PROTEIN OVERVIEW

ERBB2Receptor tyrosine-protein kinase erbB-2

P04626Homo sapiensReviewed · UniProt

Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding.

Sequence1255 aa

Source mass137.91 kDa

Recorded PDB entries63

Isoforms listed6

UniProt locations Cell membrane · Cell projection, ruffle membrane · Early endosome · Cytoplasm, perinuclear region · Nucleus · Cytoplasm

Function

Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor.

Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane.

In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization

Curator inference

Evidence & references

ECO:0000305

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization"
    }
  ],
  "commentType": "FUNCTION"
}

In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC.

Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth

Experimental evidence 3 publications

Evidence & references

ECO:0000269 PubMed:10358079 ↗
ECO:0000269 PubMed:15380516 ↗
ECO:0000269 PubMed:21555369 ↗

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10358079"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15380516"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21555369"
        }
      ],
      "value": "In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth"
    }
  ],
  "commentType": "FUNCTION"
}

Additional functional context

Isoform 2

Produced by alternative initiation at Met-611 of isoform 1

Curator inference

Evidence & references

ECO:0000305

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Produced by alternative initiation at Met-611 of isoform 1"
    }
  ],
  "commentType": "MISCELLANEOUS",
  "molecule": "Isoform 2"
}

Isoform 3

Produced by alternative initiation at Met-687 of isoform 1

Curator inference

Evidence & references

ECO:0000305

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Produced by alternative initiation at Met-687 of isoform 1"
    }
  ],
  "commentType": "MISCELLANEOUS",
  "molecule": "Isoform 3"
}

Isoform 4

Produced by alternative splicing of isoform 1

Curator inference

Evidence & references

ECO:0000305

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Produced by alternative splicing of isoform 1"
    }
  ],
  "commentType": "MISCELLANEOUS",
  "molecule": "Isoform 4"
}

Catalytic activity

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

Evidence

ECO:0000255 PROSITE-ProRule:PRU10028
ECO:0000269 PubMed:21454582 ↗

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": "21454582"
      }
    ]
  }
}

Activity regulation

Activated by dimerization. Not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity

Experimental evidence 2 publications

Evidence & references

ECO:0000269 PubMed:18719096 ↗
ECO:0000269 PubMed:21454582 ↗

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18719096"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21454582"
        }
      ],
      "value": "Activated by dimerization. Not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity"
    }
  ],
  "commentType": "ACTIVITY REGULATION"
}

GO functions & biological processes

cell surface receptor signaling pathwayacts upstream of or withinUniProtKB:P04626

GO:0007166 · evidence & context

ECO:0000314 PMID:9685399 ↗ IDA · MGI · 20101102
qualifier: acts_upstream_of_or_within

ERBB2-EGFR signaling pathwayacts upstream of or withinUniProtKB:P04626

GO:0038134 · evidence & context

ECO:0000314 PMID:8702723 ↗ IDA · MGI · 20220307
qualifier: acts_upstream_of_or_within

growth factor bindingcontributes toUniProtKB:P04626

GO:0019838 · evidence & context

ECO:0000314 PMID:7514177 ↗ IDA · BHF-UCL · 20080226
qualifier: contributes_to

RNA polymerase I core bindingenablesUniProtKB:P04626

GO:0001042 · evidence & context

ECO:0000314 PMID:21555369 ↗ IDA · UniProt · 20110824
qualifier: enables

protein kinase activityenablesUniProtKB:P04626

GO:0004672 · evidence & context

ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR001245"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR008266"}]}]

All recorded function and process assertions (62)

protein tyrosine kinase activityenablesUniProtKB:P04626

GO:0004713 · evidence & context

ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR020635"}]}, {"connectedXrefs": [{"db": "RHEA", "id": "10596"}]}]
ECO:0000314 PMID:12000754 ↗ IDA · UniProt · 20191129
qualifier: enables
ECO:0000269 PMID:21454582 ↗ EXP · UniProt · 20251027
qualifier: enables
ECO:0000304 Reactome:R-HSA-373750 TAS · Reactome · 20240809
qualifier: enables

protein tyrosine kinase activityenablesUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0004713 · evidence & context

ECO:0000314 PMID:7556068 ↗ IDA · BHF-UCL · 20230822
qualifier: enables
extensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860", "relation": "has_input"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626", "relation": "has_input"}]}]

transmembrane receptor protein tyrosine kinase activityenablesUniProtKB:P04626

GO:0004714 · evidence & context

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003366"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0003733"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0010389"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0040505"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0283499"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0285896"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:104771"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:107381"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1339758"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:1345277"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95522"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95524"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95558"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95561"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96433"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96575"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96677"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96683"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96969"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:97384"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:97531"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:97902"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:99654"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN001230349"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2611"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2612"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2621"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2869"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2917"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2965"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3214"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3284"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3285"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620144"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620714"}]}, {"connectedXrefs": [{"db": "RGD", "id": "621737"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "O73798"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04629"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P07333"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P08069"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P09619"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P11362"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P14616"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P17948"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21709"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21802"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P22455"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P22607"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P29317"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P29376"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35916"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35968"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P54760"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q08345"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16832"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q91987"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9PVZ4"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00000289"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00002299"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00006868"}]}, {"connectedXrefs": [{"db": "ZFIN", "id": "ZDB-GENE-980526-255"}]}]
ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027626"}]}, {"connectedXrefs": [{"db": "EC", "id": "2.7.10.1"}]}]
ECO:0000314 PMID:7514177 ↗ IDA · BHF-UCL · 20080226
qualifier: enables

transmembrane signaling receptor activityenablesUniProtKB:P04626

GO:0004888 · evidence & context

ECO:0000314 PMID:7514177 ↗ IDA · BHF-UCL · 20080226
qualifier: enables

signaling receptor bindingenablesUniProtKB:P04626

GO:0005102 · evidence & context

ECO:0000353 PMID:7556068 ↗ IPI · BHF-UCL · 20230822
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]

protein bindingenablesUniProtKB:P04626

GO:0005515 · evidence & context

ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:10572067 ↗ IPI · UniProt · 20060227
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
ECO:0000353 PMID:10572067 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
ECO:0000353 PMID:10805725 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00750"}]}]
ECO:0000353 PMID:11940572 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
ECO:0000353 PMID:12061724 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14451"}]}]
ECO:0000353 PMID:12122014 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42679"}]}]
ECO:0000353 PMID:12975581 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14451"}]}]
ECO:0000353 PMID:15282549 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
ECO:0000353 PMID:15345710 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
ECO:0000353 PMID:15520177 ↗ IPI · UniProt · 20090403
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96EY1-1"}]}]
ECO:0000353 PMID:15520177 ↗ IPI · UniProt · 20090403
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96EY1-2"}]}]
ECO:0000353 PMID:15657067 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:15899872 ↗ IPI · UniProt · 20221220
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15262"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00213"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00459"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O15524"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43639"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75791"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75815"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00519"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P09769"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16885"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P19174"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20936"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23458"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P35568"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42224"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42679"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42684"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P43405"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46109"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P52735"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P98077"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q08881"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13387"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14451"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q63HR2"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q68CZ2"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q7KZ85"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q7Z7G1"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8TEW6"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92529"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92569"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92625"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96D37"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99704"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9H6Q3"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NP31"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9NSE2"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQF2"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y490"}]}]
ECO:0000353 PMID:16314522 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14980"}]}]
ECO:0000353 PMID:16516204 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:16767099 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
ECO:0000353 PMID:16843263 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:16843263 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:16843263 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
ECO:0000353 PMID:16843263 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:17426253 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:18719096 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13882"}]}]
ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08575"}]}]
ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23467"}]}]
ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P26045"}]}]
ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05209"}]}]
ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12913"}]}]
ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15262"}]}]
ECO:0000353 PMID:19167335 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16827"}]}]
ECO:0000353 PMID:19372587 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
ECO:0000353 PMID:19411071 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:19650109 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:19933325 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q93034"}]}]
ECO:0000353 PMID:20010870 ↗ IPI · UniProt · 20150806
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75131"}]}]
ECO:0000353 PMID:20227043 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:20558745 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
ECO:0000353 PMID:20650008 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
ECO:0000353 PMID:20700126 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q13882"}]}]
ECO:0000353 PMID:21075308 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P12931"}]}]
ECO:0000353 PMID:21075308 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:21075308 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
ECO:0000353 PMID:21203579 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:21203579 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:21203579 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
ECO:0000353 PMID:21255571 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O95980"}]}]
ECO:0000353 PMID:21278786 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:21278786 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:21278786 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
ECO:0000353 PMID:21376233 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q05209"}]}]
ECO:0000353 PMID:21724847 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P46940"}]}]
ECO:0000353 PMID:21840311 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y316"}]}]
ECO:0000353 PMID:22589551 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75367-3"}]}]
ECO:0000353 PMID:22733765 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:22806884 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:22939624 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
ECO:0000353 PMID:23436906 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:23436906 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:23680147 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:23688700 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:23723069 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96JA1"}]}]
ECO:0000353 PMID:23866081 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:23866081 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:23995768 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
ECO:0000353 PMID:23995768 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P14625"}]}]
ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P11021"}]}]
ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16543"}]}]
ECO:0000353 PMID:24189400 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
ECO:0000353 PMID:24412244 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P20936"}]}]
ECO:0000353 PMID:24557338 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:24557338 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:24557338 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
ECO:0000353 PMID:24658140 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
ECO:0000353 PMID:24815698 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P06241"}]}]
ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31948"}]}]
ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16543"}]}]
ECO:0000353 PMID:25036637 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9HB71"}]}]
ECO:0000353 PMID:25081058 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99952"}]}]
ECO:0000353 PMID:25081058 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99952-1"}]}]
ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75791"}]}]
ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}]
ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P16885"}]}]
ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:25241761 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P42224"}]}]
ECO:0000353 PMID:25326665 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:25640309 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
ECO:0000353 PMID:26517842 ↗ IPI · UniProt · 20170102
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
ECO:0000353 PMID:26517842 ↗ IPI · UniProt · 20170102
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
ECO:0000353 PMID:28065597 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15256"}]}]
ECO:0000353 PMID:31862538 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P10599"}]}]
ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P11021"}]}]
ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P31948"}]}]
ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P84085"}]}]
ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96NW7"}]}]
ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9HB71"}]}]
ECO:0000353 PMID:31980649 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UQF2"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O00459"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O14980"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P07900"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P08238"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P11021"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P27986"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P29353"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62993"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q16543"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92569"}]}]
ECO:0000353 PMID:35384245 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UJM3"}]}]
ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O43791"}]}]
ECO:0000353 PMID:35512704 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q06124"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "A4D2P6"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75970"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P26045"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P78352"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q02410"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q12959"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14160"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15700"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q5T2W1"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q68DX3"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86UL8"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q86UT5"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8N448"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8NI35"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q8TBB1"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q92796"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96NW7"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q96QZ7"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q99767"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9C0E4"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9P202"}]}]
ECO:0000353 PMID:36115835 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q9Y3R0"}]}]
ECO:0000353 PMID:36931259 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62258"}]}]
ECO:0000353 PMID:38884001 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P10599"}]}]
ECO:0000353 PMID:38884001 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P23458"}]}]
ECO:0000353 PMID:38884001 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P62258"}]}]
ECO:0000353 PMID:38884001 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P84085"}]}]
ECO:0000353 PMID:7556068 ↗ IPI · BHF-UCL · 20230822
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:7592681 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000353 PMID:7592681 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q02297-7"}]}]
ECO:0000353 PMID:9079677 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14451"}]}]
ECO:0000353 PMID:9705354 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P15309"}]}]

