EGFREpidermal growth factor receptor
Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses.
UniProt locations Cell membrane · Endoplasmic reticulum membrane · Golgi apparatus membrane · Nucleus membrane · Endosome · Endosome membrane · Nucleus · Secreted
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)
Evidence & references
- ECO:0000250 UniProtKB:Q01279
- ECO:0000269 PubMed:10026169 ↗
- ECO:0000269 PubMed:10805725 ↗
- ECO:0000269 PubMed:11116146 ↗
- ECO:0000269 PubMed:11483589 ↗
- ECO:0000269 PubMed:11602604 ↗
- ECO:0000269 PubMed:12297049 ↗
- ECO:0000269 PubMed:12297050 ↗
- ECO:0000269 PubMed:12620237 ↗
- ECO:0000269 PubMed:12873986 ↗
- ECO:0000269 PubMed:15374980 ↗
- ECO:0000269 PubMed:15590694 ↗
- ECO:0000269 PubMed:15611079 ↗
- ECO:0000269 PubMed:17115032 ↗
- ECO:0000269 PubMed:17349580 ↗
- ECO:0000269 PubMed:17909029 ↗
- ECO:0000269 PubMed:18046415 ↗
- ECO:0000269 PubMed:19560417 ↗
- ECO:0000269 PubMed:19836242 ↗
- ECO:0000269 PubMed:20462955 ↗
- ECO:0000269 PubMed:20837704 ↗
- ECO:0000269 PubMed:21258366 ↗
- ECO:0000269 PubMed:27153536 ↗
- ECO:0000269 PubMed:2790960 ↗
- ECO:0000269 PubMed:32926474 ↗
- ECO:0000269 PubMed:35538033 ↗
- ECO:0000269 PubMed:7679104 ↗
- ECO:0000269 PubMed:8144591 ↗
- ECO:0000269 PubMed:9419975 ↗
- ECO:0000269 PubMed:9488479 ↗
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"
}May act as an antagonist of EGF action
Evidence & references
- ECO:0000269 PubMed:8918811 ↗
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
Evidence & references
- ECO:0000269 PubMed:21516087 ↗
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
- ECO:0000255 PROSITE-ProRule:PRU10028
- ECO:0000269 PubMed:15374980 ↗
- ECO:0000269 PubMed:17349580 ↗
- ECO:0000269 PubMed:18046415 ↗
- ECO:0000269 PubMed:18227510 ↗
- ECO:0000269 PubMed:19560417 ↗
- ECO:0000269 PubMed:19563760 ↗
- ECO:0000269 PubMed:32926474 ↗
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
Evidence & references
- ECO:0000269 PubMed:15282549 ↗
- ECO:0000269 PubMed:15590694 ↗
- ECO:0000269 PubMed:17334392 ↗
- ECO:0000269 PubMed:18046415 ↗
- ECO:0000269 PubMed:19836242 ↗
- ECO:0000269 PubMed:25922362 ↗
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
GO:1900087 · evidence & context
- ECO:0000315 PMID:18483258 ↗ IMP · BHF-UCL · 20241216qualifier: acts_upstream_of
GO:0007166 · evidence & context
- ECO:0000314 PMID:7736574 ↗ IDA · MGI · 20101102qualifier: acts_upstream_of_or_within
GO:0007173 · evidence & context
- ECO:0000314 PMID:7736574 ↗ IDA · MGI · 20101102qualifier: acts_upstream_of_or_within
- ECO:0000314 PMID:9890893 ↗ IDA · MGI · 20220304qualifier: acts_upstream_of_or_within
GO:0008284 · evidence & context
- ECO:0000314 PMID:7736574 ↗ IDA · MGI · 20101102qualifier: acts_upstream_of_or_within
GO:0038134 · evidence & context
- ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20220304qualifier: acts_upstream_of_or_within
All recorded function and process assertions (83)
GO:0005006 · evidence & context
- ECO:0000314 PMID:12828935 ↗ IDA · UniProt · 20231211qualifier: contributes_to
GO:0003682 · evidence & context
- ECO:0000314 PMID:20551055 ↗ IDA · UniProt · 20130828qualifier: enables
GO:0003690 · evidence & context
- ECO:0000303 PMID:6325948 ↗ NAS · UniProt · 20050809qualifier: enables
GO:0004672 · evidence & context
- ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR001245"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008266"}]}]
GO:0004709 · evidence & context
- ECO:0000303 PMID:15542601 ↗ NAS · UniProt · 20050812qualifier: enables
GO:0004713 · evidence & context
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727qualifier: enableswithFrom: [{"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 · 20050812qualifier: enables
- ECO:0000269 PMID:15374980 ↗ EXP · UniProt · 20251027qualifier: enables
- ECO:0000304 PMID:16076471 ↗ TAS · UniProt · 20050809qualifier: enables
- ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011qualifier: enables
- ECO:0000269 PMID:17349580 ↗ EXP · UniProt · 20251027qualifier: enables
- ECO:0000314 PMID:17599051 ↗ IDA · UniProt · 20100226qualifier: enables
- ECO:0000269 PMID:19560417 ↗ EXP · UniProt · 20251027qualifier: enables
- ECO:0000269 PMID:19563760 ↗ EXP · UniProt · 20251027qualifier: enables
- ECO:0000315 PMID:20878056 ↗ IMP · UniProt · 20170522qualifier: enables
- ECO:0000314 PMID:2472218 ↗ IDA · MGI · 20220118qualifier: enables
- ECO:0000314 PMID:2472218 ↗ IDA · MGI · 20220304qualifier: enables
- ECO:0000314 PMID:9890893 ↗ IDA · MGI · 20220118qualifier: enables
- ECO:0000304 Reactome:R-HSA-177934 TAS · Reactome · 20240809qualifier: enables
- ECO:0000304 Reactome:R-HSA-182969 TAS · Reactome · 20240809qualifier: enables
- ECO:0000304 Reactome:R-HSA-183058 TAS · Reactome · 20240809qualifier: enables
- ECO:0000304 Reactome:R-HSA-212710 TAS · Reactome · 20240809qualifier: enables
- ECO:0000304 Reactome:R-HSA-8867041 TAS · Reactome · 20240809qualifier: enables
GO:0004713 · evidence & context
- ECO:0000314 PMID:32926474 ↗ IDA · UniProt · 20260420qualifier: enablesextensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86WV6", "relation": "has_input"}, {"db": "GO", "id": "0141111", "relation": "part_of"}, {"db": "GO", "id": "0016242", "relation": "part_of"}]}]
GO:0004714 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529qualifier: enableswithFrom: [{"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 · 20260727qualifier: enableswithFrom: [{"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 · 20260222qualifier: enables
- ECO:0000304 Reactome:R-HSA-177933 TAS · Reactome · 20260222qualifier: enables
GO:0004888 · evidence & context
- ECO:0000314 PMID:7736574 ↗ IDA · MGI · 20101102qualifier: enables
GO:0005006 · evidence & context
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00086054"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
- ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20211214qualifier: enables
- ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20220304qualifier: enables
- ECO:0000314 PMID:12435727 ↗ IDA · UniProt · 20050812qualifier: enables
- ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011qualifier: enables
- ECO:0000314 PMID:2176151 ↗ IDA · MGI · 20220118qualifier: enables
- ECO:0000314 PMID:2176151 ↗ IDA · MGI · 20220304qualifier: enables
- ECO:0000315 PMID:22732145 ↗ IMP · ParkinsonsUK-UCL · 20161111qualifier: enables
- ECO:0000303 PMID:2790960 ↗ NAS · UniProt · 20050809qualifier: enables
- ECO:0000303 PMID:6325948 ↗ NAS · UniProt · 20050809qualifier: enables
GO:0005515 · evidence & context
- ECO:0000353 PMID:10026169 ↗ IPI · UniProt · 20111121qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43639"}]}]
- ECO:0000353 PMID:10026169 ↗ IPI · UniProt · 20111121qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16333"}]}]
- ECO:0000353 PMID:10026169 ↗ IPI · UniProt · 20111121qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:10229072 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
- ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
- ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
- ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
- ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
- ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
- ECO:0000353 PMID:10805725 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00750"}]}]
- ECO:0000353 PMID:11279102 ↗ IPI · HGNC-UCL · 20061026qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UNH7"}]}]
- ECO:0000353 PMID:11896612 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:12070153 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42224"}]}]
- ECO:0000353 PMID:12297049 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01135"}]}]
- ECO:0000353 PMID:12297050 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
- ECO:0000353 PMID:12577067 ↗ IPI · UniProt · 20090424qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:12577067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:12620237 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
- ECO:0000353 PMID:14568990 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
- ECO:0000353 PMID:14679214 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:15225635 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P63104"}]}]
- ECO:0000353 PMID:15282549 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
- ECO:0000353 PMID:15345710 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
- ECO:0000353 PMID:15590694 ↗ IPI · UniProt · 20111012qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75159"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60716"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06493"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07947"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P10599"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P11142"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27348"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31947"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P38646"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P63104"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q03135"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05397"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q71U36"}]}]
- ECO:0000353 PMID:15962011 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
- ECO:0000353 PMID:16253990 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQC2"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00213"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00459"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14654"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O95704"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00519"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16333"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16885"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20936"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42684"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P43403"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P43405"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46108"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49757"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51451"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P98077"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13239"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13387"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13882"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6PKX4"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q7Z7G1"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8IZW8"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92569"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92625"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92870"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NRF2"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NSE2"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UKG1"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQF2"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQQ2"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y490"}]}]
- ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y6R0"}]}]
- ECO:0000353 PMID:16499958 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJ41"}]}]
- ECO:0000353 PMID:16516204 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
- ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04406"}]}]
- ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07948"}]}]
- ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31947"}]}]
- ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51636"}]}]
- ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:16799092 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q03135"}]}]
- ECO:0000353 PMID:16843263 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
- ECO:0000353 PMID:16914641 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
- ECO:0000353 PMID:16954185 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15109"}]}]
- ECO:0000353 PMID:17115032 ↗ IPI · UniProt · 20111011qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12004"}]}]
- ECO:0000353 PMID:17126326 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O60603"}]}]
- ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
- ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
- ECO:0000353 PMID:17182860 ↗ IPI · UniProt · 20110301qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O54967"}]}]
- ECO:0000353 PMID:17284441 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P03372"}]}]
- ECO:0000353 PMID:17284441 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
- ECO:0000353 PMID:17334392 ↗ IPI · UniProt · 20200707qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQ49"}]}]
- ECO:0000353 PMID:17599051 ↗ IPI · UniProt · 20100226qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P05432"}]}]
- ECO:0000353 PMID:17697999 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
- ECO:0000353 PMID:17726113 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96FE5"}]}]
- ECO:0000353 PMID:17909029 ↗ IPI · UniProt · 20080602qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y2I7"}]}]
- ECO:0000353 PMID:18046415 ↗ IPI · UniProt · 20100302qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
- ECO:0000353 PMID:18046415 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
- ECO:0000353 PMID:18273061 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P22681"}]}]
- ECO:0000353 PMID:18455122 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P13866"}]}]
- ECO:0000353 PMID:18542056 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
- ECO:0000353 PMID:18602463 ↗ IPI · UniProt · 20120427qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99700"}]}]
- ECO:0000353 PMID:18722344 ↗ IPI · UniProt · 20191101qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75815"}]}]
- ECO:0000353 PMID:18776048 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
- ECO:0000353 PMID:18824549 ↗ IPI · UniProt · 20100224qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BZP6"}]}]
- ECO:0000353 PMID:18824549 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9BZP6"}]}]
- ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08575"}]}]
- ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23467"}]}]
- ECO:0000353 PMID:19172738 ↗ IPI · UniProt · 20091118qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQC2"}]}]
- ECO:0000353 PMID:19172738 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQC2"}]}]
- ECO:0000353 PMID:19509291 ↗ IPI · UniProt · 20121207qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9H706"}]}]
- ECO:0000353 PMID:19602593 ↗ IPI · UniProt · 20090916qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P60468"}]}]
- ECO:0000353 PMID:19650109 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
- ECO:0000353 PMID:19798056 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75674"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00170"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04083"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04406"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P09936"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P10599"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P17174"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23528"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27348"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31948"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P34932"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P38646"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P60520"}]}]
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- ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31947"}]}]
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- ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42684"}]}]
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- ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46109"}]}]
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- ECO:0000353 PMID:8621392 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20417"}]}]
- ECO:0000353 PMID:8887653 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:8940013 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:9020117 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
- ECO:0000353 PMID:9020117 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
- ECO:0000353 PMID:9135143 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P01133"}]}]
- ECO:0000353 PMID:9135143 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99075"}]}]
- ECO:0000353 PMID:9419975 ↗ IPI · UniProt · 20060120qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14944"}]}]
- ECO:0000353 PMID:9506989 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13322"}]}]
- ECO:0000353 PMID:9544989 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
- ECO:0000353 PMID:9852145 ↗ IPI · UniProt · 20140307qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q62384"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:14966128 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:21266349 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P97313"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:24135280 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:24780295 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07992"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:15611079 ↗ IPI · HGNC-UCL · 20240211qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q6UW88"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0007173", "relation": "part_of"}, {"db": "GO", "id": "0008284", "relation": "part_of"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:17403676 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13671"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005768", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:25594178 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86VI4"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005768", "relation": "occurs_in"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:21349850 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"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"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:23178489 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"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"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:24034250 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14457"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0031410", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14457"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0031410", "relation": "occurs_in"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:25796184 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:9050838 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:9355745 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P18031"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:24854121 ↗ IPI · ARUK-UCL · 20190920qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99962"}]}]extensions: [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "occurs_in"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:25353163 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O94898"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005886", "relation": "occurs_in"}]}]
GO:0005515 · evidence & context
- ECO:0000353 PMID:30662352 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43752"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005802", "relation": "occurs_in"}]}]
GO:0005524 · evidence & context
- ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR000719"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR017441"}]}]
GO:0016301 · evidence & context
- ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
GO:0019899 · evidence & context
- ECO:0000353 PMID:12009895 ↗ IPI · UniProt · 20110815qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O15162"}]}]
GO:0019900 · evidence & context
- ECO:0000353 PMID:18722344 ↗ IPI · UniProt · 20200619qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46108"}]}]
- ECO:0000353 PMID:22732145 ↗ IPI · ParkinsonsUK-UCL · 20241220qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P52824"}]}]
GO:0019903 · evidence & context
- ECO:0000353 PMID:15899872 ↗ IPI · UniProt · 20081218qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15262"}]}]
- ECO:0000353 PMID:28759036 ↗ IPI · BHF-UCL · 20180719qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P51452"}]}]
GO:0030296 · evidence & context
- ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20211214qualifier: enables
- ECO:0000314 PMID:2176151 ↗ IDA · MGI · 20220118qualifier: enables
GO:0031625 · evidence & context
- ECO:0000353 PMID:23418353 ↗ IPI · UniProt · 20140827qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q91YL2"}]}]
- ECO:0000353 PMID:23418353 ↗ IPI · UniProt · 20140827qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9D0C1"}]}]
GO:0042802 · evidence & context
- ECO:0000353 PMID:16777603 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:18042729 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:19563760 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:19650109 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:20007378 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:20029029 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:20359299 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:21278786 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:21480528 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:21482778 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:22232519 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:22579287 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:23273428 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:23374349 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:23436906 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:23636329 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:24135280 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:28988771 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
- ECO:0000353 PMID:38572507 ↗ IPI · IntAct · 20260725qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005938", "relation": "occurs_in"}]}]
GO:0045296 · evidence & context
- ECO:0007005 PMID:25468996 ↗ HDA · BHF-UCL · 20180328qualifier: enables
GO:0048408 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20200401qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN002814603"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}]
- ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
GO:0051015 · evidence & context
- ECO:0000314 PMID:14702346 ↗ IDA · UniProt · 20050812qualifier: enables
GO:0051117 · evidence & context
- ECO:0000250 GO_REF:0000024 ISS · ARUK-UCL · 20251229qualifier: enableswithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "F1N7F3"}]}]extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000019", "relation": "occurs_in"}, {"db": "GO", "id": "0045121", "relation": "occurs_in"}]}]
GO:0000165 · evidence & context
- ECO:0000364 GO_REF:0000108 IEA · GOC · 20260727qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "GO", "id": "0004709"}]}]
GO:0001503 · evidence & context
- ECO:0000303 PMID:12925580 ↗ NAS · UniProt · 20050811qualifier: involved_in
GO:0001934 · evidence & context
- ECO:0000314 PMID:20551055 ↗ IDA · UniProt · 20130828qualifier: involved_in
GO:0007165 · evidence & context
- ECO:0000314 PMID:10572067 ↗ IDA · UniProt · 20060227qualifier: involved_in
- ECO:0000304 Reactome:R-HSA-212718 TAS · Reactome · 20260316qualifier: involved_in
GO:0007169 · evidence & context
- ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}]
GO:0007173 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20240924qualifier: involved_inwithFrom: [{"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 · 20050812qualifier: involved_in
- ECO:0000315 PMID:17655843 ↗ IMP · BHF-UCL · 20230717qualifier: involved_in
- ECO:0000315 PMID:20878056 ↗ IMP · UniProt · 20170522qualifier: involved_in
- ECO:0000314 PMID:9890893 ↗ IDA · MGI · 20220118qualifier: involved_in
- ECO:0000304 Reactome:R-HSA-177929 TAS · Reactome · 20260316qualifier: involved_in
GO:0007173 · evidence & context
- ECO:0000314 PMID:12828935 ↗ IDA · UniProt · 20231211qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "GO", "id": "0004517", "relation": "positively_regulates"}]}]
GO:0007173 · evidence & context
- ECO:0000315 PMID:18483258 ↗ IMP · BHF-UCL · 20241216qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "GO", "id": "0070141", "relation": "part_of"}, {"db": "GO", "id": "1900087", "relation": "causally_upstream_of"}, {"db": "CL", "id": "0000312", "relation": "occurs_in"}]}]
GO:0007173 · evidence & context
- ECO:0000314 PMID:24854121 ↗ IDA · ARUK-UCL · 20241213qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "occurs_in"}]}]
GO:0007611 · evidence & context
- ECO:0000250 GO_REF:0000024 ISS · UniProt · 20131108qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "G3V6K6"}]}]
GO:0008284 · evidence & context
