwayacts upstream of or withinUniProtKB:P00533
GO
GO:0038134 · evidence & context
  • ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20220304
    qualifier: acts_upstream_of_or_within
All recorded function and process assertions (83)
epidermal growth factor receptor activitycontributes toUniProtKB:P00533
GO
GO:0005006 · evidence & context
chromatin bindingenablesUniProtKB:P00533
GO
GO:0003682 · evidence & context
double-stranded DNA bindingenablesUniProtKB:P00533
GO
GO:0003690 · evidence & context
protein kinase activityenablesUniProtKB:P00533
GO
GO:0004672 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR001245"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008266"}]}]
MAP kinase kinase kinase activityenablesUniProtKB:P00533
GO
GO:0004709 · evidence & context
protein tyrosine kinase activityenablesUniProtKB:P00533
GO
GO:0004713 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR020635"}]}, {"connectedXrefs": [{"db": "RHEA", "id": "10596"}]}]
  • ECO:0000315 PMID:14702346 ↗ IMP · UniProt · 20050812
    qualifier: enables
  • ECO:0000269 PMID:15374980 ↗ EXP · UniProt · 20251027
    qualifier: enables
  • ECO:0000304 PMID:16076471 ↗ TAS · UniProt · 20050809
    qualifier: enables
  • ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011
    qualifier: enables
  • ECO:0000269 PMID:17349580 ↗ EXP · UniProt · 20251027
    qualifier: enables
  • ECO:0000314 PMID:17599051 ↗ IDA · UniProt · 20100226
    qualifier: enables
  • ECO:0000269 PMID:19560417 ↗ EXP · UniProt · 20251027
    qualifier: enables
  • ECO:0000269 PMID:19563760 ↗ EXP · UniProt · 20251027
    qualifier: enables
  • ECO:0000315 PMID:20878056 ↗ IMP · UniProt · 20170522
    qualifier: enables
  • ECO:0000314 PMID:2472218 ↗ IDA · MGI · 20220118
    qualifier: enables
  • ECO:0000314 PMID:2472218 ↗ IDA · MGI · 20220304
    qualifier: enables
  • ECO:0000314 PMID:9890893 ↗ IDA · MGI · 20220118
    qualifier: enables
  • ECO:0000304 Reactome:R-HSA-177934 TAS · Reactome · 20240809
    qualifier: enables
  • ECO:0000304 Reactome:R-HSA-182969 TAS · Reactome · 20240809
    qualifier: enables
  • ECO:0000304 Reactome:R-HSA-183058 TAS · Reactome · 20240809
    qualifier: enables
  • ECO:0000304 Reactome:R-HSA-212710 TAS · Reactome · 20240809
    qualifier: enables
  • ECO:0000304 Reactome:R-HSA-8867041 TAS · Reactome · 20240809
    qualifier: enables
protein tyrosine kinase activityenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0004713 · evidence & context
  • ECO:0000314 PMID:32926474 ↗ IDA · UniProt · 20260420
    qualifier: enables
    extensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86WV6", "relation": "has_input"}, {"db": "GO", "id": "0141111", "relation": "part_of"}, {"db": "GO", "id": "0016242", "relation": "part_of"}]}]
transmembrane receptor protein tyrosine kinase activityenablesUniProtKB:P00533
GO
GO:0004714 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003366"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0003733"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0010389"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0040505"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0283499"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0285896"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:104771"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:107381"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1339758"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1345277"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95522"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95524"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95558"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95561"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96433"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96575"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96677"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96683"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96969"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:97384"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:97531"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:97902"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:99654"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN001230349"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2611"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2612"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2621"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2869"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2917"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2965"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3214"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3284"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3285"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620144"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620714"}]}, {"connectedXrefs": [{"db": "RGD", "id": "621737"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "O73798"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04629"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P07333"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P08069"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P09619"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P11362"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P14616"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P17948"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21709"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21802"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P22455"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P22607"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P29317"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P29376"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35916"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35968"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P54760"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q08345"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16832"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q91987"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9PVZ4"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00000289"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00002299"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00006868"}]}, {"connectedXrefs": [{"db": "ZFIN", "id": "ZDB-GENE-980526-255"}]}]
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}, {"connectedXrefs": [{"db": "EC", "id": "2.7.10.1"}]}]
  • ECO:0000304 Reactome:R-HSA-177930 TAS · Reactome · 20260222
    qualifier: enables
  • ECO:0000304 Reactome:R-HSA-177933 TAS · Reactome · 20260222
    qualifier: enables
transmembrane signaling receptor activityenablesUniProtKB:P00533
GO
GO:0004888 · evidence & context
epidermal growth factor receptor activityenablesUniProtKB:P00533
GO
GO:0005006 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00086054"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
  • ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20211214
    qualifier: enables
  • ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20220304
    qualifier: enables
  • ECO:0000314 PMID:12435727 ↗ IDA · UniProt · 20050812
    qualifier: enables
  • ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011
    qualifier: enables
  • ECO:0000314 PMID:2176151 ↗ IDA · MGI · 20220118
    qualifier: enables
  • ECO:0000314 PMID:2176151 ↗ IDA · MGI · 20220304
    qualifier: enables
  • ECO:0000315 PMID:22732145 ↗ IMP · ParkinsonsUK-UCL · 20161111
    qualifier: enables
  • ECO:0000303 PMID:2790960 ↗ NAS · UniProt · 20050809
    qualifier: enables
  • ECO:0000303 PMID:6325948 ↗ NAS · UniProt · 20050809
    qualifier: enables
protein bindingenablesUniProtKB:P00533
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:10026169 ↗ IPI · UniProt · 20111121
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43639"}]}]
  • ECO:0000353 PMID:10026169 ↗ IPI · UniProt · 20111121
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16333"}]}]
  • ECO:0000353 PMID:10026169 ↗ IPI · UniProt · 20111121
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:10229072 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
  • ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
  • ECO:0000353 PMID:10805725 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00750"}]}]
  • ECO:0000353 PMID:11279102 ↗ IPI · HGNC-UCL · 20061026
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UNH7"}]}]
  • ECO:0000353 PMID:11896612 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:12070153 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42224"}]}]
  • ECO:0000353 PMID:12297049 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01135"}]}]
  • ECO:0000353 PMID:12297050 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:12577067 ↗ IPI · UniProt · 20090424
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:12577067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:12620237 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:14568990 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
  • ECO:0000353 PMID:14679214 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:15225635 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P63104"}]}]
  • ECO:0000353 PMID:15282549 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
  • ECO:0000353 PMID:15345710 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
  • ECO:0000353 PMID:15590694 ↗ IPI · UniProt · 20111012
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75159"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60716"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06493"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07947"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P10599"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P11142"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27348"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31947"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P38646"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P63104"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q03135"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05397"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q71U36"}]}]
  • ECO:0000353 PMID:15962011 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:16253990 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQC2"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00213"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00459"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14654"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O95704"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00519"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16333"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16885"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20936"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42684"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P43403"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P43405"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46108"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49757"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51451"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P98077"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13239"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13387"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13882"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6PKX4"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q7Z7G1"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8IZW8"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92569"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92625"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92870"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NRF2"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NSE2"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UKG1"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQF2"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQQ2"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y490"}]}]
  • ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y6R0"}]}]
  • ECO:0000353 PMID:16499958 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJ41"}]}]
  • ECO:0000353 PMID:16516204 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04406"}]}]
  • ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07948"}]}]
  • ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31947"}]}]
  • ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51636"}]}]
  • ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q03135"}]}]
  • ECO:0000353 PMID:16843263 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:16914641 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:16954185 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15109"}]}]
  • ECO:0000353 PMID:17115032 ↗ IPI · UniProt · 20111011
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12004"}]}]
  • ECO:0000353 PMID:17126326 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60603"}]}]
  • ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:17182860 ↗ IPI · UniProt · 20110301
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O54967"}]}]
  • ECO:0000353 PMID:17284441 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P03372"}]}]
  • ECO:0000353 PMID:17284441 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
  • ECO:0000353 PMID:17334392 ↗ IPI · UniProt · 20200707
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQ49"}]}]
  • ECO:0000353 PMID:17599051 ↗ IPI · UniProt · 20100226
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P05432"}]}]
  • ECO:0000353 PMID:17697999 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:17726113 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96FE5"}]}]
  • ECO:0000353 PMID:17909029 ↗ IPI · UniProt · 20080602
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y2I7"}]}]
  • ECO:0000353 PMID:18046415 ↗ IPI · UniProt · 20100302
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
  • ECO:0000353 PMID:18046415 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
  • ECO:0000353 PMID:18273061 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:18455122 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P13866"}]}]
  • ECO:0000353 PMID:18542056 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
  • ECO:0000353 PMID:18602463 ↗ IPI · UniProt · 20120427
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99700"}]}]
  • ECO:0000353 PMID:18722344 ↗ IPI · UniProt · 20191101
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75815"}]}]
  • ECO:0000353 PMID:18776048 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
  • ECO:0000353 PMID:18824549 ↗ IPI · UniProt · 20100224
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BZP6"}]}]
  • ECO:0000353 PMID:18824549 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BZP6"}]}]
  • ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08575"}]}]
  • ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23467"}]}]
  • ECO:0000353 PMID:19172738 ↗ IPI · UniProt · 20091118
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQC2"}]}]
  • ECO:0000353 PMID:19172738 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQC2"}]}]
  • ECO:0000353 PMID:19509291 ↗ IPI · UniProt · 20121207
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9H706"}]}]
  • ECO:0000353 PMID:19602593 ↗ IPI · UniProt · 20090916
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P60468"}]}]
  • ECO:0000353 PMID:19650109 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:19798056 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75674"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00170"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04083"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04406"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P09936"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P10599"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P17174"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23528"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27348"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31948"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P34932"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P38646"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P60520"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q02952"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05209"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q09666"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12852"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14318"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96CW1"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9P0L0"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UBN7"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UNE7"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y2H9"}]}]
  • ECO:0000353 PMID:20153921 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BXH1"}]}]
  • ECO:0000353 PMID:20308550 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:20403327 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8K424"}]}]
  • ECO:0000353 PMID:20462955 ↗ IPI · UniProt · 20191018
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q3V6T2"}]}]
  • ECO:0000353 PMID:20473329 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:20473329 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05397"}]}]
  • ECO:0000353 PMID:20473329 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
  • ECO:0000353 PMID:20473329 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q07889"}]}]
  • ECO:0000353 PMID:20551055 ↗ IPI · UniProt · 20130828
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99527"}]}]
  • ECO:0000353 PMID:20562913 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:20624308 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08581"}]}]
  • ECO:0000353 PMID:20624308 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
  • ECO:0000353 PMID:20878056 ↗ IPI · UniProt · 20170522
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75420"}, {"db": "UniProtKB", "id": "P31749"}, {"db": "UniProtKB", "id": "Q13322"}, {"db": "UniProtKB", "id": "Q6Y7W6"}, {"db": "UniProtKB", "id": "Q92600"}]}]
  • ECO:0000353 PMID:20878056 ↗ IPI · UniProt · 20170522
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92600"}]}]
  • ECO:0000353 PMID:20935677 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P03372-4"}]}]
  • ECO:0000353 PMID:20935677 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
  • ECO:0000353 PMID:20935677 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:21203579 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:21258405 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P15941"}]}]
  • ECO:0000353 PMID:21278786 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:21278786 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:21278786 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:21278788 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
  • ECO:0000353 PMID:21278788 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:21278788 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:21278788 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13480"}]}]
  • ECO:0000353 PMID:21376233 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05209"}]}]
  • ECO:0000353 PMID:21439278 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:21706016 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:2176151 ↗ IPI · UniProt · 20051128
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20936"}]}]
  • ECO:0000353 PMID:21822280 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:21951318 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92731"}]}]
  • ECO:0000353 PMID:22298428 ↗ IPI · UniProt · 20181115
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6ZTN6"}]}]
  • ECO:0000353 PMID:22298428 ↗ IPI · UniProt · 20181115
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86YJ7"}]}]
  • ECO:0000353 PMID:22298428 ↗ IPI · UniProt · 20181115
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8IZ07"}]}]
  • ECO:0000353 PMID:22411794 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q03135"}]}]
  • ECO:0000353 PMID:22439932 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:22439932 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01973"}]}]
  • ECO:0000353 PMID:22939624 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
  • ECO:0000353 PMID:23178716 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:23178716 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:23273428 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
  • ECO:0000353 PMID:23397142 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08631"}]}]
  • ECO:0000353 PMID:23397142 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46109"}]}]
  • ECO:0000353 PMID:23436906 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:23436906 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:23520446 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14965"}]}]
  • ECO:0000353 PMID:23597562 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:23636329 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UKV8"}]}]
  • ECO:0000353 PMID:23764002 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07948"}]}]
  • ECO:0000353 PMID:23764002 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07948-1"}]}]
  • ECO:0000353 PMID:23799367 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:23799367 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:23799367 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:23866081 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:23866081 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07947"}]}]
  • ECO:0000353 PMID:23866081 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07948"}]}]
  • ECO:0000353 PMID:23866081 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08581"}]}]
  • ECO:0000353 PMID:23866081 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:23912460 ↗ IPI · UniProt · 20150902
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q5T0W9"}]}]
  • ECO:0000353 PMID:24034250 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92622"}]}]
  • ECO:0000353 PMID:24076656 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q70E73"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60716"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04083"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08581"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P11142"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12830"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27348"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31947"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P38646"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q09666"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q10567"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16543"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q71U36"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96CW1"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQB8"}]}]
  • ECO:0000353 PMID:24557338 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00459"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00750"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43561"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60603"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60716"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75791"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00519"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01135"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04049"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04150"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04406"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06493"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07948"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08631"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P09769"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P10599"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P11142"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12830"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P14923"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P15311"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P15941"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16234"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16333"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16885"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P17252"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23528"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P26447"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27348"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353-7"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31749"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31947"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P32121"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P34932"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42224"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42229"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42684"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P43403"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46108"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46108-1"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46109"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49069"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49407"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51451"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51636"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P63104"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q03135"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05209"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05397"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12929"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12933"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13094"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13239"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13322"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13387"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13480"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14247"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15750"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q68CZ2"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6S5L8"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q71U36"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8WUI4"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92569"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92625"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92870"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BRG2"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NRF2"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NSE2"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NZM3"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UBN7"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UNE7"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UPY6"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQB8"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y2R2"}]}]
  • ECO:0000353 PMID:24947832 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q38SD2"}]}]
  • ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13451"}]}]
  • ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16543"}]}]
  • ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q53FC7"}]}]
  • ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6PK50"}]}]
  • ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96BE0"}]}]
  • ECO:0000353 PMID:25136068 ↗ IPI · AgBase · 20170807
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07355"}]}]
  • ECO:0000353 PMID:25136068 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07355"}]}]
  • ECO:0000353 PMID:25187647 ↗ IPI · UniProt · 20191107
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q3V6T2"}]}]
  • ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12830"}]}]
  • ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16885"}]}]
  • ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
  • ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92569"}]}]
  • ECO:0000353 PMID:25311788 ↗ IPI · UniProt · 20150722
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8NFJ5"}]}]
  • ECO:0000353 PMID:25594178 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q80U62"}]}]
  • ECO:0000353 PMID:25594178 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92622"}]}]
  • ECO:0000353 PMID:25594178 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96A65"}]}]
  • ECO:0000353 PMID:25666625 ↗ IPI · UniProt · 20150420
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O95994"}]}]
  • ECO:0000353 PMID:25873175 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P30530"}]}]
  • ECO:0000353 PMID:25970784 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23470"}]}]
  • ECO:0000353 PMID:26005835 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q07889"}]}]
  • ECO:0000353 PMID:26280537 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:26280537 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P14174"}]}]
  • ECO:0000353 PMID:26551075 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08581"}]}]
  • ECO:0000353 PMID:26551075 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:26751287 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14956"}]}]
  • ECO:0000353 PMID:26751287 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14956-1"}]}]
  • ECO:0000353 PMID:26988023 ↗ IPI · UniProt · 20191218
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00264"}]}]
  • ECO:0000353 PMID:27059931 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:27059931 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:27569582 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8NBJ4"}]}]
  • ECO:0000353 PMID:27872189 ↗ IPI · DisProt · 20250508
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:2790960 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:27956147 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75563"}]}]
  • ECO:0000353 PMID:27956147 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49418"}]}]
  • ECO:0000353 PMID:27956147 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q7L591"}]}]
  • ECO:0000353 PMID:27956147 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8TEY7"}]}]
  • ECO:0000353 PMID:27956147 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8WXI2"}]}]
  • ECO:0000353 PMID:27956147 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BRK4"}]}]
  • ECO:0000353 PMID:27956147 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NS73"}]}]
  • ECO:0000353 PMID:27956147 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y6A5"}]}]
  • ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
  • ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18433"}]}]
  • ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23467"}]}]
  • ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P35813"}]}]
  • ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05209"}]}]
  • ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
  • ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9HD43"}]}]
  • ECO:0000353 PMID:28479384 ↗ IPI · UniProt · 20170828
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86VI4"}]}]
  • ECO:0000353 PMID:28988771 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14944"}]}]
  • ECO:0000353 PMID:28988771 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:28988771 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01135"}]}]
  • ECO:0000353 PMID:28988771 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6UW88"}]}]
  • ECO:0000353 PMID:28988771 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99075"}]}]
  • ECO:0000353 PMID:29455656 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46934"}]}]
  • ECO:0000353 PMID:29844572 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y6Q6-2"}]}]
  • ECO:0000353 PMID:30083275 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:30083275 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P26447"}]}]
  • ECO:0000353 PMID:31585087 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:31585087 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:31585087 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NRF2"}]}]
  • ECO:0000353 PMID:31585087 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9QZC5"}]}]
  • ECO:0000353 PMID:31585087 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQC2"}]}]
  • ECO:0000353 PMID:31862538 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00170"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00459"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00750"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43561"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60603"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60716"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75791"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00519"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01135"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04049"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04083"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04150"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04406"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06493"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07948"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08575"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08631"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P09769"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P09936"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P10599"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P11142"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12830"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P14923"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P15311"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P15941"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16234"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16333"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16885"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P17174"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P17252"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18433"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23467"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23470"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23528"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P26447"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27348"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31749"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31947"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31948"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P32121"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P34932"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P38646"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42224"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42229"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42684"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P43403"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46108"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46109"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49069"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49407"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51451"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51636"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P60520"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P63104"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q02952"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q03135"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05209"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05397"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q09666"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12852"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12929"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12933"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13094"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13239"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13322"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13387"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13480"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14247"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14318"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15750"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16543"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q68CZ2"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6S5L8"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q71U36"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8WUI4"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92569"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92625"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92870"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96CW1"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BRG2"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NRF2"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NSE2"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NZM3"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9P0L0"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UBN7"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UNE7"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UPY6"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQB8"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y2H9"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y2R2"}]}]
  • ECO:0000353 PMID:33420426 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P0DTC2"}]}]
  • ECO:0000353 PMID:34591612 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13451"}]}]
  • ECO:0000353 PMID:34591642 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:34591642 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q07889"}]}]
  • ECO:0000353 PMID:34591642 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13438"}]}]
  • ECO:0000353 PMID:34591642 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8IZW8"}]}]
  • ECO:0000353 PMID:34591642 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
  • ECO:0000353 PMID:34718348 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60493"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00459"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60493"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07355"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P14923"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P15311"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16333"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P47869"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49757"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P61619"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q10567"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12929"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13438"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13480"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13885"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15750"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16543"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92625"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96CW1"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BXW9"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NZM3"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9P0L0"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UBV2"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UKG1"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQB8"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y6R0"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14965"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P03372"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04049"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16885"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P17174"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P30530"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31749"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P32121"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P43405"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49407"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13882"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92622"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BXW9"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NS73"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UPY6"}]}]
  • ECO:0000353 PMID:37100772 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96CW1"}]}]
  • ECO:0000353 PMID:39073202 ↗ IPI · UniProt · 20250430
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86XE0"}]}]
  • ECO:0000353 PMID:7518560 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:7518560 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:7542744 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:7657591 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
  • ECO:0000353 PMID:7657591 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22682"}]}]
  • ECO:0000353 PMID:7685104 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20417"}]}]
  • ECO:0000353 PMID:7693694 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
  • ECO:0000353 PMID:7693694 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20417"}]}]
  • ECO:0000353 PMID:7797556 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
  • ECO:0000353 PMID:7993895 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
  • ECO:0000353 PMID:8034616 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:8305738 ↗ IPI · WB · 20141120
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29355"}]}]
  • ECO:0000353 PMID:8621392 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20417"}]}]
  • ECO:0000353 PMID:8887653 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:8940013 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:9020117 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
  • ECO:0000353 PMID:9020117 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
  • ECO:0000353 PMID:9135143 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
  • ECO:0000353 PMID:9135143 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99075"}]}]
  • ECO:0000353 PMID:9419975 ↗ IPI · UniProt · 20060120
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14944"}]}]
  • ECO:0000353 PMID:9506989 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13322"}]}]
  • ECO:0000353 PMID:9544989 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
  • ECO:0000353 PMID:9852145 ↗ IPI · UniProt · 20140307
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q62384"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:14966128 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:21266349 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P97313"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:24135280 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:24780295 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07992"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:15611079 ↗ IPI · HGNC-UCL · 20240211
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6UW88"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0007173", "relation": "part_of"}, {"db": "GO", "id": "0008284", "relation": "part_of"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:17403676 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13671"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005768", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:25594178 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86VI4"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005768", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:21349850 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46940"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005911", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0001726", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0030027", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:23178489 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P17936"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0045121", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:24034250 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14457"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0031410", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14457"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0031410", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:25796184 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:9050838 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:9355745 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:24854121 ↗ IPI · ARUK-UCL · 20190920
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99962"}]}]
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:25353163 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O94898"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005886", "relation": "occurs_in"}]}]
protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0005515 · evidence & context
  • ECO:0000353 PMID:30662352 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43752"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005802", "relation": "occurs_in"}]}]
ATP bindingenablesUniProtKB:P00533
GO
GO:0005524 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR000719"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR017441"}]}]
kinase activityenablesUniProtKB:P00533
GO
GO:0016301 · evidence & context
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
enzyme bindingenablesUniProtKB:P00533
GO
GO:0019899 · evidence & context
  • ECO:0000353 PMID:12009895 ↗ IPI · UniProt · 20110815
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O15162"}]}]
kinase bindingenablesUniProtKB:P00533
GO
GO:0019900 · evidence & context
  • ECO:0000353 PMID:18722344 ↗ IPI · UniProt · 20200619
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46108"}]}]
  • ECO:0000353 PMID:22732145 ↗ IPI · ParkinsonsUK-UCL · 20241220
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P52824"}]}]
protein phosphatase bindingenablesUniProtKB:P00533
GO
GO:0019903 · evidence & context
  • ECO:0000353 PMID:15899872 ↗ IPI · UniProt · 20081218
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15262"}]}]
  • ECO:0000353 PMID:28759036 ↗ IPI · BHF-UCL · 20180719
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51452"}]}]
protein tyrosine kinase activator activityenablesUniProtKB:P00533
GO
GO:0030296 · evidence & context
ubiquitin protein ligase bindingenablesUniProtKB:P00533
GO
GO:0031625 · evidence & context
  • ECO:0000353 PMID:23418353 ↗ IPI · UniProt · 20140827
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q91YL2"}]}]
  • ECO:0000353 PMID:23418353 ↗ IPI · UniProt · 20140827
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9D0C1"}]}]
identical protein bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0042802 · evidence & context
  • ECO:0000353 PMID:16777603 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:18042729 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:19563760 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:19650109 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:20007378 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:20359299 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:21278786 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:21480528 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:21482778 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:22232519 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:22579287 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:23273428 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:23374349 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:23436906 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:23636329 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:24135280 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:28988771 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
  • ECO:0000353 PMID:38572507 ↗ IPI · IntAct · 20260725
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
cadherin bindingenablesUniProtKB:P00533
GO
GO:0045296 · evidence & context
epidermal growth factor bindingenablesUniProtKB:P00533
GO
GO:0048408 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20200401
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN002814603"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}]
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
actin filament bindingenablesUniProtKB:P00533
GO
GO:0051015 · evidence & context
ATPase bindingenablesUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0051117 · evidence & context
  • ECO:0000250 GO_REF:0000024 ISS · ARUK-UCL · 20251229
    qualifier: enables
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "F1N7F3"}]}]
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000019", "relation": "occurs_in"}, {"db": "GO", "id": "0045121", "relation": "occurs_in"}]}]
MAPK cascadeinvolved inUniProtKB:P00533
GO
GO:0000165 · evidence & context
  • ECO:0000364 GO_REF:0000108 IEA · GOC · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "GO", "id": "0004709"}]}]
ossificationinvolved inUniProtKB:P00533
GO
GO:0001503 · evidence & context
positive regulation of protein phosphorylationinvolved inUniProtKB:P00533
GO
GO:0001934 · evidence & context
signal transductioninvolved inUniProtKB:P00533
GO
GO:0007165 · evidence & context
  • ECO:0000314 PMID:10572067 ↗ IDA · UniProt · 20060227
    qualifier: involved_in
  • ECO:0000304 Reactome:R-HSA-212718 TAS · Reactome · 20260316
    qualifier: involved_in
cell surface receptor protein tyrosine kinase signaling pathwayinvolved inUniProtKB:P00533
GO
GO:0007169 · evidence & context
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}]
epidermal growth factor receptor signaling pathwayinvolved inUniProtKB:P00533
GO
GO:0007173 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20240924
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "69323"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00002299"}]}]
  • ECO:0000314 PMID:12435727 ↗ IDA · UniProt · 20050812
    qualifier: involved_in
  • ECO:0000315 PMID:17655843 ↗ IMP · BHF-UCL · 20230717
    qualifier: involved_in
  • ECO:0000315 PMID:20878056 ↗ IMP · UniProt · 20170522
    qualifier: involved_in
  • ECO:0000314 PMID:9890893 ↗ IDA · MGI · 20220118
    qualifier: involved_in
  • ECO:0000304 Reactome:R-HSA-177929 TAS · Reactome · 20260316
    qualifier: involved_in
epidermal growth factor receptor signaling pathwayinvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0007173 · evidence & context
  • ECO:0000314 PMID:12828935 ↗ IDA · UniProt · 20231211
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0004517", "relation": "positively_regulates"}]}]
epidermal growth factor receptor signaling pathwayinvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0007173 · evidence & context
  • ECO:0000315 PMID:18483258 ↗ IMP · BHF-UCL · 20241216
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0070141", "relation": "part_of"}, {"db": "GO", "id": "1900087", "relation": "causally_upstream_of"}, {"db": "CL", "id": "0000312", "relation": "occurs_in"}]}]
epidermal growth factor receptor signaling pathwayinvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0007173 · evidence & context
  • ECO:0000314 PMID:24854121 ↗ IDA · ARUK-UCL · 20241213
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "occurs_in"}]}]
learning or memoryinvolved inUniProtKB:P00533
GO
GO:0007611 · evidence & context
  • ECO:0000250 GO_REF:0000024 ISS · UniProt · 20131108
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "G3V6K6"}]}]
positive regulation of cell population proliferationinvolved inUniProtKB:P00533
GO
GO:0008284 · evidence & context
negative regulation of macroautophagyinvolved inUniProtKB:P00533
GO
GO:0016242 · evidence & context
neuron differentiationinvolved inUniProtKB:P00533
GO
GO:0030182 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:104771"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "RGD", "id": "69323"}]}, {"connectedXrefs": [{"db": "ZFIN", "id": "ZDB-GENE-031118-121"}]}]
positive regulation of cell growthinvolved inUniProtKB:P00533
GO
GO:0030307 · evidence & context
positive regulation of cell migrationinvolved inUniProtKB:P00533
GO
GO:0030335 · evidence & context
positive regulation of peptidyl-serine phosphorylationinvolved inUniProtKB:P00533
GO
GO:0033138 · evidence & context
positive regulation of toll-like receptor 9 signaling pathwayinvolved inUniProtKB:P00533
GO
GO:0034165 · evidence & context
ERBB2-EGFR signaling pathwayinvolved inUniProtKB:P00533
GO
GO:0038134 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00087731"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
  • ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20211214
    qualifier: involved_in
negative regulation of epidermal growth factor receptor signaling pathwayinvolved inUniProtKB:P00533
GO
GO:0042059 · evidence & context
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00086227"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
  • ECO:0000304 Reactome:R-HSA-182971 TAS · Reactome · 20260316
    qualifier: involved_in
negative regulation of protein catabolic processinvolved inUniProtKB:P00533
GO
GO:0042177 · evidence & context
positive regulation of phosphorylationinvolved inUniProtKB:P00533
GO
GO:0042327 · evidence & context
negative regulation of apoptotic processinvolved inUniProtKB:P00533
GO
GO:0043066 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:104771"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95411"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620486"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
  • ECO:0000315 PMID:18070883 ↗ IMP · UniProt · 20110318
    qualifier: involved_in
positive regulation of MAPK cascadeinvolved inUniProtKB:P00533
GO
GO:0043410 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95411"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
positive regulation of MAPK cascadeinvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0043410 · evidence & context
  • ECO:0000314 PMID:24854121 ↗ IDA · ARUK-UCL · 20241213
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "occurs_in"}, {"db": "GO", "id": "0007173", "relation": "part_of"}]}]
phosphatidylinositol 3-kinase/protein kinase B signal transductioninvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0043491 · evidence & context
  • ECO:0000315 PMID:18483258 ↗ IMP · BHF-UCL · 20241216
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0070141", "relation": "part_of"}, {"db": "GO", "id": "1900087", "relation": "causally_upstream_of"}, {"db": "CL", "id": "0000312", "relation": "occurs_in"}]}]
positive regulation of DNA repairinvolved inUniProtKB:P00533
GO
GO:0045739 · evidence & context
positive regulation of DNA replicationinvolved inUniProtKB:P00533
GO
GO:0045740 · evidence & context
positive regulation of transcription by RNA polymerase IIinvolved inUniProtKB:P00533
GO
GO:0045944 · evidence & context
positive regulation of fibroblast proliferationinvolved inUniProtKB:P00533
GO
GO:0048146 · evidence & context
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
positive regulation of epithelial cell proliferationinvolved inUniProtKB:P00533
GO
GO:0050679 · evidence & context
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20240924
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620486"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
  • ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00089519"}]}]
  • ECO:0000314 PMID:10572067 ↗ IDA · UniProt · 20060227
    qualifier: involved_in
regulation of peptidyl-tyrosine phosphorylationinvolved inUniProtKB:P00533
GO
GO:0050730 · evidence & context
protein insertion into membraneinvolved inUniProtKB:P00533
GO
GO:0051205 · evidence & context
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transductioninvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0051897 · evidence & context
  • ECO:0000315 PMID:17655843 ↗ IMP · BHF-UCL · 20230717
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0007173", "relation": "part_of"}]}]
response to UV-Ainvolved inUniProtKB:P00533
GO
GO:0070141 · evidence & context
positive regulation of ERK1 and ERK2 cascadeinvolved inUniProtKB:P00533
GO
GO:0070374 · evidence & context
  • ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00085202"}]}]
  • ECO:0000314 PMID:20551055 ↗ IDA · UniProt · 20130828
    qualifier: involved_in
  • ECO:0000315 PMID:21673316 ↗ IMP · BHF-UCL · 20160504
    qualifier: involved_in
cellular response to amino acid stimulusinvolved inUniProtKB:P00533
GO
GO:0071230 · evidence & context
  • ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
cellular response to epidermal growth factor stimulusinvolved inUniProtKB:P00533
GO
GO:0071364 · evidence & context
  • ECO:0000250 GO_REF:0000024 ISS · UniProt · 20131108
    qualifier: involved_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "G3V6K6"}]}]
cellular response to estradiol stimulusinvolved inUniProtKB:P00533
GO
GO:0071392 · evidence & context
positive regulation of protein kinase C signalinginvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:0090037 · evidence & context
  • ECO:0000314 PMID:22732145 ↗ IDA · ParkinsonsUK-UCL · 20241220
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "GO", "id": "0072659", "relation": "positively_regulates"}, {"db": "GO", "id": "0007173", "relation": "part_of"}]}]
positive regulation of canonical Wnt signaling pathwayinvolved inUniProtKB:P00533
GO
GO:0090263 · evidence & context
cell-cell adhesioninvolved inUniProtKB:P00533
GO
GO:0098609 · evidence & context
positive regulation of cGAS/STING signaling pathwayinvolved inUniProtKB:P00533
GO
GO:0141111 · evidence & context
positive regulation of miRNA transcriptioninvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:1902895 · evidence & context
  • ECO:0000315 PMID:21673316 ↗ IMP · BHF-UCL · 20220905
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "RNAcentral", "id": "URS0000245997_9606", "relation": "has_input"}]}, {"connectedXrefs": [{"db": "RNAcentral", "id": "URS000077BBBB_9606", "relation": "has_input"}]}]
positive regulation of protein localization to plasma membraneinvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:1903078 · evidence & context
  • ECO:0000314 PMID:22732145 ↗ IDA · ParkinsonsUK-UCL · 20161110
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P52824", "relation": "has_input"}]}]
negative regulation of cardiocyte differentiationinvolved inUniProtKB:P00533 · Context-qualified assertion; see evidence
GO
GO:1905208 · evidence & context
  • ECO:0000315 PMID:23069713 ↗ IMP · BHF-UCL · 20160929
    qualifier: involved_in
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000134", "relation": "occurs_in"}]}]
02