protein bindingenablesUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0005515 · evidence & context

ECO:0000353 PMID:11940572 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
ECO:0000353 PMID:16273093 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
ECO:0000353 PMID:19372587 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
ECO:0000353 PMID:20876300 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P40763"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]
ECO:0000353 PMID:21555369 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O95602"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}]

protein bindingenablesUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0005515 · evidence & context

ECO:0000353 PMID:16314522 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P49792"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]

protein bindingenablesUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0005515 · evidence & context

ECO:0000353 PMID:16314522 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q14974"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005635", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0010008", "relation": "occurs_in"}]}]

protein bindingenablesUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0005515 · evidence & context

ECO:0000353 PMID:16314522 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q15075"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
ECO:0000353 PMID:21555369 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P60709"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
ECO:0000353 PMID:22589551 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "O75367"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]
ECO:0000353 PMID:38884001 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P60709"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0005634", "relation": "occurs_in"}]}, {"connectedXrefs": [{"db": "GO", "id": "0005737", "relation": "occurs_in"}]}]

protein bindingenablesUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0005515 · evidence & context

ECO:0000353 PMID:22279592 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P98172"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0016020", "relation": "occurs_in"}]}]
ECO:0000353 PMID:33961781 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P98172"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0016020", "relation": "occurs_in"}]}]

ATP bindingenablesUniProtKB:P04626

GO:0005524 · evidence & context

ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR000719"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}, {"connectedXrefs": [{"db": "InterPro", "id": "IPR017441"}]}]

coreceptor activityenablesUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0015026 · evidence & context

ECO:0000250 GO_REF:0000024 ISS · BHF-UCL · 20230823
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}]
extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000062", "relation": "occurs_in"}, {"db": "GO", "id": "0071526", "relation": "part_of"}, {"db": "UniProtKB", "id": "O43157", "relation": "has_input"}]}]

coreceptor activityenablesUniProtKB:P04626

GO:0015026 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

receptor tyrosine kinase bindingenablesUniProtKB:P04626

GO:0030971 · evidence & context

ECO:0000353 PMID:7556068 ↗ IPI · BHF-UCL · 20230822
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]

identical protein bindingenablesUniProtKB:P04626

GO:0042802 · evidence & context

ECO:0000353 PMID:12000754 ↗ IPI · UniProt · 20191129
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:16843263 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:17148612 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:19650109 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:21203579 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:21255571 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:21480528 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:22733765 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000353 PMID:23436906 ↗ IPI · IntAct · 20260725
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]

ErbB-3 class receptor bindingenablesUniProtKB:P04626

GO:0043125 · evidence & context

ECO:0000353 PMID:12000754 ↗ IPI · UniProt · 20191129
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]
ECO:0000304 PMID:9590694 ↗ TAS · PINC · 20040308
qualifier: enables

protein heterodimerization activityenablesUniProtKB:P04626

GO:0046982 · evidence & context

ECO:0000353 PMID:7556068 ↗ IPI · BHF-UCL · 20080226
qualifier: enables
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}]

protein phosphorylationinvolved inUniProtKB:P04626

GO:0006468 · evidence & context

ECO:0000304 PMID:10851066 ↗ TAS · PINC · 20030904
qualifier: involved_in

signal transductioninvolved inUniProtKB:P04626

GO:0007165 · evidence & context

ECO:0000314 PMID:10572067 ↗ IDA · UniProt · 20060227
qualifier: involved_in

enzyme-linked receptor protein signaling pathwayinvolved inUniProtKB:P04626

GO:0007167 · evidence & context

ECO:0000304 PMID:9590694 ↗ TAS · PINC · 20030904
qualifier: involved_in

cell surface receptor protein tyrosine kinase signaling pathwayinvolved inUniProtKB:P04626

GO:0007169 · evidence & context

ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}]
ECO:0000314 PMID:7514177 ↗ IDA · BHF-UCL · 20080226
qualifier: involved_in

cell surface receptor protein tyrosine kinase signaling pathwayinvolved inUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0007169 · evidence & context

ECO:0000314 PMID:7556068 ↗ IDA · BHF-UCL · 20230822
qualifier: involved_in
extensions: [{"connectedXrefs": [{"db": "UniProtKB", "id": "Q02297-1", "relation": "has_input"}]}]

epidermal growth factor receptor signaling pathwayinvolved inUniProtKB:P04626

GO:0007173 · evidence & context

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20240924
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "69323"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00002299"}]}]

cell population proliferationinvolved inUniProtKB:P04626

GO:0008283 · evidence & context

ECO:0000314 PMID:36949068 ↗ IDA · UniProt · 20240627
qualifier: involved_in

Schwann cell developmentinvolved inUniProtKB:P04626

GO:0014044 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

peptidyl-tyrosine phosphorylationinvolved inUniProtKB:P04626

GO:0018108 · evidence & context

ECO:0000314 PMID:12000754 ↗ IDA · UniProt · 20191129
qualifier: involved_in

neuron differentiationinvolved inUniProtKB:P04626

GO:0030182 · evidence & context

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:104771"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "RGD", "id": "69323"}]}, {"connectedXrefs": [{"db": "ZFIN", "id": "ZDB-GENE-031118-121"}]}]

positive regulation of cell growthinvolved inUniProtKB:P04626

GO:0030307 · evidence & context

ECO:0000315 PMID:21555369 ↗ IMP · UniProt · 20110824
qualifier: involved_in

regulation of microtubule-based processinvolved inUniProtKB:P04626

GO:0032886 · evidence & context

ECO:0000314 PMID:20937854 ↗ IDA · UniProt · 20110501
qualifier: involved_in

positive regulation of Rho protein signal transductioninvolved inUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0035025 · evidence & context

ECO:0000250 GO_REF:0000024 ISS · BHF-UCL · 20230823
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}]
extensions: [{"connectedXrefs": [{"db": "GO", "id": "0071526", "relation": "part_of"}]}]

positive regulation of Rho protein signal transductioninvolved inUniProtKB:P04626

GO:0035025 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

intracellular signal transductioninvolved inUniProtKB:P04626

GO:0035556 · evidence & context

ECO:0000314 PMID:19372587 ↗ IDA · UniProt · 20181025
qualifier: involved_in

ERBB signaling pathwayinvolved inUniProtKB:P04626

GO:0038127 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

ERBB2 signaling pathwayinvolved inUniProtKB:P04626

GO:0038128 · evidence & context

ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00087673"}]}]

ERBB2-ERBB3 signaling pathwayinvolved inUniProtKB:P04626

GO:0038133 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

ERBB2-EGFR signaling pathwayinvolved inUniProtKB:P04626

GO:0038134 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]
ECO:0000314 PMID:8702723 ↗ IDA · MGI · 20220314
qualifier: involved_in

ERBB2-ERBB4 signaling pathwayinvolved inUniProtKB:P04626

GO:0038135 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

wound healinginvolved inUniProtKB:P04626

GO:0042060 · evidence & context

ECO:0000314 PMID:12646923 ↗ IDA · BHF-UCL · 20080227
qualifier: involved_in

regulation of cell population proliferationinvolved inUniProtKB:P04626

GO:0042127 · evidence & context

ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027546"}]}]

negative regulation of apoptotic processinvolved inUniProtKB:P04626

GO:0043066 · evidence & context

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:104771"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95411"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620486"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]

positive regulation of MAP kinase activityinvolved inUniProtKB:P04626

GO:0043406 · evidence & context

ECO:0000314 PMID:10572067 ↗ IDA · UniProt · 20060227
qualifier: involved_in

positive regulation of MAPK cascadeinvolved inUniProtKB:P04626

GO:0043410 · evidence & context

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20250904
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003731"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95411"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}]
ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00027228"}]}]

phosphatidylinositol 3-kinase/protein kinase B signal transductioninvolved inUniProtKB:P04626

GO:0043491 · evidence & context

ECO:0000314 PMID:7556068 ↗ IDA · BHF-UCL · 20080226
qualifier: involved_in

positive regulation of translationinvolved inUniProtKB:P04626

GO:0045727 · evidence & context

ECO:0000315 PMID:21555369 ↗ IMP · UniProt · 20110824
qualifier: involved_in

regulation of angiogenesisinvolved inUniProtKB:P04626

GO:0045765 · evidence & context

ECO:0000303 PMID:15609325 ↗ NAS · UniProt · 20050527
qualifier: involved_in

positive regulation of cell adhesioninvolved inUniProtKB:P04626

GO:0045785 · evidence & context

ECO:0000314 PMID:7556068 ↗ IDA · BHF-UCL · 20080226
qualifier: involved_in

positive regulation of transcription by RNA polymerase Iinvolved inUniProtKB:P04626