- ECO:0000315 PMID:27057632 ↗ IMP · BHF-UCL · 20160517qualifier: involved_in
GO:0016242 · evidence & context
- ECO:0000314 PMID:32926474 ↗ IDA · UniProt · 20260420qualifier: involved_in
GO:0030182 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904qualifier: involved_inwithFrom: [{"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"}]}]
GO:0030307 · evidence & context
- ECO:0000314 PMID:15467833 ↗ IDA · UniProt · 20160401qualifier: involved_in
GO:0030335 · evidence & context
- ECO:0000315 PMID:12435727 ↗ IMP · UniProt · 20050812qualifier: involved_in
- ECO:0000315 PMID:25678558 ↗ IMP · UniProt · 20170831qualifier: involved_in
GO:0033138 · evidence & context
- ECO:0000315 PMID:20878056 ↗ IMP · UniProt · 20170522qualifier: involved_in
GO:0034165 · evidence & context
- ECO:0000314 PMID:40980882 ↗ IDA · UniProt · 20251124qualifier: involved_in
GO:0038134 · evidence & context
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00087731"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
- ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20211214qualifier: involved_in
GO:0042059 · evidence & context
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00086227"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
- ECO:0000304 Reactome:R-HSA-182971 TAS · Reactome · 20260316qualifier: involved_in
GO:0042177 · evidence & context
- ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011qualifier: involved_in
GO:0042327 · evidence & context
- ECO:0000314 PMID:15082764 ↗ IDA · UniProt · 20050811qualifier: involved_in
GO:0043066 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904qualifier: involved_inwithFrom: [{"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 · 20110318qualifier: involved_in
GO:0043410 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904qualifier: involved_inwithFrom: [{"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"}]}]
GO:0043410 · evidence & context
- ECO:0000314 PMID:24854121 ↗ IDA · ARUK-UCL · 20241213qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "occurs_in"}, {"db": "GO", "id": "0007173", "relation": "part_of"}]}]
GO:0043491 · evidence & context
- ECO:0000315 PMID:18483258 ↗ IMP · BHF-UCL · 20241216qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "GO", "id": "0070141", "relation": "part_of"}, {"db": "GO", "id": "1900087", "relation": "causally_upstream_of"}, {"db": "CL", "id": "0000312", "relation": "occurs_in"}]}]
GO:0045739 · evidence & context
- ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011qualifier: involved_in
GO:0045740 · evidence & context
- ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011qualifier: involved_in
GO:0045944 · evidence & context
- ECO:0000314 PMID:20551055 ↗ IDA · UniProt · 20130828qualifier: involved_in
GO:0048146 · evidence & context
- ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
GO:0050679 · evidence & context
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20240924qualifier: involved_inwithFrom: [{"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 · 20260727qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00089519"}]}]
- ECO:0000314 PMID:10572067 ↗ IDA · UniProt · 20060227qualifier: involved_in
GO:0050730 · evidence & context
- ECO:0000315 PMID:12435727 ↗ IMP · UniProt · 20050812qualifier: involved_in
GO:0051205 · evidence & context
- ECO:0000304 PMID:12435727 ↗ TAS · UniProt · 20050812qualifier: involved_in
GO:0051897 · evidence & context
- ECO:0000315 PMID:17655843 ↗ IMP · BHF-UCL · 20230717qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "GO", "id": "0007173", "relation": "part_of"}]}]
GO:0070141 · evidence & context
- ECO:0000314 PMID:18483258 ↗ IDA · BHF-UCL · 20081126qualifier: involved_in
GO:0070374 · evidence & context
- ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00085202"}]}]
- ECO:0000314 PMID:20551055 ↗ IDA · UniProt · 20130828qualifier: involved_in
- ECO:0000315 PMID:21673316 ↗ IMP · BHF-UCL · 20160504qualifier: involved_in
GO:0071230 · evidence & context
- ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
GO:0071364 · evidence & context
- ECO:0000250 GO_REF:0000024 ISS · UniProt · 20131108qualifier: involved_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "G3V6K6"}]}]
GO:0071392 · evidence & context
- ECO:0000314 PMID:20551055 ↗ IDA · UniProt · 20130828qualifier: involved_in
GO:0090037 · evidence & context
- ECO:0000314 PMID:22732145 ↗ IDA · ParkinsonsUK-UCL · 20241220qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "GO", "id": "0072659", "relation": "positively_regulates"}, {"db": "GO", "id": "0007173", "relation": "part_of"}]}]
GO:0090263 · evidence & context
- ECO:0000315 PMID:20302655 ↗ IMP · BHF-UCL · 20100721qualifier: involved_in
GO:0098609 · evidence & context
- ECO:0000315 PMID:12435727 ↗ IMP · UniProt · 20050812qualifier: involved_in
GO:0141111 · evidence & context
- ECO:0000314 PMID:32926474 ↗ IDA · UniProt · 20260420qualifier: involved_in
GO:1902895 · evidence & context
- ECO:0000315 PMID:21673316 ↗ IMP · BHF-UCL · 20220905qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "RNAcentral", "id": "URS0000245997_9606", "relation": "has_input"}]}, {"connectedXrefs": [{"db": "RNAcentral", "id": "URS000077BBBB_9606", "relation": "has_input"}]}]
GO:1903078 · evidence & context
- ECO:0000314 PMID:22732145 ↗ IDA · ParkinsonsUK-UCL · 20161110qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P52824", "relation": "has_input"}]}]
GO:1905208 · evidence & context
- ECO:0000315 PMID:23069713 ↗ IMP · BHF-UCL · 20160929qualifier: involved_inextensions: [{"connectedXrefs": [{"db": "CL", "id": "0000134", "relation": "occurs_in"}]}]
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"
}
]
}
]
}Subcellular Location
UniProt locations and GO cellular-component assertions. Relations and contexts remain distinct; “part of” is not automatically a residence claim.
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]
Evidence & references
- ECO:0000269 PubMed:17182860 ↗
- ECO:0000269 PubMed:20462955 ↗
- ECO:0000269 PubMed:23589287 ↗
- ECO:0000269 PubMed:26918609 ↗
- ECO:0000269 PubMed:27153536 ↗
- ECO:0000269 PubMed:2790960 ↗
- ECO:0000269 PubMed:35538033 ↗
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]
Evidence & references
- ECO:0000269 PubMed:27153536 ↗
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]
Evidence & references
No separate evidence record is supplied for this statement.
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]
Evidence & references
No separate evidence record is supplied for this statement.
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]
Evidence & references
- ECO:0000269 PubMed:17182860 ↗
- ECO:0000269 PubMed:27153536 ↗
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]
Evidence & references
No separate evidence record is supplied for this statement.
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]
Evidence & references
- ECO:0000269 PubMed:17115032 ↗
- ECO:0000269 PubMed:17909029 ↗
- ECO:0000269 PubMed:20551055 ↗
- ECO:0000269 PubMed:20674546 ↗
Isoform 2
Evidence & references
No separate evidence record is supplied for this statement.
All recorded location assertions (40)
Evidence & references
- ECO:0000314 PMID:16554368 ↗ IDA · ParkinsonsUK-UCL · 20160801qualifier: colocalizes_with
Evidence & references
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529qualifier: is_active_inwithFrom: [{"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 · 20210224qualifier: is_active_in
- ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20211214qualifier: is_active_in
- ECO:0000314 PMID:15611079 ↗ IDA · MGI · 20220309qualifier: is_active_in
Evidence & references
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20210227qualifier: is_active_inwithFrom: [{"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"}]}]
Evidence & references
- ECO:0000314 PMID:40980882 ↗ IDA · UniProt · 20251124qualifier: is_active_in
Evidence & references
- ECO:0000314 PMID:11331309 ↗ IDA · ARUK-UCL · 20210224qualifier: is_active_in
Evidence & references
- ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0134"}]}]
Evidence & references
- ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0243"}]}]
- ECO:0000303 PMID:9103388 ↗ NAS · UniProt · 20050811qualifier: located_in
Evidence & references
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"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 · 20050812qualifier: located_in
- ECO:0000314 PMID:17115032 ↗ IDA · UniProt · 20111011qualifier: located_in
- ECO:0000269 PMID:17909029 ↗ EXP · UniProt · 20251027qualifier: located_in
- ECO:0000314 PMID:20551055 ↗ IDA · UniProt · 20130828qualifier: located_in
- ECO:0000269 PMID:20674546 ↗ EXP · UniProt · 20251027qualifier: located_in
Evidence & references
- ECO:0000314 PMID:12435727 ↗ IDA · UniProt · 20050812qualifier: located_in
- ECO:0000314 PMID:22298428 ↗ IDA · UniProt · 20181116qualifier: located_in
- ECO:0000314 PMID:7588596 ↗ IDA · UniProt · 20091203qualifier: located_in
Evidence & references
- ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0101"}]}]
- ECO:0000314 PMID:14702346 ↗ IDA · UniProt · 20050812qualifier: located_in
- ECO:0000314 PMID:17182860 ↗ IDA · UniProt · 20110301qualifier: located_in
- ECO:0000314 PMID:22732145 ↗ IDA · ParkinsonsUK-UCL · 20241220qualifier: located_in
- ECO:0000269 PMID:27153536 ↗ EXP · UniProt · 20251027qualifier: located_in
Evidence & references
- ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0097"}]}]
- ECO:0000269 PMID:27153536 ↗ EXP · UniProt · 20251027qualifier: located_in
Evidence & references
- ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115qualifier: located_in
Evidence & references
- ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115qualifier: located_in
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0039"}]}]
- ECO:0000314 PMID:11336639 ↗ IDA · MGI · 20220304qualifier: located_in
- ECO:0000314 PMID:15465819 ↗ IDA · HGNC-UCL · 20050704qualifier: located_in
- ECO:0000314 PMID:15611079 ↗ IDA · MGI · 20220309qualifier: located_in
- ECO:0000269 PMID:17182860 ↗ EXP · UniProt · 20251027qualifier: located_in
- ECO:0000314 PMID:20462955 ↗ IDA · UniProt · 20191114qualifier: located_in
- ECO:0000314 PMID:22298428 ↗ IDA · UniProt · 20181116qualifier: located_in
- ECO:0000314 PMID:22732145 ↗ IDA · ParkinsonsUK-UCL · 20161109qualifier: located_in
- ECO:0000269 PMID:23589287 ↗ EXP · UniProt · 20251027qualifier: located_in
- ECO:0000314 PMID:26918609 ↗ IDA · UniProt · 20251218qualifier: located_in
- ECO:0000269 PMID:27153536 ↗ EXP · UniProt · 20251027qualifier: located_in
- ECO:0000269 PMID:2790960 ↗ EXP · UniProt · 20251027qualifier: located_in
- ECO:0000269 PMID:35538033 ↗ EXP · UniProt · 20251027qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1169421 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1218833 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1220610 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1220611 TAS · Reactome · 20181029qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1220612 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1220613 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1220614 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225947 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225949 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225950 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225951 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225952 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225956 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225957 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225960 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225961 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1225978 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1226012 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1226014 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1226016 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1247841 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1247842 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1247844 TAS · Reactome · 20181108qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1247999 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1248002 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1248655 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1248677 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1250195 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1306957 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1306963 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1306965 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177922 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177923 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177924 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177925 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177926 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177927 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177930 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177933 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177934 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177935 TAS · Reactome · 20230122qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177936 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177937 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177938 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177939 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177941 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177942 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177943 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177944 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-177945 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-182969 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-182986 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-182990 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-182993 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-182994 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183002 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183036 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183051 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183055 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183058 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183067 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183072 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183084 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-183089 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1963563 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1963581 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1963582 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1963586 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1963589 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-1977959 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-212706 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-212710 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-212713 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-2179387 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-2179407 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-2179415 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-2316434 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-2400009 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-445069 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637764 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637765 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637766 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637770 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637792 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637794 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637795 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637796 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637798 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637800 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637801 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637806 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5637808 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5638137 TAS · Reactome · 20130606qualifier: located_in
- ECO:0000304 Reactome:R-HSA-5672965 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-6785636 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-6785648 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8847995 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8848005 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8857549 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8857555 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8857565 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8857577 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8857583 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8863804 TAS · Reactome · 20230122qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8864029 TAS · Reactome · 20230122qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8864105 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8864125 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8866279 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8867041 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8867044 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8867047 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8867754 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8867756 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868071 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868072 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868230 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868236 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868648 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868651 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868661 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8874797 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8951490 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9018572 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9018573 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9609689 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9610867 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9611147 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9611158 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9625482 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9625487 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9634702 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664567 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664588 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664918 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664933 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664940 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664950 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664976 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664983 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9664991 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665000 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665009 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665032 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665034 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665388 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665389 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665404 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665406 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665407 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665408 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665409 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665410 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665411 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665413 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665415 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665416 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665417 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665697 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665698 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665699 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665700 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665701 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665704 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665705 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665706 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665707 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9665709 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9674531 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9851407 TAS · Reactome · 20060509qualifier: located_in
- ECO:0000304 Reactome:R-NUL-1248744 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-NUL-1251923 TAS · Reactome · 20130516qualifier: located_in
- ECO:0000304 Reactome:R-NUL-1251929 TAS · Reactome · 20130516qualifier: located_in
UniProtKB:P00533 · [{"connectedXrefs": [{"db": "CL", "id": "0000057", "relation": "part_of"}]}]
Evidence & references
- ECO:0007005 PMID:21423176 ↗ HDA · UniProt · 20140715qualifier: located_inextensions: [{"connectedXrefs": [{"db": "CL", "id": "0000057", "relation": "part_of"}]}]
Evidence & references
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027349"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
- ECO:0000314 PMID:25666625 ↗ IDA · UniProt · 20150420qualifier: located_in
Evidence & references
- ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0100"}]}]
- ECO:0000314 PMID:22719997 ↗ IDA · UniProt · 20140723qualifier: located_in
- ECO:0000304 Reactome:R-HSA-9611147 TAS · Reactome · 20180615qualifier: located_in
Evidence & references
- ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}]
- ECO:0000314 PMID:12435727 ↗ IDA · UniProt · 20050812qualifier: located_in
Evidence & references
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00086715"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
- ECO:0000314 PMID:12646923 ↗ IDA · BHF-UCL · 20080227qualifier: located_in
Evidence & references
- ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115qualifier: located_in
Evidence & references
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027489"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
Evidence & references
- ECO:0000304 Reactome:R-HSA-8868658 TAS · Reactome · 20190206qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868659 TAS · Reactome · 20190206qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868660 TAS · Reactome · 20190206qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8868661 TAS · Reactome · 20190206qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8869438 TAS · Reactome · 20190206qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8871193 TAS · Reactome · 20190206qualifier: located_in
- ECO:0000304 Reactome:R-HSA-8871194 TAS · Reactome · 20190206qualifier: located_in
Evidence & references
- ECO:0000314 PMID:17714434 ↗ IDA · UniProt · 20150227qualifier: located_in
Evidence & references
- ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0182"}]}]
UniProtKB:P00533 · [{"connectedXrefs": [{"db": "CL", "id": "0000019", "relation": "part_of"}]}]
Evidence & references
- ECO:0000250 GO_REF:0000024 ISS · ARUK-UCL · 20190919qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "F1N7F3"}]}]extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000019", "relation": "part_of"}]}]
Evidence & references
- ECO:0000314 PMID:12009895 ↗ IDA · UniProt · 20110815qualifier: located_in
Evidence & references
- ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260724qualifier: located_inwithFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00091589"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01279"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000020329"}]}]
UniProtKB:P00533 · [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "part_of"}]}]
Evidence & references
- ECO:0000315 PMID:24854121 ↗ IMP · ARUK-UCL · 20190920qualifier: located_inextensions: [{"connectedXrefs": [{"db": "CL", "id": "2000044", "relation": "part_of"}]}]
Evidence & references
- ECO:0000314 PMID:17714434 ↗ IDA · UniProt · 20150227qualifier: located_in
Evidence & references
- ECO:0000314 PMID:11331309 ↗ IDA · ARUK-UCL · 20210224qualifier: located_in
Evidence & references
- ECO:0000314 PMID:20878056 ↗ IDA · UniProt · 20170522qualifier: part_of
Evidence & references
- ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529qualifier: part_ofwithFrom: [{"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 · 20131224qualifier: part_of
Evidence & references
- ECO:0000250 GO_REF:0000024 ISS · BHF-UCL · 20090415qualifier: part_ofwithFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9QX70"}]}]
Membrane topology 3
Scroll across the table for evidence and actions.