Names & Taxonomy

Recommended name
Epidermal growth factor receptor
Gene
EGFR
Accession / entry
P00533 · EGFR_HUMAN
Species
Homo sapiens · NCBI 9606
Recorded aliases
ERBB · ERBB1 · HER1 · Proto-oncogene c-ErbB-1 · Receptor tyrosine-protein kinase erbB-1
Full taxonomy & recorded names

Eukaryota → Metazoa → Chordata → Craniata → Vertebrata → Euteleostomi → Mammalia → Eutheria → Euarchontoglires → Primates → Haplorrhini → Catarrhini → Hominidae → Homo

{
  "names": {
    "recommendedName": {
      "fullName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000305"
          }
        ],
        "value": "Epidermal growth factor receptor"
      },
      "ecNumbers": [
        {
          "evidences": [
            {
              "evidenceCode": "ECO:0000269",
              "source": "PubMed",
              "id": "32926474"
            }
          ],
          "value": "2.7.10.1"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "value": "Proto-oncogene c-ErbB-1"
        }
      },
      {
        "fullName": {
          "value": "Receptor tyrosine-protein kinase erbB-1"
        }
      }
    ],
    "flag": "Precursor"
  },
  "genes": [
    {
      "geneName": {
        "evidences": [
          {
            "evidenceCode": "ECO:0000303",
            "source": "PubMed",
            "id": "32926474"
          },
          {
            "evidenceCode": "ECO:0000312",
            "source": "HGNC",
            "id": "HGNC:3236"
          }
        ],
        "value": "EGFR"
      },
      "synonyms": [
        {
          "value": "ERBB"
        },
        {
          "value": "ERBB1"
        },
        {
          "value": "HER1"
        }
      ]
    }
  ]
}
03

Subcellular Location

UniProt locations and GO cellular-component assertions. Relations and contexts remain distinct; “part of” is not automatically a residence claim.

Cell membraneReported location

Single-pass type I membrane protein

In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER [52, 68]. Endocytosed upon activation by ligand [54, 52, 88, 24]. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) [69]

UniProt
Experimental evidence 7 publications
Evidence & references
Endoplasmic reticulum membraneReported location

Single-pass type I membrane protein

In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER [52, 68]. Endocytosed upon activation by ligand [54, 52, 88, 24]. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) [69]

UniProt
Experimental evidence 1 publication
Evidence & references
Golgi apparatus membraneReported location

Single-pass type I membrane protein

In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER [52, 68]. Endocytosed upon activation by ligand [54, 52, 88, 24]. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) [69]

UniProt
Evidence & references

No separate evidence record is supplied for this statement.

Nucleus membraneReported location

Single-pass type I membrane protein

In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER [52, 68]. Endocytosed upon activation by ligand [54, 52, 88, 24]. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) [69]

UniProt
Evidence & references

No separate evidence record is supplied for this statement.

EndosomeReported location

In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER [52, 68]. Endocytosed upon activation by ligand [54, 52, 88, 24]. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) [69]

UniProt
Experimental evidence 2 publications
Evidence & references
Endosome membraneReported location

In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER [52, 68]. Endocytosed upon activation by ligand [54, 52, 88, 24]. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) [69]

UniProt
Evidence & references

No separate evidence record is supplied for this statement.

NucleusReported location

In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER [52, 68]. Endocytosed upon activation by ligand [54, 52, 88, 24]. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) [69]

UniProt
Experimental evidence 4 publications
Evidence & references
SecretedReported location

Isoform 2

UniProt
Evidence & references

No separate evidence record is supplied for this statement.

All recorded location assertions (40)
endosomecolocalizes with
GO
1 publication
Evidence & references
  • ECO:0000314 PMID:16554368 ↗ IDA · ParkinsonsUK-UCL · 20160801
    qualifier: colocalizes_with
plasma membraneis active in
GO
3 publications
Evidence & references
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529
    qualifier: is_active_in
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003366"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0010389"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0011829"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0015380"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0032006"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0285896"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:101766"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:103581"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95524"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95559"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96433"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96575"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96677"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96683"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96840"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:97384"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:99614"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:99654"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN001230349"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2252"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2869"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2917"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3211"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3213"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3284"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3285"}]}, {"connectedXrefs": [{"db": "RGD", "id": "619855"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620144"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620568"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620713"}]}, {"connectedXrefs": [{"db": "RGD", "id": "69323"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "G1K218"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "O15146"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P08069"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P09619"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P10721"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P11362"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P17948"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21709"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21802"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P22455"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P22607"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35590"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35968"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01973"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q05688"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q08345"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q12866"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16832"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q91987"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9PVZ4"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UM73"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00000289"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00000898"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00002299"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00003007"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00006868"}]}, {"connectedXrefs": [{"db": "ZFIN", "id": "ZDB-GENE-070209-277"}]}]
  • ECO:0000314 PMID:11331309 ↗ IDA · ARUK-UCL · 20210224
    qualifier: is_active_in
  • ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20211214
    qualifier: is_active_in
  • ECO:0000314 PMID:15611079 ↗ IDA · MGI · 20220309
    qualifier: is_active_in
basal plasma membraneis active in
GO
Evidence & references
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20210227
    qualifier: is_active_in
    withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00002299"}]}]
early endosome membraneis active in
GO
1 publication
Evidence & references
ruffle membraneis active in
GO
1 publication
Evidence & references
Golgi membranelocated in
GO
Evidence & references
  • ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0134"}]}]
extracellular regionlocated in
GO
Published statement 1 publication
Evidence & references
  • ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0243"}]}]
  • ECO:0000303 PMID:9103388 ↗ NAS · UniProt · 20050811
    qualifier: located_in
nucleuslocated in
GO
Experimental evidence 5 publications
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00026330"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0191"}]}]
  • ECO:0000314 PMID:12828935 ↗ IDA · UniProt · 20050812
    qualifier: located_in
  • ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011
    qualifier: located_in
  • ECO:0000269 PMID:17909029 ↗ EXP · UniProt · 20251027
    qualifier: located_in
  • ECO:0000314 PMID:20551055 ↗ IDA · UniProt · 20130828
    qualifier: located_in
  • ECO:0000269 PMID:20674546 ↗ EXP · UniProt · 20251027
    qualifier: located_in
cytoplasmlocated in
GO
3 publications
Evidence & references
endosomelocated in
GO
Experimental evidence 4 publications
Evidence & references
  • ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0101"}]}]
  • ECO:0000314 PMID:14702346 ↗ IDA · UniProt · 20050812
    qualifier: located_in
  • ECO:0000314 PMID:17182860 ↗ IDA · UniProt · 20110301
    qualifier: located_in
  • ECO:0000314 PMID:22732145 ↗ IDA · ParkinsonsUK-UCL · 20241220
    qualifier: located_in
  • ECO:0000269 PMID:27153536 ↗ EXP · UniProt · 20251027
    qualifier: located_in
endoplasmic reticulum membranelocated in
GO
Experimental evidence 1 publication
Evidence & references
  • ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0097"}]}]
  • ECO:0000269 PMID:27153536 ↗ EXP · UniProt · 20251027
    qualifier: located_in
Golgi apparatuslocated in
GO
Evidence & references
  • ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115
    qualifier: located_in
plasma membranelocated in
GO
Experimental evidence 12 publications
Evidence & references
  • ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115
    qualifier: located_in
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0039"}]}]
  • ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20220304
    qualifier: located_in
  • ECO:0000314 PMID:15465819 ↗ IDA · HGNC-UCL · 20050704
    qualifier: located_in
  • ECO:0000314 PMID:15611079 ↗ IDA · MGI · 20220309
    qualifier: located_in
  • ECO:0000269 PMID:17182860 ↗ EXP · UniProt · 20251027
    qualifier: located_in
  • ECO:0000314 PMID:20462955 ↗ IDA · UniProt · 20191114
    qualifier: located_in
  • ECO:0000314 PMID:22298428 ↗ IDA · UniProt · 20181116
    qualifier: located_in
  • ECO:0000314 PMID:22732145 ↗ IDA · ParkinsonsUK-UCL · 20161109
    qualifier: located_in
  • ECO:0000269 PMID:23589287 ↗ EXP · UniProt · 20251027
    qualifier: located_in
  • ECO:0000314 PMID:26918609 ↗ IDA · UniProt · 20251218
    qualifier: located_in
  • ECO:0000269 PMID:27153536 ↗ EXP · UniProt · 20251027
    qualifier: located_in
  • ECO:0000269 PMID:2790960 ↗ EXP · UniProt · 20251027
    qualifier: located_in
  • ECO:0000269 PMID:35538033 ↗ EXP · UniProt · 20251027
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1169421 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1218833 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1220610 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1220611 TAS · Reactome · 20181029
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1220612 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1220613 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1220614 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225947 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225949 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225950 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225951 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225952 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225956 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225957 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225960 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225961 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1225978 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1226012 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1226014 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1226016 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1247841 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1247842 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1247844 TAS · Reactome · 20181108
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1247999 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1248002 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1248655 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1248677 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1250195 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1306957 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1306963 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1306965 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177922 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177923 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177924 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177925 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177926 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177927 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177930 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177933 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177934 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177935 TAS · Reactome · 20230122
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177936 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177937 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177938 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177939 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177941 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177942 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177943 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177944 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-177945 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-182969 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-182986 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-182990 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-182993 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-182994 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183002 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183036 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183051 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183055 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183058 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183067 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183072 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183084 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-183089 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1963563 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1963581 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1963582 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1963586 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1963589 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-1977959 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-212706 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-212710 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-212713 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2179387 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2179407 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2179415 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2316434 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-2400009 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-445069 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637764 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637765 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637766 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637770 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637792 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637794 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637795 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637796 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637798 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637800 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637801 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637806 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5637808 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5638137 TAS · Reactome · 20130606
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-5672965 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-6785636 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-6785648 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8847995 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8848005 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8857549 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8857555 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8857565 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8857577 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8857583 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8863804 TAS · Reactome · 20230122
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8864029 TAS · Reactome · 20230122
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8864105 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8864125 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8866279 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8867041 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8867044 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8867047 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8867754 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8867756 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868071 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868072 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868230 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868236 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868648 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868651 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868661 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8874797 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8951490 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9018572 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9018573 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9609689 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9610867 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9611147 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9611158 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9625482 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9625487 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9634702 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664567 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664588 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664918 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664933 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664940 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664950 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664976 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664983 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9664991 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665000 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665009 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665032 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665034 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665388 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665389 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665404 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665406 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665407 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665408 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665409 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665410 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665411 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665413 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665415 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665416 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665417 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665697 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665698 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665699 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665700 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665701 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665704 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665705 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665706 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665707 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9665709 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9674531 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9851407 TAS · Reactome · 20060509
    qualifier: located_in
  • ECO:0000304 Reactome:R-NUL-1248744 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-NUL-1251923 TAS · Reactome · 20130516
    qualifier: located_in
  • ECO:0000304 Reactome:R-NUL-1251929 TAS · Reactome · 20130516
    qualifier: located_in
focal adhesionlocated in

UniProtKB:P00533 · [{"connectedXrefs": [{"db": "CL", "id": "0000057", "relation": "part_of"}]}]

GO
1 publication
Evidence & references
  • ECO:0007005 PMID:21423176 ↗ HDA · UniProt · 20140715
    qualifier: located_in
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000057", "relation": "part_of"}]}]
cell surfacelocated in
GO
1 publication
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027349"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
  • ECO:0000314 PMID:25666625 ↗ IDA · UniProt · 20150420
    qualifier: located_in
endosome membranelocated in
GO
1 publication
Evidence & references
  • ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0100"}]}]
  • ECO:0000314 PMID:22719997 ↗ IDA · UniProt · 20140723
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-9611147 TAS · Reactome · 20180615
    qualifier: located_in
membranelocated in
GO
1 publication
Evidence & references
  • ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}]
  • ECO:0000314 PMID:12435727 ↗ IDA · UniProt · 20050812
    qualifier: located_in
basolateral plasma membranelocated in
GO
1 publication
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00086715"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
  • ECO:0000314 PMID:12646923 ↗ IDA · BHF-UCL · 20080227
    qualifier: located_in
cell junctionlocated in
GO
Evidence & references
  • ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115
    qualifier: located_in
endocytic vesiclelocated in
GO
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027489"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
clathrin-coated endocytic vesicle membranelocated in
GO
Evidence & references
  • ECO:0000304 Reactome:R-HSA-8868658 TAS · Reactome · 20190206
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868659 TAS · Reactome · 20190206
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868660 TAS · Reactome · 20190206
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8868661 TAS · Reactome · 20190206
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8869438 TAS · Reactome · 20190206
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8871193 TAS · Reactome · 20190206
    qualifier: located_in
  • ECO:0000304 Reactome:R-HSA-8871194 TAS · Reactome · 20190206
    qualifier: located_in
early endosome membranelocated in
GO
1 publication
Evidence & references
nuclear membranelocated in
GO
Evidence & references
  • ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0182"}]}]
membrane raftlocated in

UniProtKB:P00533 · [{"connectedXrefs": [{"db": "CL", "id": "0000019", "relation": "part_of"}]}]

GO
By similarity
Evidence & references
  • ECO:0000250 GO_REF:0000024 ISS · ARUK-UCL · 20190919
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "F1N7F3"}]}]
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000019", "relation": "part_of"}]}]
membrane raftlocated in
GO
1 publication
Evidence & references
perinuclear region of cytoplasmlocated in
GO
Evidence & references
  • ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724
    qualifier: located_in
    withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00091589"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
perinuclear region of cytoplasmlocated in

UniProtKB:P00533 · [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "part_of"}]}]

GO
1 publication
Evidence & references
  • ECO:0000315 PMID:24854121 ↗ IMP · ARUK-UCL · 20190920
    qualifier: located_in
    extensions: [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "part_of"}]}]
multivesicular body, internal vesicle lumenlocated in
GO
1 publication
Evidence & references
intracellular vesiclelocated in
GO
1 publication
Evidence & references
protein-containing complexpart of
GO
1 publication
Evidence & references
signaling receptor complexpart of
GO
1 publication
Evidence & references
  • ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529
    qualifier: part_of
    withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0015380"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0024245"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0033791"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0283499"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN001230349"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "A6QR62"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "O15146"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04629"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P06213"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P07333"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P07949"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P08069"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P11362"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P14616"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P17948"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35916"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01973"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q08345"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16288"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}]
  • ECO:0000314 PMID:23382219 ↗ IDA · MGI · 20131224
    qualifier: part_of
Shc-EGFR complexpart of
GO
By similarity
Evidence & references
  • ECO:0000250 GO_REF:0000024 ISS · BHF-UCL · 20090415
    qualifier: part_of
    withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9QX70"}]}]

Membrane topology 3

Scroll across the table for evidence and actions.