GO:0045943 · evidence & context

ECO:0000315 PMID:21555369 ↗ IMP · UniProt · 20110824
qualifier: involved_in

positive regulation of JNK cascadeinvolved inUniProtKB:P04626

GO:0046330 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

positive regulation of epithelial cell proliferationinvolved inUniProtKB:P04626

GO:0050679 · evidence & context

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20240924
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620486"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}]
ECO:0000314 PMID:10572067 ↗ IDA · UniProt · 20060227
qualifier: involved_in

regulation of ERK1 and ERK2 cascadeinvolved inUniProtKB:P04626

GO:0070372 · evidence & context

ECO:0000315 PMID:16314522 ↗ IMP · UniProt · 20110823
qualifier: involved_in

cellular response to growth factor stimulusinvolved inUniProtKB:P04626

GO:0071363 · evidence & context

ECO:0000314 PMID:20010870 ↗ IDA · UniProt · 20150806
qualifier: involved_in

cellular response to epidermal growth factor stimulusinvolved inUniProtKB:P04626

GO:0071364 · evidence & context

ECO:0000315 PMID:27134172 ↗ IMP · UniProt · 20160602
qualifier: involved_in

semaphorin-plexin signaling pathwayinvolved inUniProtKB:P04626 · Context-qualified assertion; see evidence

GO:0071526 · evidence & context

ECO:0000250 GO_REF:0000024 ISS · BHF-UCL · 20230823
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}]
extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000062", "relation": "occurs_in"}]}]

semaphorin-plexin signaling pathwayinvolved inUniProtKB:P04626

GO:0071526 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

positive regulation of protein targeting to membraneinvolved inUniProtKB:P04626

GO:0090314 · evidence & context

ECO:0000314 PMID:20010870 ↗ IDA · UniProt · 20150806
qualifier: involved_in

neurotransmitter receptor localization to postsynaptic specialization membraneinvolved inUniProtKB:P04626

GO:0099645 · evidence & context

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: involved_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

Names & Taxonomy

Recommended name: Receptor tyrosine-protein kinase erbB-2
Gene: ERBB2
Accession / entry: P04626 · ERBB2_HUMAN
Species: Homo sapiens · NCBI 9606
Recorded aliases: HER2 · MLN 19 · MLN19 · Metastatic lymph node gene 19 protein · NEU · NGL · Proto-oncogene Neu · Proto-oncogene c-ErbB-2 · Tyrosine kinase-type cell surface receptor HER2 · p185erbB2

Full taxonomy & recorded names

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

{
  "names": {
    "recommendedName": {
      "fullName": {
        "value": "Receptor tyrosine-protein kinase erbB-2"
      },
      "ecNumbers": [
        {
          "value": "2.7.10.1"
        }
      ]
    },
    "alternativeNames": [
      {
        "fullName": {
          "value": "Metastatic lymph node gene 19 protein"
        },
        "shortNames": [
          {
            "value": "MLN 19"
          }
        ]
      },
      {
        "fullName": {
          "value": "Proto-oncogene Neu"
        }
      },
      {
        "fullName": {
          "value": "Proto-oncogene c-ErbB-2"
        }
      },
      {
        "fullName": {
          "value": "Tyrosine kinase-type cell surface receptor HER2"
        }
      },
      {
        "fullName": {
          "value": "p185erbB2"
        }
      }
    ],
    "cdAntigenNames": [
      {
        "value": "CD340"
      }
    ],
    "flag": "Precursor"
  },
  "genes": [
    {
      "geneName": {
        "value": "ERBB2"
      },
      "synonyms": [
        {
          "value": "HER2"
        },
        {
          "value": "MLN19"
        },
        {
          "value": "NEU"
        },
        {
          "value": "NGL"
        }
      ]
    }
  ]
}

Subcellular Location

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

Cell membraneReported location

Single-pass type I membrane protein

Internalized from the cell membrane in response to EGF stimulation

UniProt

Experimental evidence 1 publication

Evidence & references

ECO:0000269 PubMed:32381043 ↗

Cell projection, ruffle membraneReported location

Single-pass type I membrane protein

Internalized from the cell membrane in response to EGF stimulation

UniProt

Experimental evidence 1 publication

Evidence & references

ECO:0000269 PubMed:34380438 ↗

Cell membraneReported location

Isoform 1; Single-pass type I membrane protein

Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in VPS35-positive endosome-to-TGN retrograde vesicles ^[38]

UniProt

Experimental evidence 2 publications

Evidence & references

ECO:0000269 PubMed:31138794 ↗
ECO:0000269 PubMed:33497358 ↗

Early endosomeReported location

Isoform 1

Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in VPS35-positive endosome-to-TGN retrograde vesicles ^[38]

UniProt

Experimental evidence 1 publication

Evidence & references

ECO:0000269 PubMed:31138794 ↗

Cytoplasm, perinuclear regionReported location

Isoform 1

Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in VPS35-positive endosome-to-TGN retrograde vesicles ^[38]

UniProt

Evidence & references

No separate evidence record is supplied for this statement.

NucleusReported location

Isoform 1

Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in VPS35-positive endosome-to-TGN retrograde vesicles ^[38]

UniProt

Evidence & references

No separate evidence record is supplied for this statement.

CytoplasmReported location

Isoform 2

UniProt

Evidence & references

No separate evidence record is supplied for this statement.

NucleusReported location

Isoform 2

UniProt

Evidence & references

No separate evidence record is supplied for this statement.

All recorded location assertions (33)

CytoplasmReported location

Isoform 3

UniProt

Evidence & references

No separate evidence record is supplied for this statement.

NucleusReported location

Isoform 3

UniProt

Evidence & references

No separate evidence record is supplied for this statement.

plasma membraneis active in

Evidence & references

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529
qualifier: is_active_in
withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0003366"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0010389"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0011829"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0015380"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0032006"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0285896"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:101766"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:103581"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95524"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95559"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96433"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96575"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96677"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96683"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:96840"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:97384"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:99614"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:99654"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN001230349"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2252"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2869"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2917"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3211"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3213"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3284"}]}, {"connectedXrefs": [{"db": "RGD", "id": "3285"}]}, {"connectedXrefs": [{"db": "RGD", "id": "619855"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620144"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620568"}]}, {"connectedXrefs": [{"db": "RGD", "id": "620713"}]}, {"connectedXrefs": [{"db": "RGD", "id": "69323"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "G1K218"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "O15146"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P08069"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P09619"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P10721"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P11362"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P17948"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21709"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21802"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P22455"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P22607"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35590"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35968"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01973"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q05688"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q08345"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q12866"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16832"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q91987"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9PVZ4"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q9UM73"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00000289"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00000898"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00002299"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00003007"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00006868"}]}, {"connectedXrefs": [{"db": "ZFIN", "id": "ZDB-GENE-070209-277"}]}]

basal plasma membraneis active in

Evidence & references

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20210227
qualifier: is_active_in
withFrom: [{"connectedXrefs": [{"db": "MGI", "id": "MGI:95294"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN000698827"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2543"}]}, {"connectedXrefs": [{"db": "RGD", "id": "2561"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}, {"connectedXrefs": [{"db": "WB", "id": "WBGene00002299"}]}]

neuromuscular junctionis active in

Evidence & references

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: is_active_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

presynaptic membraneis active in

Evidence & references

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: is_active_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

postsynaptic membraneis active in

Evidence & references

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: is_active_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

nucleuslocated in

2 publications

Evidence & references

ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0191"}]}]
ECO:0000314 PMID:16314522 ↗ IDA · UniProt · 20110823
qualifier: located_in
ECO:0000314 PMID:21555369 ↗ IDA · UniProt · 20110824
qualifier: located_in

nucleoplasmlocated in

Evidence & references

ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115
qualifier: located_in

cytoplasmlocated in

Evidence & references

ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00026971"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0086"}]}]

early endosomelocated in

Experimental evidence 1 publication

Evidence & references

ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0094"}]}]
ECO:0000269 PMID:31138794 ↗ EXP · UniProt · 20251027
qualifier: located_in