3 recorded rows
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Topological domain | 25–645 | Extracellular | Sequence analysis Evidence & references
| No verified residues in this structure |
| Transmembrane | 646–668 | Helical | Sequence analysis Evidence & references
| No verified residues in this structure |
| Topological domain | 669–1210 | Cytoplasmic | Sequence analysis Evidence & references
| No verified residues in this structure |
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.
Evidence & references
- ECO:0000269 PubMed:15118125 ↗
- ECO:0000269 PubMed:16533793 ↗
- ECO:0000269 PubMed:16672372 ↗
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.
Evidence & references
- ECO:0000269 PubMed:24691054 ↗
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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Natural variantVAR_066493 | 30–297 | variant 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_019293 | 98 | in dbSNP:rs17289589 R → Q | Experimental evidence Evidence & references
| No verified residues in this structure |
| P266RVAR_019294 | 266 | in dbSNP:rs17336639 P → R | Experimental evidence Evidence & references
| No verified residues in this structure |
| G428DVAR_072435 | 428 | in 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_019295 | 521 | in dbSNP:rs2227983 R → K | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| V674IVAR_019296 | 674 | in dbSNP:rs17337079 V → I | Experimental evidence Evidence & references
| No verified residues in this structure |
| E709AVAR_026084 | 709 | found 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_069498 | 709 | found 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_026085 | 709 | found in a lung cancer sample; dbSNP:rs727504256 E → K | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| G719AVAR_026086 | 719 | found in a lung cancer sample; dbSNP:rs121913428 G → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| G719CVAR_026087 | 719 | found in a lung cancer sample; dbSNP:rs28929495 G → C | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| G719DVAR_026088 | 719 | found in a lung cancer sample; dbSNP:rs121913428 G → D | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| G719SVAR_019297 | 719 | found 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_026089 | 724 | found in a lung cancer sample; dbSNP:rs1051753269 G → S | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| E734KVAR_026090 | 734 | found in a lung cancer sample; dbSNP:rs121913420 E → K | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| ELREATS746DVAR_069499 | 746–752 | found in a lung cancer sample ELREATS → D | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| ELREAT746AVAR_069500 | 746–751 | found in a lung cancer sample ELREAT → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Natural variantVAR_026092 | 746–750 | found in a lung cancer sample | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Natural variantVAR_026091 | 746 | found in a lung cancer sample | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Natural variantVAR_069501 | 747–751 | found in a lung cancer sample | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Natural variantVAR_026094 | 747–749 | found in a lung cancer sample | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| L747FVAR_026093 | 747 | found in a lung cancer sample; dbSNP:rs2128954811 L → F | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| R748PVAR_026095 | 748 | found in a lung cancer sample R → P | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Natural variantVAR_026096 | 752–759 | found in a lung cancer sample | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| S768IVAR_069502 | 768 | found 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_069503 | 769 | found in a lung cancer sample; dbSNP:rs147149347 V → M | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Q787RVAR_026097 | 787 | found in a lung cancer sample Q → R | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| T790MVAR_026098 | 790 | found 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_026099 | 833 | found 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_026100 | 834 | found in a lung cancer sample; dbSNP:rs397517127 V → L | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| H835LVAR_069504 | 835 | found 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_069505 | 838 | found 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_026101 | 858 | found in a lung cancer sample; dbSNP:rs121913443 L → M | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| L858RVAR_019298 | 858 | found 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_026102 | 861 | found 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_026103 | 873 | found in a lung cancer sample; dbSNP:rs2128964711 G → E | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| R962GVAR_019299 | 962 | in dbSNP:rs17337451 R → G | Experimental evidence Evidence & references
| No verified residues in this structure |
| H988PVAR_019300 | 988 | in dbSNP:rs17290699 H → P | Experimental evidence Evidence & references
| No verified residues in this structure |
| L1034RVAR_042095 | 1034 | in dbSNP:rs34352568 L → R | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| A1210VVAR_042096 | 1210 | in 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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Y275A | 275 | Strongly 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 |
| F287A | 287 | Strongly 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 |
| R309S | 309 | Strongly 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 |
| R429E | 429 | Abolishes autophosphorylation and activation of downstream kinases. R → E | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Mutagenesis | 525–1210 | Increased EGF binding. | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| DGPH587AGPA | 587–590 | Decreases intramolecular interactions and facilitates EGF binding. DGPH → AGPA | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| D587A | 587 | Increased EGF binding; when associated with A-590 and A-609. D → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| H590A | 590 | Increased 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 |
| K609A | 609 | Decreases 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 |
| L688A | 688 | Strongly reduced phosphorylation. L → A | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| V689A | 689 | Reduced autophosphorylation. V → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| V689M | 689 | Constitutively activated kinase. V → M | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| E690A | 690 | Reduced phosphorylation. E → A | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| L692A / L692P | 692 | Strongly reduced phosphorylation. L → A, P | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| T693A | 693 | Increased phosphorylation. T → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| T693D | 693 | Strongly reduced phosphorylation. T → D | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| P694A | 694 | Strongly reduced phosphorylation. P → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| P699A | 699 | Reduced phosphorylation. P → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| N700A | 700 | Abolishes phosphorylation. N → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| L704A | 704 | Abolishes phosphorylation. L → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| R705A | 705 | Abolishes phosphorylation. R → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| I706A | 706 | Abolishes phosphorylation. I → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| K745A / K745M | 745 | Abolishes kinase activity. K → A, M | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| D974A | 974 | Strongly reduced phosphorylation. D → A | Evidence & referencesNo separate evidence record is supplied for this statement. | No verified residues in this structure |
| R977A | 977 | Reduced phosphorylation. R → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| ED1005RK | 1005–1006 | Constitutively activated kinase. ED → RK | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Y1016F | 1016 | 50% 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 |
| Mutagenesis | 1048–1210 | Abolishes palmitoylation. | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| C1049A | 1049 | Decreased palmitoylation. C → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Q1067G | 1067 | No effect on interaction with CBLC. Q → G | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| R1068G | 1068 | Strongly decreases interaction with CBLC. R → G | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Y1069F | 1069 | Abolishes interaction with CBLC. Y → F | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Y1092F | 1092 | No 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 |
| Y1110F | 1110 | No change in interaction with PIK3C2B. Y → F | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| C1146A | 1146 | Decreased palmitoylation. C → A | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Y1172F | 1172 | No change in interaction with PIK3C2B. Y → F | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Y1197F | 1197 | No 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 |
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
Evidence & references
- ECO:0000269 PubMed:10523301 ↗
- ECO:0000269 PubMed:12873986 ↗
- ECO:0000269 PubMed:16083266 ↗
- ECO:0000269 PubMed:19563760 ↗
- ECO:0000269 PubMed:19836242 ↗
- ECO:0000269 PubMed:20462955 ↗
- ECO:0000269 PubMed:21258366 ↗
- ECO:0000269 PubMed:2543678 ↗
- ECO:0000269 PubMed:27153536 ↗
- ECO:0000269 PubMed:3138233 ↗
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)
Evidence & references
- ECO:0000250 UniProtKB:Q01279
- ECO:0000269 PubMed:16543144 ↗
- ECO:0000269 PubMed:22179831 ↗
- ECO:0000269 PubMed:22298428 ↗
- ECO:0000269 PubMed:27153536 ↗
- ECO:0000269 PubMed:33996800 ↗
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
Evidence & references
- ECO:0000269 PubMed:27153536 ↗
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]
Evidence & references
- ECO:0000269 PubMed:28891468 ↗
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
Evidence & references
- ECO:0000269 PubMed:19563760 ↗
- ECO:0000269 PubMed:19836242 ↗
- ECO:0000269 PubMed:21258366 ↗
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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Signal | 1–24 | Signal | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| ChainPRO_0000016665 | 25–1210 | Epidermal growth factor receptor | Evidence & referencesNo 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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Modified residue | 229 | Phosphoserine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 678 | Phosphothreonine; by PKC and PKD/PRKD1 | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 693 | Phosphothreonine; by PKD/PRKD1 | Experimental evidence 7 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 695 | Phosphoserine | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 745 | N6-(2-hydroxyisobutyryl)lysine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 869 | Phosphotyrosine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 991 | Phosphoserine | Experimental evidence 4 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 995 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 998 | Phosphotyrosine; by autocatalysis | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1016 | Phosphotyrosine; by autocatalysis | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1026 | Phosphoserine | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1039 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 1041 | Phosphothreonine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 1042 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 1064 | Phosphoserine | 4 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1069 | Phosphotyrosine | Experimental evidenceCurator inference 2 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1070 | Phosphoserine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 1071 | Phosphoserine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 1081 | Phosphoserine | 1 publication Evidence & references
| No verified residues in this structure |
| Modified residue | 1092 | Phosphotyrosine; by autocatalysis | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1110 | Phosphotyrosine; by autocatalysis | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1166 | Phosphoserine | 3 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1172 | Phosphotyrosine; by autocatalysis | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1197 | Phosphotyrosine; by autocatalysis | Experimental evidence 7 publications Evidence & references
| No verified residues in this structure |
| Modified residue | 1199 | Omega-N-methylarginine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Lipidation | 1049 | S-palmitoyl cysteine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Lipidation | 1146 | S-palmitoyl cysteine | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| GlycosylationCAR_000227 | 56 | N-linked (GlcNAc...) (complex) asparagine; atypical; partial | Experimental evidence 6 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 73 | N-linked (GlcNAc...) asparagine; atypical | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Glycosylation | 128 | N-linked (GlcNAc...) asparagine | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 175 | N-linked (GlcNAc...) asparagine | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 196 | N-linked (GlcNAc...) asparagine | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 352 | N-linked (GlcNAc...) asparagine | Experimental evidence 8 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 361 | N-linked (GlcNAc...) asparagine | Experimental evidence 6 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 413 | N-linked (GlcNAc...) asparagine | Experimental evidence 4 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 444 | N-linked (GlcNAc...) asparagine | Experimental evidence 6 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 528 | N-linked (GlcNAc...) asparagine | Experimental evidence 6 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 568 | N-linked (GlcNAc...) asparagine; partial | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 603 | N-linked (GlcNAc...) asparagine; partial | Experimental evidence 4 publications Evidence & references
| No verified residues in this structure |
| Glycosylation | 623 | N-linked (GlcNAc...) (high mannose) asparagine | Curator inference 1 publication Evidence & references
| No verified residues in this structure |
| Disulfide bond | 31, 58 | Disulfide bond | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 157, 187 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 190, 199 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 194, 207 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 215, 223 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 219, 231 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 232, 240 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 236, 248 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 251, 260 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 264, 291 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 295, 307 | Disulfide bond | Evidence & references
| No verified residues in this structure |
| Disulfide bond | 311, 326 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 329, 333 | Disulfide bond | Evidence & references
| No verified residues in this structure |
| Disulfide bond | 337, 362 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 470, 499 | Disulfide bond | Evidence & references
| No verified residues in this structure |
| Disulfide bond | 506, 515 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 510, 523 | Disulfide bond | Experimental evidence 5 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 526, 535 | Disulfide bond | Experimental evidence 4 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 539, 555 | Disulfide bond | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 558, 571 | Disulfide bond | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 562, 579 | Disulfide bond | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 582, 591 | Disulfide bond | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 595, 617 | Disulfide bond | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 620, 628 | Disulfide bond | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Disulfide bond | 624, 636 | Disulfide bond | Experimental evidence 3 publications Evidence & references
| No verified residues in this structure |
| Cross-link | 716 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Cross-link | 737 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Cross-link | 754 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Cross-link | 757 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Cross-link | 867 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Cross-link | 929 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Cross-link | 960 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Cross-link | 970 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
Expression
Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers
Evidence & references
- ECO:0000269 PubMed:17671655 ↗
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"
}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.