3 recorded rows

FeaturePositionDescriptionEvidenceInspect
Topological domain25–645Extracellular
Sequence analysis
Evidence & references
  • ECO:0000255
No verified residues in this structure
Transmembrane646–668Helical
Sequence analysis
Evidence & references
  • ECO:0000255
No verified residues in this structure
Topological domain669–1210Cytoplasmic
Sequence analysis
Evidence & references
  • ECO:0000255
No verified residues in this structure
04

Disease & Variants

Source annotations; a recorded variant is not automatically a clinical classification.

Lung cancer LNCR

A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.

Experimental evidence 3 publications
Evidence & references

The gene represented in this entry is involved in disease pathogenesis

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Lung cancer",
    "diseaseAccession": "DI-02205",
    "acronym": "LNCR",
    "description": "A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "211980"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "15118125"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "16533793"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "16672372"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The gene represented in this entry is involved in disease pathogenesis"
      }
    ]
  }
}

Neonatal nephrocutaneous inflammatory syndrome NNCIS

An autosomal recessive disorder characterized by intrauterine growth retardation, premature birth, fragile skin, recurrent skin infections and sepsis, failure to thrive, nephrocalcinosis, and nephromegaly with tubular dysfunction. Some patients have chronic diarrhea, and necrotizing enterocolitis.

Experimental evidence 1 publication
Evidence & references

The disease is caused by variants affecting the gene represented in this entry

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation
{
  "commentType": "DISEASE",
  "disease": {
    "diseaseId": "Neonatal nephrocutaneous inflammatory syndrome",
    "diseaseAccession": "DI-04271",
    "acronym": "NNCIS",
    "description": "An autosomal recessive disorder characterized by intrauterine growth retardation, premature birth, fragile skin, recurrent skin infections and sepsis, failure to thrive, nephrocalcinosis, and nephromegaly with tubular dysfunction. Some patients have chronic diarrhea, and necrotizing enterocolitis.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "616069"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "24691054"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The disease is caused by variants affecting the gene represented in this entry"
      }
    ]
  }
}

Natural variants 40

Scroll across the table for evidence and actions.

40 recorded rows

FeaturePositionDescriptionEvidenceInspect
Natural variantVAR_06649330–297variant EGFR vIII; found in a lung cancer sample; somatic mutation; induces lung cancer when exogenously expressed
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R98QVAR_01929398in dbSNP:rs17289589
R → Q
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.7
No verified residues in this structure
P266RVAR_019294266in dbSNP:rs17336639
P → R
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.7
No verified residues in this structure
G428DVAR_072435428in NNCIS; loss of function; the mutant does not localize to the cell membrane; has diffuse cytoplasmic localization; dbSNP:rs606231253
G → D
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R521KVAR_019295521in dbSNP:rs2227983
R → K
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
V674IVAR_019296674in dbSNP:rs17337079
V → I
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.7
No verified residues in this structure
E709AVAR_026084709found in a lung cancer sample; more sensitive to gefitinib than wild-type; dbSNP:rs397517085
E → A
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
E709GVAR_069498709found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type; dbSNP:rs397517085
E → G
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
E709KVAR_026085709found in a lung cancer sample; dbSNP:rs727504256
E → K
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
G719AVAR_026086719found in a lung cancer sample; dbSNP:rs121913428
G → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
G719CVAR_026087719found in a lung cancer sample; dbSNP:rs28929495
G → C
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
G719DVAR_026088719found in a lung cancer sample; dbSNP:rs121913428
G → D
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
G719SVAR_019297719found in a lung cancer sample; somatic mutation; strongly increased kinase activity; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type; dbSNP:rs28929495
G → S
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
G724SVAR_026089724found in a lung cancer sample; dbSNP:rs1051753269
G → S
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
E734KVAR_026090734found in a lung cancer sample; dbSNP:rs121913420
E → K
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
ELREATS746DVAR_069499746–752found in a lung cancer sample
ELREATS → D
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
ELREAT746AVAR_069500746–751found in a lung cancer sample
ELREAT → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Natural variantVAR_026092746–750found in a lung cancer sample
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Natural variantVAR_026091746found in a lung cancer sample
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Natural variantVAR_069501747–751found in a lung cancer sample
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Natural variantVAR_026094747–749found in a lung cancer sample
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
L747FVAR_026093747found in a lung cancer sample; dbSNP:rs2128954811
L → F
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R748PVAR_026095748found in a lung cancer sample
R → P
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Natural variantVAR_026096752–759found in a lung cancer sample
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
S768IVAR_069502768found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type; dbSNP:rs121913465
S → I
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
V769MVAR_069503769found in a lung cancer sample; dbSNP:rs147149347
V → M
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Q787RVAR_026097787found in a lung cancer sample
Q → R
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
T790MVAR_026098790found in a lung cancer sample; increased kinase activity; dbSNP:rs121434569
T → M
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
L833VVAR_026099833found in a lung cancer sample; more sensitive to gefitinib than wild-type; dbSNP:rs397517126
L → V
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
V834LVAR_026100834found in a lung cancer sample; dbSNP:rs397517127
V → L
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
H835LVAR_069504835found in a lung cancer sample; more sensitive to gefitinib than wild-type; dbSNP:rs397517128
H → L
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
L838VVAR_069505838found in a lung cancer sample; more sensitive to gefitinib than wild-type; dbSNP:rs864621996
L → V
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
L858MVAR_026101858found in a lung cancer sample; dbSNP:rs121913443
L → M
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
L858RVAR_019298858found in a lung cancer sample; somatic mutation; constitutively activated enzyme with strongly increased kinase activity; more sensitive to gefitinib than wild-type; dbSNP:rs121434568
L → R
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
L861QVAR_026102861found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type; dbSNP:rs121913444
L → Q
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
G873EVAR_026103873found in a lung cancer sample; dbSNP:rs2128964711
G → E
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R962GVAR_019299962in dbSNP:rs17337451
R → G
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.7
No verified residues in this structure
H988PVAR_019300988in dbSNP:rs17290699
H → P
Experimental evidence
Evidence & references
  • ECO:0000269 Reference:Ref.7
No verified residues in this structure
L1034RVAR_0420951034in dbSNP:rs34352568
L → R
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
A1210VVAR_0420961210in dbSNP:rs35918369
A → V
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure

Laboratory mutagenesis 37

Scroll across the table for evidence and actions.

37 recorded rows

FeaturePositionDescriptionEvidenceInspect
Y275A275Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309.
Y → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
F287A287Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309.
F → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R309S309Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-275. Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-287.
R → S
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R429E429Abolishes autophosphorylation and activation of downstream kinases.
R → E
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Mutagenesis525–1210Increased EGF binding.
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
DGPH587AGPA587–590Decreases intramolecular interactions and facilitates EGF binding.
DGPH → AGPA
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
D587A587Increased EGF binding; when associated with A-590 and A-609.
D → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
H590A590Increased EGF binding; when associated with A-587; A-590 and A-609.
H → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
K609A609Decreases intramolecular interactions and facilitates EGF binding. Increased EGF binding; when associated with A-587; A-590 and A-609.
K → A
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
L688A688Strongly reduced phosphorylation.
L → A
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
V689A689Reduced autophosphorylation.
V → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
V689M689Constitutively activated kinase.
V → M
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
E690A690Reduced phosphorylation.
E → A
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
L692A / L692P692Strongly reduced phosphorylation.
L → A, P
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
T693A693Increased phosphorylation.
T → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
T693D693Strongly reduced phosphorylation.
T → D
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
P694A694Strongly reduced phosphorylation.
P → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
P699A699Reduced phosphorylation.
P → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
N700A700Abolishes phosphorylation.
N → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
L704A704Abolishes phosphorylation.
L → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R705A705Abolishes phosphorylation.
R → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
I706A706Abolishes phosphorylation.
I → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
K745A / K745M745Abolishes kinase activity.
K → A, M
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
D974A974Strongly reduced phosphorylation.
D → A
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure
R977A977Reduced phosphorylation.
R → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
ED1005RK1005–1006Constitutively activated kinase.
ED → RK
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Y1016F101650% decrease in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1197. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1092.
Y → F
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Mutagenesis1048–1210Abolishes palmitoylation.
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
C1049A1049Decreased palmitoylation.
C → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Q1067G1067No effect on interaction with CBLC.
Q → G
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
R1068G1068Strongly decreases interaction with CBLC.
R → G
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Y1069F1069Abolishes interaction with CBLC.
Y → F
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Y1092F1092No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016.
Y → F
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Y1110F1110No change in interaction with PIK3C2B.
Y → F
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
C1146A1146Decreased palmitoylation.
C → A
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Y1172F1172No change in interaction with PIK3C2B.
Y → F
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Y1197F1197No change in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1016. Abolishes interaction with PIK3C2B; when associated with F-1092 and F-1016.
Y → F
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
05

PTM/Processing

Phosphorylated on Tyr residues in response to EGF [70, 88]. Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation.

Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3.

Dephosphorylated by PTPN1 and PTPN2

Experimental evidence 10 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10523301"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12873986"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16083266"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19563760"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19836242"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20462955"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21258366"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "2543678"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "27153536"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "3138233"
        }
      ],
      "value": "Phosphorylated on Tyr residues in response to EGF (PubMed:20462955, PubMed:27153536). Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2"
    }
  ],
  "commentType": "PTM"
}

Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting [88]. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation.

Ubiquitinated by RNF115 and RNF126 (By similarity). Ubiquitinated by ZNRF1 or CBL at different lysines in response to EGF stimulation; leading to recruitment of the ESCRT machinery and subsequent degradation in the lysosomes [96]. Deubiquitinated by UCHL1 leading to the inhibition of its degradation (By similarity)

By similarityExperimental evidence 5 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "Q01279"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16543144"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "22179831"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "22298428"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "27153536"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "33996800"
        }
      ],
      "value": "Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting (PubMed:27153536). Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by RNF115 and RNF126 (By similarity). Ubiquitinated by ZNRF1 or CBL at different lysines in response to EGF stimulation; leading to recruitment of the ESCRT machinery and subsequent degradation in the lysosomes (PubMed:33996800). Deubiquitinated by UCHL1 leading to the inhibition of its degradation (By similarity)"
    }
  ],
  "commentType": "PTM"
}

Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "27153536"
        }
      ],
      "value": "Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling"
    }
  ],
  "commentType": "PTM"
}

Neddylated; by NEDD8 [91]. Neddylation results in localization to the cell membrane when activated by EGF. Neddylation also increases protein stability [91]

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "28891468"
        }
      ],
      "value": "Neddylated; by NEDD8 (PubMed:28891468). Neddylation results in localization to the cell membrane when activated by EGF. Neddylation also increases protein stability (PubMed:28891468)"
    }
  ],
  "commentType": "PTM"
}

Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197

Experimental evidence 3 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19563760"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19836242"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21258366"
        }
      ],
      "value": "Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197"
    }
  ],
  "commentType": "PTM"
}

Processed chains & precursor regions 2

Scroll across the table for evidence and actions.

2 recorded rows

FeaturePositionDescriptionEvidenceInspect
Signal1–24Signal
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
ChainPRO_000001666525–1210Epidermal growth factor receptor
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure

Modifications 73

Scroll across the table for evidence and actions.

73 recorded rows

FeaturePositionDescriptionEvidenceInspect
Modified residue229Phosphoserine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue678Phosphothreonine; by PKC and PKD/PRKD1
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue693Phosphothreonine; by PKD/PRKD1
Experimental evidence 7 publications
Evidence & references
No verified residues in this structure
Modified residue695Phosphoserine
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Modified residue745N6-(2-hydroxyisobutyryl)lysine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue869Phosphotyrosine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue991Phosphoserine
Experimental evidence 4 publications
Evidence & references
No verified residues in this structure
Modified residue995Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue998Phosphotyrosine; by autocatalysis
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Modified residue1016Phosphotyrosine; by autocatalysis
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Modified residue1026Phosphoserine
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Modified residue1039Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue1041Phosphothreonine
1 publication
Evidence & references
No verified residues in this structure
Modified residue1042Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue1064Phosphoserine
4 publications
Evidence & references
No verified residues in this structure
Modified residue1069Phosphotyrosine
Experimental evidenceCurator inference 2 publications
Evidence & references
No verified residues in this structure
Modified residue1070Phosphoserine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue1071Phosphoserine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Modified residue1081Phosphoserine
1 publication
Evidence & references
No verified residues in this structure
Modified residue1092Phosphotyrosine; by autocatalysis
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
Modified residue1110Phosphotyrosine; by autocatalysis
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Modified residue1166Phosphoserine
3 publications
Evidence & references
No verified residues in this structure
Modified residue1172Phosphotyrosine; by autocatalysis
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
Modified residue1197Phosphotyrosine; by autocatalysis
Experimental evidence 7 publications
Evidence & references
No verified residues in this structure
Modified residue1199Omega-N-methylarginine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Lipidation1049S-palmitoyl cysteine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Lipidation1146S-palmitoyl cysteine
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
GlycosylationCAR_00022756N-linked (GlcNAc...) (complex) asparagine; atypical; partial
Experimental evidence 6 publications
Evidence & references
No verified residues in this structure
Glycosylation73N-linked (GlcNAc...) asparagine; atypical
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Glycosylation128N-linked (GlcNAc...) asparagine
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
Glycosylation175N-linked (GlcNAc...) asparagine
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Glycosylation196N-linked (GlcNAc...) asparagine
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Glycosylation352N-linked (GlcNAc...) asparagine
Experimental evidence 8 publications
Evidence & references
No verified residues in this structure
Glycosylation361N-linked (GlcNAc...) asparagine
Experimental evidence 6 publications
Evidence & references
No verified residues in this structure
Glycosylation413N-linked (GlcNAc...) asparagine
Experimental evidence 4 publications
Evidence & references
No verified residues in this structure
Glycosylation444N-linked (GlcNAc...) asparagine
Experimental evidence 6 publications
Evidence & references
No verified residues in this structure
Glycosylation528N-linked (GlcNAc...) asparagine
Experimental evidence 6 publications
Evidence & references
No verified residues in this structure
Glycosylation568N-linked (GlcNAc...) asparagine; partial
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Glycosylation603N-linked (GlcNAc...) asparagine; partial
Experimental evidence 4 publications
Evidence & references
No verified residues in this structure
Glycosylation623N-linked (GlcNAc...) (high mannose) asparagine
Curator inference 1 publication
Evidence & references
No verified residues in this structure
Disulfide bond31, 58Disulfide bond
Experimental evidence 3 publications
Evidence & references
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5WB7
  • ECO:0007744 PDB:5WB8
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond157, 187Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond190, 199Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond194, 207Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond215, 223Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond219, 231Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond232, 240Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond236, 248Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond251, 260Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond264, 291Disulfide bond
Experimental evidence 5 publications
Evidence & references
No verified residues in this structure
Disulfide bond295, 307Disulfide bond
Evidence & references
  • ECO:0007744 PDB:1IVO
  • ECO:0007744 PDB:1MOX
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5WB7
  • ECO:0007744 PDB:5WB8
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond311, 326Disulfide bond
Experimental evidence 5 publications
Evidence & references
  • ECO:0000269 PubMed:12297049 ↗
  • ECO:0000269 PubMed:12297050 ↗
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1IVO
  • ECO:0007744 PDB:1MOX
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3G5V
  • ECO:0007744 PDB:3G5Y
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5WB7
  • ECO:0007744 PDB:5WB8
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond329, 333Disulfide bond
Evidence & references
  • ECO:0007744 PDB:1IVO
  • ECO:0007744 PDB:1MOX
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5WB7
  • ECO:0007744 PDB:5WB8
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond337, 362Disulfide bond
Experimental evidence 5 publications
Evidence & references
  • ECO:0000269 PubMed:12297049 ↗
  • ECO:0000269 PubMed:12297050 ↗
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1IVO
  • ECO:0007744 PDB:1MOX
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2U
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3C09
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3P0Y
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRL
  • ECO:0007744 PDB:4KRM
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5SX4
  • ECO:0007744 PDB:5SX5
  • ECO:0007744 PDB:5WB7
  • ECO:0007744 PDB:5WB8
  • ECO:0007744 PDB:5XWD
  • ECO:0007744 PDB:6B3S
No verified residues in this structure
Disulfide bond470, 499Disulfide bond
Evidence & references
  • ECO:0007744 PDB:1IVO
  • ECO:0007744 PDB:1MOX
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2U
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3C09
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3P0Y
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRL
  • ECO:0007744 PDB:4KRM
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5SX4
  • ECO:0007744 PDB:5SX5
  • ECO:0007744 PDB:5WB7
  • ECO:0007744 PDB:5WB8
  • ECO:0007744 PDB:5XWD
  • ECO:0007744 PDB:6B3S
No verified residues in this structure
Disulfide bond506, 515Disulfide bond
Experimental evidence 5 publications
Evidence & references
  • ECO:0000269 PubMed:12297049 ↗
  • ECO:0000269 PubMed:12297050 ↗
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1IVO
  • ECO:0007744 PDB:1MOX
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2U
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3P0Y
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRL
  • ECO:0007744 PDB:4KRM
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5SX4
  • ECO:0007744 PDB:5SX5
  • ECO:0007744 PDB:5WB7
  • ECO:0007744 PDB:5WB8
  • ECO:0007744 PDB:5XWD
  • ECO:0007744 PDB:6B3S
No verified residues in this structure
Disulfide bond510, 523Disulfide bond
Experimental evidence 5 publications
Evidence & references
  • ECO:0000269 PubMed:12297049 ↗
  • ECO:0000269 PubMed:12297050 ↗
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1IVO
  • ECO:0007744 PDB:1MOX
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2U
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3C09
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3P0Y
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRL
  • ECO:0007744 PDB:4KRM
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5SX4
  • ECO:0007744 PDB:5SX5
  • ECO:0007744 PDB:5WB7
  • ECO:0007744 PDB:5WB8
  • ECO:0007744 PDB:5XWD
  • ECO:0007744 PDB:6B3S
No verified residues in this structure
Disulfide bond526, 535Disulfide bond
Experimental evidence 4 publications
Evidence & references
  • ECO:0000269 PubMed:12297050 ↗
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1IVO
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRL
  • ECO:0007744 PDB:4KRM
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond539, 555Disulfide bond
Experimental evidence 3 publications
Evidence & references
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond558, 571Disulfide bond
Experimental evidence 3 publications
Evidence & references
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond562, 579Disulfide bond
Experimental evidence 3 publications
Evidence & references
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond582, 591Disulfide bond
Experimental evidence 3 publications
Evidence & references
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond595, 617Disulfide bond
Experimental evidence 3 publications
Evidence & references
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond620, 628Disulfide bond
Experimental evidence 3 publications
Evidence & references
  • ECO:0000269 PubMed:12620237 ↗
  • ECO:0000269 PubMed:15837620 ↗
  • ECO:0000269 PubMed:20837704 ↗
  • ECO:0007744 PDB:1NQL
  • ECO:0007744 PDB:1YY9
  • ECO:0007744 PDB:3B2V
  • ECO:0007744 PDB:3NJP
  • ECO:0007744 PDB:3QWQ
  • ECO:0007744 PDB:4KRO
  • ECO:0007744 PDB:4KRP
  • ECO:0007744 PDB:4UIP
  • ECO:0007744 PDB:4UV7
  • ECO:0007744 PDB:5XWD
No verified residues in this structure
Disulfide bond624, 636Disulfide bond
Experimental evidence 3 publications
Evidence & references
No verified residues in this structure
Cross-link716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Cross-link737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Cross-link754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Cross-link757Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Cross-link867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental evidence 2 publications
Evidence & references
No verified residues in this structure
Cross-link929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Cross-link960Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
Cross-link970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental evidence 1 publication
Evidence & references
No verified residues in this structure
06

Expression

Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers

Experimental evidence 1 publication
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17671655"
        }
      ],
      "value": "Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers"
    }
  ],
  "commentType": "TISSUE SPECIFICITY"
}
07

Interaction

Documented interaction partners

UniProt’s filtered IntAct records. Experiment counts describe reported experiments, not binding strength or independent publications. Separate products remain separate rows.

200 records
Partner / productSpeciesExperimentsEvidence & actions
ABL1P00519With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P00519. Reported experiment count: 3.

Open protein ↗
ABL2P42684With P00533Homo sapiens9
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P42684. Reported experiment count: 9.

Open protein ↗
AGERQ15109With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q15109. Reported experiment count: 2.

Open protein ↗
AGO2Q9UKV8With P00533Homo sapiens11
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UKV8. Reported experiment count: 11.

Open protein ↗
AHNAKQ09666With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q09666. Reported experiment count: 4.

Open protein ↗
AIPO00170With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O00170. Reported experiment count: 2.

Open protein ↗
AKAP12Q02952With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q02952. Reported experiment count: 3.

Open protein ↗
AKT1P31749With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P31749. Reported experiment count: 4.

Open protein ↗
AMPHP49418With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P49418. Reported experiment count: 2.

Open protein ↗
ANKS1AQ92625With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q92625. Reported experiment count: 7.

Open protein ↗
ANXA1P04083With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P04083. Reported experiment count: 3.

Open protein ↗
ANXA2P07355With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P07355. Reported experiment count: 4.

Open protein ↗
AP1B1Q10567With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q10567. Reported experiment count: 4.

Open protein ↗
AP2M1Q96CW1With P00533Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q96CW1. Reported experiment count: 8.

Open protein ↗
APBB1O00213With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O00213. Reported experiment count: 4.

Open protein ↗
APBB2Q92870With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q92870. Reported experiment count: 7.

Open protein ↗
APBB3O95704With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O95704. Reported experiment count: 2.

Open protein ↗
APPL1Q9UKG1With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UKG1. Reported experiment count: 3.

Open protein ↗
ARRB1P49407With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P49407. Reported experiment count: 3.

Open protein ↗
ARRB2P32121With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P32121. Reported experiment count: 3.

Open protein ↗
AURKAO14965With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O14965. Reported experiment count: 5.

Open protein ↗
AXLP30530With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P30530. Reported experiment count: 5.

Open protein ↗
BAIAP2Q9UQB8With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UQB8. Reported experiment count: 4.

Open protein ↗
BBC3Q9BXH1With P00533Homo sapiens10
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9BXH1. Reported experiment count: 10.

Open protein ↗
BECN1Q14457With P00533Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q14457. Reported experiment count: 8.

Open protein ↗
BLKP51451With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P51451. Reported experiment count: 3.

Open protein ↗
CALM3P62158With P00533Species not verified6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P62158. Reported experiment count: 6.

Open protein ↗
CAMLGP49069With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P49069. Reported experiment count: 3.

Open protein ↗
CAV1Q03135With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q03135. Reported experiment count: 7.

Open protein ↗
CAV2P51636With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P51636. Reported experiment count: 3.

Open protein ↗
CBLP22681With P00533Homo sapiens22
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P22681. Reported experiment count: 22.

Open protein ↗
CDC37Q16543With P00533Homo sapiens13
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q16543. Reported experiment count: 13.

Open protein ↗
CDH1P12830With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P12830. Reported experiment count: 4.

Open protein ↗
CDK1P06493With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P06493. Reported experiment count: 3.

Open protein ↗
CFL1P23528With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P23528. Reported experiment count: 3.

Open protein ↗
CHIAQ9BZP6With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9BZP6. Reported experiment count: 2.

Open protein ↗
CISHQ9NSE2With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9NSE2. Reported experiment count: 4.

Open protein ↗
CLNKQ7Z7G1With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q7Z7G1. Reported experiment count: 2.

Open protein ↗
CNKSR2Q8WXI2With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q8WXI2. Reported experiment count: 2.

Open protein ↗
CRKP46108With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P46108. Reported experiment count: 4.

Open protein ↗
CRKP46108-1With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P46108-1. Reported experiment count: 3.

Open protein ↗
CRKLP46109With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P46109. Reported experiment count: 4.

Open protein ↗
CTNND1O60716With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O60716. Reported experiment count: 5.

Open protein ↗
CTTNQ14247With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q14247. Reported experiment count: 4.