cytosollocated in

Evidence & references

ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115
qualifier: located_in

plasma membranelocated in

Published statementExperimental evidence 5 publications

Evidence & references

ECO:0000314 GO_REF:0000052 IDA · HPA · 20251115
qualifier: located_in
ECO:0000501 GO_REF:0000120 IEA · UniProt · 20260727
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}, {"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0039"}]}]
ECO:0000303 PMID:12000754 ↗ NAS · UniProt · 20050531
qualifier: located_in
ECO:0000314 PMID:20010870 ↗ IDA · UniProt · 20150806
qualifier: located_in
ECO:0000269 PMID:31138794 ↗ EXP · UniProt · 20251027
qualifier: located_in
ECO:0000269 PMID:32381043 ↗ EXP · UniProt · 20251027
qualifier: located_in
ECO:0000269 PMID:33497358 ↗ EXP · UniProt · 20251027
qualifier: located_in
ECO:0000304 Reactome:R-HSA-1227964 TAS · Reactome · 20130503
qualifier: located_in
ECO:0000304 Reactome:R-HSA-1248694 TAS · Reactome · 20130516
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ECO:0000304 Reactome:R-HSA-1250189 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-1250195 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-1250346 TAS · Reactome · 20130516
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ECO:0000304 Reactome:R-HSA-1250462 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-1306953 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-1306957 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-1306963 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-1306965 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-1306969 TAS · Reactome · 20130516
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ECO:0000304 Reactome:R-HSA-1306972 TAS · Reactome · 20130516
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ECO:0000304 Reactome:R-HSA-1306979 TAS · Reactome · 20130516
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ECO:0000304 Reactome:R-HSA-1358792 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-1358798 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-1918092 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-1918095 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-1963563 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-1963581 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-1963582 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-1963586 TAS · Reactome · 20130508
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ECO:0000304 Reactome:R-HSA-1963589 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-2316434 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-2400009 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-373750 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-416588 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-416594 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-5672965 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-6785636 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-6785648 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-8847995 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-8848005 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-8863804 TAS · Reactome · 20160716
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ECO:0000304 Reactome:R-HSA-8864105 TAS · Reactome · 20160519
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ECO:0000304 Reactome:R-HSA-8864125 TAS · Reactome · 20160716
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ECO:0000304 Reactome:R-HSA-8864466 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-9634390 TAS · Reactome · 20130516
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ECO:0000304 Reactome:R-HSA-9634402 TAS · Reactome · 20130516
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ECO:0000304 Reactome:R-HSA-9634418 TAS · Reactome · 20130516
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ECO:0000304 Reactome:R-HSA-9649393 TAS · Reactome · 20190620
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ECO:0000304 Reactome:R-HSA-9652264 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-9652277 TAS · Reactome · 20130503
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ECO:0000304 Reactome:R-HSA-9664567 TAS · Reactome · 20230322
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ECO:0000304 Reactome:R-HSA-9664588 TAS · Reactome · 20230322
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ECO:0000304 Reactome:R-HSA-9664646 TAS · Reactome · 20230321
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ECO:0000304 Reactome:R-HSA-9664664 TAS · Reactome · 20230321
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ECO:0000304 Reactome:R-HSA-9664918 TAS · Reactome · 20230321
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ECO:0000304 Reactome:R-HSA-9664933 TAS · Reactome · 20230321
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ECO:0000304 Reactome:R-HSA-9664940 TAS · Reactome · 20230321
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ECO:0000304 Reactome:R-HSA-9664950 TAS · Reactome · 20230321
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ECO:0000304 Reactome:R-HSA-9664976 TAS · Reactome · 20230321
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ECO:0000304 Reactome:R-HSA-9665032 TAS · Reactome · 20230318
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ECO:0000304 Reactome:R-HSA-9665034 TAS · Reactome · 20230318
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ECO:0000304 Reactome:R-HSA-9665121 TAS · Reactome · 20230318
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ECO:0000304 Reactome:R-HSA-9665232 TAS · Reactome · 20230318
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ECO:0000304 Reactome:R-HSA-9665278 TAS · Reactome · 20190614
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ECO:0000304 Reactome:R-HSA-9665280 TAS · Reactome · 20190529
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ECO:0000304 Reactome:R-HSA-9665284 TAS · Reactome · 20190529
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ECO:0000304 Reactome:R-HSA-9665286 TAS · Reactome · 20190529
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ECO:0000304 Reactome:R-HSA-9665304 TAS · Reactome · 20190614
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ECO:0000304 Reactome:R-HSA-9665311 TAS · Reactome · 20190529
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ECO:0000304 Reactome:R-HSA-9665315 TAS · Reactome · 20190528
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ECO:0000304 Reactome:R-HSA-9665388 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665389 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665404 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665405 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665406 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665407 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665408 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665409 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665410 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665411 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665412 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665413 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665415 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665416 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665417 TAS · Reactome · 20191111
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ECO:0000304 Reactome:R-HSA-9665696 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665697 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665698 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665699 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665700 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665701 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665702 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665703 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665704 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665705 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665706 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665707 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665708 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665709 TAS · Reactome · 20191108
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ECO:0000304 Reactome:R-HSA-9665726 TAS · Reactome · 20130503
qualifier: located_in
ECO:0000304 Reactome:R-NUL-1248744 TAS · Reactome · 20160519
qualifier: located_in
ECO:0000304 Reactome:R-NUL-1248753 TAS · Reactome · 20130503
qualifier: located_in
ECO:0000304 Reactome:R-NUL-1251923 TAS · Reactome · 20160519
qualifier: located_in
ECO:0000304 Reactome:R-NUL-1251929 TAS · Reactome · 20160519
qualifier: located_in

endosome membranelocated in

1 publication

Evidence & references

ECO:0000314 PMID:16314522 ↗ IDA · UniProt · 20110823
qualifier: located_in

membranelocated in

Published statement 1 publication

Evidence & references

ECO:0000256 GO_REF:0000002 IEA · InterPro · 20260727
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "InterPro", "id": "IPR016245"}]}]
ECO:0000303 PMID:15609325 ↗ NAS · UniProt · 20050527
qualifier: located_in

basolateral plasma membranelocated in

1 publication

Evidence & references

ECO:0000256 GO_REF:0000117 IEA · UniProt · 20260727
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "ARBA", "id": "ARBA00086715"}]}]
ECO:0000314 PMID:12646923 ↗ IDA · BHF-UCL · 20080227
qualifier: located_in

apical plasma membranelocated in

Evidence & references

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

cytoplasmic vesiclelocated in

Evidence & references

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

ruffle membranelocated in

Evidence & references

ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0301"}]}]

myelin sheathlocated in

Evidence & references

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

perinuclear region of cytoplasmlocated in

Evidence & references

ECO:0007322 GO_REF:0000044 IEA · UniProt · 20260727
qualifier: located_in
withFrom: [{"connectedXrefs": [{"db": "UniProtKB-SubCell", "id": "SL-0198"}]}]

semaphorin receptor complexpart of

UniProtKB:P04626 · [{"connectedXrefs": [{"db": "CL", "id": "0000062", "relation": "occurs_in"}]}]

By similarity

Evidence & references

ECO:0000250 GO_REF:0000024 ISS · BHF-UCL · 20241217
qualifier: part_of
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}]
extensions: [{"connectedXrefs": [{"db": "CL", "id": "0000062", "relation": "occurs_in"}]}]

semaphorin receptor complexpart of

Evidence & references

ECO:0000265 GO_REF:0000107 IEA · Ensembl · 20260724
qualifier: part_of
withFrom: [{"connectedXrefs": [{"db": "UniProtKB", "id": "P70424"}]}, {"connectedXrefs": [{"db": "ensembl", "id": "ENSMUSP00000053897"}]}]

ERBB3:ERBB2 complexpart of

1 publication

Evidence & references

ECO:0000314 PMID:12000754 ↗ IDA · UniProt · 20191129
qualifier: part_of

signaling receptor complexpart of

3 publications

Evidence & references

ECO:0000318 GO_REF:0000033 IBA · GO_Central · 20260529
qualifier: part_of
withFrom: [{"connectedXrefs": [{"db": "FB", "id": "FBgn0015380"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0024245"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0033791"}]}, {"connectedXrefs": [{"db": "FB", "id": "FBgn0283499"}]}, {"connectedXrefs": [{"db": "MGI", "id": "MGI:95410"}]}, {"connectedXrefs": [{"db": "PANTHER", "id": "PTN001230349"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "A6QR62"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "O15146"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P00533"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04626"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P04629"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P06213"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P07333"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P07949"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P08069"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P11362"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P14616"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P17948"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P21860"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "P35916"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q01973"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q08345"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q15303"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16288"}]}, {"connectedXrefs": [{"db": "UniProtKB", "id": "Q16620"}]}]
ECO:0000314 PMID:23382219 ↗ IDA · MGI · 20131224
qualifier: part_of
ECO:0000314 PMID:7514177 ↗ IDA · BHF-UCL · 20080226
qualifier: part_of
ECO:0000304 PMID:7556068 ↗ TAS · BHF-UCL · 20080226
qualifier: part_of

Membrane topology 3

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3 recorded rows

Feature	Position	Description	Evidence	Inspect
Topological domain	23–652	Extracellular	Sequence analysis Evidence & references ECO:0000255	No verified residues in this structure
Transmembrane	653–675	Helical	Sequence analysis Evidence & references ECO:0000255	No verified residues in this structure
Topological domain	676–1255	Cytoplasmic	Sequence analysis Evidence & references ECO:0000255	No verified residues in this structure

Disease & Variants

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

Glioma GLM

Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.

Experimental evidence 1 publication

Evidence & references

ECO:0000269 PubMed:15457249 ↗

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": "Glioma",
    "diseaseAccession": "DI-02566",
    "acronym": "GLM",
    "description": "Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "137800"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "15457249"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The gene represented in this entry is involved in disease pathogenesis"
      }
    ]
  }
}

Ovarian cancer OC

The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.

Experimental evidence 2 publications

Evidence & references

ECO:0000269 PubMed:15457249 ↗
ECO:0000269 PubMed:17344846 ↗

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": "Ovarian cancer",
    "diseaseAccession": "DI-01655",
    "acronym": "OC",
    "description": "The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "167000"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "15457249"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "17344846"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The gene represented in this entry is involved in disease pathogenesis"
      }
    ]
  }
}

Lung cancer LNCR

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

Experimental evidence 1 publication

Evidence & references

ECO:0000269 PubMed:15457249 ↗

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": "15457249"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The gene represented in this entry is involved in disease pathogenesis"
      }
    ]
  }
}

Gastric cancer GASC

A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.

Experimental evidence 2 publications

Evidence & references

ECO:0000269 PubMed:15457249 ↗
ECO:0000269 PubMed:17344846 ↗

The protein 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": "Gastric cancer",
    "diseaseAccession": "DI-02971",
    "acronym": "GASC",
    "description": "A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "613659"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "15457249"
      },
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "17344846"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The protein represented in this entry is involved in disease pathogenesis"
      }
    ]
  }
}

Chromosomal aberrations involving ERBB2 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with CDK12, leading to CDK12-ERBB2 fusion leading to truncated CDK12 protein not in-frame with ERBB2

Experimental evidence 1 publication

Evidence & references

ECO:0000269 PubMed:21097718 ↗

Complete source annotation

{
  "commentType": "DISEASE",
  "note": {
    "texts": [
      {
        "evidences": [
          {
            "evidenceCode": "ECO:0000269",
            "source": "PubMed",
            "id": "21097718"
          }
        ],
        "value": "Chromosomal aberrations involving ERBB2 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with CDK12, leading to CDK12-ERBB2 fusion leading to truncated CDK12 protein not in-frame with ERBB2"
      }
    ]
  }
}

Visceral neuropathy, familial, 2, autosomal recessive VSCN2

An autosomal recessive disorder characterized by intestinal dysmotility due to aganglionosis (Hirschsprung disease), hypoganglionosis, and/or chronic intestinal pseudoobstruction. Patients also show peripheral axonal neuropathy, hypotonia, mild developmental delay, unilateral ptosis, and sensorineural hearing loss.