| Partner / product | Species | Experiments | Evidence & actions |
|---|---|---|---|
| ABL1P00519With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P00519. Reported experiment count: 3. |
| ABL2P42684With P00533 | Homo sapiens | 9 | IntAct evidenceSource product: P00533. Partner: P42684. Reported experiment count: 9. |
| AGERQ15109With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q15109. Reported experiment count: 2. |
| AGO2Q9UKV8With P00533 | Homo sapiens | 11 | IntAct evidenceSource product: P00533. Partner: Q9UKV8. Reported experiment count: 11. |
| AHNAKQ09666With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q09666. Reported experiment count: 4. |
| AIPO00170With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: O00170. Reported experiment count: 2. |
| AKAP12Q02952With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q02952. Reported experiment count: 3. |
| AKT1P31749With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P31749. Reported experiment count: 4. |
| AMPHP49418With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: P49418. Reported experiment count: 2. |
| ANKS1AQ92625With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: Q92625. Reported experiment count: 7. |
| ANXA1P04083With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P04083. Reported experiment count: 3. |
| ANXA2P07355With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P07355. Reported experiment count: 4. |
| AP1B1Q10567With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q10567. Reported experiment count: 4. |
| AP2M1Q96CW1With P00533 | Homo sapiens | 8 | IntAct evidenceSource product: P00533. Partner: Q96CW1. Reported experiment count: 8. |
| APBB1O00213With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: O00213. Reported experiment count: 4. |
| APBB2Q92870With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: Q92870. Reported experiment count: 7. |
| APBB3O95704With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: O95704. Reported experiment count: 2. |
| APPL1Q9UKG1With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9UKG1. Reported experiment count: 3. |
| ARRB1P49407With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P49407. Reported experiment count: 3. |
| ARRB2P32121With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P32121. Reported experiment count: 3. |
| AURKAO14965With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: O14965. Reported experiment count: 5. |
| AXLP30530With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: P30530. Reported experiment count: 5. |
| BAIAP2Q9UQB8With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q9UQB8. Reported experiment count: 4. |
| BBC3Q9BXH1With P00533 | Homo sapiens | 10 | IntAct evidenceSource product: P00533. Partner: Q9BXH1. Reported experiment count: 10. |
| BECN1Q14457With P00533 | Homo sapiens | 8 | IntAct evidenceSource product: P00533. Partner: Q14457. Reported experiment count: 8. |
| BLKP51451With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P51451. Reported experiment count: 3. |
| CALM3P62158With P00533 | Species not verified | 6 | IntAct evidenceSource product: P00533. Partner: P62158. Reported experiment count: 6. |
| CAMLGP49069With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P49069. Reported experiment count: 3. |
| CAV1Q03135With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: Q03135. Reported experiment count: 7. |
| CAV2P51636With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P51636. Reported experiment count: 3. |
| CBLP22681With P00533 | Homo sapiens | 22 | IntAct evidenceSource product: P00533. Partner: P22681. Reported experiment count: 22. |
| CDC37Q16543With P00533 | Homo sapiens | 13 | IntAct evidenceSource product: P00533. Partner: Q16543. Reported experiment count: 13. |
| CDH1P12830With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P12830. Reported experiment count: 4. |
| CDK1P06493With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P06493. Reported experiment count: 3. |
| CFL1P23528With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P23528. Reported experiment count: 3. |
| CHIAQ9BZP6With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q9BZP6. Reported experiment count: 2. |
| CISHQ9NSE2With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q9NSE2. Reported experiment count: 4. |
| CLNKQ7Z7G1With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q7Z7G1. Reported experiment count: 2. |
| CNKSR2Q8WXI2With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q8WXI2. Reported experiment count: 2. |
| CRKP46108With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P46108. Reported experiment count: 4. |
| CRKP46108-1With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P46108-1. Reported experiment count: 3. |
| CRKLP46109With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P46109. Reported experiment count: 4. |
| CTNND1O60716With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: O60716. Reported experiment count: 5. |
| CTTNQ14247With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q14247. Reported experiment count: 4. |
| DOK3Q7L591With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q7L591. Reported experiment count: 2. |
| DOK6Q6PKX4With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q6PKX4. Reported experiment count: 2. |
| EGFP01133With P00533 | Homo sapiens | 29 | IntAct evidenceSource product: P00533. Partner: P01133. Reported experiment count: 29. |
| EGFRP00533With P00533 | Homo sapiens | 31 | IntAct evidenceSource product: P00533. Partner: P00533. Reported experiment count: 31. |
| EPGNQ6UW88With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q6UW88. Reported experiment count: 3. |
| EPS8Q12929With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q12929. Reported experiment count: 4. |
| ERBB2P04626With P00533 | Homo sapiens | 25 | IntAct evidenceSource product: P00533. Partner: P04626. Reported experiment count: 25. |
| ERBB3P21860With P00533 | Homo sapiens | 15 | IntAct evidenceSource product: P00533. Partner: P21860. Reported experiment count: 15. |
| ERBB4Q15303With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q15303. Reported experiment count: 4. |
| ERCC1P07992With P00533 | Homo sapiens | 21 | IntAct evidenceSource product: P00533. Partner: P07992. Reported experiment count: 21. |
| EREGO14944With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: O14944. Reported experiment count: 3. |
| ERRFI1Q9UJM3With P00533 | Homo sapiens | 16 | IntAct evidenceSource product: P00533. Partner: Q9UJM3. Reported experiment count: 16. |
| ESR1P03372With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P03372. Reported experiment count: 3. |
| ESR1P03372-4With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P03372-4. Reported experiment count: 4. |
| ESR2Q92731With P00533 | Homo sapiens | 8 | IntAct evidenceSource product: P00533. Partner: Q92731. Reported experiment count: 8. |
| EXOC4Q96A65With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q96A65. Reported experiment count: 2. |
| EZRP15311With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P15311. Reported experiment count: 3. |
| FANCD2Q9BXW9With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9BXW9. Reported experiment count: 3. |
| FGRP09769With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P09769. Reported experiment count: 3. |
| FKBP5Q13451With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q13451. Reported experiment count: 2. |
| FKBP8Q14318With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q14318. Reported experiment count: 4. |
| GAB1Q13480With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: Q13480. Reported experiment count: 5. |
| GAB2Q9UQC2With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9UQC2. Reported experiment count: 3. |
| GABARAPL2P60520With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P60520. Reported experiment count: 3. |
| GABRA2P47869With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: P47869. Reported experiment count: 2. |
| GAPDHP04406With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: P04406. Reported experiment count: 7. |
| GOLM1Q8NBJ4With P00533 | Homo sapiens | 13 | IntAct evidenceSource product: P00533. Partner: Q8NBJ4. Reported experiment count: 13. |
| GOT1P17174With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P17174. Reported experiment count: 3. |
| GPNMBQ14956With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q14956. Reported experiment count: 3. |
| GPNMBQ14956-1With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q14956-1. Reported experiment count: 2. |
| GRAP2O75791With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: O75791. Reported experiment count: 3. |
| GRB10Q13322With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q13322. Reported experiment count: 3. |
| GRB2P62993With P00533 | Homo sapiens | 48 | IntAct evidenceSource product: P00533. Partner: P62993. Reported experiment count: 48. |
| HBEGFQ99075With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q99075. Reported experiment count: 3. |
| HCKP08631With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P08631. Reported experiment count: 3. |
| HDAC6Q9UBN7With P00533 | Homo sapiens | 12 | IntAct evidenceSource product: P00533. Partner: Q9UBN7. Reported experiment count: 12. |
| HDAC7Q8WUI4With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q8WUI4. Reported experiment count: 3. |
| HSP90AA1P07900With P00533 | Homo sapiens | 8 | IntAct evidenceSource product: P00533. Partner: P07900. Reported experiment count: 8. |
| HSP90AB1P08238With P00533 | Homo sapiens | 10 | IntAct evidenceSource product: P00533. Partner: P08238. Reported experiment count: 10. |
| HSP90AB1Q6PK50With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q6PK50. Reported experiment count: 2. |
| HSPA1BP08107With P00533 | Species not verified | 6 | IntAct evidenceSource product: P00533. Partner: P08107. Reported experiment count: 6. |
| HSPA4P34932With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P34932. Reported experiment count: 3. |
| HSPA8P11142With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: P11142. Reported experiment count: 7. |
| HSPA9P38646With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: P38646. Reported experiment count: 5. |
| IGFBP3P17936With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P17936. Reported experiment count: 3. |
| IQGAP1P46940With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P46940. Reported experiment count: 4. |
| IRS4O14654With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: O14654. Reported experiment count: 2. |
| ITSN2Q9NZM3With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9NZM3. Reported experiment count: 3. |
| JUPP14923With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P14923. Reported experiment count: 3. |
| LAPTM4BQ86VI4With P00533 | Homo sapiens | 10 | IntAct evidenceSource product: P00533. Partner: Q86VI4. Reported experiment count: 10. |
| LATO43561With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: O43561. Reported experiment count: 3. |
| LCP2Q13094With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q13094. Reported experiment count: 3. |
| LINGO1Q96FE5With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q96FE5. Reported experiment count: 2. |
| LRIG1Q96JA1With P00533 | Homo sapiens | 6 | IntAct evidenceSource product: P00533. Partner: Q96JA1. Reported experiment count: 6. |
| LRIG2O94898With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: O94898. Reported experiment count: 4. |
| LRRK1Q38SD2With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q38SD2. Reported experiment count: 2. |
| LYNP07948With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: P07948. Reported experiment count: 7. |
| LYNP07948-1With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: P07948-1. Reported experiment count: 2. |
| LZTS2Q9BRK4With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q9BRK4. Reported experiment count: 2. |
| MAP3K12Q12852With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q12852. Reported experiment count: 3. |
| MAPK8IP1Q9UQF2With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9UQF2. Reported experiment count: 3. |
| MAPK8IP2Q13387With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: Q13387. Reported experiment count: 5. |
| MAST1Q9Y2H9With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9Y2H9. Reported experiment count: 3. |
| MBIPQ9NS73With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9NS73. Reported experiment count: 3. |
| METP08581With P00533 | Homo sapiens | 8 | IntAct evidenceSource product: P00533. Partner: P08581. Reported experiment count: 8. |
| MIFP14174With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P14174. Reported experiment count: 3. |
| MUC1P15941With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P15941. Reported experiment count: 4. |
| NCK1P16333With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: P16333. Reported experiment count: 5. |
| NEDD4P46934With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P46934. Reported experiment count: 3. |
| NR3C1P04150With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P04150. Reported experiment count: 3. |
| NTRK2Q16620With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q16620. Reported experiment count: 3. |
| NUMBP49757With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: P49757. Reported experiment count: 2. |
| NUMBLQ9Y6R0With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q9Y6R0. Reported experiment count: 2. |
| OS9Q13438With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q13438. Reported experiment count: 3. |
| PDGFRAP16234With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P16234. Reported experiment count: 4. |
| PIK3C2BO00750With P00533 | Homo sapiens | 10 | IntAct evidenceSource product: P00533. Partner: O00750. Reported experiment count: 10. |
| PIK3R1P27986With P00533 | Homo sapiens | 6 | IntAct evidenceSource product: P00533. Partner: P27986. Reported experiment count: 6. |
| PIK3R2O00459With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: O00459. Reported experiment count: 5. |
| PIK3R3Q92569With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: Q92569. Reported experiment count: 7. |
| PLCG1P19174With P00533 | Homo sapiens | 6 | IntAct evidenceSource product: P00533. Partner: P19174. Reported experiment count: 6. |
| PLCG2P16885With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: P16885. Reported experiment count: 7. |
| PPM1AP35813With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: P35813. Reported experiment count: 2. |
| PRKCAP17252With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P17252. Reported experiment count: 3. |
| PTK2Q05397With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: Q05397. Reported experiment count: 7. |
| PTK6Q13882With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q13882. Reported experiment count: 2. |
| PTPN1P18031With P00533 | Homo sapiens | 9 | IntAct evidenceSource product: P00533. Partner: P18031. Reported experiment count: 9. |
| PTPN11Q06124With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: Q06124. Reported experiment count: 7. |
| PTPN12Q05209With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: Q05209. Reported experiment count: 5. |
| PTPN22Q9Y2R2With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9Y2R2. Reported experiment count: 3. |
| PTPRAP18433With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P18433. Reported experiment count: 3. |
| PTPRBP23467With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P23467. Reported experiment count: 3. |
| PTPRCP08575With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: P08575. Reported experiment count: 2. |
| PTPRGP23470With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P23470. Reported experiment count: 3. |
| PTPRHQ9HD43With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9HD43. Reported experiment count: 3. |
| RABGEF1Q9UJ41With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q9UJ41. Reported experiment count: 4. |
| RAF1P04049With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P04049. Reported experiment count: 3. |
| RAPH1Q70E73With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q70E73. Reported experiment count: 2. |
| RASA1P20936With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: P20936. Reported experiment count: 7. |
| RIN1Q13671With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q13671. Reported experiment count: 3. |
| ROR1Q01973With P00533 | Homo sapiens | 8 | IntAct evidenceSource product: P00533. Partner: Q01973. Reported experiment count: 8. |
| RUBCNQ92622With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q92622. Reported experiment count: 4. |
| S100A4P26447With P00533 | Homo sapiens | 6 | IntAct evidenceSource product: P00533. Partner: P26447. Reported experiment count: 6. |
| SEC61A1P61619With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: P61619. Reported experiment count: 2. |
| SEL1LQ9UBV2With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q9UBV2. Reported experiment count: 2. |
| SFNP31947With P00533 | Homo sapiens | 9 | IntAct evidenceSource product: P00533. Partner: P31947. Reported experiment count: 9. |
| SH2B1Q9NRF2With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q9NRF2. Reported experiment count: 4. |
| SH2B3Q9UQQ2With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q9UQQ2. Reported experiment count: 2. |
| SH2D3AQ9BRG2With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9BRG2. Reported experiment count: 3. |
| SHC1P29353With P00533 | Homo sapiens | 37 | IntAct evidenceSource product: P00533. Partner: P29353. Reported experiment count: 37. |
| SHC1P29353-7With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P29353-7. Reported experiment count: 4. |
| SHC2P98077With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P98077. Reported experiment count: 3. |
| SHC4Q6S5L8With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q6S5L8. Reported experiment count: 3. |
| SKAP2O75563With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: O75563. Reported experiment count: 2. |
| SLAQ13239With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q13239. Reported experiment count: 3. |
| SLC5A1P13866With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P13866. Reported experiment count: 3. |
| SNX3O60493With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: O60493. Reported experiment count: 4. |
| SOS1Q07889With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q07889. Reported experiment count: 3. |
| SRCP12931With P00533 | Homo sapiens | 10 | IntAct evidenceSource product: P00533. Partner: P12931. Reported experiment count: 10. |
| STAT1P42224With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: P42224. Reported experiment count: 7. |
| STAT3P40763With P00533 | Homo sapiens | 16 | IntAct evidenceSource product: P00533. Partner: P40763. Reported experiment count: 16. |
| STAT5AP42229With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P42229. Reported experiment count: 4. |
| STIP1P31948With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P31948. Reported experiment count: 3. |
| STUB1Q9UNE7With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q9UNE7. Reported experiment count: 4. |
| STX6O43752With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: O43752. Reported experiment count: 3. |
| SYKP43405With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: P43405. Reported experiment count: 7. |
| TAB1Q15750With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q15750. Reported experiment count: 3. |
| TACC3Q9Y6A5With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9Y6A5. Reported experiment count: 3. |
| TGFAP01135With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: P01135. Reported experiment count: 4. |
| TLN1Q9Y490With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q9Y490. Reported experiment count: 2. |
| TLR2O60603With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: O60603. Reported experiment count: 3. |
| TNFRSF11AQ9Y6Q6-2With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9Y6Q6-2. Reported experiment count: 3. |
| TNS3Q68CZ2With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: Q68CZ2. Reported experiment count: 5. |
| TNS4Q8IZW8With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q8IZW8. Reported experiment count: 2. |
| TOM1L1O75674With P00533 | Homo sapiens | 6 | IntAct evidenceSource product: P00533. Partner: O75674. Reported experiment count: 6. |
| TRAF2Q12933With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q12933. Reported experiment count: 4. |
| TUBA1AQ71U36With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q71U36. Reported experiment count: 4. |
| TUBB2AQ13885With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q13885. Reported experiment count: 2. |
| TXNP10599With P00533 | Homo sapiens | 5 | IntAct evidenceSource product: P00533. Partner: P10599. Reported experiment count: 5. |
| UCHL1P09936With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P09936. Reported experiment count: 3. |
| USP33Q8TEY7With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q8TEY7. Reported experiment count: 2. |
| VAPAQ9P0L0With P00533 | Homo sapiens | 4 | IntAct evidenceSource product: P00533. Partner: Q9P0L0. Reported experiment count: 4. |
| WASF3Q9UPY6With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q9UPY6. Reported experiment count: 3. |
| YES1P07947With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P07947. Reported experiment count: 3. |
| YWHAQP27348With P00533 | Homo sapiens | 7 | IntAct evidenceSource product: P00533. Partner: P27348. Reported experiment count: 7. |
| YWHAZP63104With P00533 | Homo sapiens | 6 | IntAct evidenceSource product: P00533. Partner: P63104. Reported experiment count: 6. |
| ZAP70P43403With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: P43403. Reported experiment count: 3. |
| Heat shock 70 kDa protein 6Q53FC7With P00533 | Homo sapiens | 3 | IntAct evidenceSource product: P00533. Partner: Q53FC7. Reported experiment count: 3. |
| Heat shock cognate 71 kDa proteinQ96BE0With P00533 | Homo sapiens | 2 | IntAct evidenceSource product: P00533. Partner: Q96BE0. Reported experiment count: 2. |
| Calm3P62161With P00533 | Species not verifiedCross-species | 6 | IntAct evidenceSource product: P00533. Partner: P62161. Reported experiment count: 6. |
| CblP22682With P00533 | Mus musculusCross-species | 2 | IntAct evidenceSource product: P00533. Partner: P22682. Reported experiment count: 2. |
| Grb7Q9QZC5With P00533 | Rattus norvegicusCross-species | 7 | IntAct evidenceSource product: P00533. Partner: Q9QZC5. Reported experiment count: 7. |
| PrkdcP97313With P00533 | Mus musculusCross-species | 4 | IntAct evidenceSource product: P00533. Partner: P97313. Reported experiment count: 4. |
| Ptpn1P20417With P00533 | Rattus norvegicusCross-species | 11 | IntAct evidenceSource product: P00533. Partner: P20417. Reported experiment count: 11. |
| RubcnQ80U62With P00533 | Mus musculusCross-species | 2 | IntAct evidenceSource product: P00533. Partner: Q80U62. Reported experiment count: 2. |
| SP0DTC2With P00533 | Severe acute respiratory syndrome coronavirus 2Cross-species | 4 | IntAct evidenceSource product: P00533. Partner: P0DTC2. Reported experiment count: 4. |
| Trpv3Q8K424With P00533 | Mus musculusCross-species | 2 | IntAct evidenceSource product: P00533. Partner: Q8K424. Reported experiment count: 2. |
No partners match this filter.