Open protein ↗
DOK3Q7L591With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q7L591. Reported experiment count: 2.

Open protein ↗
DOK6Q6PKX4With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q6PKX4. Reported experiment count: 2.

Open protein ↗
EGFP01133With P00533Homo sapiens29
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P01133. Reported experiment count: 29.

Open protein ↗
EGFRP00533With P00533Homo sapiens31
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P00533. Reported experiment count: 31.

Open protein ↗
EPGNQ6UW88With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q6UW88. Reported experiment count: 3.

Open protein ↗
EPS8Q12929With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q12929. Reported experiment count: 4.

Open protein ↗
ERBB2P04626With P00533Homo sapiens25
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P04626. Reported experiment count: 25.

Open protein ↗
ERBB3P21860With P00533Homo sapiens15
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P21860. Reported experiment count: 15.

Open protein ↗
ERBB4Q15303With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q15303. Reported experiment count: 4.

Open protein ↗
ERCC1P07992With P00533Homo sapiens21
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P07992. Reported experiment count: 21.

Open protein ↗
EREGO14944With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O14944. Reported experiment count: 3.

Open protein ↗
ERRFI1Q9UJM3With P00533Homo sapiens16
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UJM3. Reported experiment count: 16.

Open protein ↗
ESR1P03372With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P03372. Reported experiment count: 3.

Open protein ↗
ESR1P03372-4With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P03372-4. Reported experiment count: 4.

Open protein ↗
ESR2Q92731With P00533Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q92731. Reported experiment count: 8.

Open protein ↗
EXOC4Q96A65With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q96A65. Reported experiment count: 2.

Open protein ↗
EZRP15311With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P15311. Reported experiment count: 3.

Open protein ↗
FANCD2Q9BXW9With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9BXW9. Reported experiment count: 3.

Open protein ↗
FGRP09769With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P09769. Reported experiment count: 3.

Open protein ↗
FKBP5Q13451With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13451. Reported experiment count: 2.

Open protein ↗
FKBP8Q14318With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q14318. Reported experiment count: 4.

Open protein ↗
GAB1Q13480With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13480. Reported experiment count: 5.

Open protein ↗
GAB2Q9UQC2With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UQC2. Reported experiment count: 3.

Open protein ↗
GABARAPL2P60520With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P60520. Reported experiment count: 3.

Open protein ↗
GABRA2P47869With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P47869. Reported experiment count: 2.

Open protein ↗
GAPDHP04406With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P04406. Reported experiment count: 7.

Open protein ↗
GOLM1Q8NBJ4With P00533Homo sapiens13
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q8NBJ4. Reported experiment count: 13.

Open protein ↗
GOT1P17174With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P17174. Reported experiment count: 3.

Open protein ↗
GPNMBQ14956With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q14956. Reported experiment count: 3.

Open protein ↗
GPNMBQ14956-1With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q14956-1. Reported experiment count: 2.

Open protein ↗
GRAP2O75791With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O75791. Reported experiment count: 3.

Open protein ↗
GRB10Q13322With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13322. Reported experiment count: 3.

Open protein ↗
GRB2P62993With P00533Homo sapiens48
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P62993. Reported experiment count: 48.

Open protein ↗
HBEGFQ99075With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q99075. Reported experiment count: 3.

Open protein ↗
HCKP08631With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P08631. Reported experiment count: 3.

Open protein ↗
HDAC6Q9UBN7With P00533Homo sapiens12
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UBN7. Reported experiment count: 12.

Open protein ↗
HDAC7Q8WUI4With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q8WUI4. Reported experiment count: 3.

Open protein ↗
HSP90AA1P07900With P00533Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P07900. Reported experiment count: 8.

Open protein ↗
HSP90AB1P08238With P00533Homo sapiens10
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P08238. Reported experiment count: 10.

Open protein ↗
HSP90AB1Q6PK50With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q6PK50. Reported experiment count: 2.

Open protein ↗
HSPA1BP08107With P00533Species not verified6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P08107. Reported experiment count: 6.

Open protein ↗
HSPA4P34932With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P34932. Reported experiment count: 3.

Open protein ↗
HSPA8P11142With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P11142. Reported experiment count: 7.

Open protein ↗
HSPA9P38646With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P38646. Reported experiment count: 5.

Open protein ↗
IGFBP3P17936With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P17936. Reported experiment count: 3.

Open protein ↗
IQGAP1P46940With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P46940. Reported experiment count: 4.

Open protein ↗
IRS4O14654With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O14654. Reported experiment count: 2.

Open protein ↗
ITSN2Q9NZM3With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9NZM3. Reported experiment count: 3.

Open protein ↗
JUPP14923With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P14923. Reported experiment count: 3.

Open protein ↗
LAPTM4BQ86VI4With P00533Homo sapiens10
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q86VI4. Reported experiment count: 10.

Open protein ↗
LATO43561With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O43561. Reported experiment count: 3.

Open protein ↗
LCP2Q13094With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13094. Reported experiment count: 3.

Open protein ↗
LINGO1Q96FE5With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q96FE5. Reported experiment count: 2.

Open protein ↗
LRIG1Q96JA1With P00533Homo sapiens6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q96JA1. Reported experiment count: 6.

Open protein ↗
LRIG2O94898With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O94898. Reported experiment count: 4.

Open protein ↗
LRRK1Q38SD2With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q38SD2. Reported experiment count: 2.

Open protein ↗
LYNP07948With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P07948. Reported experiment count: 7.

Open protein ↗
LYNP07948-1With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P07948-1. Reported experiment count: 2.

Open protein ↗
LZTS2Q9BRK4With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9BRK4. Reported experiment count: 2.

Open protein ↗
MAP3K12Q12852With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q12852. Reported experiment count: 3.

Open protein ↗
MAPK8IP1Q9UQF2With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UQF2. Reported experiment count: 3.

Open protein ↗
MAPK8IP2Q13387With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13387. Reported experiment count: 5.

Open protein ↗
MAST1Q9Y2H9With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9Y2H9. Reported experiment count: 3.

Open protein ↗
MBIPQ9NS73With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9NS73. Reported experiment count: 3.

Open protein ↗
METP08581With P00533Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P08581. Reported experiment count: 8.

Open protein ↗
MIFP14174With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P14174. Reported experiment count: 3.

Open protein ↗
MUC1P15941With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P15941. Reported experiment count: 4.

Open protein ↗
NCK1P16333With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P16333. Reported experiment count: 5.

Open protein ↗
NEDD4P46934With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P46934. Reported experiment count: 3.

Open protein ↗
NR3C1P04150With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P04150. Reported experiment count: 3.

Open protein ↗
NTRK2Q16620With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q16620. Reported experiment count: 3.

Open protein ↗
NUMBP49757With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P49757. Reported experiment count: 2.

Open protein ↗
NUMBLQ9Y6R0With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9Y6R0. Reported experiment count: 2.

Open protein ↗
OS9Q13438With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13438. Reported experiment count: 3.

Open protein ↗
PDGFRAP16234With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P16234. Reported experiment count: 4.

Open protein ↗
PIK3C2BO00750With P00533Homo sapiens10
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O00750. Reported experiment count: 10.

Open protein ↗
PIK3R1P27986With P00533Homo sapiens6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P27986. Reported experiment count: 6.

Open protein ↗
PIK3R2O00459With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O00459. Reported experiment count: 5.

Open protein ↗
PIK3R3Q92569With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q92569. Reported experiment count: 7.

Open protein ↗
PLCG1P19174With P00533Homo sapiens6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P19174. Reported experiment count: 6.

Open protein ↗
PLCG2P16885With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P16885. Reported experiment count: 7.

Open protein ↗
PPM1AP35813With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P35813. Reported experiment count: 2.

Open protein ↗
PRKCAP17252With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P17252. Reported experiment count: 3.

Open protein ↗
PTK2Q05397With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q05397. Reported experiment count: 7.

Open protein ↗
PTK6Q13882With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13882. Reported experiment count: 2.

Open protein ↗
PTPN1P18031With P00533Homo sapiens9
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P18031. Reported experiment count: 9.

Open protein ↗
PTPN11Q06124With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q06124. Reported experiment count: 7.

Open protein ↗
PTPN12Q05209With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q05209. Reported experiment count: 5.

Open protein ↗
PTPN22Q9Y2R2With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9Y2R2. Reported experiment count: 3.

Open protein ↗
PTPRAP18433With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P18433. Reported experiment count: 3.

Open protein ↗
PTPRBP23467With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P23467. Reported experiment count: 3.

Open protein ↗
PTPRCP08575With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P08575. Reported experiment count: 2.

Open protein ↗
PTPRGP23470With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P23470. Reported experiment count: 3.

Open protein ↗
PTPRHQ9HD43With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9HD43. Reported experiment count: 3.

Open protein ↗
RABGEF1Q9UJ41With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UJ41. Reported experiment count: 4.

Open protein ↗
RAF1P04049With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P04049. Reported experiment count: 3.

Open protein ↗
RAPH1Q70E73With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q70E73. Reported experiment count: 2.

Open protein ↗
RASA1P20936With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P20936. Reported experiment count: 7.

Open protein ↗
RIN1Q13671With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13671. Reported experiment count: 3.

Open protein ↗
ROR1Q01973With P00533Homo sapiens8
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q01973. Reported experiment count: 8.

Open protein ↗
RUBCNQ92622With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q92622. Reported experiment count: 4.

Open protein ↗
S100A4P26447With P00533Homo sapiens6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P26447. Reported experiment count: 6.

Open protein ↗
SEC61A1P61619With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P61619. Reported experiment count: 2.

Open protein ↗
SEL1LQ9UBV2With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UBV2. Reported experiment count: 2.

Open protein ↗
SFNP31947With P00533Homo sapiens9
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P31947. Reported experiment count: 9.

Open protein ↗
SH2B1Q9NRF2With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9NRF2. Reported experiment count: 4.

Open protein ↗
SH2B3Q9UQQ2With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UQQ2. Reported experiment count: 2.

Open protein ↗
SH2D3AQ9BRG2With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9BRG2. Reported experiment count: 3.

Open protein ↗
SHC1P29353With P00533Homo sapiens37
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P29353. Reported experiment count: 37.

Open protein ↗
SHC1P29353-7With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P29353-7. Reported experiment count: 4.

Open protein ↗
SHC2P98077With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P98077. Reported experiment count: 3.

Open protein ↗
SHC4Q6S5L8With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q6S5L8. Reported experiment count: 3.

Open protein ↗
SKAP2O75563With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O75563. Reported experiment count: 2.

Open protein ↗
SLAQ13239With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13239. Reported experiment count: 3.

Open protein ↗
SLC5A1P13866With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P13866. Reported experiment count: 3.

Open protein ↗
SNX3O60493With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O60493. Reported experiment count: 4.

Open protein ↗
SOS1Q07889With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q07889. Reported experiment count: 3.

Open protein ↗
SRCP12931With P00533Homo sapiens10
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P12931. Reported experiment count: 10.

Open protein ↗
STAT1P42224With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P42224. Reported experiment count: 7.

Open protein ↗
STAT3P40763With P00533Homo sapiens16
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P40763. Reported experiment count: 16.

Open protein ↗
STAT5AP42229With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P42229. Reported experiment count: 4.

Open protein ↗
STIP1P31948With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P31948. Reported experiment count: 3.

Open protein ↗
STUB1Q9UNE7With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UNE7. Reported experiment count: 4.

Open protein ↗
STX6O43752With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O43752. Reported experiment count: 3.

Open protein ↗
SYKP43405With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P43405. Reported experiment count: 7.

Open protein ↗
TAB1Q15750With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q15750. Reported experiment count: 3.

Open protein ↗
TACC3Q9Y6A5With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9Y6A5. Reported experiment count: 3.

Open protein ↗
TGFAP01135With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P01135. Reported experiment count: 4.

Open protein ↗
TLN1Q9Y490With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9Y490. Reported experiment count: 2.

Open protein ↗
TLR2O60603With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O60603. Reported experiment count: 3.

Open protein ↗
TNFRSF11AQ9Y6Q6-2With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9Y6Q6-2. Reported experiment count: 3.

Open protein ↗
TNS3Q68CZ2With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q68CZ2. Reported experiment count: 5.

Open protein ↗
TNS4Q8IZW8With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q8IZW8. Reported experiment count: 2.

Open protein ↗
TOM1L1O75674With P00533Homo sapiens6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: O75674. Reported experiment count: 6.

Open protein ↗
TRAF2Q12933With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q12933. Reported experiment count: 4.

Open protein ↗
TUBA1AQ71U36With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q71U36. Reported experiment count: 4.

Open protein ↗
TUBB2AQ13885With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q13885. Reported experiment count: 2.

Open protein ↗
TXNP10599With P00533Homo sapiens5
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P10599. Reported experiment count: 5.

Open protein ↗
UCHL1P09936With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P09936. Reported experiment count: 3.

Open protein ↗
USP33Q8TEY7With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q8TEY7. Reported experiment count: 2.

Open protein ↗
VAPAQ9P0L0With P00533Homo sapiens4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9P0L0. Reported experiment count: 4.

Open protein ↗
WASF3Q9UPY6With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9UPY6. Reported experiment count: 3.

Open protein ↗
YES1P07947With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P07947. Reported experiment count: 3.

Open protein ↗
YWHAQP27348With P00533Homo sapiens7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P27348. Reported experiment count: 7.

Open protein ↗
YWHAZP63104With P00533Homo sapiens6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P63104. Reported experiment count: 6.

Open protein ↗
ZAP70P43403With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P43403. Reported experiment count: 3.

Open protein ↗
Heat shock 70 kDa protein 6Q53FC7With P00533Homo sapiens3
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q53FC7. Reported experiment count: 3.

Open protein ↗
Heat shock cognate 71 kDa proteinQ96BE0With P00533Homo sapiens2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q96BE0. Reported experiment count: 2.

Open protein ↗
Calm3P62161With P00533Species not verifiedCross-species6
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P62161. Reported experiment count: 6.

Open protein ↗
CblP22682With P00533Mus musculusCross-species2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P22682. Reported experiment count: 2.

Open protein ↗
Grb7Q9QZC5With P00533Rattus norvegicusCross-species7
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q9QZC5. Reported experiment count: 7.

Open protein ↗
PrkdcP97313With P00533Mus musculusCross-species4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P97313. Reported experiment count: 4.

Open protein ↗
Ptpn1P20417With P00533Rattus norvegicusCross-species11
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P20417. Reported experiment count: 11.

Open protein ↗
RubcnQ80U62With P00533Mus musculusCross-species2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q80U62. Reported experiment count: 2.

Open protein ↗
SP0DTC2With P00533Severe acute respiratory syndrome coronavirus 2Cross-species4
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: P0DTC2. Reported experiment count: 4.

Open protein ↗
Trpv3Q8K424With P00533Mus musculusCross-species2
IntAct evidence

Pair evidence in IntAct ↗

Source product: P00533. Partner: Q8K424. Reported experiment count: 2.

Open protein ↗

Complex membership & assembly descriptions

Co-membership does not by itself prove direct binding between every pair.

No Complex Portal cross-reference was recorded for this entry.

UniProt subunit description

Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2 [42]. Forms a complex with CCDC88A/GIV (via SH2-like regions) and GNAI3 which leads to enhanced EGFR signaling and triggering of cell migration; binding to CCDC88A requires autophosphorylation of the EGFR C-terminal region, and ligand stimulation is required for recruitment of GNAI3 to the complex [70, 83].

Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation [106]. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B [42]. Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways.

Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation.

Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation; interaction with CBL is reduced in the presence of tensin TNS4 [79]. Interacts with SOCS5; regulates EGFR degradation through ELOC- and ELOB-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6.

Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR.

Interacts with PCNA; positively regulates PCNA [50]. Interacts with PELP1. Interacts with MUC1.

Interacts with AP2M1. Interacts with FER. May interact with EPS8; mediates EPS8 phosphorylation.

Interacts (via SH2 domains) with GRB2, NCK1 and NCK2 [36]. Interacts with ATXN2. Interacts with GAREM1.

Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers).

Interacts with RNF115 and RNF126 [80]. Interacts with GPRC5A (via its transmembrane domain) [85]. Interacts with FAM83B; positively regulates EGFR inducing its autophosphorylation in absence of stimulation by EGF [86].

Interacts with LAPTM4B; positively correlates with EGFR activation [92]. Interacts with STX19 [51]. Interacts with CD44 [84].

Interacts with PGRMC1; the interaction requires PGRMC1 homodimerization [89]. Interacts with PIKFYVE [52]. Interacts with NEU3.

Interacts with TRAF4 [94]. Interacts with the ant venom OMEGA-myrmeciitoxin(02)-Mg1a (By similarity). Interacts with CD82; this interaction facilitates ligand-induced endocytosis of the receptor and its subsequent desensitization [97].

Interacts with SNX32; the interaction is required for endolysosomal EGFR trafficking [98]

By similarityExperimental evidence 48 publications
Evidence & references
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "Q01279"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10026169"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10228163"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10805725"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11116146"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "11483589"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12297050"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12620237"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12873986"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15282549"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15374980"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15590694"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15837620"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16140940"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16420529"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17115032"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17182860"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17334392"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17909029"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18046415"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18602463"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19172738"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19509291"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19560417"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19563760"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19749156"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "19836242"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20462955"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20471394"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20551055"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20674546"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20837704"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21258366"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21518868"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "22298428"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "22888118"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "23418353"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "23589287"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "23774213"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "23912460"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "25187647"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "25311788"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "26988023"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "28479384"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "35538033"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "39073202"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "7657591"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "8650580"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "9852145"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "Reference",
          "id": "Ref.112"
        }
      ],
      "value": "Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2 (PubMed:10805725). Forms a complex with CCDC88A/GIV (via SH2-like regions) and GNAI3 which leads to enhanced EGFR signaling and triggering of cell migration; binding to CCDC88A requires autophosphorylation of the EGFR C-terminal region, and ligand stimulation is required for recruitment of GNAI3 to the complex (PubMed:20462955, PubMed:25187647). Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation (PubMed:18046415). Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B (PubMed:10805725). Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation; interaction with CBL is reduced in the presence of tensin TNS4 (PubMed:23774213). Interacts with SOCS5; regulates EGFR degradation through ELOC- and ELOB-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA (PubMed:17115032). Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2 (PubMed:10026169). Interacts with ATXN2. Interacts with GAREM1. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126 (PubMed:23418353). Interacts with GPRC5A (via its transmembrane domain) (PubMed:25311788). Interacts with FAM83B; positively regulates EGFR inducing its autophosphorylation in absence of stimulation by EGF (PubMed:23912460). Interacts with LAPTM4B; positively correlates with EGFR activation (PubMed:28479384). Interacts with STX19 (PubMed:16420529). Interacts with CD44 (PubMed:23589287). Interacts with PGRMC1; the interaction requires PGRMC1 homodimerization (PubMed:26988023). Interacts with PIKFYVE (PubMed:17909029). Interacts with NEU3. Interacts with TRAF4 (PubMed:30352854). Interacts with the ant venom OMEGA-myrmeciitoxin(02)-Mg1a (By similarity). Interacts with CD82; this interaction facilitates ligand-induced endocytosis of the receptor and its subsequent desensitization (PubMed:35538033). Interacts with SNX32; the interaction is required for endolysosomal EGFR trafficking (PubMed:39073202)"
    }
  ],
  "commentType": "SUBUNIT"
}

Other association resources

Resource links only; their association networks and counts are not added to the partner table.

08

Structure

7SYD · Cryo-EM structure of the extracellular module of the full-length EGFR bound to EGF "tips-juxtaposed" conformation

ELECTRON MICROSCOPY · 3.1 Å

Recorded components

ComponentSpeciesChainsProtein identities
Epidermal growth factor receptorprotein · Entity 1Homo sapiensA, CP00533
Epidermal growth factorprotein · Entity 2Homo sapiensB, DP01133

Biological assemblies

Assembly 1 · author_defined_assembly
Recorded chains: A, B, C, D

Assembly membership does not establish direct binding. Observed residue coverage is checked against the loaded coordinates; it is not inferred from construct metadata.

Publication

A molecular mechanism for the generation of ligand-dependent differential outputs by the epidermal growth factor receptor.

30/11/2021 · Read publication ↗

Detailed validation, construct lengths and deposition dates are not included in this published record. See the source record for those details.

PDB source record ↗

Structure references are from the dated source record. Opening another structure follows your existing Atlas account permissions.

Available structures 389

Scroll across the table for evidence and actions.