Experimental evidence 1 publication

Evidence & references

ECO:0000269 PubMed:33497358 ↗

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": "Visceral neuropathy, familial, 2, autosomal recessive",
    "diseaseAccession": "DI-06182",
    "acronym": "VSCN2",
    "description": "An autosomal recessive disorder characterized by intestinal dysmotility due to aganglionosis (Hirschsprung disease), hypoganglionosis, and/or chronic intestinal pseudoobstruction. Patients also show peripheral axonal neuropathy, hypotonia, mild developmental delay, unilateral ptosis, and sensorineural hearing loss.",
    "diseaseCrossReference": {
      "database": "MIM",
      "id": "619465"
    },
    "evidences": [
      {
        "evidenceCode": "ECO:0000269",
        "source": "PubMed",
        "id": "33497358"
      }
    ]
  },
  "note": {
    "texts": [
      {
        "value": "The disease is caused by variants affecting the gene represented in this entry"
      }
    ]
  }
}

Polymorphism notes

There are four alleles due to the variations in positions 654 and 655. Allele B1 (Ile-654/Ile-655) has a frequency of 0.782; allele B2 (Ile-654/Val-655) has a frequency of 0.206; allele B3 (Val-654/Val-655) has a frequency of 0.012

Evidence & references

No separate evidence record is supplied for this statement.

Complete source annotation

{
  "texts": [
    {
      "value": "There are four alleles due to the variations in positions 654 and 655. Allele B1 (Ile-654/Ile-655) has a frequency of 0.782; allele B2 (Ile-654/Val-655) has a frequency of 0.206; allele B3 (Val-654/Val-655) has a frequency of 0.012"
    }
  ],
  "commentType": "POLYMORPHISM"
}

Natural variants 13

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13 recorded rows

Feature	Position	Description	Evidence	Inspect
W452CVAR_016317	452	in dbSNP:rs4252633 W → C	Experimental evidence Evidence & references ECO:0000269 Reference:Ref.3	No verified residues in this structure
I654VVAR_004077	654	in allele B3; dbSNP:rs1801201 I → V	Experimental evidence 2 publications Evidence & references ECO:0000269 PubMed:17344846 ↗ ECO:0000269 PubMed:8095488 ↗	No verified residues in this structure
I655VVAR_004078	655	in allele B2 and allele B3; dbSNP:rs1136201 I → V	Experimental evidence 2 publications Evidence & references ECO:0000269 PubMed:17344846 ↗ ECO:0000269 PubMed:8095488 ↗ ECO:0000269 Reference:Ref.3	No verified residues in this structure
A710VVAR_086107	710	in VSCN2; almost complete loss of ERBB2 and ERBB3 phosphorylation in the presence or in the absence of NRG1 stimulation, suggesting alteration of downstream signaling; does not affect the subcellular localization at the cell membrane; dbSNP:rs2145813505 A → V	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:33497358 ↗	No verified residues in this structure
L755PVAR_055432	755	in LNCR; uncertain significance; somatic mutation; dbSNP:rs121913469 L → P	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:15457249 ↗	No verified residues in this structure
L768SVAR_042097	768	in dbSNP:rs56366519 L → S	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:17344846 ↗	No verified residues in this structure
M774MAYVMVAR_055433	774	in LNCR; uncertain significance; somatic mutation M → MAYVM	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:15457249 ↗	No verified residues in this structure
G776SVAR_042098	776	in GASC; uncertain significance; somatic mutation; dbSNP:rs28933369 G → S	Experimental evidence 2 publications Evidence & references ECO:0000269 PubMed:15457249 ↗ ECO:0000269 PubMed:17344846 ↗	No verified residues in this structure
S779SVGSVAR_055434	779	in LNCR; uncertain significance; somatic mutation S → SVGS	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:15457249 ↗	No verified residues in this structure
N857SVAR_042099	857	in OC; uncertain significance; somatic mutation; dbSNP:rs28933370 N → S	Experimental evidence 2 publications Evidence & references ECO:0000269 PubMed:15457249 ↗ ECO:0000269 PubMed:17344846 ↗	No verified residues in this structure
E914KVAR_055435	914	in GLM; uncertain significance; somatic mutation; dbSNP:rs28933368 E → K	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:15457249 ↗	No verified residues in this structure
P1170AVAR_016318	1170	in dbSNP:rs1058808 P → A	Experimental evidence 3 publications Evidence & references ECO:0000269 PubMed:17344846 ↗ ECO:0000269 PubMed:2999974 ↗ ECO:0000269 PubMed:8104414 ↗ ECO:0000269 Reference:Ref.3	No verified residues in this structure
A1216DVAR_042100	1216	in dbSNP:rs55943169 A → D	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:17344846 ↗	No verified residues in this structure

Laboratory mutagenesis 5

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5 recorded rows

Feature	Position	Description	Evidence	Inspect
LH317AA	317–318	Reduces dimerization with ERBB3. LH → AA	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:15093539 ↗	No verified residues in this structure
M611A	611	Prevents synthesis of isoform 2. M → A	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:16794579 ↗	No verified residues in this structure
M687A	687	Prevents synthesis of isoform 3. M → A	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:16794579 ↗	No verified residues in this structure
M706A	706	No effect on isoform production. M → A	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:16794579 ↗	No verified residues in this structure
M712A	712	No effect on isoform production. M → A	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:16794579 ↗	No verified residues in this structure

PTM/Processing

Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit (Probable). Ligand-binding increases phosphorylation on tyrosine residues ^{[37, 53]}.

Signaling via SEMA4C promotes phosphorylation at Tyr-1248 ^[22]. Dephosphorylated by PTPN12 ^[37]

Experimental evidenceCurator inference 3 publications

Evidence & references

ECO:0000269 PubMed:17554007 ↗
ECO:0000269 PubMed:27134172 ↗
ECO:0000269 PubMed:33497358 ↗
ECO:0000305

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "17554007"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "27134172"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "33497358"
        },
        {
          "evidenceCode": "ECO:0000305"
        }
      ],
      "value": "Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit (Probable). Ligand-binding increases phosphorylation on tyrosine residues (PubMed:27134172, PubMed:33497358). Signaling via SEMA4C promotes phosphorylation at Tyr-1248 (PubMed:17554007). Dephosphorylated by PTPN12 (PubMed:27134172)"
    }
  ],
  "commentType": "PTM"
}

Processed chains & precursor regions 2

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2 recorded rows

Feature	Position	Description	Evidence	Inspect
Signal	1–22	Signal	Sequence analysis Evidence & references ECO:0000255	No verified residues in this structure
ChainPRO_0000016669	23–1255	Receptor tyrosine-protein kinase erbB-2	Evidence & references No separate evidence record is supplied for this statement.	No verified residues in this structure

Modifications 44

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44 recorded rows

Feature	Position	Description	Evidence	Inspect
Modified residue	182	Phosphothreonine	1 publication Evidence & references ECO:0007744 PubMed:23186163 ↗	No verified residues in this structure
Modified residue	877	Phosphotyrosine	Curator inference 1 publication Evidence & references ECO:0000305 PubMed:32381043 ↗	No verified residues in this structure
Modified residue	1054	Phosphoserine	5 publications Evidence & references ECO:0007744 PubMed:18669648 ↗ ECO:0007744 PubMed:18691976 ↗ ECO:0007744 PubMed:21406692 ↗ ECO:0007744 PubMed:23186163 ↗ ECO:0007744 PubMed:24275569 ↗	No verified residues in this structure
Modified residue	1078	Phosphoserine	By similarity Evidence & references ECO:0000250 UniProtKB:P06494	No verified residues in this structure
Modified residue	1083	Phosphoserine	1 publication Evidence & references ECO:0007744 PubMed:23186163 ↗	No verified residues in this structure
Modified residue	1107	Phosphoserine	1 publication Evidence & references ECO:0007744 PubMed:20068231 ↗	No verified residues in this structure
Modified residue	1112	Phosphotyrosine	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:27134172 ↗	No verified residues in this structure
Modified residue	1139	Phosphotyrosine	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:27134172 ↗	No verified residues in this structure
Modified residue	1151	Phosphoserine	1 publication Evidence & references ECO:0007744 PubMed:24275569 ↗	No verified residues in this structure
Modified residue	1166	Phosphothreonine	1 publication Evidence & references ECO:0007744 PubMed:23186163 ↗	No verified residues in this structure
Modified residue	1196	Phosphotyrosine	Experimental evidenceCurator inference 2 publications Evidence & references ECO:0000269 PubMed:27134172 ↗ ECO:0000305 PubMed:32381043 ↗	No verified residues in this structure
Modified residue	1248	Phosphotyrosine; by autocatalysis	Experimental evidence 3 publications Evidence & references ECO:0000269 PubMed:17554007 ↗ ECO:0000269 PubMed:27134172 ↗ ECO:0007744 PubMed:17081983 ↗	No verified residues in this structure
Glycosylation	68	N-linked (GlcNAc...) asparagine	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:20696930 ↗ ECO:0007744 PDB:2A91 ECO:0007744 PDB:3MZW	No verified residues in this structure
Glycosylation	124	N-linked (GlcNAc...) asparagine	Sequence analysis Evidence & references ECO:0000255	No verified residues in this structure
Glycosylation	187	N-linked (GlcNAc...) asparagine	Sequence analysis Evidence & references ECO:0000255 ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3N85	No verified residues in this structure
Glycosylation	259	N-linked (GlcNAc...) asparagine	Experimental evidence 3 publications Evidence & references ECO:0000269 PubMed:15093539 ↗ ECO:0000269 PubMed:19299620 ↗ ECO:0000269 PubMed:20696930 ↗ ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85	No verified residues in this structure
Glycosylation	530	N-linked (GlcNAc...) asparagine	Experimental evidence 2 publications Evidence & references ECO:0000269 PubMed:15093539 ↗ ECO:0000269 PubMed:19299620 ↗ ECO:0007744 PDB:1S78	No verified residues in this structure
Glycosylation	571	N-linked (GlcNAc...) asparagine	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:20696930 ↗ ECO:0007744 PDB:3MZW	No verified residues in this structure
Glycosylation	629	N-linked (GlcNAc...) asparagine	Sequence analysis Evidence & references ECO:0000255	No verified residues in this structure
Disulfide bond	26, 53	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3H3B ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ ECO:0007744 PDB:4HRL ECO:0007744 PDB:4HRM	No verified residues in this structure
Disulfide bond	162, 192	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3H3B ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ ECO:0007744 PDB:4HRL ECO:0007744 PDB:4HRM	No verified residues in this structure
Disulfide bond	195, 204	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3H3B ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ ECO:0007744 PDB:4HRL ECO:0007744 PDB:4HRM	No verified residues in this structure
Disulfide bond	199, 212	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3H3B ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ ECO:0007744 PDB:4HRL ECO:0007744 PDB:4HRM	No verified residues in this structure
Disulfide bond	220, 227	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	224, 235	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	236, 244	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	240, 252	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	255, 264	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	268, 295	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	299, 311	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	315, 331	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	334, 338	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	342, 367	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	475, 504	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	511, 520	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	515, 528	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:2A91 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ	No verified residues in this structure
Disulfide bond	531, 540	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ ECO:0007744 PDB:4HRN	No verified residues in this structure
Disulfide bond	544, 560	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ ECO:0007744 PDB:4HRN	No verified residues in this structure
Disulfide bond	563, 576	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ ECO:0007744 PDB:4HRN	No verified residues in this structure
Disulfide bond	567, 584	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:3WLW ECO:0007744 PDB:3WSQ ECO:0007744 PDB:4HRN	No verified residues in this structure
Disulfide bond	587, 596	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:1S78 ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3MZW ECO:0007744 PDB:3N85 ECO:0007744 PDB:4HRN	No verified residues in this structure
Disulfide bond	600, 623	Disulfide bond	Evidence & references ECO:0007744 PDB:1N8Z ECO:0007744 PDB:3BE1 ECO:0007744 PDB:3N85	No verified residues in this structure
Disulfide bond	626, 634	Disulfide bond	Evidence & references ECO:0007744 PDB:3N85	No verified residues in this structure
Disulfide bond	630, 642	Disulfide bond	Evidence & references ECO:0007744 PDB:3N85	No verified residues in this structure