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]
Evidence & references
- ECO:0000250 UniProtKB:Q01279
- ECO:0000269 PubMed:10026169 ↗
- ECO:0000269 PubMed:10228163 ↗
- ECO:0000269 PubMed:10805725 ↗
- ECO:0000269 PubMed:11116146 ↗
- ECO:0000269 PubMed:11483589 ↗
- ECO:0000269 PubMed:12297050 ↗
- ECO:0000269 PubMed:12620237 ↗
- ECO:0000269 PubMed:12873986 ↗
- ECO:0000269 PubMed:15282549 ↗
- ECO:0000269 PubMed:15374980 ↗
- ECO:0000269 PubMed:15590694 ↗
- ECO:0000269 PubMed:15837620 ↗
- ECO:0000269 PubMed:16140940 ↗
- ECO:0000269 PubMed:16420529 ↗
- ECO:0000269 PubMed:17115032 ↗
- ECO:0000269 PubMed:17182860 ↗
- ECO:0000269 PubMed:17334392 ↗
- ECO:0000269 PubMed:17909029 ↗
- ECO:0000269 PubMed:18046415 ↗
- ECO:0000269 PubMed:18602463 ↗
- ECO:0000269 PubMed:19172738 ↗
- ECO:0000269 PubMed:19509291 ↗
- ECO:0000269 PubMed:19560417 ↗
- ECO:0000269 PubMed:19563760 ↗
- ECO:0000269 PubMed:19749156 ↗
- ECO:0000269 PubMed:19836242 ↗
- ECO:0000269 PubMed:20462955 ↗
- ECO:0000269 PubMed:20471394 ↗
- ECO:0000269 PubMed:20551055 ↗
- ECO:0000269 PubMed:20674546 ↗
- ECO:0000269 PubMed:20837704 ↗
- ECO:0000269 PubMed:21258366 ↗
- ECO:0000269 PubMed:21518868 ↗
- ECO:0000269 PubMed:22298428 ↗
- ECO:0000269 PubMed:22888118 ↗
- ECO:0000269 PubMed:23418353 ↗
- ECO:0000269 PubMed:23589287 ↗
- ECO:0000269 PubMed:23774213 ↗
- ECO:0000269 PubMed:23912460 ↗
- ECO:0000269 PubMed:25187647 ↗
- ECO:0000269 PubMed:25311788 ↗
- ECO:0000269 PubMed:26988023 ↗
- ECO:0000269 PubMed:28479384 ↗
- ECO:0000269 PubMed:35538033 ↗
- ECO:0000269 PubMed:39073202 ↗
- ECO:0000269 PubMed:7657591 ↗
- ECO:0000269 PubMed:8650580 ↗
- ECO:0000269 PubMed:9852145 ↗
- ECO:0000269 Reference:Ref.112
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.
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
| Component | Species | Chains | Protein identities |
|---|---|---|---|
| Epidermal growth factor receptorprotein · Entity 1 | Homo sapiens | A, C | P00533 |
| Epidermal growth factorprotein · Entity 2 | Homo sapiens | B, D | P01133 |
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
| Record | Evidence type | Method | Resolution | Open |
|---|---|---|---|---|
| 7SYD | experimental | EM | 3.10 A | Open in Atlas ↗ |
| 7SYE | experimental | EM | 3.30 A | Open in Atlas ↗ |
| 7SZ0 | experimental | EM | 3.30 A | Open in Atlas ↗ |
| 7SZ1 | experimental | EM | 3.40 A | Open in Atlas ↗ |
| 7SZ7 | experimental | EM | 3.40 A | Open in Atlas ↗ |
| 7SZ5 | experimental | EM | 3.60 A | Open in Atlas ↗ |
| 4UV7 | experimental | X-ray | 2.10 A | Open in Atlas ↗ |
| 9Z9E | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 3QWQ | experimental | X-ray | 2.75 A | Open in Atlas ↗ |
| 8HGO | experimental | EM | 3.31 A | Open in Atlas ↗ |
| 5XWD | experimental | X-ray | 2.89 A | Open in Atlas ↗ |
| 1YY9 | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 1NQL | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 4KRP | experimental | X-ray | 2.82 A | Open in Atlas ↗ |
| 9IPB | experimental | EM | 2.93 A | Open in Atlas ↗ |
| 8HGS | experimental | EM | 3.81 A | Open in Atlas ↗ |
| 9Z9F | experimental | X-ray | 3.06 A | Open in Atlas ↗ |
| 4UIP | experimental | X-ray | 2.95 A | Open in Atlas ↗ |
| 4KRO | experimental | X-ray | 3.05 A | Open in Atlas ↗ |
| 8HGP | experimental | EM | 4.53 A | Open in Atlas ↗ |
| 9IP7 | experimental | EM | 3.21 A | Open in Atlas ↗ |
| 6ARU | experimental | X-ray | 3.20 A | Open in Atlas ↗ |
| 1IVO | experimental | X-ray | 3.30 A | Open in Atlas ↗ |
| 9IPD | experimental | EM | 3.29 A | Open in Atlas ↗ |
| 9IPE | experimental | EM | 3.31 A | Open in Atlas ↗ |
| 3B2V | experimental | X-ray | 3.30 A | Open in Atlas ↗ |
| 3NJP | experimental | X-ray | 3.30 A | Open in Atlas ↗ |
| 9IPC | experimental | EM | 3.40 A | Open in Atlas ↗ |
| 9IP9 | experimental | EM | 3.64 A | Open in Atlas ↗ |
| 9IPA | experimental | EM | 3.85 A | Open in Atlas ↗ |
| 9IP8 | experimental | EM | 3.91 A | Open in Atlas ↗ |
| 7OM4 | experimental | X-ray | 6.05 A | Open in Atlas ↗ |
| 1MOX | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 7LEN | experimental | X-ray | 2.90 A | Open in Atlas ↗ |
| 5WB7 | experimental | X-ray | 2.94 A | Open in Atlas ↗ |
| 5WB8 | experimental | X-ray | 3.00 A | Open in Atlas ↗ |
| 7LFR | experimental | X-ray | 3.20 A | Open in Atlas ↗ |
| 8A27 | experimental | X-ray | 1.07 A | Open in Atlas ↗ |
| 8A2D | experimental | X-ray | 1.11 A | Open in Atlas ↗ |
| 7LFS | experimental | X-ray | 3.50 A | Open in Atlas ↗ |
| 5UG9 | experimental | X-ray | 1.33 A | Open in Atlas ↗ |
| 5HG8 | experimental | X-ray | 1.42 A | Open in Atlas ↗ |
| 5UG8 | experimental | X-ray | 1.46 A | Open in Atlas ↗ |
| 8A2A | experimental | X-ray | 1.43 A | Open in Atlas ↗ |
| 6TFV | experimental | X-ray | 1.50 A | Open in Atlas ↗ |
| 6TG0 | experimental | X-ray | 1.50 A | Open in Atlas ↗ |
| 3POZ | experimental | X-ray | 1.50 A | Open in Atlas ↗ |
| 5HG5 | experimental | X-ray | 1.52 A | Open in Atlas ↗ |
| 5CNO | experimental | X-ray | 1.55 A | Open in Atlas ↗ |
| 5UGC | experimental | X-ray | 1.58 A | Open in Atlas ↗ |
| 5U8L | experimental | X-ray | 1.60 A | Open in Atlas ↗ |
| 6TG1 | experimental | X-ray | 1.60 A | Open in Atlas ↗ |
| 7SI1 | experimental | X-ray | 1.60 A | Open in Atlas ↗ |
| 8PO4 | experimental | X-ray | 1.62 A | Open in Atlas ↗ |
| 9GL8 | experimental | X-ray | 1.63 A | Open in Atlas ↗ |
| 5CNN | experimental | X-ray | 1.90 A | Open in Atlas ↗ |
| 9DF3 | experimental | X-ray | 1.68 A | Open in Atlas ↗ |
| 6TFY | experimental | X-ray | 1.70 A | Open in Atlas ↗ |
| 4I22 | experimental | X-ray | 1.71 A | Open in Atlas ↗ |
| 3W33 | experimental | X-ray | 1.70 A | Open in Atlas ↗ |
| 8A2B | experimental | X-ray | 1.69 A | Open in Atlas ↗ |
| 6WXN | experimental | X-ray | 1.76 A | Open in Atlas ↗ |
| 9FQS | experimental | X-ray | 1.78 A | Open in Atlas ↗ |
| 9DF4 | experimental | X-ray | 1.78 A | Open in Atlas ↗ |
| 4I24 | experimental | X-ray | 1.80 A | Open in Atlas ↗ |
| 6TFZ | experimental | X-ray | 1.80 A | Open in Atlas ↗ |
| 6V66 | experimental | X-ray | 1.79 A | Open in Atlas ↗ |
| 3W32 | experimental | X-ray | 1.80 A | Open in Atlas ↗ |
| 5UGA | experimental | X-ray | 1.82 A | Open in Atlas ↗ |
| 7JXQ | experimental | X-ray | 1.83 A | Open in Atlas ↗ |
| 5HG7 | experimental | X-ray | 1.85 A | Open in Atlas ↗ |
| 4WKQ | experimental | X-ray | 1.85 A | Open in Atlas ↗ |
| 5X2A | experimental | X-ray | 1.85 A | Open in Atlas ↗ |
| 9GL7 | experimental | X-ray | 1.88 A | Open in Atlas ↗ |
| 7A2A | experimental | X-ray | 1.90 A | Open in Atlas ↗ |
| 9GC6 | experimental | X-ray | 1.90 A | Open in Atlas ↗ |
| 9GC5 | experimental | X-ray | 1.91 A | Open in Atlas ↗ |
| 3W2S | experimental | X-ray | 1.90 A | Open in Atlas ↗ |
| 4WRG | experimental | X-ray | 1.90 A | Open in Atlas ↗ |
| 6P8Q | experimental | X-ray | 1.90 A | Open in Atlas ↗ |
| 9MSR | experimental | X-ray | 1.93 A | Open in Atlas ↗ |
| 5YU9 | experimental | X-ray | 1.95 A | Open in Atlas ↗ |
| 4ZSE | experimental | X-ray | 1.97 A | Open in Atlas ↗ |
| 8SC7 | experimental | X-ray | 1.98 A | Open in Atlas ↗ |
| 6TFU | experimental | X-ray | 2.00 A | Open in Atlas ↗ |
| 6TFW | experimental | X-ray | 2.00 A | Open in Atlas ↗ |
| 6Z4D | experimental | X-ray | 2.00 A | Open in Atlas ↗ |
| 7A6J | experimental | X-ray | 2.00 A | Open in Atlas ↗ |
| 7A6K | experimental | X-ray | 2.00 A | Open in Atlas ↗ |
| 9FZR | experimental | X-ray | 1.99 A | Open in Atlas ↗ |
| 6LUD | experimental | X-ray | 2.05 A | Open in Atlas ↗ |
| 6XL4 | experimental | X-ray | 2.06 A | Open in Atlas ↗ |
| 5X2C | experimental | X-ray | 2.05 A | Open in Atlas ↗ |
| 9FRD | experimental | X-ray | 2.06 A | Open in Atlas ↗ |
| 3W2P | experimental | X-ray | 2.05 A | Open in Atlas ↗ |
| 3W2R | experimental | X-ray | 2.05 A | Open in Atlas ↗ |
| 5CAS | experimental | X-ray | 2.10 A | Open in Atlas ↗ |
| 7ZYQ | experimental | X-ray | 2.10 A | Open in Atlas ↗ |
| 8FV3 | experimental | X-ray | 2.10 A | Open in Atlas ↗ |
| 9GHR | experimental | X-ray | 2.10 A | Open in Atlas ↗ |
| 9MSS | experimental | X-ray | 2.09 A | Open in Atlas ↗ |
| 8PO1 | experimental | X-ray | 2.11 A | Open in Atlas ↗ |
| 6V6O | experimental | X-ray | 2.10 A | Open in Atlas ↗ |
| 9OU9 | experimental | X-ray | 2.10 A | Open in Atlas ↗ |
| 8PO3 | experimental | X-ray | 2.13 A | Open in Atlas ↗ |
| 9FZS | experimental | X-ray | 2.12 A | Open in Atlas ↗ |
| 9DM8 | experimental | X-ray | 2.13 A | Open in Atlas ↗ |
| 5HG9 | experimental | X-ray | 2.15 A | Open in Atlas ↗ |
| 9QXN | experimental | X-ray | 2.14 A | Open in Atlas ↗ |
| 7JXP | experimental | X-ray | 2.16 A | Open in Atlas ↗ |
| 9GL9 | experimental | X-ray | 2.15 A | Open in Atlas ↗ |
| 8UKW | experimental | X-ray | 2.39 A | Open in Atlas ↗ |
| 8D73 | experimental | X-ray | 2.17 A | Open in Atlas ↗ |
| 2RGP | experimental | X-ray | 2.00 A | Open in Atlas ↗ |
| 7JXM | experimental | X-ray | 2.19 A | Open in Atlas ↗ |
| 6DUK | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 8FV4 | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 8HV4 | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 8HV5 | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 8HV6 | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 5X2F | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 6JRX | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 6V6K | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 7T4J | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 9GDV | experimental | X-ray | 2.22 A | Open in Atlas ↗ |
| 3W2Q | experimental | X-ray | 2.20 A | Open in Atlas ↗ |
| 9NIS | experimental | X-ray | 2.23 A | Open in Atlas ↗ |
| 5CAU | experimental | X-ray | 2.25 A | Open in Atlas ↗ |
| 9GHU | experimental | X-ray | 2.25 A | Open in Atlas ↗ |
| 9NJN | experimental | X-ray | 2.24 A | Open in Atlas ↗ |
| 5GNK | experimental | X-ray | 1.80 A | Open in Atlas ↗ |
| 8PO2 | experimental | X-ray | 2.28 A | Open in Atlas ↗ |
| 6V5P | experimental | X-ray | 2.30 A | Open in Atlas ↗ |
| 7LTX | experimental | X-ray | 2.30 A | Open in Atlas ↗ |
| 7ZYN | experimental | X-ray | 2.30 A | Open in Atlas ↗ |
| 8F1X | experimental | X-ray | 2.30 A | Open in Atlas ↗ |
| 8GK5 | experimental | X-ray | 2.30 A | Open in Atlas ↗ |
| 5D41 | experimental | X-ray | 2.31 A | Open in Atlas ↗ |
| 6LUB | experimental | X-ray | 2.31 A | Open in Atlas ↗ |
| 6JXT | experimental | X-ray | 2.31 A | Open in Atlas ↗ |
| 9BY4 | experimental | X-ray | 2.31 A | Open in Atlas ↗ |
| 9D3V | experimental | X-ray | 2.32 A | Open in Atlas ↗ |
| 9KL4 | experimental | X-ray | 2.32 A | Open in Atlas ↗ |
| 3VJN | experimental | X-ray | 2.34 A | Open in Atlas ↗ |
| 9PMZ | experimental | X-ray | 2.33 A | Open in Atlas ↗ |
| 5XDK | experimental | X-ray | 2.35 A | Open in Atlas ↗ |
| 3W2O | experimental | X-ray | 2.35 A | Open in Atlas ↗ |
| 1XKK | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 5C8N | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 5CAP | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 6V5N | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 6WA2 | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 6WAK | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 7A6I | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 7JXL | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 7KXZ | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 7UKV | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 8D76 | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 8F1Z | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 8HV1 | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 8HV3 | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 8HV8 | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 8DSW | experimental | X-ray | 2.39 A | Open in Atlas ↗ |
| 6P1D | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 6VHN | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 9NGP | experimental | X-ray | 2.40 A | Open in Atlas ↗ |
| 9GC4 | experimental | X-ray | 2.42 A | Open in Atlas ↗ |
| 7VRA | experimental | X-ray | 2.41 A | Open in Atlas ↗ |
| 9EWS | experimental | X-ray | 2.44 A | Open in Atlas ↗ |
| 9HBO | experimental | X-ray | 2.45 A | Open in Atlas ↗ |
| 3GOP | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 3BEL | experimental | X-ray | 2.30 A | Open in Atlas ↗ |
| 9S3X | experimental | X-ray | 2.42 A | Open in Atlas ↗ |
| 5HCY | experimental | X-ray | 2.46 A | Open in Atlas ↗ |
| 9Q0S | experimental | X-ray | 2.46 A | Open in Atlas ↗ |
| 2ITN | experimental | X-ray | 2.47 A | Open in Atlas ↗ |
| 2ITV | experimental | X-ray | 2.47 A | Open in Atlas ↗ |
| 4LQM | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 8TO3 | experimental | X-ray | 2.49 A | Open in Atlas ↗ |
| 2EB2 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 3UG2 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 4RJ8 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 5CAQ | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 6Z4B | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 7B85 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 7JXW | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 7U99 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 7ZYM | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 8HV9 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 9FQP | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 9GHV | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 8PNZ | experimental | X-ray | 2.51 A | Open in Atlas ↗ |