389 recorded rows

RecordEvidence typeMethodResolutionOpen
7SYDexperimentalEM3.10 AOpen in Atlas ↗
7SYEexperimentalEM3.30 AOpen in Atlas ↗
7SZ0experimentalEM3.30 AOpen in Atlas ↗
7SZ1experimentalEM3.40 AOpen in Atlas ↗
7SZ7experimentalEM3.40 AOpen in Atlas ↗
7SZ5experimentalEM3.60 AOpen in Atlas ↗
4UV7experimentalX-ray2.10 AOpen in Atlas ↗
9Z9EexperimentalX-ray2.40 AOpen in Atlas ↗
3QWQexperimentalX-ray2.75 AOpen in Atlas ↗
8HGOexperimentalEM3.31 AOpen in Atlas ↗
5XWDexperimentalX-ray2.89 AOpen in Atlas ↗
1YY9experimentalX-ray2.60 AOpen in Atlas ↗
1NQLexperimentalX-ray2.80 AOpen in Atlas ↗
4KRPexperimentalX-ray2.82 AOpen in Atlas ↗
9IPBexperimentalEM2.93 AOpen in Atlas ↗
8HGSexperimentalEM3.81 AOpen in Atlas ↗
9Z9FexperimentalX-ray3.06 AOpen in Atlas ↗
4UIPexperimentalX-ray2.95 AOpen in Atlas ↗
4KROexperimentalX-ray3.05 AOpen in Atlas ↗
8HGPexperimentalEM4.53 AOpen in Atlas ↗
9IP7experimentalEM3.21 AOpen in Atlas ↗
6ARUexperimentalX-ray3.20 AOpen in Atlas ↗
1IVOexperimentalX-ray3.30 AOpen in Atlas ↗
9IPDexperimentalEM3.29 AOpen in Atlas ↗
9IPEexperimentalEM3.31 AOpen in Atlas ↗
3B2VexperimentalX-ray3.30 AOpen in Atlas ↗
3NJPexperimentalX-ray3.30 AOpen in Atlas ↗
9IPCexperimentalEM3.40 AOpen in Atlas ↗
9IP9experimentalEM3.64 AOpen in Atlas ↗
9IPAexperimentalEM3.85 AOpen in Atlas ↗
9IP8experimentalEM3.91 AOpen in Atlas ↗
7OM4experimentalX-ray6.05 AOpen in Atlas ↗
1MOXexperimentalX-ray2.50 AOpen in Atlas ↗
7LENexperimentalX-ray2.90 AOpen in Atlas ↗
5WB7experimentalX-ray2.94 AOpen in Atlas ↗
5WB8experimentalX-ray3.00 AOpen in Atlas ↗
7LFRexperimentalX-ray3.20 AOpen in Atlas ↗
8A27experimentalX-ray1.07 AOpen in Atlas ↗
8A2DexperimentalX-ray1.11 AOpen in Atlas ↗
7LFSexperimentalX-ray3.50 AOpen in Atlas ↗
5UG9experimentalX-ray1.33 AOpen in Atlas ↗
5HG8experimentalX-ray1.42 AOpen in Atlas ↗
5UG8experimentalX-ray1.46 AOpen in Atlas ↗
8A2AexperimentalX-ray1.43 AOpen in Atlas ↗
6TFVexperimentalX-ray1.50 AOpen in Atlas ↗
6TG0experimentalX-ray1.50 AOpen in Atlas ↗
3POZexperimentalX-ray1.50 AOpen in Atlas ↗
5HG5experimentalX-ray1.52 AOpen in Atlas ↗
5CNOexperimentalX-ray1.55 AOpen in Atlas ↗
5UGCexperimentalX-ray1.58 AOpen in Atlas ↗
5U8LexperimentalX-ray1.60 AOpen in Atlas ↗
6TG1experimentalX-ray1.60 AOpen in Atlas ↗
7SI1experimentalX-ray1.60 AOpen in Atlas ↗
8PO4experimentalX-ray1.62 AOpen in Atlas ↗
9GL8experimentalX-ray1.63 AOpen in Atlas ↗
5CNNexperimentalX-ray1.90 AOpen in Atlas ↗
9DF3experimentalX-ray1.68 AOpen in Atlas ↗
6TFYexperimentalX-ray1.70 AOpen in Atlas ↗
4I22experimentalX-ray1.71 AOpen in Atlas ↗
3W33experimentalX-ray1.70 AOpen in Atlas ↗
8A2BexperimentalX-ray1.69 AOpen in Atlas ↗
6WXNexperimentalX-ray1.76 AOpen in Atlas ↗
9FQSexperimentalX-ray1.78 AOpen in Atlas ↗
9DF4experimentalX-ray1.78 AOpen in Atlas ↗
4I24experimentalX-ray1.80 AOpen in Atlas ↗
6TFZexperimentalX-ray1.80 AOpen in Atlas ↗
6V66experimentalX-ray1.79 AOpen in Atlas ↗
3W32experimentalX-ray1.80 AOpen in Atlas ↗
5UGAexperimentalX-ray1.82 AOpen in Atlas ↗
7JXQexperimentalX-ray1.83 AOpen in Atlas ↗
5HG7experimentalX-ray1.85 AOpen in Atlas ↗
4WKQexperimentalX-ray1.85 AOpen in Atlas ↗
5X2AexperimentalX-ray1.85 AOpen in Atlas ↗
9GL7experimentalX-ray1.88 AOpen in Atlas ↗
7A2AexperimentalX-ray1.90 AOpen in Atlas ↗
9GC6experimentalX-ray1.90 AOpen in Atlas ↗
9GC5experimentalX-ray1.91 AOpen in Atlas ↗
3W2SexperimentalX-ray1.90 AOpen in Atlas ↗
4WRGexperimentalX-ray1.90 AOpen in Atlas ↗
6P8QexperimentalX-ray1.90 AOpen in Atlas ↗
9MSRexperimentalX-ray1.93 AOpen in Atlas ↗
5YU9experimentalX-ray1.95 AOpen in Atlas ↗
4ZSEexperimentalX-ray1.97 AOpen in Atlas ↗
8SC7experimentalX-ray1.98 AOpen in Atlas ↗
6TFUexperimentalX-ray2.00 AOpen in Atlas ↗
6TFWexperimentalX-ray2.00 AOpen in Atlas ↗
6Z4DexperimentalX-ray2.00 AOpen in Atlas ↗
7A6JexperimentalX-ray2.00 AOpen in Atlas ↗
7A6KexperimentalX-ray2.00 AOpen in Atlas ↗
9FZRexperimentalX-ray1.99 AOpen in Atlas ↗
6LUDexperimentalX-ray2.05 AOpen in Atlas ↗
6XL4experimentalX-ray2.06 AOpen in Atlas ↗
5X2CexperimentalX-ray2.05 AOpen in Atlas ↗
9FRDexperimentalX-ray2.06 AOpen in Atlas ↗
3W2PexperimentalX-ray2.05 AOpen in Atlas ↗
3W2RexperimentalX-ray2.05 AOpen in Atlas ↗
5CASexperimentalX-ray2.10 AOpen in Atlas ↗
7ZYQexperimentalX-ray2.10 AOpen in Atlas ↗
8FV3experimentalX-ray2.10 AOpen in Atlas ↗
9GHRexperimentalX-ray2.10 AOpen in Atlas ↗
9MSSexperimentalX-ray2.09 AOpen in Atlas ↗
8PO1experimentalX-ray2.11 AOpen in Atlas ↗
6V6OexperimentalX-ray2.10 AOpen in Atlas ↗
9OU9experimentalX-ray2.10 AOpen in Atlas ↗
8PO3experimentalX-ray2.13 AOpen in Atlas ↗
9FZSexperimentalX-ray2.12 AOpen in Atlas ↗
9DM8experimentalX-ray2.13 AOpen in Atlas ↗
5HG9experimentalX-ray2.15 AOpen in Atlas ↗
9QXNexperimentalX-ray2.14 AOpen in Atlas ↗
7JXPexperimentalX-ray2.16 AOpen in Atlas ↗
9GL9experimentalX-ray2.15 AOpen in Atlas ↗
8UKWexperimentalX-ray2.39 AOpen in Atlas ↗
8D73experimentalX-ray2.17 AOpen in Atlas ↗
2RGPexperimentalX-ray2.00 AOpen in Atlas ↗
7JXMexperimentalX-ray2.19 AOpen in Atlas ↗
6DUKexperimentalX-ray2.20 AOpen in Atlas ↗
8FV4experimentalX-ray2.20 AOpen in Atlas ↗
8HV4experimentalX-ray2.20 AOpen in Atlas ↗
8HV5experimentalX-ray2.20 AOpen in Atlas ↗
8HV6experimentalX-ray2.20 AOpen in Atlas ↗
5X2FexperimentalX-ray2.20 AOpen in Atlas ↗
6JRXexperimentalX-ray2.20 AOpen in Atlas ↗
6V6KexperimentalX-ray2.20 AOpen in Atlas ↗
7T4JexperimentalX-ray2.20 AOpen in Atlas ↗
9GDVexperimentalX-ray2.22 AOpen in Atlas ↗
3W2QexperimentalX-ray2.20 AOpen in Atlas ↗
9NISexperimentalX-ray2.23 AOpen in Atlas ↗
5CAUexperimentalX-ray2.25 AOpen in Atlas ↗
9GHUexperimentalX-ray2.25 AOpen in Atlas ↗
9NJNexperimentalX-ray2.24 AOpen in Atlas ↗
5GNKexperimentalX-ray1.80 AOpen in Atlas ↗
8PO2experimentalX-ray2.28 AOpen in Atlas ↗
6V5PexperimentalX-ray2.30 AOpen in Atlas ↗
7LTXexperimentalX-ray2.30 AOpen in Atlas ↗
7ZYNexperimentalX-ray2.30 AOpen in Atlas ↗
8F1XexperimentalX-ray2.30 AOpen in Atlas ↗
8GK5experimentalX-ray2.30 AOpen in Atlas ↗
5D41experimentalX-ray2.31 AOpen in Atlas ↗
6LUBexperimentalX-ray2.31 AOpen in Atlas ↗
6JXTexperimentalX-ray2.31 AOpen in Atlas ↗
9BY4experimentalX-ray2.31 AOpen in Atlas ↗
9D3VexperimentalX-ray2.32 AOpen in Atlas ↗
9KL4experimentalX-ray2.32 AOpen in Atlas ↗
3VJNexperimentalX-ray2.34 AOpen in Atlas ↗
9PMZexperimentalX-ray2.33 AOpen in Atlas ↗
5XDKexperimentalX-ray2.35 AOpen in Atlas ↗
3W2OexperimentalX-ray2.35 AOpen in Atlas ↗
1XKKexperimentalX-ray2.40 AOpen in Atlas ↗
5C8NexperimentalX-ray2.40 AOpen in Atlas ↗
5CAPexperimentalX-ray2.40 AOpen in Atlas ↗
6V5NexperimentalX-ray2.40 AOpen in Atlas ↗
6WA2experimentalX-ray2.40 AOpen in Atlas ↗
6WAKexperimentalX-ray2.40 AOpen in Atlas ↗
7A6IexperimentalX-ray2.40 AOpen in Atlas ↗
7JXLexperimentalX-ray2.40 AOpen in Atlas ↗
7KXZexperimentalX-ray2.40 AOpen in Atlas ↗
7UKVexperimentalX-ray2.40 AOpen in Atlas ↗
8D76experimentalX-ray2.40 AOpen in Atlas ↗
8F1ZexperimentalX-ray2.40 AOpen in Atlas ↗
8HV1experimentalX-ray2.40 AOpen in Atlas ↗
8HV3experimentalX-ray2.40 AOpen in Atlas ↗
8HV8experimentalX-ray2.40 AOpen in Atlas ↗
8DSWexperimentalX-ray2.39 AOpen in Atlas ↗
6P1DexperimentalX-ray2.40 AOpen in Atlas ↗
6VHNexperimentalX-ray2.40 AOpen in Atlas ↗
9NGPexperimentalX-ray2.40 AOpen in Atlas ↗
9GC4experimentalX-ray2.42 AOpen in Atlas ↗
7VRAexperimentalX-ray2.41 AOpen in Atlas ↗
9EWSexperimentalX-ray2.44 AOpen in Atlas ↗
9HBOexperimentalX-ray2.45 AOpen in Atlas ↗
3GOPexperimentalX-ray2.80 AOpen in Atlas ↗
3BELexperimentalX-ray2.30 AOpen in Atlas ↗
9S3XexperimentalX-ray2.42 AOpen in Atlas ↗
5HCYexperimentalX-ray2.46 AOpen in Atlas ↗
9Q0SexperimentalX-ray2.46 AOpen in Atlas ↗
2ITNexperimentalX-ray2.47 AOpen in Atlas ↗
2ITVexperimentalX-ray2.47 AOpen in Atlas ↗
4LQMexperimentalX-ray2.50 AOpen in Atlas ↗
8TO3experimentalX-ray2.49 AOpen in Atlas ↗
2EB2experimentalX-ray2.50 AOpen in Atlas ↗
3UG2experimentalX-ray2.50 AOpen in Atlas ↗
4RJ8experimentalX-ray2.50 AOpen in Atlas ↗
5CAQexperimentalX-ray2.50 AOpen in Atlas ↗
6Z4BexperimentalX-ray2.50 AOpen in Atlas ↗
7B85experimentalX-ray2.50 AOpen in Atlas ↗
7JXWexperimentalX-ray2.50 AOpen in Atlas ↗
7U99experimentalX-ray2.50 AOpen in Atlas ↗
7ZYMexperimentalX-ray2.50 AOpen in Atlas ↗
8HV9experimentalX-ray2.50 AOpen in Atlas ↗
9FQPexperimentalX-ray2.50 AOpen in Atlas ↗
9GHVexperimentalX-ray2.50 AOpen in Atlas ↗
8PNZexperimentalX-ray2.51 AOpen in Atlas ↗
8G63experimentalX-ray2.50 AOpen in Atlas ↗
9DF2experimentalX-ray2.50 AOpen in Atlas ↗
8PO0experimentalX-ray2.52 AOpen in Atlas ↗
7VREexperimentalX-ray2.51 AOpen in Atlas ↗
5UGBexperimentalX-ray2.53 AOpen in Atlas ↗
5J9ZexperimentalX-ray2.50 AOpen in Atlas ↗
6JX0experimentalX-ray2.53 AOpen in Atlas ↗
6JX4experimentalX-ray2.53 AOpen in Atlas ↗
9D3WexperimentalX-ray2.53 AOpen in Atlas ↗
9NJ7experimentalX-ray2.53 AOpen in Atlas ↗
4RJ7experimentalX-ray2.55 AOpen in Atlas ↗
6D8EexperimentalX-ray2.54 AOpen in Atlas ↗
6JWLexperimentalX-ray2.55 AOpen in Atlas ↗
8WD4experimentalX-ray2.55 AOpen in Atlas ↗
9BY6experimentalX-ray2.55 AOpen in Atlas ↗
9MSTexperimentalX-ray2.57 AOpen in Atlas ↗
5CZIexperimentalX-ray2.60 AOpen in Atlas ↗
8GB4experimentalX-ray2.59 AOpen in Atlas ↗
7OXBexperimentalX-ray2.56 AOpen in Atlas ↗
1M14experimentalX-ray2.60 AOpen in Atlas ↗
1M17experimentalX-ray2.60 AOpen in Atlas ↗
5CAOexperimentalX-ray2.60 AOpen in Atlas ↗
5EDRexperimentalX-ray2.60 AOpen in Atlas ↗
5HICexperimentalX-ray2.60 AOpen in Atlas ↗
6S8AexperimentalX-ray2.60 AOpen in Atlas ↗
7K1HexperimentalX-ray2.60 AOpen in Atlas ↗
7U9AexperimentalX-ray2.60 AOpen in Atlas ↗
7UKWexperimentalX-ray2.60 AOpen in Atlas ↗
9GHSexperimentalX-ray2.60 AOpen in Atlas ↗
9GHTexperimentalX-ray2.60 AOpen in Atlas ↗
9NM0experimentalX-ray2.59 AOpen in Atlas ↗
2GS6experimentalX-ray2.60 AOpen in Atlas ↗
2GS7experimentalX-ray2.60 AOpen in Atlas ↗
5HCXexperimentalX-ray2.60 AOpen in Atlas ↗
9H42experimentalX-ray2.60 AOpen in Atlas ↗
7T4IexperimentalX-ray2.61 AOpen in Atlas ↗
5HCZexperimentalX-ray2.62 AOpen in Atlas ↗
5ZWJexperimentalX-ray2.90 AOpen in Atlas ↗
3VJOexperimentalX-ray2.64 AOpen in Atlas ↗
5EM5experimentalX-ray2.65 AOpen in Atlas ↗
7AEIexperimentalX-ray2.65 AOpen in Atlas ↗
7AEMexperimentalX-ray2.65 AOpen in Atlas ↗
5FEDexperimentalX-ray2.65 AOpen in Atlas ↗
5ZTOexperimentalX-ray2.65 AOpen in Atlas ↗
7ER2experimentalX-ray2.66 AOpen in Atlas ↗
4LI5experimentalX-ray2.64 AOpen in Atlas ↗
6S9DexperimentalX-ray2.67 AOpen in Atlas ↗
9KLWexperimentalX-ray2.67 AOpen in Atlas ↗
8HV7experimentalX-ray2.69 AOpen in Atlas ↗
2ITQexperimentalX-ray2.68 AOpen in Atlas ↗
4RJ6experimentalX-ray2.70 AOpen in Atlas ↗
4ZJVexperimentalX-ray2.70 AOpen in Atlas ↗
5CALexperimentalX-ray2.70 AOpen in Atlas ↗
6S89experimentalX-ray2.70 AOpen in Atlas ↗
8TJLexperimentalX-ray2.70 AOpen in Atlas ↗
5FEEexperimentalX-ray2.70 AOpen in Atlas ↗
5XDLexperimentalX-ray2.70 AOpen in Atlas ↗
8UKVexperimentalX-ray2.94 AOpen in Atlas ↗
4JR3experimentalX-ray2.70 AOpen in Atlas ↗
5CAVexperimentalX-ray2.73 AOpen in Atlas ↗
2ITZexperimentalX-ray2.72 AOpen in Atlas ↗
2ITTexperimentalX-ray2.73 AOpen in Atlas ↗
6S9CexperimentalX-ray2.73 AOpen in Atlas ↗
9NHWexperimentalX-ray2.73 AOpen in Atlas ↗
3UG1experimentalX-ray2.75 AOpen in Atlas ↗
8F1YexperimentalX-ray2.75 AOpen in Atlas ↗
2ITPexperimentalX-ray2.74 AOpen in Atlas ↗
4JQ7experimentalX-ray2.73 AOpen in Atlas ↗
4HJOexperimentalX-ray2.75 AOpen in Atlas ↗
9OS6experimentalX-ray2.75 AOpen in Atlas ↗
8HVAexperimentalX-ray2.77 AOpen in Atlas ↗
4RJ4experimentalX-ray2.78 AOpen in Atlas ↗
5EM6experimentalX-ray2.78 AOpen in Atlas ↗
5CZHexperimentalX-ray2.80 AOpen in Atlas ↗
8HV2experimentalX-ray2.80 AOpen in Atlas ↗
4I23experimentalX-ray2.80 AOpen in Atlas ↗
5CANexperimentalX-ray2.80 AOpen in Atlas ↗
5EDQexperimentalX-ray2.80 AOpen in Atlas ↗
5EM8experimentalX-ray2.80 AOpen in Atlas ↗
7ZYPexperimentalX-ray2.80 AOpen in Atlas ↗
8F1HexperimentalX-ray2.80 AOpen in Atlas ↗
4RIYexperimentalX-ray2.98 AOpen in Atlas ↗
5EM7experimentalX-ray2.81 AOpen in Atlas ↗
2GS2experimentalX-ray2.80 AOpen in Atlas ↗
2ITUexperimentalX-ray2.80 AOpen in Atlas ↗
4G5JexperimentalX-ray2.80 AOpen in Atlas ↗
4ZAUexperimentalX-ray2.80 AOpen in Atlas ↗
5GMPexperimentalX-ray2.80 AOpen in Atlas ↗
6JRKexperimentalX-ray2.80 AOpen in Atlas ↗
6P1LexperimentalX-ray2.80 AOpen in Atlas ↗
6VH4experimentalX-ray2.80 AOpen in Atlas ↗
4JRVexperimentalX-ray2.80 AOpen in Atlas ↗
9XU9experimentalX-ray2.84 AOpen in Atlas ↗
2EB3experimentalX-ray2.84 AOpen in Atlas ↗
5HIBexperimentalX-ray2.85 AOpen in Atlas ↗
4JQ8experimentalX-ray2.83 AOpen in Atlas ↗
5J9YexperimentalX-ray2.80 AOpen in Atlas ↗
6JZ0experimentalX-ray2.86 AOpen in Atlas ↗
3IKAexperimentalX-ray2.90 AOpen in Atlas ↗
2ITWexperimentalX-ray2.88 AOpen in Atlas ↗
5C8MexperimentalX-ray2.90 AOpen in Atlas ↗
5EDPexperimentalX-ray2.90 AOpen in Atlas ↗
8HY7experimentalX-ray2.91 AOpen in Atlas ↗
4RIWexperimentalX-ray3.10 AOpen in Atlas ↗
4RIXexperimentalX-ray3.10 AOpen in Atlas ↗
7LG8experimentalX-ray2.93 AOpen in Atlas ↗
9U91experimentalX-ray3.20 AOpen in Atlas ↗
9VV1experimentalX-ray2.95 AOpen in Atlas ↗
6JRJexperimentalX-ray2.94 AOpen in Atlas ↗
5X26experimentalX-ray2.95 AOpen in Atlas ↗
5X27experimentalX-ray2.95 AOpen in Atlas ↗
5X28experimentalX-ray2.95 AOpen in Atlas ↗
5XGMexperimentalX-ray2.95 AOpen in Atlas ↗
4R3PexperimentalX-ray2.90 AOpen in Atlas ↗
3GT8experimentalX-ray2.96 AOpen in Atlas ↗
7TVDexperimentalX-ray2.96 AOpen in Atlas ↗
8TO4experimentalX-ray2.99 AOpen in Atlas ↗
2RFEexperimentalX-ray2.90 AOpen in Atlas ↗
2ITXexperimentalX-ray2.98 AOpen in Atlas ↗
4I1ZexperimentalX-ray3.00 AOpen in Atlas ↗
5C8KexperimentalX-ray3.00 AOpen in Atlas ↗
7JXIexperimentalX-ray3.00 AOpen in Atlas ↗
9H47experimentalX-ray2.99 AOpen in Atlas ↗
2J5FexperimentalX-ray3.00 AOpen in Atlas ↗
4R5SexperimentalX-ray3.00 AOpen in Atlas ↗
5GTZexperimentalX-ray3.00 AOpen in Atlas ↗
5XGNexperimentalX-ray3.00 AOpen in Atlas ↗
9EWTexperimentalX-ray3.02 AOpen in Atlas ↗
9JQ1experimentalX-ray3.02 AOpen in Atlas ↗
2JIUexperimentalX-ray3.05 AOpen in Atlas ↗
5UWDexperimentalX-ray3.06 AOpen in Atlas ↗
8UKXexperimentalX-ray3.30 AOpen in Atlas ↗
4RJ5experimentalX-ray3.10 AOpen in Atlas ↗
7JXKexperimentalX-ray3.10 AOpen in Atlas ↗
7KY0experimentalX-ray3.10 AOpen in Atlas ↗
2J5EexperimentalX-ray3.10 AOpen in Atlas ↗
2J6MexperimentalX-ray3.10 AOpen in Atlas ↗
2JITexperimentalX-ray3.10 AOpen in Atlas ↗
7LGSexperimentalX-ray3.10 AOpen in Atlas ↗
9GI9experimentalX-ray3.12 AOpen in Atlas ↗
5Y25experimentalX-ray3.10 AOpen in Atlas ↗
5GTYexperimentalX-ray3.14 AOpen in Atlas ↗
9H46experimentalX-ray3.16 AOpen in Atlas ↗
4G5PexperimentalX-ray3.17 AOpen in Atlas ↗
4TKSexperimentalX-ray3.20 AOpen in Atlas ↗
7K1IexperimentalX-ray3.20 AOpen in Atlas ↗
8F1WexperimentalX-ray3.20 AOpen in Atlas ↗
5X2KexperimentalX-ray3.20 AOpen in Atlas ↗
3LZBexperimentalX-ray2.70 AOpen in Atlas ↗
5Y9TexperimentalX-ray3.25 AOpen in Atlas ↗
2ITOexperimentalX-ray3.25 AOpen in Atlas ↗
6S9BexperimentalX-ray3.25 AOpen in Atlas ↗
9P9UexperimentalEM3.27 AOpen in Atlas ↗
4WD5experimentalX-ray3.30 AOpen in Atlas ↗
8KFQexperimentalX-ray3.22 AOpen in Atlas ↗
5JEBexperimentalX-ray3.30 AOpen in Atlas ↗
4R3RexperimentalX-ray3.25 AOpen in Atlas ↗
8EMEexperimentalX-ray3.32 AOpen in Atlas ↗
4I20experimentalX-ray3.34 AOpen in Atlas ↗
4I21experimentalX-ray3.37 AOpen in Atlas ↗
5FEQexperimentalX-ray3.40 AOpen in Atlas ↗
8H7XexperimentalX-ray3.40 AOpen in Atlas ↗
7U98experimentalX-ray3.42 AOpen in Atlas ↗
3P0YexperimentalX-ray1.80 AOpen in Atlas ↗
2ITYexperimentalX-ray3.42 AOpen in Atlas ↗
2JIVexperimentalX-ray3.50 AOpen in Atlas ↗
2RF9experimentalX-ray3.50 AOpen in Atlas ↗
9U8CexperimentalX-ray3.50 AOpen in Atlas ↗
4LRMexperimentalX-ray3.53 AOpen in Atlas ↗
6VHPexperimentalX-ray3.60 AOpen in Atlas ↗
2RFDexperimentalX-ray3.60 AOpen in Atlas ↗
4LL0experimentalX-ray4.00 AOpen in Atlas ↗
3B2UexperimentalX-ray2.58 AOpen in Atlas ↗
4KRMexperimentalX-ray2.66 AOpen in Atlas ↗
5SX5experimentalX-ray2.50 AOpen in Atlas ↗
6B3SexperimentalX-ray2.80 AOpen in Atlas ↗
4KRLexperimentalX-ray2.85 AOpen in Atlas ↗
5SX4experimentalX-ray2.80 AOpen in Atlas ↗
3C09experimentalX-ray3.20 AOpen in Atlas ↗
3VRPexperimentalX-ray1.52 AOpen in Atlas ↗
3G5YexperimentalX-ray1.59 AOpen in Atlas ↗
8S1MexperimentalX-ray2.05 AOpen in Atlas ↗
3G5VexperimentalX-ray2.00 AOpen in Atlas ↗
3VRRexperimentalX-ray2.00 AOpen in Atlas ↗
3OB2experimentalX-ray2.10 AOpen in Atlas ↗
3PFVexperimentalX-ray2.27 AOpen in Atlas ↗
9Z2HexperimentalX-ray2.45 AOpen in Atlas ↗
3OP0experimentalX-ray2.52 AOpen in Atlas ↗
3BUOexperimentalX-ray2.60 AOpen in Atlas ↗
9OLBexperimentalX-ray2.62 AOpen in Atlas ↗
2M20experimentalNMR-Open in Atlas ↗
1Z9IexperimentalNMR-Open in Atlas ↗
2N5SexperimentalNMR-Open in Atlas ↗
2KS1experimentalNMR-Open in Atlas ↗
2M0BexperimentalNMR-Open in Atlas ↗
5LV6experimentalNMR-Open in Atlas ↗
AF-P00533-F1predictedAlphaFoldNot applicableOpen in Atlas ↗
09

Family & Domains

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily

Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU00159
Complete source annotation
{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000255",
          "source": "PROSITE-ProRule",
          "id": "PRU00159"
        }
      ],
      "value": "Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily"
    }
  ],
  "commentType": "SIMILARITY"
}

Domain architecture

Canonical sequence11210 aa

Canonical coordinates. Overlapping marks share a lane; individual records and evidence are in the tables below. Gaps in coverage are not selectable in 3D. Use the track links and tables for keyboard inspection.