Expression

Expressed in a variety of tumor tissues including primary breast tumors and tumors from small bowel, esophagus, kidney and mouth

Experimental evidence 1 publication

Evidence & references

ECO:0000269 PubMed:15380516 ↗

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15380516"
        }
      ],
      "value": "Expressed in a variety of tumor tissues including primary breast tumors and tumors from small bowel, esophagus, kidney and mouth"
    }
  ],
  "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.

Find a partner110 records

Partner / product	Species	Experiments	Evidence & actions
ABL1P00519With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P00519. Reported experiment count: 2. Open protein ↗
ABL2P42684With P04626	Homo sapiens	6	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P42684. Reported experiment count: 6. Open protein ↗
ACP3P15309With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P15309. Reported experiment count: 2. Open protein ↗
ACTBP60709With P04626	Homo sapiens	11	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P60709. Reported experiment count: 11. Open protein ↗
ANKS1AQ92625With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q92625. Reported experiment count: 2. Open protein ↗
APBA1Q02410With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q02410. Reported experiment count: 2. Open protein ↗
APBA2Q99767With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q99767. Reported experiment count: 2. Open protein ↗
APBB1O00213With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O00213. Reported experiment count: 2. Open protein ↗
ARF5P84085With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P84085. Reported experiment count: 3. Open protein ↗
BCAR3O75815With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O75815. Reported experiment count: 2. Open protein ↗
CACYBPQ9HB71With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9HB71. Reported experiment count: 2. Open protein ↗
CDC37Q16543With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q16543. Reported experiment count: 5. Open protein ↗
CISHQ9NSE2With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9NSE2. Reported experiment count: 4. Open protein ↗
CLNKQ7Z7G1With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q7Z7G1. Reported experiment count: 2. Open protein ↗
CRKLP46109With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P46109. Reported experiment count: 2. Open protein ↗
CUL5Q93034With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q93034. Reported experiment count: 2. Open protein ↗
DLG1Q12959With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q12959. Reported experiment count: 3. Open protein ↗
DLG2Q15700With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q15700. Reported experiment count: 2. Open protein ↗
DLG3Q92796With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q92796. Reported experiment count: 2. Open protein ↗
DLG4P78352With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P78352. Reported experiment count: 2. Open protein ↗
DOK1Q99704With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q99704. Reported experiment count: 2. Open protein ↗
DOK4Q8TEW6With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q8TEW6. Reported experiment count: 2. Open protein ↗
EEA1Q15075With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q15075. Reported experiment count: 5. Open protein ↗
EFNB1P98172With P04626	Homo sapiens	12	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P98172. Reported experiment count: 12. Open protein ↗
EGFRP00533With P04626	Homo sapiens	25	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P00533. Reported experiment count: 25. Open protein ↗
ERBB2P04626With P04626	Homo sapiens	12	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P04626. Reported experiment count: 12. Open protein ↗
ERBB3P21860With P04626	Homo sapiens	30	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P21860. Reported experiment count: 30. Open protein ↗
ERBB4Q15303With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q15303. Reported experiment count: 5. Open protein ↗
ERRFI1Q9UJM3With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9UJM3. Reported experiment count: 4. Open protein ↗
FGRP09769With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P09769. Reported experiment count: 3. Open protein ↗
FRMPD2Q68DX3With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q68DX3. Reported experiment count: 2. Open protein ↗
FYNP06241With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P06241. Reported experiment count: 2. Open protein ↗
GRAP2O75791With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O75791. Reported experiment count: 2. Open protein ↗
GRB2P62993With P04626	Homo sapiens	7	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P62993. Reported experiment count: 7. Open protein ↗
GRB7Q14451With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q14451. Reported experiment count: 5. Open protein ↗
GRID2IPA4D2P6With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: A4D2P6. Reported experiment count: 2. Open protein ↗
GRIP1Q9Y3R0With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9Y3R0. Reported experiment count: 4. Open protein ↗
GRIP2Q9C0E4With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9C0E4. Reported experiment count: 5. Open protein ↗
HSP90AA1P07900With P04626	Homo sapiens	6	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P07900. Reported experiment count: 6. Open protein ↗
HSP90AB1P08238With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P08238. Reported experiment count: 5. Open protein ↗
HSP90B1P14625With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P14625. Reported experiment count: 2. Open protein ↗
HSPA5P11021With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P11021. Reported experiment count: 3. Open protein ↗
IQGAP1P46940With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P46940. Reported experiment count: 5. Open protein ↗
IRS1P35568With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P35568. Reported experiment count: 2. Open protein ↗
ITKQ08881With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q08881. Reported experiment count: 2. Open protein ↗
JAK1P23458With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P23458. Reported experiment count: 3. Open protein ↗
KPNB1Q14974With P04626	Homo sapiens	14	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q14974. Reported experiment count: 14. Open protein ↗
LNX1Q8TBB1With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q8TBB1. Reported experiment count: 2. Open protein ↗
LNX2Q8N448With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q8N448. Reported experiment count: 2. Open protein ↗
LRIG1Q96JA1With P04626	Homo sapiens	7	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q96JA1. Reported experiment count: 7. Open protein ↗
LRRC7Q96NW7With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q96NW7. Reported experiment count: 2. Open protein ↗
MACROH2A1O75367With P04626	Homo sapiens	6	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O75367. Reported experiment count: 6. Open protein ↗
MACROH2A1O75367-3With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O75367-3. Reported experiment count: 3. Open protein ↗
MAGI1Q96QZ7With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q96QZ7. Reported experiment count: 2. Open protein ↗
MAGI2Q86UL8With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q86UL8. Reported experiment count: 4. Open protein ↗
MAPK8IP1Q9UQF2With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9UQF2. Reported experiment count: 4. Open protein ↗
MAPK8IP2Q13387With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q13387. Reported experiment count: 3. Open protein ↗
MATKP42679With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P42679. Reported experiment count: 2. Open protein ↗
MEMO1Q9Y316With P04626	Homo sapiens	6	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9Y316. Reported experiment count: 6. Open protein ↗
MPDZO75970With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O75970. Reported experiment count: 3. Open protein ↗
NCK2O43639With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O43639. Reported experiment count: 2. Open protein ↗
NHERF4Q86UT5With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q86UT5. Reported experiment count: 2. Open protein ↗
NRG1Q02297-7With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q02297-7. Reported experiment count: 2. Open protein ↗
PATJQ8NI35With P04626	Homo sapiens	8	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q8NI35. Reported experiment count: 8. Open protein ↗
PDZK1Q5T2W1With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q5T2W1. Reported experiment count: 2. Open protein ↗
PIK3C2BO00750With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O00750. Reported experiment count: 2. Open protein ↗
PIK3R1P27986With P04626	Homo sapiens	12	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P27986. Reported experiment count: 12. Open protein ↗
PIK3R2O00459With P04626	Homo sapiens	7	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O00459. Reported experiment count: 7. Open protein ↗
PIK3R3Q92569With P04626	Homo sapiens	10	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q92569. Reported experiment count: 10. Open protein ↗
PLCG1P19174With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P19174. Reported experiment count: 5. Open protein ↗
PLCG2P16885With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P16885. Reported experiment count: 3. Open protein ↗
POLR1AO95602With P04626	Homo sapiens	16	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O95602. Reported experiment count: 16. Open protein ↗
PTK6Q13882With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q13882. Reported experiment count: 4. Open protein ↗
PTPN11Q06124With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q06124. Reported experiment count: 4. Open protein ↗
PTPN12Q05209With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q05209. Reported experiment count: 4. Open protein ↗
PTPN18Q99952With P04626	Homo sapiens	6	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q99952. Reported experiment count: 6. Open protein ↗
PTPN18Q99952-1With P04626	Homo sapiens	5	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q99952-1. Reported experiment count: 5. Open protein ↗
PTPN3P26045With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P26045. Reported experiment count: 2. Open protein ↗
PTPRBP23467With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P23467. Reported experiment count: 2. Open protein ↗
PTPRCP08575With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P08575. Reported experiment count: 2. Open protein ↗
PTPRJQ12913With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q12913. Reported experiment count: 2. Open protein ↗
PTPRKQ15262With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q15262. Reported experiment count: 2. Open protein ↗
PTPROQ16827With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q16827. Reported experiment count: 2. Open protein ↗
PTPRRQ15256With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q15256. Reported experiment count: 2. Open protein ↗
RANBP2P49792With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P49792. Reported experiment count: 3. Open protein ↗
RASA1P20936With P04626	Homo sapiens	8	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P20936. Reported experiment count: 8. Open protein ↗
RECKO95980With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O95980. Reported experiment count: 4. Open protein ↗
SCRIBQ14160With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q14160. Reported experiment count: 3. Open protein ↗
SH2D2AQ9NP31With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9NP31. Reported experiment count: 2. Open protein ↗
SHC1P29353With P04626	Homo sapiens	11	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P29353. Reported experiment count: 11. Open protein ↗
SHC2P98077With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P98077. Reported experiment count: 3. Open protein ↗
SHC3Q92529With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q92529. Reported experiment count: 2. Open protein ↗
SLA2Q9H6Q3With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9H6Q3. Reported experiment count: 2. Open protein ↗
SOCS1O15524With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O15524. Reported experiment count: 2. Open protein ↗
SPOPO43791With P04626	Homo sapiens	6	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O43791. Reported experiment count: 6. Open protein ↗
SRCP12931With P04626	Homo sapiens	11	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P12931. Reported experiment count: 11. Open protein ↗
STAT1P42224With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P42224. Reported experiment count: 3. Open protein ↗
STAT3P40763With P04626	Homo sapiens	9	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P40763. Reported experiment count: 9. Open protein ↗
STIP1P31948With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P31948. Reported experiment count: 2. Open protein ↗
SUPT6HQ7KZ85With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q7KZ85. Reported experiment count: 2. Open protein ↗
SYKP43405With P04626	Homo sapiens	7	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P43405. Reported experiment count: 7. Open protein ↗
TLN1Q9Y490With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9Y490. Reported experiment count: 3. Open protein ↗
TNS2Q63HR2With P04626	Homo sapiens	4	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q63HR2. Reported experiment count: 4. Open protein ↗
TNS3Q68CZ2With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q68CZ2. Reported experiment count: 2. Open protein ↗
TXNP10599With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P10599. Reported experiment count: 3. Open protein ↗
VAV1Q96D37With P04626	Homo sapiens	2	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q96D37. Reported experiment count: 2. Open protein ↗
VAV2P52735With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P52735. Reported experiment count: 3. Open protein ↗
WHRNQ9P202With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: Q9P202. Reported experiment count: 3. Open protein ↗
XPO1O14980With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: O14980. Reported experiment count: 3. Open protein ↗
YWHAEP62258With P04626	Homo sapiens	3	IntAct evidence Pair evidence in IntAct ↗ Source product: P04626. Partner: P62258. Reported experiment count: 3. Open protein ↗