| 8G63 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 9DF2 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 8PO0 | experimental | X-ray | 2.52 A | Open in Atlas ↗ |
| 7VRE | experimental | X-ray | 2.51 A | Open in Atlas ↗ |
| 5UGB | experimental | X-ray | 2.53 A | Open in Atlas ↗ |
| 5J9Z | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 6JX0 | experimental | X-ray | 2.53 A | Open in Atlas ↗ |
| 6JX4 | experimental | X-ray | 2.53 A | Open in Atlas ↗ |
| 9D3W | experimental | X-ray | 2.53 A | Open in Atlas ↗ |
| 9NJ7 | experimental | X-ray | 2.53 A | Open in Atlas ↗ |
| 4RJ7 | experimental | X-ray | 2.55 A | Open in Atlas ↗ |
| 6D8E | experimental | X-ray | 2.54 A | Open in Atlas ↗ |
| 6JWL | experimental | X-ray | 2.55 A | Open in Atlas ↗ |
| 8WD4 | experimental | X-ray | 2.55 A | Open in Atlas ↗ |
| 9BY6 | experimental | X-ray | 2.55 A | Open in Atlas ↗ |
| 9MST | experimental | X-ray | 2.57 A | Open in Atlas ↗ |
| 5CZI | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 8GB4 | experimental | X-ray | 2.59 A | Open in Atlas ↗ |
| 7OXB | experimental | X-ray | 2.56 A | Open in Atlas ↗ |
| 1M14 | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 1M17 | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 5CAO | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 5EDR | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 5HIC | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 6S8A | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 7K1H | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 7U9A | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 7UKW | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 9GHS | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 9GHT | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 9NM0 | experimental | X-ray | 2.59 A | Open in Atlas ↗ |
| 2GS6 | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 2GS7 | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 5HCX | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 9H42 | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 7T4I | experimental | X-ray | 2.61 A | Open in Atlas ↗ |
| 5HCZ | experimental | X-ray | 2.62 A | Open in Atlas ↗ |
| 5ZWJ | experimental | X-ray | 2.90 A | Open in Atlas ↗ |
| 3VJO | experimental | X-ray | 2.64 A | Open in Atlas ↗ |
| 5EM5 | experimental | X-ray | 2.65 A | Open in Atlas ↗ |
| 7AEI | experimental | X-ray | 2.65 A | Open in Atlas ↗ |
| 7AEM | experimental | X-ray | 2.65 A | Open in Atlas ↗ |
| 5FED | experimental | X-ray | 2.65 A | Open in Atlas ↗ |
| 5ZTO | experimental | X-ray | 2.65 A | Open in Atlas ↗ |
| 7ER2 | experimental | X-ray | 2.66 A | Open in Atlas ↗ |
| 4LI5 | experimental | X-ray | 2.64 A | Open in Atlas ↗ |
| 6S9D | experimental | X-ray | 2.67 A | Open in Atlas ↗ |
| 9KLW | experimental | X-ray | 2.67 A | Open in Atlas ↗ |
| 8HV7 | experimental | X-ray | 2.69 A | Open in Atlas ↗ |
| 2ITQ | experimental | X-ray | 2.68 A | Open in Atlas ↗ |
| 4RJ6 | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 4ZJV | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 5CAL | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 6S89 | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 8TJL | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 5FEE | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 5XDL | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 8UKV | experimental | X-ray | 2.94 A | Open in Atlas ↗ |
| 4JR3 | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 5CAV | experimental | X-ray | 2.73 A | Open in Atlas ↗ |
| 2ITZ | experimental | X-ray | 2.72 A | Open in Atlas ↗ |
| 2ITT | experimental | X-ray | 2.73 A | Open in Atlas ↗ |
| 6S9C | experimental | X-ray | 2.73 A | Open in Atlas ↗ |
| 9NHW | experimental | X-ray | 2.73 A | Open in Atlas ↗ |
| 3UG1 | experimental | X-ray | 2.75 A | Open in Atlas ↗ |
| 8F1Y | experimental | X-ray | 2.75 A | Open in Atlas ↗ |
| 2ITP | experimental | X-ray | 2.74 A | Open in Atlas ↗ |
| 4JQ7 | experimental | X-ray | 2.73 A | Open in Atlas ↗ |
| 4HJO | experimental | X-ray | 2.75 A | Open in Atlas ↗ |
| 9OS6 | experimental | X-ray | 2.75 A | Open in Atlas ↗ |
| 8HVA | experimental | X-ray | 2.77 A | Open in Atlas ↗ |
| 4RJ4 | experimental | X-ray | 2.78 A | Open in Atlas ↗ |
| 5EM6 | experimental | X-ray | 2.78 A | Open in Atlas ↗ |
| 5CZH | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 8HV2 | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 4I23 | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 5CAN | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 5EDQ | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 5EM8 | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 7ZYP | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 8F1H | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 4RIY | experimental | X-ray | 2.98 A | Open in Atlas ↗ |
| 5EM7 | experimental | X-ray | 2.81 A | Open in Atlas ↗ |
| 2GS2 | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 2ITU | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 4G5J | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 4ZAU | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 5GMP | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 6JRK | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 6P1L | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 6VH4 | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 4JRV | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 9XU9 | experimental | X-ray | 2.84 A | Open in Atlas ↗ |
| 2EB3 | experimental | X-ray | 2.84 A | Open in Atlas ↗ |
| 5HIB | experimental | X-ray | 2.85 A | Open in Atlas ↗ |
| 4JQ8 | experimental | X-ray | 2.83 A | Open in Atlas ↗ |
| 5J9Y | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 6JZ0 | experimental | X-ray | 2.86 A | Open in Atlas ↗ |
| 3IKA | experimental | X-ray | 2.90 A | Open in Atlas ↗ |
| 2ITW | experimental | X-ray | 2.88 A | Open in Atlas ↗ |
| 5C8M | experimental | X-ray | 2.90 A | Open in Atlas ↗ |
| 5EDP | experimental | X-ray | 2.90 A | Open in Atlas ↗ |
| 8HY7 | experimental | X-ray | 2.91 A | Open in Atlas ↗ |
| 4RIW | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 4RIX | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 7LG8 | experimental | X-ray | 2.93 A | Open in Atlas ↗ |
| 9U91 | experimental | X-ray | 3.20 A | Open in Atlas ↗ |
| 9VV1 | experimental | X-ray | 2.95 A | Open in Atlas ↗ |
| 6JRJ | experimental | X-ray | 2.94 A | Open in Atlas ↗ |
| 5X26 | experimental | X-ray | 2.95 A | Open in Atlas ↗ |
| 5X27 | experimental | X-ray | 2.95 A | Open in Atlas ↗ |
| 5X28 | experimental | X-ray | 2.95 A | Open in Atlas ↗ |
| 5XGM | experimental | X-ray | 2.95 A | Open in Atlas ↗ |
| 4R3P | experimental | X-ray | 2.90 A | Open in Atlas ↗ |
| 3GT8 | experimental | X-ray | 2.96 A | Open in Atlas ↗ |
| 7TVD | experimental | X-ray | 2.96 A | Open in Atlas ↗ |
| 8TO4 | experimental | X-ray | 2.99 A | Open in Atlas ↗ |
| 2RFE | experimental | X-ray | 2.90 A | Open in Atlas ↗ |
| 2ITX | experimental | X-ray | 2.98 A | Open in Atlas ↗ |
| 4I1Z | experimental | X-ray | 3.00 A | Open in Atlas ↗ |
| 5C8K | experimental | X-ray | 3.00 A | Open in Atlas ↗ |
| 7JXI | experimental | X-ray | 3.00 A | Open in Atlas ↗ |
| 9H47 | experimental | X-ray | 2.99 A | Open in Atlas ↗ |
| 2J5F | experimental | X-ray | 3.00 A | Open in Atlas ↗ |
| 4R5S | experimental | X-ray | 3.00 A | Open in Atlas ↗ |
| 5GTZ | experimental | X-ray | 3.00 A | Open in Atlas ↗ |
| 5XGN | experimental | X-ray | 3.00 A | Open in Atlas ↗ |
| 9EWT | experimental | X-ray | 3.02 A | Open in Atlas ↗ |
| 9JQ1 | experimental | X-ray | 3.02 A | Open in Atlas ↗ |
| 2JIU | experimental | X-ray | 3.05 A | Open in Atlas ↗ |
| 5UWD | experimental | X-ray | 3.06 A | Open in Atlas ↗ |
| 8UKX | experimental | X-ray | 3.30 A | Open in Atlas ↗ |
| 4RJ5 | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 7JXK | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 7KY0 | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 2J5E | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 2J6M | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 2JIT | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 7LGS | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 9GI9 | experimental | X-ray | 3.12 A | Open in Atlas ↗ |
| 5Y25 | experimental | X-ray | 3.10 A | Open in Atlas ↗ |
| 5GTY | experimental | X-ray | 3.14 A | Open in Atlas ↗ |
| 9H46 | experimental | X-ray | 3.16 A | Open in Atlas ↗ |
| 4G5P | experimental | X-ray | 3.17 A | Open in Atlas ↗ |
| 4TKS | experimental | X-ray | 3.20 A | Open in Atlas ↗ |
| 7K1I | experimental | X-ray | 3.20 A | Open in Atlas ↗ |
| 8F1W | experimental | X-ray | 3.20 A | Open in Atlas ↗ |
| 5X2K | experimental | X-ray | 3.20 A | Open in Atlas ↗ |
| 3LZB | experimental | X-ray | 2.70 A | Open in Atlas ↗ |
| 5Y9T | experimental | X-ray | 3.25 A | Open in Atlas ↗ |
| 2ITO | experimental | X-ray | 3.25 A | Open in Atlas ↗ |
| 6S9B | experimental | X-ray | 3.25 A | Open in Atlas ↗ |
| 9P9U | experimental | EM | 3.27 A | Open in Atlas ↗ |
| 4WD5 | experimental | X-ray | 3.30 A | Open in Atlas ↗ |
| 8KFQ | experimental | X-ray | 3.22 A | Open in Atlas ↗ |
| 5JEB | experimental | X-ray | 3.30 A | Open in Atlas ↗ |
| 4R3R | experimental | X-ray | 3.25 A | Open in Atlas ↗ |
| 8EME | experimental | X-ray | 3.32 A | Open in Atlas ↗ |
| 4I20 | experimental | X-ray | 3.34 A | Open in Atlas ↗ |
| 4I21 | experimental | X-ray | 3.37 A | Open in Atlas ↗ |
| 5FEQ | experimental | X-ray | 3.40 A | Open in Atlas ↗ |
| 8H7X | experimental | X-ray | 3.40 A | Open in Atlas ↗ |
| 7U98 | experimental | X-ray | 3.42 A | Open in Atlas ↗ |
| 3P0Y | experimental | X-ray | 1.80 A | Open in Atlas ↗ |
| 2ITY | experimental | X-ray | 3.42 A | Open in Atlas ↗ |
| 2JIV | experimental | X-ray | 3.50 A | Open in Atlas ↗ |
| 2RF9 | experimental | X-ray | 3.50 A | Open in Atlas ↗ |
| 9U8C | experimental | X-ray | 3.50 A | Open in Atlas ↗ |
| 4LRM | experimental | X-ray | 3.53 A | Open in Atlas ↗ |
| 6VHP | experimental | X-ray | 3.60 A | Open in Atlas ↗ |
| 2RFD | experimental | X-ray | 3.60 A | Open in Atlas ↗ |
| 4LL0 | experimental | X-ray | 4.00 A | Open in Atlas ↗ |
| 3B2U | experimental | X-ray | 2.58 A | Open in Atlas ↗ |
| 4KRM | experimental | X-ray | 2.66 A | Open in Atlas ↗ |
| 5SX5 | experimental | X-ray | 2.50 A | Open in Atlas ↗ |
| 6B3S | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 4KRL | experimental | X-ray | 2.85 A | Open in Atlas ↗ |
| 5SX4 | experimental | X-ray | 2.80 A | Open in Atlas ↗ |
| 3C09 | experimental | X-ray | 3.20 A | Open in Atlas ↗ |
| 3VRP | experimental | X-ray | 1.52 A | Open in Atlas ↗ |
| 3G5Y | experimental | X-ray | 1.59 A | Open in Atlas ↗ |
| 8S1M | experimental | X-ray | 2.05 A | Open in Atlas ↗ |
| 3G5V | experimental | X-ray | 2.00 A | Open in Atlas ↗ |
| 3VRR | experimental | X-ray | 2.00 A | Open in Atlas ↗ |
| 3OB2 | experimental | X-ray | 2.10 A | Open in Atlas ↗ |
| 3PFV | experimental | X-ray | 2.27 A | Open in Atlas ↗ |
| 9Z2H | experimental | X-ray | 2.45 A | Open in Atlas ↗ |
| 3OP0 | experimental | X-ray | 2.52 A | Open in Atlas ↗ |
| 3BUO | experimental | X-ray | 2.60 A | Open in Atlas ↗ |
| 9OLB | experimental | X-ray | 2.62 A | Open in Atlas ↗ |
| 2M20 | experimental | NMR | - | Open in Atlas ↗ |
| 1Z9I | experimental | NMR | - | Open in Atlas ↗ |
| 2N5S | experimental | NMR | - | Open in Atlas ↗ |
| 2KS1 | experimental | NMR | - | Open in Atlas ↗ |
| 2M0B | experimental | NMR | - | Open in Atlas ↗ |
| 5LV6 | experimental | NMR | - | Open in Atlas ↗ |
| AF-P00533-F1 | predicted | AlphaFold | Not applicable | Open in Atlas ↗ |
Family & Domains
Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily
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 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
| Annotation | Position | Source & interpretation | Inspect |
|---|---|---|---|
| Receptor L-domainIPR000494 | 57–167 | INTERPROdomain 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 descriptionThe 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. | No verified residues in this structure |
| ApproximateUNI_REPEAT_75_300 | 75–300 | UNIPROTrepeat Approximate Source entry ↗ | No verified residues in this structure |
| Furin-like cysteine-rich domainIPR006211 | 185–338 | INTERPROdomain 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 repeatIPR006212 | 228–274 | INTERPROrepeat 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-domainIPR000494 | 361–480 | INTERPROdomain 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 descriptionThe 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. | No verified residues in this structure |
| ApproximateUNI_REPEAT_390_600 | 390–600 | UNIPROTrepeat Approximate Source entry ↗ | No verified residues in this structure |
| Furin-like repeatIPR006212 | 496–601 | INTERPROrepeat 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 4IPR032778 | 505–636 | INTERPROdomain 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 segmentIPR049328 | 646–681 | INTERPROdomain 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 descriptionEpidermal 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. | No verified residues in this structure |
| Protein kinase domainIPR000719 | 712–979 | INTERPROdomain 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 descriptionThis 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. | No verified residues in this structure |
UniProt domains, repeats & motifs 3
Scroll across the table for evidence and actions.