Atlas domains, motifs & repeats 10

Scroll across the table for evidence and actions.

10 recorded rows

AnnotationPositionSource & interpretationInspect
Receptor L-domainIPR00049457–167INTERPROdomain

The structure for the first three domains of the extracellular portion of IGF-1R (type-1 insulin-like growth-factor receptor) has been solved and consists of two L-domains and a cysteine rich region (L1-Cys-rich-L2). The L-domains each consist of a single-stranded right-handed β-helix.

Full source description

The structure for the first three domains of the extracellular portion of IGF-1R (type-1 insulin-like growth-factor receptor) has been solved and consists of two L-domains and a cysteine rich region (L1-Cys-rich-L2). The L-domains each consist of a single-stranded right-handed β-helix. The Cys-rich region is composed of eight disulphide-bonded modules, seven of which form a rod-shaped domain with modules associated in an unusual manner. The three domains surround a central space of sufficient size to accommodate a ligand molecule. This entry represents the L-domain. This domain can also be found in insulin receptor(IR) and epidermal growth-factor receptor (EGFR) family members, and in yeast cell surface GPI proteins PST1 and ECM33.

Source entry ↗
No verified residues in this structure
ApproximateUNI_REPEAT_75_30075–300UNIPROTrepeat

Approximate

Source entry ↗
No verified residues in this structure
Furin-like cysteine-rich domainIPR006211185–338INTERPROdomain

The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation. This entry includes Epidermal growth factor receptor, Receptor tyrosine-protein kinase erbB-2 and related proteins.

Source entry ↗
No verified residues in this structure
Furin-like repeatIPR006212228–274INTERPROrepeat

The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation. This entry includes Epidermal growth factor receptor, Receptor tyrosine-protein kinase erbB-2 and related proteins.

Source entry ↗
No verified residues in this structure
Receptor L-domainIPR000494361–480INTERPROdomain

The structure for the first three domains of the extracellular portion of IGF-1R (type-1 insulin-like growth-factor receptor) has been solved and consists of two L-domains and a cysteine rich region (L1-Cys-rich-L2). The L-domains each consist of a single-stranded right-handed β-helix.

Full source description

The structure for the first three domains of the extracellular portion of IGF-1R (type-1 insulin-like growth-factor receptor) has been solved and consists of two L-domains and a cysteine rich region (L1-Cys-rich-L2). The L-domains each consist of a single-stranded right-handed β-helix. The Cys-rich region is composed of eight disulphide-bonded modules, seven of which form a rod-shaped domain with modules associated in an unusual manner. The three domains surround a central space of sufficient size to accommodate a ligand molecule. This entry represents the L-domain. This domain can also be found in insulin receptor(IR) and epidermal growth-factor receptor (EGFR) family members, and in yeast cell surface GPI proteins PST1 and ECM33.

Source entry ↗
No verified residues in this structure
ApproximateUNI_REPEAT_390_600390–600UNIPROTrepeat

Approximate

Source entry ↗
No verified residues in this structure
Furin-like repeatIPR006212496–601INTERPROrepeat

The furin-like cysteine rich region has been found in a variety of proteins from eukaryotes that are involved in the mechanism of signal transduction by receptor tyrosine kinases, which involves receptor aggregation. This entry includes Epidermal growth factor receptor, Receptor tyrosine-protein kinase erbB-2 and related proteins.

Source entry ↗
No verified residues in this structure
Growth factor receptor domain 4IPR032778505–636INTERPROdomain

This is the fourth extracellular domain of receptor tyrosine protein kinases. Interaction between this domain and the furin-like domain ([interpro:IPR006211]) regulates the binding of ligands to the receptor L domains ([interpro:IPR000494]).

Source entry ↗
No verified residues in this structure
Epidermal growth factor receptor-like, transmembrane-juxtamembrane segmentIPR049328646–681INTERPROdomain

Epidermal growth factor receptor (ErbB) family is a class of receptor tyrosine kinases (RTKs) that have a pivotal role in the processes of cell growth, proliferation, and differentiation. They exist on the cell surface as dimers in both active and inactive states, which switch between them through conformational changes upon ligand binding.

Full source description

Epidermal growth factor receptor (ErbB) family is a class of receptor tyrosine kinases (RTKs) that have a pivotal role in the processes of cell growth, proliferation, and differentiation. They exist on the cell surface as dimers in both active and inactive states, which switch between them through conformational changes upon ligand binding. They suffer a strong lateral dimerization that leads to proper assembly of their extracellular ligand-binding, single-span transmembrane, and cytoplasmic kinase domains which is key for ErbB activation. The transmembrane (TM) and juxtamembrane region of these receptors are essential for dimerization and activation. This entry represents the TM and juxtamembrane segment of EGFR, ErbB2 and ErbB4 and similar sequences.

Source entry ↗
No verified residues in this structure
Protein kinase domainIPR000719712–979INTERPROdomain

This entry represents the protein kinase domain containing the catalytic function of protein kinases. This domain is found in serine/threonine-protein kinases, tyrosine-protein kinases and dual specificity protein kinases.

Full source description

This entry represents the protein kinase domain containing the catalytic function of protein kinases. This domain is found in serine/threonine-protein kinases, tyrosine-protein kinases and dual specificity protein kinases. Eukaryotic protein kinases are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue which is important for the catalytic activity of the enzyme. Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity: Serine/threonine-protein kinases Tyrosine-protein kinases Dual specificity protein kinases (e.g. MEK -phosphorylates both Thr and Tyr on target proteins) Protein kinase function is evolutionarily conserved from Escherichia coli to human. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved, leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases.

Source entry ↗
No verified residues in this structure

UniProt domains, repeats & motifs 3

Scroll across the table for evidence and actions.

3 recorded rows

FeaturePositionDescriptionEvidenceInspect
Repeat75–300Approximate
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure
Repeat390–600Approximate
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure
Domain712–979Protein kinase
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU00159
No verified residues in this structure

Functional sites 6

Scroll across the table for evidence and actions.

6 recorded rows

FeaturePositionDescriptionEvidenceInspect
Active site837Proton acceptor
Sequence analysis
Evidence & references
  • ECO:0000255 PROSITE-ProRule:PRU00159
  • ECO:0000255 PROSITE-ProRule:PRU10028
No verified residues in this structure
Binding site718–726Binding site
Experimental evidence 1 publication
Evidence & references
  • ECO:0000269 PubMed:19563760 ↗
  • ECO:0007744 PDB:2GS7
  • ECO:0007744 PDB:3GT8
  • ECO:0007744 PDB:4ZSE
  • ECO:0007744 PDB:5CNN
  • ECO:0007744 PDB:5CNO
  • ECO:0007744 PDB:5D41
No verified residues in this structure
Binding site745Binding site
Experimental evidence 2 publications
Evidence & references
  • ECO:0000269 PubMed:17349580 ↗
  • ECO:0000269 PubMed:19563760 ↗
  • ECO:0007744 PDB:2EB3
  • ECO:0007744 PDB:2GS7
  • ECO:0007744 PDB:2ITN
  • ECO:0007744 PDB:3GT8
  • ECO:0007744 PDB:3VJN
  • ECO:0007744 PDB:3VJO
  • ECO:0007744 PDB:4RIW
  • ECO:0007744 PDB:4RIY
  • ECO:0007744 PDB:4ZSE
  • ECO:0007744 PDB:5CNN
  • ECO:0007744 PDB:5CNO
  • ECO:0007744 PDB:5D41
No verified residues in this structure
Binding site790–791Binding site
Experimental evidence 2 publications
Evidence & references
  • ECO:0000269 PubMed:17349580 ↗
  • ECO:0000269 PubMed:19563760 ↗
  • ECO:0007744 PDB:2EB3
  • ECO:0007744 PDB:2GS7
  • ECO:0007744 PDB:2ITN
  • ECO:0007744 PDB:2ITV
  • ECO:0007744 PDB:2ITX
  • ECO:0007744 PDB:3GT8
  • ECO:0007744 PDB:3VJN
  • ECO:0007744 PDB:3VJO
  • ECO:0007744 PDB:4RIW
  • ECO:0007744 PDB:4RIX
  • ECO:0007744 PDB:4RIY
  • ECO:0007744 PDB:4ZSE
  • ECO:0007744 PDB:5CNN
  • ECO:0007744 PDB:5CNO
  • ECO:0007744 PDB:5D41
No verified residues in this structure
Binding site855Binding site
Experimental evidence 2 publications
Evidence & references
  • ECO:0000269 PubMed:17349580 ↗
  • ECO:0000269 PubMed:19563760 ↗
  • ECO:0007744 PDB:2EB3
  • ECO:0007744 PDB:2GS7
  • ECO:0007744 PDB:2ITN
  • ECO:0007744 PDB:2ITV
  • ECO:0007744 PDB:2ITX
  • ECO:0007744 PDB:3GT8
  • ECO:0007744 PDB:3VJN
  • ECO:0007744 PDB:4RIW
  • ECO:0007744 PDB:4RIX
  • ECO:0007744 PDB:4RIY
  • ECO:0007744 PDB:4ZSE
  • ECO:0007744 PDB:5CNN
  • ECO:0007744 PDB:5CNO
  • ECO:0007744 PDB:5D41
No verified residues in this structure
Site1016Important for interaction with PIK3C2B
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure

Sequence regions 4

Scroll across the table for evidence and actions.

4 recorded rows

FeaturePositionDescriptionEvidenceInspect
Region688–704Important for dimerization, phosphorylation and activation
Evidence & references

No separate evidence record is supplied for this statement.

No verified residues in this structure
Region1097–1137Disordered
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias1104–1115Polar residues
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
Compositional bias1128–1137Polar residues
Evidence & references
  • ECO:0000256 SAM:MobiDB-lite
No verified residues in this structure
10

Sequence & Isoforms

Sequence & isoforms

UniProt’s canonical sequence is its selected representative. It is not necessarily the dominant isoform in every tissue.

UniProt’s canonical sequence · P00533-11210 aa134,277 Da · source sequence mass

Full precursor sequence, including processing regions. The mass describes this unmodified source sequence, not every mature or modified product.

MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGA

Source isoform notes & selection

Alternative splicing

Complete source annotation
{
  "commentType": "ALTERNATIVE PRODUCTS",
  "events": [
    "Alternative splicing"
  ],
  "isoforms": [
    {
      "name": {
        "value": "1"
      },
      "synonyms": [
        {
          "value": "p170"
        }
      ],
      "isoformIds": [
        "P00533-1"
      ],
      "isoformSequenceStatus": "Displayed"
    },
    {
      "name": {
        "value": "2"
      },
      "synonyms": [
        {
          "value": "p60"
        },
        {
          "value": "Truncated"
        },
        {
          "value": "TEGFR"
        }
      ],
      "isoformIds": [
        "P00533-2"
      ],
      "sequenceIds": [
        "VSP_002887",
        "VSP_002888"
      ],
      "isoformSequenceStatus": "Described"
    },
    {
      "name": {
        "value": "3"
      },
      "synonyms": [
        {
          "value": "p110"
        }
      ],
      "isoformIds": [
        "P00533-3"
      ],
      "sequenceIds": [
        "VSP_002889",
        "VSP_002890"
      ],
      "isoformSequenceStatus": "Described"
    },
    {
      "name": {
        "value": "4"
      },
      "isoformIds": [
        "P00533-4"
      ],
      "sequenceIds": [
        "VSP_002891",
        "VSP_002892"
      ],
      "isoformSequenceStatus": "Described"
    }
  ]
}
  • P00533-1 · 1 · Displayed · p170
    Complete source annotation
    {
      "name": {
        "value": "1"
      },
      "synonyms": [
        {
          "value": "p170"
        }
      ],
      "isoformIds": [
        "P00533-1"
      ],
      "isoformSequenceStatus": "Displayed"
    }
  • P00533-2 · 2 · Described · p60, Truncated, TEGFR · VSP_002887, VSP_002888
    Complete source annotation
    {
      "name": {
        "value": "2"
      },
      "synonyms": [
        {
          "value": "p60"
        },
        {
          "value": "Truncated"
        },
        {
          "value": "TEGFR"
        }
      ],
      "isoformIds": [
        "P00533-2"
      ],
      "sequenceIds": [
        "VSP_002887",
        "VSP_002888"
      ],
      "isoformSequenceStatus": "Described"
    }
  • P00533-3 · 3 · Described · p110 · VSP_002889, VSP_002890
    Complete source annotation
    {
      "name": {
        "value": "3"
      },
      "synonyms": [
        {
          "value": "p110"
        }
      ],
      "isoformIds": [
        "P00533-3"
      ],
      "sequenceIds": [
        "VSP_002889",
        "VSP_002890"
      ],
      "isoformSequenceStatus": "Described"
    }
  • P00533-4 · 4 · Described · VSP_002891, VSP_002892
    Complete source annotation
    {
      "name": {
        "value": "4"
      },
      "isoformIds": [
        "P00533-4"
      ],
      "sequenceIds": [
        "VSP_002891",
        "VSP_002892"
      ],
      "isoformSequenceStatus": "Described"
    }

Isoform sequence differences 6

Scroll across the table for evidence and actions.

6 recorded rows

FeaturePositionDescriptionEvidenceInspect
Alternative sequenceVSP_002887404–405in isoform 2
FL → LS
Published statement 3 publications
Evidence & references
No verified residues in this structure
Alternative sequenceVSP_002888406–1210in isoform 2
Published statement 3 publications
Evidence & references
No verified residues in this structure
Alternative sequenceVSP_002889628–705in isoform 3
CTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR → PGNESLKAMLFCLFKLSSCNQSNDGSVSHQSGSPAAQESCLGWIPSLLPSEFQLGWGGCSHLHAWPSASVIITASSCH
Published statement 1 publication
Evidence & references
No verified residues in this structure
Alternative sequenceVSP_002891628in isoform 4
C → S
Published statement 1 publication
Evidence & references
No verified residues in this structure
Alternative sequenceVSP_002892629–1210in isoform 4
Published statement 1 publication
Evidence & references
No verified residues in this structure
Alternative sequenceVSP_002890706–1210in isoform 3
Published statement 1 publication
Evidence & references
No verified residues in this structure

Sequence conflicts & cautions 1

Scroll across the table for evidence and actions.

1 recorded rows

FeaturePositionDescriptionEvidenceInspect
Sequence conflict540in Ref. 1; CAA25240
N → K
Curator inference
Evidence & references
  • ECO:0000305
No verified residues in this structure

Recorded secondary structure 139

Scroll across the table for evidence and actions.

139 recorded rows

FeaturePositionDescriptionEvidenceInspect
Beta strand40–43Beta strand
Evidence & references
  • ECO:0007829 PDB:3QWQ
No verified residues in this structure
Helix44–55Helix
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand60–69Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Helix77–81Helix
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand84–87Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand89–93Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand96–98Beta strand
Evidence & references
  • ECO:0007829 PDB:9IPB
No verified residues in this structure
Helix101–103Helix
Evidence & references
  • ECO:0007829 PDB:1IVO
No verified residues in this structure
Turn114–116Turn
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand117–122Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand125–129Beta strand
Evidence & references
  • ECO:0007829 PDB:1MOX
No verified residues in this structure
Beta strand145–152Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Helix159–161Helix
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Helix164–166Helix
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Helix170–173Helix
Evidence & references
  • ECO:0007829 PDB:1MOX
No verified residues in this structure
Beta strand183–185Beta strand
Evidence & references
  • ECO:0007829 PDB:5XWD
No verified residues in this structure
Helix187–191Helix
Evidence & references
  • ECO:0007829 PDB:1MOX
No verified residues in this structure
Helix195–197Helix
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand199–204Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand211–214Beta strand
Evidence & references
  • ECO:0007829 PDB:1MOX
No verified residues in this structure
Beta strand217–221Beta strand
Evidence & references
  • ECO:0007829 PDB:5XWD
No verified residues in this structure
Beta strand223–227Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Helix228–230Helix
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand236–238Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand240–244Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Turn245–247Turn
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand248–256Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand259–263Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand267–271Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Turn272–275Turn
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand276–279Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand285–287Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand290–294Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Turn296–298Turn
Evidence & references
  • ECO:0007829 PDB:3B2V
No verified residues in this structure
Beta strand299–301Beta strand
Evidence & references
  • ECO:0007829 PDB:7LEN
No verified residues in this structure
Beta strand303–305Beta strand
Evidence & references
  • ECO:0007829 PDB:4KRP
No verified residues in this structure
Beta strand306–310Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand313–315Beta strand
Evidence & references
  • ECO:0007829 PDB:3B2V
No verified residues in this structure
Beta strand318–320Beta strand
Evidence & references
  • ECO:0007829 PDB:3G5Y
No verified residues in this structure
Beta strand323–325Beta strand
Evidence & references
  • ECO:0007829 PDB:3G5Y
No verified residues in this structure
Beta strand330–332Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand336–338Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Turn340–342Turn
Evidence & references
  • ECO:0007829 PDB:3QWQ
No verified residues in this structure
Helix343–345Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand349–351Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Turn353–355Turn
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Helix356–359Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand363–367Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand369–371Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Helix373–377Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Turn380–383Turn
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Helix385–388Helix
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Helix389–397Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand400–403Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand405–407Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Helix418–420Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Turn433–435Turn
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand436–442Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand458–464Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Helix472–474Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Helix477–480Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand481–483Beta strand
Evidence & references
  • ECO:0007829 PDB:1YY9
No verified residues in this structure
Beta strand488–494Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Helix496–501Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand508–510Beta strand
Evidence & references
  • ECO:0007829 PDB:5SX4
No verified residues in this structure
Beta strand515–519Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Helix520–522Helix
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand523–526Beta strand
Evidence & references
  • ECO:0007829 PDB:3P0Y
No verified residues in this structure
Beta strand531–533Beta strand
Evidence & references
  • ECO:0007829 PDB:4KRL
No verified residues in this structure
Beta strand534–537Beta strand
Evidence & references
  • ECO:0007829 PDB:8UKW
No verified residues in this structure
Beta strand540–546Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand548–551Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand554–557Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand560–562Beta strand
Evidence & references
  • ECO:0007829 PDB:4KRO
No verified residues in this structure
Beta strand566–568Beta strand
Evidence & references
  • ECO:0007829 PDB:8UKW
No verified residues in this structure
Beta strand570–575Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand578–587Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand590–594Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand597–602Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand606–611Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand615–619Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand622–624Beta strand
Evidence & references
  • ECO:0007829 PDB:7SYE
No verified residues in this structure
Beta strand629–632Beta strand
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Helix633–635Helix
Evidence & references
  • ECO:0007829 PDB:4UV7
No verified residues in this structure
Beta strand643–646Beta strand
Evidence & references
  • ECO:0007829 PDB:2KS1
No verified residues in this structure
Helix648–669Helix
Evidence & references
  • ECO:0007829 PDB:2KS1
No verified residues in this structure
Beta strand671–673Beta strand
Evidence & references
  • ECO:0007829 PDB:1Z9I
No verified residues in this structure
Helix679–684Helix
Evidence & references
  • ECO:0007829 PDB:3GOP
No verified residues in this structure
Helix685–687Helix
Evidence & references
  • ECO:0007829 PDB:3GOP
No verified residues in this structure
Beta strand688–692Beta strand
Evidence & references
  • ECO:0007829 PDB:1Z9I
No verified residues in this structure
Beta strand694–697Beta strand
Evidence & references
  • ECO:0007829 PDB:1Z9I
No verified residues in this structure
Beta strand703–706Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix709–711Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand712–720Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand722–731Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Turn734–736Turn
Evidence & references
  • ECO:0007829 PDB:5UG9
No verified residues in this structure
Beta strand740–749Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix753–767Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix768–770Helix
Evidence & references
  • ECO:0007829 PDB:9GC4
No verified residues in this structure
Beta strand772–774Beta strand
Evidence & references
  • ECO:0007829 PDB:9DF4
No verified residues in this structure
Beta strand777–781Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand783–785Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand787–791Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand794–797Beta strand
Evidence & references
  • ECO:0007829 PDB:5ZWJ
No verified residues in this structure
Helix798–804Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix806–808Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix811–830Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand833–836Beta strand
Evidence & references
  • ECO:0007829 PDB:9U91
No verified residues in this structure
Helix840–842Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand843–847Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand850–853Beta strand
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix856–858Helix
Evidence & references
  • ECO:0007829 PDB:7VRA
No verified residues in this structure
Turn859–865Turn
Evidence & references
  • ECO:0007829 PDB:8A2A
No verified residues in this structure
Helix866–868Helix
Evidence & references
  • ECO:0007829 PDB:8A2D
No verified residues in this structure
Beta strand871–873Beta strand
Evidence & references
  • ECO:0007829 PDB:6V66
No verified residues in this structure
Helix874–877Helix
Evidence & references
  • ECO:0007829 PDB:6JX0
No verified residues in this structure
Helix878–880Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix883–888Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand890–892Beta strand
Evidence & references
  • ECO:0007829 PDB:2RF9
No verified residues in this structure
Helix893–908Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Turn909–911Turn
Evidence & references
  • ECO:0007829 PDB:9EWS
No verified residues in this structure
Turn914–917Turn
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix920–922Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix923–928Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix933–936Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand937–939Beta strand
Evidence & references
  • ECO:0007829 PDB:8PO0
No verified residues in this structure
Helix941–950Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Beta strand951–953Beta strand
Evidence & references
  • ECO:0007829 PDB:5JEB
No verified residues in this structure
Helix955–957Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix961–972Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix975–977Helix
Evidence & references
  • ECO:0007829 PDB:8A27
No verified residues in this structure
Helix984–986Helix
Evidence & references
  • ECO:0007829 PDB:5HG8
No verified residues in this structure
Helix988–991Helix
Evidence & references
  • ECO:0007829 PDB:5CNO
No verified residues in this structure
Turn992–998Turn
Evidence & references
  • ECO:0007829 PDB:5HG8
No verified residues in this structure
Turn999–1001Turn
Evidence & references
  • ECO:0007829 PDB:9FZR
No verified residues in this structure
Beta strand1004–1010Beta strand
Evidence & references
  • ECO:0007829 PDB:3W2S
No verified residues in this structure
Helix1013–1016Helix
Evidence & references
  • ECO:0007829 PDB:8A2A
No verified residues in this structure
Beta strand1068–1070Beta strand
Evidence & references
  • ECO:0007829 PDB:3PFV
No verified residues in this structure
Beta strand1091–1094Beta strand
Evidence & references
  • ECO:0007829 PDB:8S1M
No verified residues in this structure
12

Homologs

OMA orthologs

Evolutionary relationships assigned by OMA, kept separate from sequence clusters. “1:1” describes an orthology relationship, not percentage identity.

Recorded preview of up to 12 orthologs; not an exhaustive list. Entries without a verified UniProt mapping open their OMA record.

13

Sources & References

Scientific descriptions and evidence come from the named sources. Atlas assembles the presentation and verifies residue mappings; it does not independently curate these claims.

Source dates & provenance

Recorded 2026-11-10. Source dates and identifiers are retained below.

Publications in this UniProt entry

1 · Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells.

1984 · Nature

PubMed 6328312 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); PROTEIN SEQUENCE OF 25-32

Ullrich A., Coussens L., Hayflick J.S., Dull T.J., Gray A., Tam A.W., Lee J., Yarden Y., Libermann T.A., Schlessinger J., Downward J., Mayes E.L.V., Whittle N., Waterfield M.D., Seeburg P.H.

2 · Possible role of variant RNA transcripts in the regulation of epidermal growth factor receptor expression in human placenta.

1995 · Mol. Reprod. Dev.