Complex membership & assembly descriptions

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

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

UniProt subunit description

Homodimer ^[49]. Heterodimer with EGFR, ERBB3 and ERBB4 ^{[12, 46, 21, 32]}. Part of a complex with EGFR and either PIK3C2A or PIK3C2B.

May interact with PIK3C2B when phosphorylated on Tyr-1196 ^[13]. Interacts with PLXNB1 ^[16]. Interacts (when phosphorylated on Tyr-1248) with MEMO1 ^[17].

Interacts with MUC1; the interaction is enhanced by heregulin (HRG) ^[14]. Interacts (when phosphorylated on Tyr-1139) with GRB7 (via SH2 domain) ^[44]. Interacts (when phosphorylated on Tyr-1248) with ERBIN ^[43].

Interacts with KPNB1, RANBP2, EEA1, CRM1 and CLTC ^[18]. Interacts with PTK6 ^[25]. Interacts with RPA194 and ACTB ^[31].

Interacts with PRKCABP, SRC and MYOC (By similarity). Interacts (preferentially with the tyrosine phosphorylated form) with CPNE3; this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner ^[27]. Interacts with HSP90AA1 and HSP90AB1 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity ^[36].

Interacts with SORL1; this interaction regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulates ERBB2-mediated signaling ^[38]. Interacts with SH3BGRL ^[39]. Interacts with ROR1 ^[41]

By similarityExperimental evidence 18 publications

Evidence & references

ECO:0000250 UniProtKB:P70424
ECO:0000269 PubMed:10358079 ↗
ECO:0000269 PubMed:10805725 ↗
ECO:0000269 PubMed:12939402 ↗
ECO:0000269 PubMed:12975581 ↗
ECO:0000269 PubMed:15093539 ↗
ECO:0000269 PubMed:15156151 ↗
ECO:0000269 PubMed:15210733 ↗
ECO:0000269 PubMed:16314522 ↗
ECO:0000269 PubMed:16978839 ↗
ECO:0000269 PubMed:18719096 ↗
ECO:0000269 PubMed:20010870 ↗
ECO:0000269 PubMed:21190959 ↗
ECO:0000269 PubMed:21454582 ↗
ECO:0000269 PubMed:21555369 ↗
ECO:0000269 PubMed:26517842 ↗
ECO:0000269 PubMed:31138794 ↗
ECO:0000269 PubMed:32381043 ↗
ECO:0000269 PubMed:36949068 ↗

Complete source annotation

{
  "texts": [
    {
      "evidences": [
        {
          "evidenceCode": "ECO:0000250",
          "source": "UniProtKB",
          "id": "P70424"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10358079"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "10805725"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12939402"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "12975581"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15093539"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15156151"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "15210733"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16314522"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "16978839"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "18719096"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "20010870"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21190959"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21454582"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "21555369"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "26517842"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "31138794"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "32381043"
        },
        {
          "evidenceCode": "ECO:0000269",
          "source": "PubMed",
          "id": "36949068"
        }
      ],
      "value": "Homodimer (PubMed:21454582). Heterodimer with EGFR, ERBB3 and ERBB4 (PubMed:10358079, PubMed:15093539, PubMed:16978839, PubMed:21190959). Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1196 (PubMed:10805725). Interacts with PLXNB1 (PubMed:15210733). Interacts (when phosphorylated on Tyr-1248) with MEMO1 (PubMed:15156151). Interacts with MUC1; the interaction is enhanced by heregulin (HRG) (PubMed:12939402). Interacts (when phosphorylated on Tyr-1139) with GRB7 (via SH2 domain) (PubMed:12975581). Interacts (when phosphorylated on Tyr-1248) with ERBIN (PubMed:12444095). Interacts with KPNB1, RANBP2, EEA1, CRM1 and CLTC (PubMed:16314522). Interacts with PTK6 (PubMed:18719096). Interacts with RPA194 and ACTB (PubMed:21555369). Interacts with PRKCABP, SRC and MYOC (By similarity). Interacts (preferentially with the tyrosine phosphorylated form) with CPNE3; this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner (PubMed:20010870). Interacts with HSP90AA1 and HSP90AB1 in an ATP-dependent manner; the interaction suppresses ERBB2 kinase activity (PubMed:26517842). Interacts with SORL1; this interaction regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulates ERBB2-mediated signaling (PubMed:31138794). Interacts with SH3BGRL (PubMed:32381043). Interacts with ROR1 (PubMed:36949068)"
    }
  ],
  "commentType": "SUBUNIT"
}

Other association resources

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

BioGRID · 108376 ↗IntAct · P04626 ↗STRING · 9606.ENSP00000269571 ↗

Structure

7MN5 · Structure of the HER2/HER3/NRG1b Heterodimer Extracellular Domain

ELECTRON MICROSCOPY · 2.93 Å

Recorded components

Component	Species	Chains	Protein identities
Receptor tyrosine-protein kinase erbB-3protein · Entity 1	Homo sapiens	A	P21860
Isoform 6 of Pro-neuregulin-1, membrane-bound isoformprotein · Entity 2	Homo sapiens	B	Q02297
Receptor tyrosine-protein kinase erbB-2,Maltose/maltodextrin-binding periplasmic proteinprotein · Entity 3	Escherichia coli K-12, Homo sapiens	C	P04626, P0AEX9
2-acetamido-2-deoxy-beta-D-glucopyranoseligand · Entity 6		G, H, I, J, K	No verified protein mapping

Biological assemblies

Assembly 1 · author_defined_assembly
Assembly membership is incomplete in this record.

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

Publication

Structures of the HER2-HER3-NRG1β complex reveal a dynamic dimer interface.