3 recorded rows
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Repeat | 75–300 | Approximate | Evidence & referencesNo separate evidence record is supplied for this statement. | No verified residues in this structure |
| Repeat | 390–600 | Approximate | Evidence & referencesNo separate evidence record is supplied for this statement. | No verified residues in this structure |
| Domain | 712–979 | Protein kinase | Sequence analysis Evidence & references
| No verified residues in this structure |
Functional sites 6
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6 recorded rows
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Active site | 837 | Proton acceptor | Sequence analysis Evidence & references
| No verified residues in this structure |
| Binding site | 718–726 | Binding site | Experimental evidence 1 publication Evidence & references
| No verified residues in this structure |
| Binding site | 745 | Binding site | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Binding site | 790–791 | Binding site | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Binding site | 855 | Binding site | Experimental evidence 2 publications Evidence & references
| No verified residues in this structure |
| Site | 1016 | Important for interaction with PIK3C2B | Evidence & referencesNo 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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Region | 688–704 | Important for dimerization, phosphorylation and activation | Evidence & referencesNo separate evidence record is supplied for this statement. | No verified residues in this structure |
| Region | 1097–1137 | Disordered | Evidence & references
| No verified residues in this structure |
| Compositional bias | 1104–1115 | Polar residues | Evidence & references
| No verified residues in this structure |
| Compositional bias | 1128–1137 | Polar residues | Evidence & references
| No verified residues in this structure |
Sequence & Isoforms
Sequence & isoforms
UniProt’s canonical sequence is its selected representative. It is not necessarily the dominant isoform in every tissue.
Full precursor sequence, including processing regions. The mass describes this unmodified source sequence, not every mature or modified product.
MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRVAPQSSEFIGASource 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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Alternative sequenceVSP_002887 | 404–405 | in isoform 2 FL → LS | Published statement 3 publications Evidence & references
| No verified residues in this structure |
| Alternative sequenceVSP_002888 | 406–1210 | in isoform 2 | Published statement 3 publications Evidence & references
| No verified residues in this structure |
| Alternative sequenceVSP_002889 | 628–705 | in isoform 3 CTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR → PGNESLKAMLFCLFKLSSCNQSNDGSVSHQSGSPAAQESCLGWIPSLLPSEFQLGWGGCSHLHAWPSASVIITASSCH | Published statement 1 publication Evidence & references
| No verified residues in this structure |
| Alternative sequenceVSP_002891 | 628 | in isoform 4 C → S | Published statement 1 publication Evidence & references
| No verified residues in this structure |
| Alternative sequenceVSP_002892 | 629–1210 | in isoform 4 | Published statement 1 publication Evidence & references
| No verified residues in this structure |
| Alternative sequenceVSP_002890 | 706–1210 | in 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
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Sequence conflict | 540 | in Ref. 1; CAA25240 N → K | Curator inference Evidence & references
| No verified residues in this structure |
Recorded secondary structure 139
Scroll across the table for evidence and actions.
139 recorded rows
| Feature | Position | Description | Evidence | Inspect |
|---|---|---|---|---|
| Beta strand | 40–43 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 44–55 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 60–69 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 77–81 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 84–87 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 89–93 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 96–98 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 101–103 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 114–116 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 117–122 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 125–129 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 145–152 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 159–161 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 164–166 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 170–173 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 183–185 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 187–191 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 195–197 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 199–204 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 211–214 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 217–221 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 223–227 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 228–230 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 236–238 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 240–244 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 245–247 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 248–256 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 259–263 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 267–271 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 272–275 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 276–279 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 285–287 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 290–294 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 296–298 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 299–301 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 303–305 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 306–310 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 313–315 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 318–320 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 323–325 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 330–332 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 336–338 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 340–342 | Turn | Evidence & references
| No verified residues in this structure |
| Helix | 343–345 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 349–351 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 353–355 | Turn | Evidence & references
| No verified residues in this structure |
| Helix | 356–359 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 363–367 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 369–371 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 373–377 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 380–383 | Turn | Evidence & references
| No verified residues in this structure |
| Helix | 385–388 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 389–397 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 400–403 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 405–407 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 418–420 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 433–435 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 436–442 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 458–464 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 472–474 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 477–480 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 481–483 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 488–494 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 496–501 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 508–510 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 515–519 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 520–522 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 523–526 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 531–533 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 534–537 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 540–546 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 548–551 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 554–557 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 560–562 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 566–568 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 570–575 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 578–587 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 590–594 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 597–602 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 606–611 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 615–619 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 622–624 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 629–632 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 633–635 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 643–646 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 648–669 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 671–673 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 679–684 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 685–687 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 688–692 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 694–697 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 703–706 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 709–711 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 712–720 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 722–731 | Beta strand | Evidence & references
| No verified residues in this structure |
| Turn | 734–736 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 740–749 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 753–767 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 768–770 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 772–774 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 777–781 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 783–785 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 787–791 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 794–797 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 798–804 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 806–808 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 811–830 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 833–836 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 840–842 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 843–847 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 850–853 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 856–858 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 859–865 | Turn | Evidence & references
| No verified residues in this structure |
| Helix | 866–868 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 871–873 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 874–877 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 878–880 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 883–888 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 890–892 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 893–908 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 909–911 | Turn | Evidence & references
| No verified residues in this structure |
| Turn | 914–917 | Turn | Evidence & references
| No verified residues in this structure |
| Helix | 920–922 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 923–928 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 933–936 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 937–939 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 941–950 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 951–953 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 955–957 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 961–972 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 975–977 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 984–986 | Helix | Evidence & references
| No verified residues in this structure |
| Helix | 988–991 | Helix | Evidence & references
| No verified residues in this structure |
| Turn | 992–998 | Turn | Evidence & references
| No verified residues in this structure |
| Turn | 999–1001 | Turn | Evidence & references
| No verified residues in this structure |
| Beta strand | 1004–1010 | Beta strand | Evidence & references
| No verified residues in this structure |
| Helix | 1013–1016 | Helix | Evidence & references
| No verified residues in this structure |
| Beta strand | 1068–1070 | Beta strand | Evidence & references
| No verified residues in this structure |
| Beta strand | 1091–1094 | Beta strand | Evidence & references
| No verified residues in this structure |
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.
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
- UniProt / The UniProt Consortium ↗ · 2026-11-09T11:39:08.493002+00:00
- InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:39:08.533244+00:00
- AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:39:21.856955+00:00
- UniProt / The UniProt Consortium ↗ · 2026-11-09T11:39:08.493002+00:00
- InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:39:08.533244+00:00
- AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:39:21.856955+00:00
- UniProt overview ↗ · 2026-11-10T20:42:43.548052+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:17.964415+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:18.001143+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:18.037255+00:00
- omabrowser.org ↗ · 2026-11-10T21:11:18.082260+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:18.085267+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:18.256504+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:18.268779+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:18.298384+00:00
- omabrowser.org ↗ · 2026-11-10T21:11:19.079343+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:19.268442+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:19.418109+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:20.185068+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:20.319501+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:20.641681+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:21.166883+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:23.036562+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:23.074994+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:23.118145+00:00
- www.ebi.ac.uk ↗ · 2026-11-10T21:11:23.143711+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:24.241975+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:25.309058+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:27.309439+00:00
- rest.uniprot.org ↗ · 2026-11-10T21:11:27.577292+00:00
Recorded 2026-11-10. Source dates and identifiers are retained below.
Publications in this UniProt entry
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.
1995 · Mol. Reprod. Dev.
PubMed 7654368 ↗Scope & authors
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)
Ilekis J.V., Stark B.C., Scoccia B.
1996 · Nucleic Acids Res.
PubMed 8918811 ↗Scope & authors
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2)
Reiter J.L., Maihle N.J.
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)
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.
JUL-2004 ·
Scope & authors
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)
Xu L., Hong A., He X.
APR-2004 ·
Scope & authors
NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS GLN-98; ARG-266; LYS-521; ILE-674; GLY-962 AND PRO-988
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.
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.
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.
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.
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.
1991 · J. Biol. Chem.
PubMed 1988448 ↗Scope & authors
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29
Haley J.D., Waterfield M.D.
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.
1984 · Science
PubMed 6324343 ↗Scope & authors
NUCLEOTIDE SEQUENCE [MRNA] OF 25-49
Weber W., Gill G.N., Spiess J.
SEP-1997 ·
Scope & authors
PROTEIN SEQUENCE OF 540
Kohda D.
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.
2004 · Protein Sci.
PubMed 15340161 ↗Scope & authors
PROTEIN SEQUENCE OF 25-39
Zhang Z., Henzel W.J.
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.
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.
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.
1984 · Nature
PubMed 6325948 ↗Scope & authors
RECEPTOR ACTIVITY
Mroczkowski B., Mosig G., Cohen S.
1987 · Annu. Rev. Biochem.
PubMed 3039909 ↗Scope & authors
REVIEW
Carpenter G.
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.
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.
1993 · J. Biol. Chem.
PubMed 7679104 ↗Scope & authors
IDENTIFICATION OF AREG AS LIGAND; FUNCTION
Johnson G.R., Kannan B., Shoyab M., Stromberg K.
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.
1998 · J. Cell Biol.
PubMed 9852145 ↗Scope & authors
INTERACTION WITH ZPR1
Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.
1999 · EMBO J.
PubMed 10523301 ↗Scope & authors
PHOSPHORYLATION AT THR-678 AND THR-693
Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.
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.
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.
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.
1997 · Oncogene
PubMed 9419975 ↗Scope & authors
IDENTIFICATION OF EPIREGULIN/EREG AS LIGAND; FUNCTION
Komurasaki T., Toyoda H., Uchida D., Morimoto S.
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.
1999 · EMBO J.
PubMed 10228163 ↗Scope & authors
INTERACTION WITH AP2M1
Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.
1999 · J. Biol. Chem.
PubMed 10026169 ↗Scope & authors
FUNCTION; INTERACTION WITH GRB2; NCK1 AND NCK2
Braverman L.E., Quilliam L.A.
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.
2001 · J. Biol. Chem.
PubMed 11602604 ↗Scope & authors
FUNCTION IN PHOSPHORYLATION OF RGS16
Derrien A., Druey K.M.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
2007 · Mol. Biol. Cell
PubMed 17182860 ↗Scope & authors
INTERACTION WITH TNF2; SUBCELLULAR LOCATION
Shen F., Lin Q., Gu Y., Childress C., Yang W.
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.
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.
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.
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
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
2010 · Cancer Res.
PubMed 20551055 ↗Scope & authors
INTERACTION WITH GPER1; SUBCELLULAR LOCATION
Madeo A., Maggiolini M.
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.
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.
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.
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.
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.
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.
2011 · Proc. Natl. Acad. Sci. U.S.A.
PubMed 21518868 ↗Scope & authors
INTERACTION WITH FER; PHOSPHORYLATION
Guo C., Stark G.R.
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.
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.
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.
2013 · J. Cell Sci.
PubMed 23418353 ↗Scope & authors
INTERACTION WITH RNF115 AND RNF126
Smith C.J., Berry D.M., McGlade C.J.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
2017 · Gene
PubMed 28479384 ↗Scope & authors
INTERACTION WITH LAPTM4B
Tian M., Chen Y., Tian D., Qiao X., Ma Z., Li J.