PubMed 7654368 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)

Ilekis J.V., Stark B.C., Scoccia B.

3 · A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor.

1996 · Nucleic Acids Res.

PubMed 8918811 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2)

Reiter J.L., Maihle N.J.

4 · Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer.

1997 · Gynecol. Oncol.

PubMed 9103388 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)

Ilekis J.V., Gariti J., Niederberger C., Scoccia B.

All source publications (120)
5 · Comparative genomic sequence analysis and isolation of human and mouse alternative EGFR transcripts encoding truncated receptor isoforms.

2001 · Genomics

PubMed 11161793 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3 AND 4)

Reiter J.L., Threadgill D.W., Eley G.D., Strunk K.E., Danielsen A.J., Schehl Sinclair C., Pearsall R.S., Green P.J., Yee D., Lampland A.L., Balasubramaniam S., Crossley T.D., Magnuson T.R., James C.D., Maihle N.J.

· Cloning of the cDNA for a short EGF receptor from human placenta.

JUL-2004 ·

Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)

Xu L., Hong A., He X.

· Reference

APR-2004 ·

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS GLN-98; ARG-266; LYS-521; ILE-674; GLY-962 AND PRO-988

· Human and mouse alternative EGFR transcripts encoding only the extracellular domain of the receptor.

FEB-1999 ·

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 575-687

Reiter J.L., Threadgill D.W., Danielsen A.J., Schehl C.M., Lampland A.L., Balasubramaniam S., Crossley T.O., Magnuson T.R., Maihle N.J.

9 · Expression cloning of human EGF receptor complementary DNA: gene amplification and three related messenger RNA products in A431 cells.

1984 · Science

PubMed 6326261 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] OF 713-924

Lin C.R., Chen W.S., Kruiger W., Stolarsky L.S., Weber W., Evans R.M., Verma I.M., Gill G.N., Rosenfeld M.G.

10 · Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells.

1984 · Nature

PubMed 6330563 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] OF 150-962

Xu Y.H., Ishii S., Clark A.J.L., Sullivan M., Wilson R.K., Ma D.P., Roe B.A., Merlino G.T., Pastan I.

11 · Isolation of an evolutionarily conserved epidermal growth factor receptor cDNA from human A431 carcinoma cells.

1984 · Biochem. Biophys. Res. Commun.

PubMed 6093780 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1210

Simmen F.A., Gope M.L., Schulz T.Z., Wright D.A., Carpenter G., O'Malley B.W.

12 · The human EGF receptor gene: structure of the 110 kb locus and identification of sequences regulating its transcription.

1987 · Oncogene Res.

PubMed 3329716 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29

Haley J.D., Whittle N., Bennett P., Kinchington D., Ullrich A., Waterfield M.D.

13 · Contributory effects of de novo transcription and premature transcript termination in the regulation of human epidermal growth factor receptor proto-oncogene RNA synthesis.

1991 · J. Biol. Chem.

PubMed 1988448 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29

Haley J.D., Waterfield M.D.

14 · Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene.

1985 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 2991899 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29

Ishii S., Xu Y.H., Stratton R.H., Roe B.A., Merlino G.T., Pastan I.

15 · Production of an epidermal growth factor receptor-related protein.

1984 · Science

PubMed 6324343 ↗
Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] OF 25-49

Weber W., Gill G.N., Spiess J.

· Reference

SEP-1997 ·

Scope & authors

PROTEIN SEQUENCE OF 540

Kohda D.

17 · Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo.

1988 · J. Biol. Chem.

PubMed 3138233 ↗
Scope & authors

PROTEIN SEQUENCE OF 687-705; 986-998; 1000-1023; 1026-1030 AND 1068-1077; PHOSPHORYLATION AT THR-693; SER-695; SER-1070 AND SER-1071

Heisermann G.J., Gill G.N.

18 · Signal peptide prediction based on analysis of experimentally verified cleavage sites.

2004 · Protein Sci.

PubMed 15340161 ↗
Scope & authors

PROTEIN SEQUENCE OF 25-39

Zhang Z., Henzel W.J.

19 · Identification of residues in the nucleotide binding site of the epidermal growth factor receptor/kinase.

1985 · J. Biol. Chem.

PubMed 2985580 ↗
Scope & authors

PROTEIN SEQUENCE OF 740-744 AND 746-747

Russo M.W., Lukas T.J., Cohen S., Staros J.V.

20 · Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain.

2006 · Mol. Cell

PubMed 16543144 ↗
Scope & authors

PROTEIN SEQUENCE OF 861-875 AND 914-932; UBIQUITINATION AT LYS-716; LYS-737; LYS-754; LYS-867; LYS-929 AND LYS-970; IDENTIFICATION BY MASS SPECTROMETRY

Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.

21 · Disulfide bond structure of human epidermal growth factor receptor.

1998 · J. Biol. Chem.

PubMed 9556602 ↗
Scope & authors

PARTIAL PROTEIN SEQUENCE; DISULFIDE BONDS

Abe Y., Odaka M., Inagaki F., Lax I., Schlessinger J., Kohda D.

22 · ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA.

1984 · Nature

PubMed 6325948 ↗
Scope & authors

RECEPTOR ACTIVITY

Mroczkowski B., Mosig G., Cohen S.

23 · Receptors for epidermal growth factor and other polypeptide mitogens.

1987 · Annu. Rev. Biochem.

PubMed 3039909 ↗
Scope & authors

REVIEW

Carpenter G.

24 · Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation.

1989 · Cell

PubMed 2790960 ↗
Scope & authors

FUNCTION; SUBCELLULAR LOCATION; LIGAND-BINDING

Chen W.S., Lazar C.S., Lund K.A., Welsh J.B., Chang C.P., Walton G.M., Der C.J., Wiley H.S., Gill G.N., Rosenfeld M.G.

25 · All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor.

1989 · J. Biol. Chem.

PubMed 2543678 ↗
Scope & authors

PHOSPHORYLATION AT TYR-1110

Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M., Howk R., Givol D., Ullrich A., Schlessinger J.

26 · Amphiregulin induces tyrosine phosphorylation of the epidermal growth factor receptor and p185erbB2. Evidence that amphiregulin acts exclusively through the epidermal growth factor receptor at the surface of human epithelial cells.

1993 · J. Biol. Chem.

PubMed 7679104 ↗
Scope & authors

IDENTIFICATION OF AREG AS LIGAND; FUNCTION

Johnson G.R., Kannan B., Shoyab M., Stromberg K.

27 · Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor.

1996 · Science

PubMed 8650580 ↗
Scope & authors

INTERACTION WITH ZPR1

Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., Barrett T., Davis R.J.

28 · Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells.

1998 · J. Cell Biol.

PubMed 9852145 ↗
Scope & authors

INTERACTION WITH ZPR1

Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.

29 · Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor.

1999 · EMBO J.

PubMed 10523301 ↗
Scope & authors

PHOSPHORYLATION AT THR-678 AND THR-693

Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.

30 · Recombinant human betacellulin. Molecular structure, biological activities, and receptor interaction.

1994 · J. Biol. Chem.

PubMed 8144591 ↗
Scope & authors

IDENTIFICATION OF BETACELLULIN/BTC AS LIGAND

Watanabe T., Shintani A., Nakata M., Shing Y., Folkman J., Igarashi K., Sasada R.

31 · Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation.

1995 · J. Biol. Chem.

PubMed 7657591 ↗
Scope & authors

FUNCTION IN PHOSPHORYLATION OF CBL; INTERACTION WITH CBL

Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.

32 · Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts.

1996 · Growth Factors

PubMed 8962717 ↗
Scope & authors

GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528

Smith K.D., Davies M.J., Bailey D., Renouf D.V., Hounsell E.F.

33 · Epiregulin binds to epidermal growth factor receptor and ErbB-4 and induces tyrosine phosphorylation of epidermal growth factor receptor, ErbB-2, ErbB-3 and ErbB-4.

1997 · Oncogene

PubMed 9419975 ↗
Scope & authors

IDENTIFICATION OF EPIREGULIN/EREG AS LIGAND; FUNCTION

Komurasaki T., Toyoda H., Uchida D., Morimoto S.

34 · Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase.

1998 · Mol. Cell. Biol.

PubMed 9488479 ↗
Scope & authors

PHOSPHORYLATION; DEPHOSPHORYLATION BY PTPN1 AND PTPN2

Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.

35 · Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis.

1999 · EMBO J.

PubMed 10228163 ↗
Scope & authors

INTERACTION WITH AP2M1

Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.

36 · Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck.

1999 · J. Biol. Chem.

PubMed 10026169 ↗
Scope & authors

FUNCTION; INTERACTION WITH GRB2; NCK1 AND NCK2

Braverman L.E., Quilliam L.A.

37 · Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.

2000 · J. Biochem.

PubMed 10731668 ↗
Scope & authors

GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603

Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.

38 · RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation.

2001 · J. Biol. Chem.

PubMed 11602604 ↗
Scope & authors

FUNCTION IN PHOSPHORYLATION OF RGS16

Derrien A., Druey K.M.

39 · Characterization of glycosylation sites of the epidermal growth factor receptor.

2003 · Biochemistry

PubMed 12731890 ↗
Scope & authors

GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361; ASN-413; ASN-444; ASN-528; ASN-568; ASN-603 AND ASN-623

Zhen Y., Caprioli R.M., Staros J.V.

40 · Identification and characterization of signal transducer and activator of transcription 3 recruitment sites within the epidermal growth factor receptor.

2003 · Cancer Res.

PubMed 12873986 ↗
Scope & authors

FUNCTION IN CELL PROLIFERATION; INTERACTION WITH STAT3; PHOSPHORYLATION AT TYR-1092 AND TYR-1110

Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.

41 · LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation.

2004 · EMBO J.

PubMed 15282549 ↗
Scope & authors

ACTIVITY REGULATION; INTERACTION WITH LRIG1

Gur G., Rubin C., Katz M., Amit I., Citri A., Nilsson J., Amariglio N., Henriksson R., Rechavi G., Hedman H., Wides R., Yarden Y.

42 · Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors.

2000 · Mol. Cell. Biol.

PubMed 10805725 ↗
Scope & authors

FUNCTION IN EGFR SIGNALING; IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND ERBB2; IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND ERBB2; INTERACTION WITH PIK3C2B; MUTAGENESIS OF TYR-1016; TYR-1092; TYR-1110; TYR-1172 AND TYR-1197

Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.

43 · The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome.

2001 · J. Biol. Chem.

PubMed 11116146 ↗
Scope & authors

FUNCTION IN NF-KAPPA-B ACTIVATION; INTERACTION WITH RIPK1

Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S., Vartanian T.

44 · The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin.

2001 · J. Biol. Chem.

PubMed 11483589 ↗
Scope & authors

FUNCTION IN PHOSPHORYLATION OF MUC1; INTERACTION WITH MUC1

Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III, Kufe D.

45 · Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling.

2005 · J. Biol. Chem.

PubMed 15590694 ↗
Scope & authors

FUNCTION; ACTIVITY REGULATION; INTERACTION WITH SOCS5

Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N., Rechavi G., Yarden Y.

46 · Epigen, the last ligand of ErbB receptors, reveals intricate relationships between affinity and mitogenicity.

2005 · J. Biol. Chem.

PubMed 15611079 ↗
Scope & authors

IDENTIFICATION OF EPIGEN/EPGN AS A LIGAND; FUNCTION

Kochupurakkal B.S., Harari D., Di-Segni A., Maik-Rachline G., Lyass L., Gur G., Kerber G., Citri A., Lavi S., Eilam R., Chalifa-Caspi V., Eshhar Z., Pikarsky E., Pinkas-Kramarski R., Bacus S.S., Yarden Y.

47 · Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR).

2005 · J. Proteome Res.

PubMed 16083266 ↗
Scope & authors

GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361; ASN-413; ASN-444; ASN-528; ASN-568 AND ASN-603; PHOSPHORYLATION AT THR-693; SER-991 AND SER-1026; IDENTIFICATION BY MASS SPECTROMETRY

Wu S.L., Kim J., Hancock W.S., Karger B.

48 · Functional implications of altered subcellular localization of PELP1 in breast cancer cells.

2005 · Cancer Res.

PubMed 16140940 ↗
Scope & authors

INTERACTION WITH PELP1

Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z., Sahin A.A., Kumar R.

49 · Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

2006 · Cell

PubMed 17081983 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1172 AND TYR-1197; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.

50 · Tyrosine phosphorylation controls PCNA function through protein stability.

2006 · Nat. Cell Biol.

PubMed 17115032 ↗
Scope & authors

FUNCTION IN CELL PROLIFERATION; FUNCTION IN PCNA PHOSPHORYLATION; INTERACTION WITH PCNA; SUBCELLULAR LOCATION

Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C., McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.

51 · Syntaxin 9 is enriched in skin hair follicle epithelium and interacts with the epidermal growth factor receptor.

2006 · Traffic

PubMed 16420529 ↗
Scope & authors

INTERACTION WITH STX19

Wang Y., Foo L.Y., Guo K., Gan B.Q., Zeng Q., Hong W., Tang B.L.

52 · The phosphoinositide kinase PIKfyve mediates epidermal growth factor receptor trafficking to the nucleus.

2007 · Cancer Res.

PubMed 17909029 ↗
Scope & authors

INTERACTION WITH PIKFYVE; SUBCELLULAR LOCATION; FUNCTION

Kim J., Jahng W.J., Di Vizio D., Lee J.S., Jhaveri R., Rubin M.A., Shisheva A., Freeman M.R.

53 · Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia.

2007 · J. Clin. Invest.

PubMed 17671655 ↗
Scope & authors

TISSUE SPECIFICITY

Groenestege W.M.T., Thebault S., van der Wijst J., van den Berg D., Janssen R., Tejpar S., van den Heuvel L.P., van Cutsem E., Hoenderop J.G., Knoers N.V., Bindels R.J.

54 · Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation.

2007 · Mol. Biol. Cell

PubMed 17182860 ↗
Scope & authors

INTERACTION WITH TNF2; SUBCELLULAR LOCATION

Shen F., Lin Q., Gu Y., Childress C., Yang W.

55 · A crucial role of plasma membrane-associated sialidase in the survival of human cancer cells.

2007 · Oncogene

PubMed 17334392 ↗
Scope & authors

INTERACTION WITH NEU3; ACTIVITY REGULATION

Wada T., Hata K., Yamaguchi K., Shiozaki K., Koseki K., Moriya S., Miyagi T.

56 · Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking.

2008 · Cell. Signal.

PubMed 18602463 ↗
Scope & authors

INTERACTION WITH ATXN2

Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J., Auburger G.

57 · Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein.

2008 · EMBO J.

PubMed 19172738 ↗
Scope & authors

INTERACTION WITH GAB2

Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.

58 · Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

2008 · J. Proteome Res.

PubMed 18220336 ↗
Scope & authors

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III

59 · Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

2008 · Mol. Cell

PubMed 18691976 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-1064; SER-1081; SER-1166 AND TYR-1197; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.

60 · A quantitative atlas of mitotic phosphorylation.

2008 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 18669648 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991; SER-995; TYR-998; SER-1039; THR-1041; SER-1042; SER-1064 AND SER-1166; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.

61 · Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

2009 · Anal. Chem.

PubMed 19413330 ↗
Scope & authors

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.

62 · An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis.

2009 · Curr. Biol.

PubMed 19836242 ↗
Scope & authors

FUNCTION; ACTIVITY REGULATION BY PTPRJ AND PTPRK; PHOSPHORYLATION AT TYR-1197; DEPHOSPHORYLATION BY PTPRJ; SUBCELLULAR LOCATION; INTERACTION WITH CBL AND GRB2

Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.

63 · GAREM, a novel adaptor protein for growth factor receptor-bound protein 2, contributes to cellular transformation through the activation of extracellular signal-regulated kinase signaling.

2009 · J. Biol. Chem.

PubMed 19509291 ↗
Scope & authors

INTERACTION WITH GAREM1

Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E., Taniguchi H., Konishi H.

64 · Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

2009 · J. Proteome Res.

PubMed 19159218 ↗
Scope & authors

GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352; ASN-413 AND ASN-568

Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.

65 · Large-scale proteomics analysis of the human kinome.

2009 · Mol. Cell. Proteomics

PubMed 19369195 ↗
Scope & authors

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.

66 · G protein-coupled receptor 30 expression is up-regulated by EGF and TGF alpha in estrogen receptor alpha-positive cancer cells.

2009 · Mol. Endocrinol.

PubMed 19749156 ↗
Scope & authors

INTERACTION WITH GPER1

Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F., Fuqua S.A., Ando S., Maggiolini M.

67 · ErbB2 resembles an autoinhibited invertebrate epidermal growth factor receptor.

2009 · Nature

PubMed 19718021 ↗
Scope & authors

MUTAGENESIS OF 525-SER--ALA-1210; ASP-587; HIS-590 AND LYS-609

Alvarado D., Klein D.E., Lemmon M.A.

68 · COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport.

2010 · Biochem. Biophys. Res. Commun.

PubMed 20674546 ↗
Scope & authors

INTERACTION WITH COPG1; SUBCELLULAR LOCATION; TOPOLOGY

Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.

69 · Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts.

2010 · Cancer Res.

PubMed 20551055 ↗
Scope & authors

INTERACTION WITH GPER1; SUBCELLULAR LOCATION

Madeo A., Maggiolini M.

70 · A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor and determines whether cells migrate or proliferate.

2010 · Mol. Biol. Cell

PubMed 20462955 ↗
Scope & authors

FUNCTION; IDENTIFICATION IN COMPLEX WITH CCDC88A AND GNAI3; SUBCELLULAR LOCATION; PHOSPHORYLATION

Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P., Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.

71 · Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

2010 · Sci. Signal.

PubMed 20068231 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1064 AND TYR-1197; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.

72 · Initial characterization of the human central proteome.

2011 · BMC Syst. Biol.

PubMed 21269460 ↗
Scope & authors

IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.

73 · Nuclear translocation of epidermal growth factor receptor by Akt-dependent phosphorylation enhances breast cancer-resistant protein expression in gefitinib-resistant cells.

2011 · J. Biol. Chem.

PubMed 21487020 ↗
Scope & authors

PHOSPHORYLATION AT SER-229

Huang W.C., Chen Y.J., Li L.Y., Wei Y.L., Hsu S.C., Tsai S.L., Chiu P.C., Huang W.P., Wang Y.N., Chen C.H., Chang W.C., Chang W.C., Chen A.J., Tsai C.H., Hung M.C.

74 · Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation.

2011 · Nat. Cell Biol.

PubMed 21258366 ↗
Scope & authors

FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION; METHYLATION AT ARG-1199 BY PRMT5; INTERACTION WITH PRMT5 AND PTPN6

Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J., Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T., Tsai C.H., Hung M.C.

75 · EGFR and EphA2 are host factors for hepatitis C virus entry and possible targets for antiviral therapy.

2011 · Nat. Med.

PubMed 21516087 ↗
Scope & authors

FUNCTION (MICROBIAL INFECTION)

Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L., Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B., Zahid M.N., Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M., Pietschmann T., Patel A.H., Pessaux P., Doffoel M., Raffelsberger W., Poch O., McKeating J.A., Brino L., Baumert T.F.

76 · FER tyrosine kinase (FER) overexpression mediates resistance to quinacrine through EGF-dependent activation of NF-kappaB.

2011 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 21518868 ↗
Scope & authors

INTERACTION WITH FER; PHOSPHORYLATION

Guo C., Stark G.R.

77 · The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane.

2012 · Mol. Biol. Cell

PubMed 22298428 ↗
Scope & authors

INTERACTION WITH ANKRD13A; ANKRD13B AND ANKRD13D; UBIQUITINATION; SUBCELLULAR LOCATION

Tanno H., Yamaguchi T., Goto E., Ishido S., Komada M.

78 · Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression.

2012 · Oncogene

PubMed 22179831 ↗
Scope & authors

UBIQUITINATION; DEUBIQUITINATION BY OTUD7B

Pareja F., Ferraro D.A., Rubin C., Cohen-Dvashi H., Zhang F., Aulmann S., Ben-Chetrit N., Pines G., Navon R., Crosetto N., Kostler W., Carvalho S., Lavi S., Schmitt F., Dikic I., Yakhini Z., Sinn P., Mills G.B., Yarden Y.

79 · CTEN prolongs signaling by EGFR through reducing its ligand-induced degradation.

2013 · Cancer Res.

PubMed 23774213 ↗
Scope & authors

INTERACTION WITH CBL; PHOSPHORYLATION AT TYR-869; TYR-1016; TYR-1069; TYR-1092 AND TYR-1197

Hong S.Y., Shih Y.P., Li T., Carraway K.L. III, Lo S.H.

80 · The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor.

2013 · J. Cell Sci.

PubMed 23418353 ↗
Scope & authors

INTERACTION WITH RNF115 AND RNF126

Smith C.J., Berry D.M., McGlade C.J.

81 · Toward a comprehensive characterization of a human cancer cell phosphoproteome.

2013 · J. Proteome Res.

PubMed 23186163 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693 AND SER-1064; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.

82 · An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

2014 · J. Proteomics

PubMed 24275569 ↗
Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1026 AND SER-1166; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.

83 · Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin.

2014 · Mol. Biol. Cell

PubMed 25187647 ↗
Scope & authors

INTERACTION WITH CCDC88A AND GNAI3

Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M., Kufareva I., Abagyan R., Ghosh P.

84 · Transforming growth factor-beta1 (TGF-beta1)-stimulated fibroblast to myofibroblast differentiation is mediated by hyaluronan (HA)-facilitated epidermal growth factor receptor (EGFR) and CD44 co-localization in lipid rafts.

2013 · J. Biol. Chem.

PubMed 23589287 ↗
Scope & authors

SUBCELLULAR LOCATION; INTERACTION WITH CD44

Midgley A.C., Rogers M., Hallett M.B., Clayton A., Bowen T., Phillips A.O., Steadman R.

85 · EGFR phosphorylates and inhibits lung tumor suppressor GPRC5A in lung cancer.

2014 · Mol. Cancer

PubMed 25311788 ↗
Scope & authors

INTERACTION WITH GPRC5A

Lin X., Zhong S., Ye X., Liao Y., Yao F., Yang X., Sun B., Zhang J., Li Q., Gao Y., Wang Y., Liu J., Han B., Chin Y.E., Zhou B.P., Deng J.

86 · Hyperactivation of EGFR and downstream effector phospholipase D1 by oncogenic FAM83B.

2014 · Oncogene

PubMed 23912460 ↗
Scope & authors

INTERACTION WITH FAM83B

Cipriano R., Bryson B.L., Miskimen K.L., Bartel C.A., Hernandez-Sanchez W., Bruntz R.C., Scott S.A., Lindsley C.W., Brown H.A., Jackson M.W.

87 · NEU3 activity enhances EGFR activation without affecting EGFR expression and acts on its sialylation levels.

2015 · Glycobiology

PubMed 25922362 ↗
Scope & authors

GLYCOSYLATION AT ASN-528; ACTIVITY REGULATION

Mozzi A., Forcella M., Riva A., Difrancesco C., Molinari F., Martin V., Papini N., Bernasconi B., Nonnis S., Tedeschi G., Mazzucchelli L., Monti E., Fusi P., Frattini M.

88 · Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling.

2016 · Mol. Cell

PubMed 27153536 ↗
Scope & authors

FUNCTION; PALMITOYLATION AT CYS-1049 AND CYS-1146; IDENTIFICATION BY MASS SPECTROMETRY; UBIQUITINATION; PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197; SUBCELLULAR LOCATION; MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146

Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.

89 · Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer proliferation and chemoresistance.

2016 · Nat. Commun.

PubMed 26988023 ↗
Scope & authors

INTERACTION WITH PGRMC1

Kabe Y., Nakane T., Koike I., Yamamoto T., Sugiura Y., Harada E., Sugase K., Shimamura T., Ohmura M., Muraoka K., Yamamoto A., Uchida T., Iwata S., Yamaguchi Y., Krayukhina E., Noda M., Handa H., Ishimori K., Uchiyama S., Kobayashi T., Suematsu M.

90 · c-Src/Cav1-dependent activation of the EGFR by Dsg2.

2016 · Oncotarget

PubMed 26918609 ↗
Scope & authors

SUBCELLULAR LOCATION; PHOSPHORYLATION AT TYR-1172

Overmiller A.M., McGuinn K.P., Roberts B.J., Cooper F., Brennan-Crispi D.M., Deguchi T., Peltonen S., Wahl J.K. III, Mahoney M.G.

91 · Epidermal Growth Factor Receptor neddylation is regulated by a desmosomal-COP9 (Constitutive Photomorphogenesis 9) signalosome complex.

2017 · Elife

PubMed 28891468 ↗
Scope & authors

NEDDYLATION

Najor N.A., Fitz G.N., Koetsier J.L., Godsel L.M., Albrecht L.V., Harmon R., Green K.J.

92 · Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric cancer cells.

2017 · Gene

PubMed 28479384 ↗
Scope & authors

INTERACTION WITH LAPTM4B

Tian M., Chen Y., Tian D., Qiao X., Ma Z., Li J.

93 · Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway.

2018 · Cell Res.

PubMed 29192674 ↗
Scope & authors

HYDROXYBUTYRYLATION AT LYS-745

Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J., Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.

94 · TRAF4 binds to the juxtamembrane region of EGFR directly and promotes kinase activation.

2018 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 30352854 ↗
Scope & authors

INTERACTION WITH TRAF4

Cai G., Zhu L., Chen X., Sun K., Liu C., Sen G.C., Stark G.R., Qin J., Li X.

95 · EGFR-mediated tyrosine phosphorylation of STING determines its trafficking route and cellular innate immunity functions.

2020 · EMBO J.

PubMed 32926474 ↗
Scope & authors

FUNCTION; CATALYTIC ACTIVITY

Wang C., Wang X., Veleeparambil M., Kessler P.M., Willard B., Chattopadhyay S., Sen G.C.

96 · ZNRF1 Mediates Epidermal Growth Factor Receptor Ubiquitination to Control Receptor Lysosomal Trafficking and Degradation.

2021 · Front. Cell Dev. Biol.

PubMed 33996800 ↗
Scope & authors

UBIQUITINATION BY ZNRF1 AND CBL

Shen C.H., Chou C.C., Lai T.Y., Hsu J.E., Lin Y.S., Liu H.Y., Chen Y.K., Ho I.L., Hsu P.H., Chuang T.H., Lee C.Y., Hsu L.C.

97 · CD82 palmitoylation site mutations at Cys5+Cys74 affect EGFR internalization and metabolism through recycling pathway.

2022 · Acta Biochim. Biophys. Sin.

PubMed 35538033 ↗
Scope & authors

FUNCTION; SUBCELLULAR LOCATION; INTERACTION WITH CD82

Bu J., Zhong W., Li M., He S., Zhang M., Zhang Y., Li Y.

98 · SNX32 regulates sorting and trafficking of activated EGFR to the lysosomal degradation pathway.

2024 · Traffic

PubMed 39073202 ↗
Scope & authors

INTERACTION WITH SNX32

Wang D., Zhao X., Wang P., Liu J.J.

99 · Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.

2002 · Cell

PubMed 12297049 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH TGFA; FUNCTION; GLYCOSYLATION AT ASN-56; ASN-196 AND ASN-352; DISULFIDE BONDS

Garrett T.P., McKern N.M., Lou M., Elleman T.C., Adams T.E., Lovrecz G.O., Zhu H.J., Walker F., Frenkel M.J., Hoyne P.A., Jorissen R.N., Nice E.C., Burgess A.W., Ward C.W.

100 · Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.

2002 · Cell

PubMed 12297050 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH EGF; FUNCTION IN MAPK1 AND/OR MAPK3 ACTIVATION; SUBUNIT; SUBCELLULAR LOCATION; MUTAGENESIS OF TYR-275; PHE-287; ARG-309 AND ARG-429; DISULFIDE BONDS; GLYCOSYLATION AT ASN-56; ASN-175; ASN-196; ASN-352; ASN-361 AND ASN-444

Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H., Saito K., Sakamoto A., Inoue M., Shirouzu M., Yokoyama S.

101 · EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.

2003 · Mol. Cell

PubMed 12620237 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH EGF; FUNCTION; SUBUNIT; MUTAGENESIS OF 587-ASP--HIS-590 AND LYS-609; DISULFIDE BONDS; GLYCOSYLATION AT ASN-352; ASN-361; ASN-444; ASN-528; ASN-568 AND ASN-603

Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J., Lemmon M.A.

102 · A unique structure for epidermal growth factor receptor bound to GW572016 (Lapatinib): relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells.

2004 · Cancer Res.

PubMed 15374980 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH GW572016; CATALYTIC ACTIVITY; FUNCTION

Wood E.R., Truesdale A.T., McDonald O.B., Yuan D., Hassell A., Dickerson S.H., Ellis B., Pennisi C., Horne E., Lackey K., Alligood K.J., Rusnak D.W., Gilmer T.M., Shewchuk L.

103 · Structural basis for inhibition of the epidermal growth factor receptor by cetuximab.

2005 · Cancer Cell

PubMed 15837620 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CETUXIMAB

Li S., Schmitz K.R., Jeffrey P.D., Wiltzius J.J., Kussie P., Ferguson K.M.

104 · A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor.

2005 · J. Biol. Chem.

PubMed 15840573 ↗
Scope & authors

STRUCTURE BY NMR OF 669-721

Choowongkomon K., Carlin C.R., Sonnichsen F.D.

105 · Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity.

2007 · Cancer Cell

PubMed 17349580 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND VARIANTS SER-719 AND ARG-858 IN COMPLEXES WITH ATP ANALOGS AND SYNTHETIC INHIBITORS; FUNCTION; CATALYTIC ACTIVITY; AUTOPHOSPHORYLATION; CHARACTERIZATION OF VARIANTS SER-719 AND ARG-858

Yun C.H., Boggon T.J., Li Y., Woo M.S., Greulich H., Meyerson M., Eck M.J.

106 · Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface.

2007 · Nature

PubMed 18046415 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ERRFI1; FUNCTION; ACTIVITY REGULATION; CATALYTIC ACTIVITY; AUTOPHOSPHORYLATION; SUBUNIT; INTERACTION WITH ERRFI1

Zhang X., Pickin K.A., Bose R., Jura N., Cole P.A., Kuriyan J.

107 · The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP.

2008 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 18227510 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY OF VARIANT MET-790; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANT MET-790

Yun C.H., Mengwasser K.E., Toms A.V., Woo M.S., Greulich H., Wong K.K., Meyerson M., Eck M.J.

108 · Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment.

2009 · Cell

PubMed 19563760 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY; CATALYTIC ACTIVITY; PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197; MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND 1005-GLU-ASP-1006; SUBUNIT

Jura N., Endres N.F., Engel K., Deindl S., Das R., Lamers M.H., Wemmer D.E., Zhang X., Kuriyan J.

109 · The juxtamembrane region of the EGF receptor functions as an activation domain.

2009 · Mol. Cell

PubMed 19560417 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY OF MUTANT MET-745; CATALYTIC ACTIVITY; FUNCTION; SUBUNIT; SUBCELLULAR LOCATION; AUTOPHOSPHORYLATION; MUTAGENESIS OF LEU-688; VAL-689; GLU-690; LEU-692; THR-693; PRO-694; PRO-699; ASN-700; LEU-704; ARG-705; ILE-706 AND LYS-745

Red Brewer M., Choi S.H., Alvarado D., Moravcevic K., Pozzi A., Lemmon M.A., Carpenter G.

110 · Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases.

2010 · J. Mol. Biol.

PubMed 20471394 ↗
Scope & authors

STRUCTURE BY NMR OF 634-677 IN COMPLEX WITH ERBB2; SUBUNIT

Mineev K.S., Bocharov E.V., Pustovalova Y.E., Bocharova O.V., Chupin V.V., Arseniev A.S.

111 · Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.

2010 · Mol. Cell. Biol.

PubMed 20837704 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH EGF; FUNCTION; SUBUNIT; DISULFIDE BONDS; GLYCOSYLATION AT ASN-56; ASN-73; ASN-175; ASN-196; ASN-352; ASN-361; ASN-444 AND ASN-528

Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S., Springer T.A.

· Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069 peptide.

OCT-2010 ·

Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CBLB; INTERACTION WITH CBLB

113 · Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.

2012 · J. Biochem.

PubMed 22888118 ↗
Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CBLC; PHOSPHORYLATION AT TYR-1069; INTERACTION WITH CBLC; MUTAGENESIS OF GLN-1067; ARG-1068 AND TYR-1069

Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M., Yamanashi Y., Yamamoto T., Nakagawa A.

114 · High frequency of epidermal growth factor receptor mutations with complex patterns in non-small cell lung cancers related to gefitinib responsiveness in Taiwan.

2004 · Clin. Cancer Res.

PubMed 15623594 ↗
Scope & authors

VARIANTS ALA-709; GLY-709; CYS-719; SER-719; 746-GLU--ALA-750 DEL; 746-GLU--THR-751 DELINS ALA; 746-GLU--SER-752 DELINS ASP; 747-LEU--THR-751 DEL; ILE-768; MET-769; VAL-833; LEU-835; VAL-838; ARG-858 AND GLN-861

Huang S.F., Liu H.P., Li L.H., Ku Y.C., Fu Y.N., Tsai H.Y., Chen Y.T., Lin Y.F., Chang W.C., Kuo H.P., Wu Y.C., Chen Y.R., Tsai S.F.

115 · EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy.

2004 · Science

PubMed 15118125 ↗
Scope & authors

VARIANTS SER-719 AND ARG-858; POSSIBLE INVOLVEMENT IN LUNG CANCER

Paez J.G., Janne P.A., Lee J.C., Tracy S., Greulich H., Gabriel S., Herman P., Kaye F.J., Lindeman N., Boggon T.J., Naoki K., Sasaki H., Fujii Y., Eck M.J., Sellers W.R., Johnson B.E., Meyerson M.

116 · Distinct epidermal growth factor receptor and KRAS mutation patterns in non-small cell lung cancer patients with different tobacco exposure and clinicopathologic features.

2006 · Clin. Cancer Res.

PubMed 16533793 ↗
Scope & authors

VARIANTS ALA-709; LYS-709; ALA-719; ASP-719; CYS-719; SER-719; SER-724; LYS-734; GLU-746 DEL; PHE-747; 747-LEU--GLU-749 DEL; PRO-748; 752-SER--ILE-759 DEL; ARG-787; MET-790; VAL-833; LEU-834; MET-858; ARG-858; GLN-861 AND GLU-873; POSSIBLE INVOLVEMENT IN LUNG CANCER

Tam I.Y.S., Chung L.P., Suen W.S., Wang E., Wong M.C.M., Ho K.K., Lam W.K., Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.

117 · Distinctive activation patterns in constitutively active and gefitinib-sensitive EGFR mutants.

2006 · Oncogene

PubMed 16205628 ↗
Scope & authors

CHARACTERIZATION OF VARIANTS ALA-709; GLY-709; SER-719; ILE-768; VAL-833; LEU-835; VAL-838; ARG-858 AND GLN-861

Chen Y.R., Fu Y.N., Lin C.H., Yang S.T., Hu S.F., Chen Y.T., Tsai S.F., Huang S.F.

118 · Epidermal growth factor receptor variant III mutations in lung tumorigenesis and sensitivity to tyrosine kinase inhibitors.

2006 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 16672372 ↗
Scope & authors

VARIANT 30-VAL--ARG-297 DEL; POSSIBLE INVOLVEMENT IN LUNG CANCER

Ji H., Zhao X., Yuza Y., Shimamura T., Li D., Protopopov A., Jung B.L., McNamara K., Xia H., Glatt K.A., Thomas R.K., Sasaki H., Horner J.W., Eck M., Mitchell A., Sun Y., Al-Hashem R., Bronson R.T., Rabindran S.K., Discafani C.M., Maher E., Shapiro G.I., Meyerson M., Wong K.K.

119 · Patterns of somatic mutation in human cancer genomes.

2007 · Nature

PubMed 17344846 ↗
Scope & authors

VARIANTS [LARGE SCALE ANALYSIS] LYS-521; ARG-1034 AND VAL-1210

Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.

120 · Epithelial inflammation resulting from an inherited loss-of-function mutation in EGFR.

2014 · J. Invest. Dermatol.

PubMed 24691054 ↗
Scope & authors

VARIANT NNCIS ASP-428; CHARACTERIZATION OF VARIANT NNCIS ASP-428; INVOLVEMENT IN NNCIS

Campbell P., Morton P.E., Takeichi T., Salam A., Roberts N., Proudfoot L.E., Mellerio J.E., Aminu K., Wellington C., Patil S.N., Akiyama M., Liu L., McMillan J.R., Aristodemou S., Ishida-Yamamoto A., Abdul-Wahab A., Petrof G., Fong K., Harnchoowong S., Stone K.L., Harper J.I., McLean W.H., Simpson M.A., Parsons M., McGrath J.A.

Wikipedia ↗

Annotation coverage audit

Every recorded UniProt comment and feature has a destination in this page. GO, Atlas annotations and interaction rows retain their separate source counts.

334 source comments and features accounted for.

View annotation inventory
Source recordTypeSection
FUNCTION:0FUNCTIONfunction
FUNCTION:1FUNCTIONfunction
FUNCTION:2FUNCTIONfunction
CATALYTIC ACTIVITY:0CATALYTIC ACTIVITYfunction
ACTIVITY REGULATION:0ACTIVITY REGULATIONfunction
SUBUNIT:0SUBUNITinteractions
INTERACTION:0INTERACTIONinteractions
SUBCELLULAR LOCATION:0SUBCELLULAR LOCATIONlocation
SUBCELLULAR LOCATION:1SUBCELLULAR LOCATIONlocation
ALTERNATIVE PRODUCTS:0ALTERNATIVE PRODUCTSsequence
TISSUE SPECIFICITY:0TISSUE SPECIFICITYexpression
PTM:0PTMprocessing
PTM:1PTMprocessing
PTM:2PTMprocessing
PTM:3PTMprocessing
PTM:4PTMprocessing
DISEASE:0DISEASEdisease
DISEASE:1DISEASEdisease
SIMILARITY:0SIMILARITYdomains
WEB RESOURCE:0WEB RESOURCEsources
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feature-1Chainprocessing
feature-2Topological domainlocation
feature-3Transmembranelocation
feature-4Topological domainlocation
feature-5Repeatdomains
feature-6Repeatdomains
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feature-8Regiondomains
feature-9Regiondomains
feature-10Compositional biasdomains
feature-11Compositional biasdomains
feature-12Active sitedomains
feature-13Binding sitedomains
feature-14Binding sitedomains
feature-15Binding sitedomains
feature-16Binding sitedomains
feature-17Sitedomains
feature-18Modified residueprocessing
feature-19Modified residueprocessing
feature-20Modified residueprocessing
feature-21Modified residueprocessing
feature-22Modified residueprocessing
feature-23Modified residueprocessing
feature-24Modified residueprocessing
feature-25Modified residueprocessing
feature-26Modified residueprocessing
feature-27Modified residueprocessing
feature-28Modified residueprocessing
feature-29Modified residueprocessing
feature-30Modified residueprocessing
feature-31Modified residueprocessing
feature-32Modified residueprocessing
feature-33Modified residueprocessing
feature-34Modified residueprocessing
feature-35Modified residueprocessing
feature-36Modified residueprocessing
feature-37Modified residueprocessing
feature-38Modified residueprocessing
feature-39Modified residueprocessing
feature-40Modified residueprocessing
feature-41Modified residueprocessing
feature-42Modified residueprocessing
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feature-44Lipidationprocessing
feature-45Glycosylationprocessing
feature-46Glycosylationprocessing
feature-47Glycosylationprocessing
feature-48Glycosylationprocessing
feature-49Glycosylationprocessing
feature-50Glycosylationprocessing
feature-51Glycosylationprocessing
feature-52Glycosylationprocessing
feature-53Glycosylationprocessing
feature-54Glycosylationprocessing
feature-55Glycosylationprocessing
feature-56Glycosylationprocessing
feature-57Glycosylationprocessing
feature-58Disulfide bondprocessing
feature-59Disulfide bondprocessing
feature-60Disulfide bondprocessing
feature-61Disulfide bondprocessing
feature-62Disulfide bondprocessing
feature-63Disulfide bondprocessing
feature-64Disulfide bondprocessing
feature-65Disulfide bondprocessing
feature-66Disulfide bondprocessing
feature-67Disulfide bondprocessing
feature-68Disulfide bondprocessing
feature-69Disulfide bondprocessing
feature-70Disulfide bondprocessing
feature-71Disulfide bondprocessing
feature-72Disulfide bondprocessing
feature-73Disulfide bondprocessing
feature-74Disulfide bondprocessing
feature-75Disulfide bondprocessing
feature-76Disulfide bondprocessing
feature-77Disulfide bondprocessing
feature-78Disulfide bondprocessing
feature-79Disulfide bondprocessing
feature-80Disulfide bondprocessing
feature-81Disulfide bondprocessing
feature-82Disulfide bondprocessing
feature-83Cross-linkprocessing
feature-84Cross-linkprocessing
feature-85Cross-linkprocessing
feature-86Cross-linkprocessing
feature-87Cross-linkprocessing
feature-88Cross-linkprocessing
feature-89Cross-linkprocessing
feature-90Cross-linkprocessing
feature-91Alternative sequencesequence
feature-92Alternative sequencesequence
feature-93Alternative sequencesequence
feature-94Alternative sequencesequence
feature-95Alternative sequencesequence
feature-96Alternative sequencesequence
feature-97Natural variantdisease
feature-98Natural variantdisease
feature-99Natural variantdisease
feature-100Natural variantdisease
feature-101Natural variantdisease
feature-102Natural variantdisease
feature-103Natural variantdisease
feature-104Natural variantdisease
feature-105Natural variantdisease
feature-106Natural variantdisease
feature-107Natural variantdisease
feature-108Natural variantdisease
feature-109Natural variantdisease
feature-110Natural variantdisease
feature-111Natural variantdisease
feature-112Natural variantdisease
feature-113Natural variantdisease
feature-114Natural variantdisease
feature-115Natural variantdisease
feature-116Natural variantdisease
feature-117Natural variantdisease
feature-118Natural variantdisease
feature-119Natural variantdisease
feature-120Natural variantdisease
feature-121Natural variantdisease
feature-122Natural variantdisease
feature-123Natural variantdisease
feature-124Natural variantdisease
feature-125Natural variantdisease
feature-126Natural variantdisease
feature-127Natural variantdisease
feature-128Natural variantdisease
feature-129Natural variantdisease
feature-130Natural variantdisease
feature-131Natural variantdisease
feature-132Natural variantdisease
feature-133Natural variantdisease
feature-134Natural variantdisease
feature-135Natural variantdisease
feature-136Natural variantdisease
feature-137Mutagenesisdisease
feature-138Mutagenesisdisease
feature-139Mutagenesisdisease
feature-140Mutagenesisdisease
feature-141Mutagenesisdisease
feature-142Mutagenesisdisease
feature-143Mutagenesisdisease
feature-144Mutagenesisdisease
feature-145Mutagenesisdisease
feature-146Mutagenesisdisease
feature-147Mutagenesisdisease
feature-148Mutagenesisdisease
feature-149Mutagenesisdisease
feature-150Mutagenesisdisease
feature-151Mutagenesisdisease
feature-152Mutagenesisdisease
feature-153Mutagenesisdisease
feature-154Mutagenesisdisease
feature-155Mutagenesisdisease
feature-156Mutagenesisdisease
feature-157Mutagenesisdisease
feature-158Mutagenesisdisease
feature-159Mutagenesisdisease
feature-160Mutagenesisdisease
feature-161Mutagenesisdisease
feature-162Mutagenesisdisease
feature-163Mutagenesisdisease
feature-164Mutagenesisdisease
feature-165Mutagenesisdisease
feature-166Mutagenesisdisease
feature-167Mutagenesisdisease
feature-168Mutagenesisdisease
feature-169Mutagenesisdisease
feature-170Mutagenesisdisease
feature-171Mutagenesisdisease
feature-172Mutagenesisdisease
feature-173Mutagenesisdisease
feature-174Sequence conflictsequence
feature-175Beta strandsequence
feature-176Helixsequence
feature-177Beta strandsequence
feature-178Helixsequence
feature-179Beta strandsequence
feature-180Beta strandsequence
feature-181Beta strandsequence
feature-182Helixsequence
feature-183Turnsequence
feature-184Beta strandsequence
feature-185Beta strandsequence
feature-186Beta strandsequence
feature-187Helixsequence
feature-188Helixsequence
feature-189Helixsequence
feature-190Beta strandsequence
feature-191Helixsequence
feature-192Helixsequence
feature-193Beta strandsequence
feature-194Beta strandsequence
feature-195Beta strandsequence
feature-196Beta strandsequence
feature-197Helixsequence
feature-198Beta strandsequence
feature-199Beta strandsequence
feature-200Turnsequence
feature-201Beta strandsequence
feature-202Beta strandsequence
feature-203Beta strandsequence
feature-204Turnsequence
feature-205Beta strandsequence
feature-206Beta strandsequence
feature-207Beta strandsequence
feature-208Turnsequence
feature-209Beta strandsequence
feature-210Beta strandsequence
feature-211Beta strandsequence
feature-212Beta strandsequence
feature-213Beta strandsequence
feature-214Beta strandsequence
feature-215Beta strandsequence
feature-216Beta strandsequence
feature-217Turnsequence
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feature-221Helixsequence
feature-222Beta strandsequence
feature-223Beta strandsequence
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feature-226Helixsequence
feature-227Helixsequence
feature-228Beta strandsequence
feature-229Beta strandsequence
feature-230Helixsequence
feature-231Turnsequence
feature-232Beta strandsequence
feature-233Beta strandsequence
feature-234Helixsequence
feature-235Helixsequence
feature-236Beta strandsequence
feature-237Beta strandsequence
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feature-239Beta strandsequence
feature-240Beta strandsequence
feature-241Helixsequence
feature-242Beta strandsequence
feature-243Beta strandsequence
feature-244Beta strandsequence
feature-245Beta strandsequence
feature-246Beta strandsequence
feature-247Beta strandsequence
feature-248Beta strandsequence
feature-249Beta strandsequence
feature-250Beta strandsequence
feature-251Beta strandsequence
feature-252Beta strandsequence
feature-253Beta strandsequence
feature-254Beta strandsequence
feature-255Beta strandsequence
feature-256Beta strandsequence
feature-257Beta strandsequence
feature-258Helixsequence
feature-259Beta strandsequence
feature-260Helixsequence
feature-261Beta strandsequence
feature-262Helixsequence
feature-263Helixsequence
feature-264Beta strandsequence
feature-265Beta strandsequence
feature-266Beta strandsequence
feature-267Helixsequence
feature-268Beta strandsequence
feature-269Beta strandsequence
feature-270Turnsequence
feature-271Beta strandsequence
feature-272Helixsequence
feature-273Helixsequence
feature-274Beta strandsequence
feature-275Beta strandsequence
feature-276Beta strandsequence
feature-277Beta strandsequence
feature-278Beta strandsequence
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feature-280Helixsequence
feature-281Helixsequence
feature-282Beta strandsequence
feature-283Helixsequence
feature-284Beta strandsequence
feature-285Beta strandsequence
feature-286Helixsequence
feature-287Turnsequence
feature-288Helixsequence
feature-289Beta strandsequence
feature-290Helixsequence
feature-291Helixsequence
feature-292Helixsequence
feature-293Beta strandsequence
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feature-295Turnsequence
feature-296Turnsequence
feature-297Helixsequence
feature-298Helixsequence
feature-299Helixsequence
feature-300Beta strandsequence
feature-301Helixsequence
feature-302Beta strandsequence
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feature-304Helixsequence
feature-305Helixsequence
feature-306Helixsequence
feature-307Helixsequence
feature-308Turnsequence
feature-309Turnsequence
feature-310Beta strandsequence
feature-311Helixsequence
feature-312Beta strandsequence
feature-313Beta strandsequence