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.
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.
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.
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.
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.
2024 · Traffic
PubMed 39073202 ↗Scope & authors
INTERACTION WITH SNX32
Wang D., Zhao X., Wang P., Liu J.J.
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.
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.
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.
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.
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.
2005 · J. Biol. Chem.
PubMed 15840573 ↗Scope & authors
STRUCTURE BY NMR OF 669-721
Choowongkomon K., Carlin C.R., Sonnichsen F.D.
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.
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.
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.
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.
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.
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.
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.
OCT-2010 ·
Scope & authors
X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH CBLB; INTERACTION WITH CBLB
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.
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.
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.
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.
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.
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.
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.
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.
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 record | Type | Section |
|---|---|---|
| FUNCTION:0 | FUNCTION | function |
| FUNCTION:1 | FUNCTION | function |
| FUNCTION:2 | FUNCTION | function |
| CATALYTIC ACTIVITY:0 | CATALYTIC ACTIVITY | function |
| ACTIVITY REGULATION:0 | ACTIVITY REGULATION | function |
| SUBUNIT:0 | SUBUNIT | interactions |
| INTERACTION:0 | INTERACTION | interactions |
| SUBCELLULAR LOCATION:0 | SUBCELLULAR LOCATION | location |
| SUBCELLULAR LOCATION:1 | SUBCELLULAR LOCATION | location |
| ALTERNATIVE PRODUCTS:0 | ALTERNATIVE PRODUCTS | sequence |
| TISSUE SPECIFICITY:0 | TISSUE SPECIFICITY | expression |
| PTM:0 | PTM | processing |
| PTM:1 | PTM | processing |
| PTM:2 | PTM | processing |
| PTM:3 | PTM | processing |
| PTM:4 | PTM | processing |
| DISEASE:0 | DISEASE | disease |
| DISEASE:1 | DISEASE | disease |
| SIMILARITY:0 | SIMILARITY | domains |
| WEB RESOURCE:0 | WEB RESOURCE | sources |
| feature-0 | Signal | processing |
| feature-1 | Chain | processing |
| feature-2 | Topological domain | location |
| feature-3 | Transmembrane | location |
| feature-4 | Topological domain | location |
| feature-5 | Repeat | domains |
| feature-6 | Repeat | domains |
| feature-7 | Domain | domains |
| feature-8 | Region | domains |
| feature-9 | Region | domains |
| feature-10 | Compositional bias | domains |
| feature-11 | Compositional bias | domains |
| feature-12 | Active site | domains |
| feature-13 | Binding site | domains |
| feature-14 | Binding site | domains |
| feature-15 | Binding site | domains |
| feature-16 | Binding site | domains |
| feature-17 | Site | domains |
| feature-18 | Modified residue | processing |
| feature-19 | Modified residue | processing |
| feature-20 | Modified residue | processing |
| feature-21 | Modified residue | processing |
| feature-22 | Modified residue | processing |
| feature-23 | Modified residue | processing |
| feature-24 | Modified residue | processing |
| feature-25 | Modified residue | processing |
| feature-26 | Modified residue | processing |
| feature-27 | Modified residue | processing |
| feature-28 | Modified residue | processing |
| feature-29 | Modified residue | processing |
| feature-30 | Modified residue | processing |
| feature-31 | Modified residue | processing |
| feature-32 | Modified residue | processing |
| feature-33 | Modified residue | processing |
| feature-34 | Modified residue | processing |
| feature-35 | Modified residue | processing |
| feature-36 | Modified residue | processing |
| feature-37 | Modified residue | processing |
| feature-38 | Modified residue | processing |
| feature-39 | Modified residue | processing |
| feature-40 | Modified residue | processing |
| feature-41 | Modified residue | processing |
| feature-42 | Modified residue | processing |
| feature-43 | Lipidation | processing |
| feature-44 | Lipidation | processing |
| feature-45 | Glycosylation | processing |
| feature-46 | Glycosylation | processing |
| feature-47 | Glycosylation | processing |
| feature-48 | Glycosylation | processing |
| feature-49 | Glycosylation | processing |
| feature-50 | Glycosylation | processing |
| feature-51 | Glycosylation | processing |
| feature-52 | Glycosylation | processing |
| feature-53 | Glycosylation | processing |
| feature-54 | Glycosylation | processing |
| feature-55 | Glycosylation | processing |
| feature-56 | Glycosylation | processing |
| feature-57 | Glycosylation | processing |
| feature-58 | Disulfide bond | processing |
| feature-59 | Disulfide bond | processing |
| feature-60 | Disulfide bond | processing |
| feature-61 | Disulfide bond | processing |
| feature-62 | Disulfide bond | processing |
| feature-63 | Disulfide bond | processing |
| feature-64 | Disulfide bond | processing |
| feature-65 | Disulfide bond | processing |
| feature-66 | Disulfide bond | processing |
| feature-67 | Disulfide bond | processing |
| feature-68 | Disulfide bond | processing |
| feature-69 | Disulfide bond | processing |
| feature-70 | Disulfide bond | processing |
| feature-71 | Disulfide bond | processing |
| feature-72 | Disulfide bond | processing |
| feature-73 | Disulfide bond | processing |
| feature-74 | Disulfide bond | processing |
| feature-75 | Disulfide bond | processing |
| feature-76 | Disulfide bond | processing |
| feature-77 | Disulfide bond | processing |
| feature-78 | Disulfide bond | processing |
| feature-79 | Disulfide bond | processing |
| feature-80 | Disulfide bond | processing |
| feature-81 | Disulfide bond | processing |
| feature-82 | Disulfide bond | processing |
| feature-83 | Cross-link | processing |
| feature-84 | Cross-link | processing |
| feature-85 | Cross-link | processing |
| feature-86 | Cross-link | processing |
| feature-87 | Cross-link | processing |
| feature-88 | Cross-link | processing |
| feature-89 | Cross-link | processing |
| feature-90 | Cross-link | processing |
| feature-91 | Alternative sequence | sequence |
| feature-92 | Alternative sequence | sequence |
| feature-93 | Alternative sequence | sequence |
| feature-94 | Alternative sequence | sequence |
| feature-95 | Alternative sequence | sequence |
| feature-96 | Alternative sequence | sequence |
| feature-97 | Natural variant | disease |
| feature-98 | Natural variant | disease |
| feature-99 | Natural variant | disease |
| feature-100 | Natural variant | disease |
| feature-101 | Natural variant | disease |
| feature-102 | Natural variant | disease |
| feature-103 | Natural variant | disease |
| feature-104 | Natural variant | disease |
| feature-105 | Natural variant | disease |
| feature-106 | Natural variant | disease |
| feature-107 | Natural variant | disease |
| feature-108 | Natural variant | disease |
| feature-109 | Natural variant | disease |
| feature-110 | Natural variant | disease |
| feature-111 | Natural variant | disease |
| feature-112 | Natural variant | disease |
| feature-113 | Natural variant | disease |
| feature-114 | Natural variant | disease |
| feature-115 | Natural variant | disease |
| feature-116 | Natural variant | disease |
| feature-117 | Natural variant | disease |
| feature-118 | Natural variant | disease |
| feature-119 | Natural variant | disease |
| feature-120 | Natural variant | disease |
| feature-121 | Natural variant | disease |
| feature-122 | Natural variant | disease |
| feature-123 | Natural variant | disease |
| feature-124 | Natural variant | disease |
| feature-125 | Natural variant | disease |
| feature-126 | Natural variant | disease |
| feature-127 | Natural variant | disease |
| feature-128 | Natural variant | disease |
| feature-129 | Natural variant | disease |
| feature-130 | Natural variant | disease |
| feature-131 | Natural variant | disease |
| feature-132 | Natural variant | disease |
| feature-133 | Natural variant | disease |
| feature-134 | Natural variant | disease |
| feature-135 | Natural variant | disease |
| feature-136 | Natural variant | disease |
| feature-137 | Mutagenesis | disease |
| feature-138 | Mutagenesis | disease |
| feature-139 | Mutagenesis | disease |
| feature-140 | Mutagenesis | disease |
| feature-141 | Mutagenesis | disease |
| feature-142 | Mutagenesis | disease |
| feature-143 | Mutagenesis | disease |
| feature-144 | Mutagenesis | disease |
| feature-145 | Mutagenesis | disease |
| feature-146 | Mutagenesis | disease |
| feature-147 | Mutagenesis | disease |
| feature-148 | Mutagenesis | disease |
| feature-149 | Mutagenesis | disease |
| feature-150 | Mutagenesis | disease |
| feature-151 | Mutagenesis | disease |
| feature-152 | Mutagenesis | disease |
| feature-153 | Mutagenesis | disease |
| feature-154 | Mutagenesis | disease |
| feature-155 | Mutagenesis | disease |
| feature-156 | Mutagenesis | disease |
| feature-157 | Mutagenesis | disease |
| feature-158 | Mutagenesis | disease |
| feature-159 | Mutagenesis | disease |
| feature-160 | Mutagenesis | disease |
| feature-161 | Mutagenesis | disease |
| feature-162 | Mutagenesis | disease |
| feature-163 | Mutagenesis | disease |
| feature-164 | Mutagenesis | disease |
| feature-165 | Mutagenesis | disease |
| feature-166 | Mutagenesis | disease |
| feature-167 | Mutagenesis | disease |
| feature-168 | Mutagenesis | disease |
| feature-169 | Mutagenesis | disease |
| feature-170 | Mutagenesis | disease |
| feature-171 | Mutagenesis | disease |
| feature-172 | Mutagenesis | disease |
| feature-173 | Mutagenesis | disease |
| feature-174 | Sequence conflict | sequence |
| feature-175 | Beta strand | sequence |
| feature-176 | Helix | sequence |
| feature-177 | Beta strand | sequence |
| feature-178 | Helix | sequence |
| feature-179 | Beta strand | sequence |
| feature-180 | Beta strand | sequence |
| feature-181 | Beta strand | sequence |
| feature-182 | Helix | sequence |
| feature-183 | Turn | sequence |
| feature-184 | Beta strand | sequence |
| feature-185 | Beta strand | sequence |
| feature-186 | Beta strand | sequence |
| feature-187 | Helix | sequence |
| feature-188 | Helix | sequence |
| feature-189 | Helix | sequence |
| feature-190 | Beta strand | sequence |
| feature-191 | Helix | sequence |
| feature-192 | Helix | sequence |
| feature-193 | Beta strand | sequence |
| feature-194 | Beta strand | sequence |
| feature-195 | Beta strand | sequence |
| feature-196 | Beta strand | sequence |
| feature-197 | Helix | sequence |
| feature-198 | Beta strand | sequence |
| feature-199 | Beta strand | sequence |
| feature-200 | Turn | sequence |
| feature-201 | Beta strand | sequence |
| feature-202 | Beta strand | sequence |
| feature-203 | Beta strand | sequence |
| feature-204 | Turn | sequence |
| feature-205 | Beta strand | sequence |
| feature-206 | Beta strand | sequence |
| feature-207 | Beta strand | sequence |
| feature-208 | Turn | sequence |
| feature-209 | Beta strand | sequence |
| feature-210 | Beta strand | sequence |
| feature-211 | Beta strand | sequence |
| feature-212 | Beta strand | sequence |
| feature-213 | Beta strand | sequence |
| feature-214 | Beta strand | sequence |
| feature-215 | Beta strand | sequence |
| feature-216 | Beta strand | sequence |
| feature-217 | Turn | sequence |
| feature-218 | Helix | sequence |
| feature-219 | Beta strand | sequence |
| feature-220 | Turn | sequence |
| feature-221 | Helix | sequence |
| feature-222 | Beta strand | sequence |
| feature-223 | Beta strand | sequence |
| feature-224 | Helix | sequence |
| feature-225 | Turn | sequence |
| feature-226 | Helix | sequence |
| feature-227 | Helix | sequence |
| feature-228 | Beta strand | sequence |
| feature-229 | Beta strand | sequence |
| feature-230 | Helix | sequence |
| feature-231 | Turn | sequence |
| feature-232 | Beta strand | sequence |
| feature-233 | Beta strand | sequence |
| feature-234 | Helix | sequence |
| feature-235 | Helix | sequence |
| feature-236 | Beta strand | sequence |
| feature-237 | Beta strand | sequence |
| feature-238 | Helix | sequence |
| feature-239 | Beta strand | sequence |
| feature-240 | Beta strand | sequence |
| feature-241 | Helix | sequence |
| feature-242 | Beta strand | sequence |
| feature-243 | Beta strand | sequence |
| feature-244 | Beta strand | sequence |
| feature-245 | Beta strand | sequence |
| feature-246 | Beta strand | sequence |
| feature-247 | Beta strand | sequence |
| feature-248 | Beta strand | sequence |
| feature-249 | Beta strand | sequence |
| feature-250 | Beta strand | sequence |
| feature-251 | Beta strand | sequence |
| feature-252 | Beta strand | sequence |
| feature-253 | Beta strand | sequence |
| feature-254 | Beta strand | sequence |
| feature-255 | Beta strand | sequence |
| feature-256 | Beta strand | sequence |
| feature-257 | Beta strand | sequence |
| feature-258 | Helix | sequence |
| feature-259 | Beta strand | sequence |
| feature-260 | Helix | sequence |
| feature-261 | Beta strand | sequence |
| feature-262 | Helix | sequence |
| feature-263 | Helix | sequence |
| feature-264 | Beta strand | sequence |
| feature-265 | Beta strand | sequence |
| feature-266 | Beta strand | sequence |
| feature-267 | Helix | sequence |
| feature-268 | Beta strand | sequence |
| feature-269 | Beta strand | sequence |
| feature-270 | Turn | sequence |
| feature-271 | Beta strand | sequence |
| feature-272 | Helix | sequence |
| feature-273 | Helix | sequence |
| feature-274 | Beta strand | sequence |
| feature-275 | Beta strand | sequence |
| feature-276 | Beta strand | sequence |
| feature-277 | Beta strand | sequence |
| feature-278 | Beta strand | sequence |
| feature-279 | Helix | sequence |
| feature-280 | Helix | sequence |
| feature-281 | Helix | sequence |
| feature-282 | Beta strand | sequence |
| feature-283 | Helix | sequence |
| feature-284 | Beta strand | sequence |
| feature-285 | Beta strand | sequence |
| feature-286 | Helix | sequence |
| feature-287 | Turn | sequence |
| feature-288 | Helix | sequence |
| feature-289 | Beta strand | sequence |
| feature-290 | Helix | sequence |
| feature-291 | Helix | sequence |
| feature-292 | Helix | sequence |
| feature-293 | Beta strand | sequence |
| feature-294 | Helix | sequence |
| feature-295 | Turn | sequence |
| feature-296 | Turn | sequence |
| feature-297 | Helix | sequence |
| feature-298 | Helix | sequence |
| feature-299 | Helix | sequence |
| feature-300 | Beta strand | sequence |
| feature-301 | Helix | sequence |
| feature-302 | Beta strand | sequence |
| feature-303 | Helix | sequence |
| feature-304 | Helix | sequence |
| feature-305 | Helix | sequence |
| feature-306 | Helix | sequence |
| feature-307 | Helix | sequence |
| feature-308 | Turn | sequence |
| feature-309 | Turn | sequence |
| feature-310 | Beta strand | sequence |
| feature-311 | Helix | sequence |
| feature-312 | Beta strand | sequence |
| feature-313 | Beta strand | sequence |