10/11/2021 · 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 64

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64 recorded rows

Record	Evidence type	Method	Resolution	Open
7MN5	experimental	EM	2.93 A	Open in Atlas ↗
7MN6	experimental	EM	3.09 A	Open in Atlas ↗
7MN8	experimental	EM	3.45 A	Open in Atlas ↗
9QBG	experimental	EM	3.60 A	Open in Atlas ↗
9QBH	experimental	EM	3.77 A	Open in Atlas ↗
9QBF	experimental	EM	3.80 A	Open in Atlas ↗
5MY6	experimental	X-ray	2.25 A	Open in Atlas ↗
6BGT	experimental	X-ray	2.70 A	Open in Atlas ↗
8HGO	experimental	EM	3.31 A	Open in Atlas ↗
8VQD	experimental	EM	2.61 A	Open in Atlas ↗
9MTE	experimental	EM	2.66 A	Open in Atlas ↗
8VQE	experimental	EM	2.67 A	Open in Atlas ↗
1N8Z	experimental	X-ray	2.52 A	Open in Atlas ↗
3BE1	experimental	X-ray	2.90 A	Open in Atlas ↗
3MZW	experimental	X-ray	2.90 A	Open in Atlas ↗
9L1S	experimental	EM	3.00 A	Open in Atlas ↗
9T3S	experimental	EM	3.00 A	Open in Atlas ↗
9MTX	experimental	EM	3.06 A	Open in Atlas ↗
6J71	experimental	X-ray	2.92 A	Open in Atlas ↗
7QVK	experimental	X-ray	3.10 A	Open in Atlas ↗
8HGP	experimental	EM	4.53 A	Open in Atlas ↗
8PWH	experimental	EM	3.17 A	Open in Atlas ↗
3N85	experimental	X-ray	3.20 A	Open in Atlas ↗
5O4G	experimental	X-ray	3.00 A	Open in Atlas ↗
1S78	experimental	X-ray	3.25 A	Open in Atlas ↗
8Q6J	experimental	EM	3.30 A	Open in Atlas ↗
9T3R	experimental	EM	3.50 A	Open in Atlas ↗
5K33	experimental	X-ray	3.30 A	Open in Atlas ↗
8U4L	experimental	EM	3.31 A	Open in Atlas ↗
6ATT	experimental	X-ray	3.77 A	Open in Atlas ↗
3WLW	experimental	X-ray	3.09 A	Open in Atlas ↗
5KWG	experimental	X-ray	4.30 A	Open in Atlas ↗
2A91	experimental	X-ray	2.50 A	Open in Atlas ↗
6OGE	experimental	EM	4.36 A	Open in Atlas ↗
8FFJ	experimental	EM	7.50 A	Open in Atlas ↗
8U4K	experimental	EM	4.27 A	Open in Atlas ↗
3WSQ	experimental	X-ray	3.50 A	Open in Atlas ↗
8VB5	experimental	X-ray	1.48 A	Open in Atlas ↗
8U8X	experimental	X-ray	1.69 A	Open in Atlas ↗
7PCD	experimental	X-ray	1.77 A	Open in Atlas ↗
3PP0	experimental	X-ray	2.25 A	Open in Atlas ↗
7JXH	experimental	X-ray	3.27 A	Open in Atlas ↗
3RCD	experimental	X-ray	3.21 A	Open in Atlas ↗
8JYR	experimental	X-ray	1.69 A	Open in Atlas ↗
3H3B	experimental	X-ray	2.45 A	Open in Atlas ↗
4HRL	experimental	X-ray	2.55 A	Open in Atlas ↗
4HRM	experimental	X-ray	3.20 A	Open in Atlas ↗
6LBX	experimental	X-ray	2.03 A	Open in Atlas ↗
1MFG	experimental	X-ray	1.25 A	Open in Atlas ↗
4HRN	experimental	X-ray	2.65 A	Open in Atlas ↗
8JYQ	experimental	X-ray	1.75 A	Open in Atlas ↗
5TQS	experimental	X-ray	1.88 A	Open in Atlas ↗
1MFL	experimental	X-ray	1.88 A	Open in Atlas ↗
4GFU	experimental	X-ray	2.00 A	Open in Atlas ↗
9IUT	experimental	X-ray	2.09 A	Open in Atlas ↗
1QR1	experimental	X-ray	2.40 A	Open in Atlas ↗
4NND	experimental	X-ray	2.50 A	Open in Atlas ↗
2N2A	experimental	NMR	-	Open in Atlas ↗
2JWA	experimental	NMR	-	Open in Atlas ↗
2KS1	experimental	NMR	-	Open in Atlas ↗
5OB4	experimental	NMR	-	Open in Atlas ↗
1MW4	experimental	NMR	-	Open in Atlas ↗
2L4K	experimental	NMR	-	Open in Atlas ↗
AF-P04626-F1	predicted	AlphaFold	Not applicable	Open in Atlas ↗

Family & Domains

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

Sequence analysis

Evidence & references

ECO:0000255 PROSITE-ProRule:PRU00159

Complete source annotation

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

Domain architecture

Canonical sequence11255 aa

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

Atlas domains, motifs & repeats 9

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9 recorded rows

Annotation	Position	Source & interpretation	Inspect
Receptor L-domainIPR000494	52–172	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 description The structure for the first three domains of the extracellular portion of IGF-1R (type-1 insulin-like growth-factor receptor) has been solved and consists of two L-domains and a cysteine rich region (L1-Cys-rich-L2). The L-domains each consist of a single-stranded right-handed β-helix. The Cys-rich region is composed of eight disulphide-bonded modules, seven of which form a rod-shaped domain with modules associated in an unusual manner. The three domains surround a central space of sufficient size to accommodate a ligand molecule. This entry represents the L-domain. This domain can also be found in insulin receptor(IR) and epidermal growth-factor receptor (EGFR) family members, and in yeast cell surface GPI proteins PST1 and ECM33. Source entry ↗	No verified residues in this structure
Furin-like cysteine-rich domainIPR006211	189–343	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	232–280	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	366–484	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 description The structure for the first three domains of the extracellular portion of IGF-1R (type-1 insulin-like growth-factor receptor) has been solved and consists of two L-domains and a cysteine rich region (L1-Cys-rich-L2). The L-domains each consist of a single-stranded right-handed β-helix. The Cys-rich region is composed of eight disulphide-bonded modules, seven of which form a rod-shaped domain with modules associated in an unusual manner. The three domains surround a central space of sufficient size to accommodate a ligand molecule. This entry represents the L-domain. This domain can also be found in insulin receptor(IR) and epidermal growth-factor receptor (EGFR) family members, and in yeast cell surface GPI proteins PST1 and ECM33. Source entry ↗	No verified residues in this structure
Furin-like repeatIPR006212	501–552	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	511–642	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
Furin-like repeatIPR006212	557–607	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
Epidermal growth factor receptor-like, transmembrane-juxtamembrane segmentIPR049328	654–688	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 description Epidermal growth factor receptor (ErbB) family is a class of receptor tyrosine kinases (RTKs) that have a pivotal role in the processes of cell growth, proliferation, and differentiation. They exist on the cell surface as dimers in both active and inactive states, which switch between them through conformational changes upon ligand binding. They suffer a strong lateral dimerization that leads to proper assembly of their extracellular ligand-binding, single-span transmembrane, and cytoplasmic kinase domains which is key for ErbB activation. The transmembrane (TM) and juxtamembrane region of these receptors are essential for dimerization and activation. This entry represents the TM and juxtamembrane segment of EGFR, ErbB2 and ErbB4 and similar sequences. Source entry ↗	No verified residues in this structure
Protein kinase domainIPR000719	720–987	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 description This entry represents the protein kinase domain containing the catalytic function of protein kinases. This domain is found in serine/threonine-protein kinases, tyrosine-protein kinases and dual specificity protein kinases. Eukaryotic protein kinases are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases. There are a number of conserved regions in the catalytic domain of protein kinases. In the N-terminal extremity of the catalytic domain there is a glycine-rich stretch of residues in the vicinity of a lysine residue, which has been shown to be involved in ATP binding. In the central part of the catalytic domain there is a conserved aspartic acid residue which is important for the catalytic activity of the enzyme. Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyse the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyse the reverse process. Protein kinases fall into three broad classes, characterised with respect to substrate specificity: Serine/threonine-protein kinases Tyrosine-protein kinases Dual specificity protein kinases (e.g. MEK -phosphorylates both Thr and Tyr on target proteins) Protein kinase function is evolutionarily conserved from Escherichia coli to human. Protein kinases play a role in a multitude of cellular processes, including division, proliferation, apoptosis, and differentiation. Phosphorylation usually results in a functional change of the target protein by changing enzyme activity, cellular location, or association with other proteins. The catalytic subunits of protein kinases are highly conserved, and several structures have been solved, leading to large screens to develop kinase-specific inhibitors for the treatments of a number of diseases. Source entry ↗	No verified residues in this structure

UniProt domains, repeats & motifs 2

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2 recorded rows

Feature	Position	Description	Evidence	Inspect
Domain	720–987	Protein kinase	Sequence analysis Evidence & references ECO:0000255 PROSITE-ProRule:PRU00159	No verified residues in this structure
Motif	676–689	Nuclear localization signal	Evidence & references No separate evidence record is supplied for this statement.	No verified residues in this structure

Functional sites 3

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3 recorded rows

Feature	Position	Description	Evidence	Inspect
Active site	845	Proton acceptor	Sequence analysis Evidence & references ECO:0000255 PROSITE-ProRule:PRU00159 ECO:0000255 PROSITE-ProRule:PRU10028	No verified residues in this structure
Binding site	726–734	Binding site	Sequence analysis Evidence & references ECO:0000255 PROSITE-ProRule:PRU00159	No verified residues in this structure
Binding site	753	Binding site	Sequence analysis Evidence & references ECO:0000255 PROSITE-ProRule:PRU00159	No verified residues in this structure

Sequence regions 5

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5 recorded rows

Feature	Position	Description	Evidence	Inspect
Region	676–689	Required for interaction with KPNB1 and EEA1	Experimental evidence 1 publication Evidence & references ECO:0000269 PubMed:16314522 ↗	No verified residues in this structure
Region	1035–1179	Disordered	Evidence & references ECO:0000256 SAM:MobiDB-lite	No verified residues in this structure
Region	1195–1197	Interaction with PIK3C2B	Curator inference Evidence & references ECO:0000305	No verified residues in this structure
Region	1196–1255	Disordered	Evidence & references ECO:0000256 SAM:MobiDB-lite	No verified residues in this structure
Compositional bias	1146–1155	Pro residues	Evidence & references ECO:0000256 SAM:MobiDB-lite	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.

Displayed sequence

UniProt’s canonical sequence · P04626-11255 aa137,910 Da · source sequence mass

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

MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV

Other recorded isoform sequences

P04626-2

645 aa · mass unavailable

MPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV

P04626-3

569 aa · mass unavailable

MRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV

P04626-4

1240 aa · mass unavailable

MPRGSWKPQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV

P04626-5

1225 aa · mass unavailable

MKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV

P04626-6

888 aa · mass unavailable

MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDETISNLFSNFAPRGPSACCEPTCWCHSGKGQDSLPREEWGRQRRFCLWGCRGEPRVLDTPGRSCPSAPPSSCLQPSLRQPLLLGPGPTRAGGSTQHLQRDTYGREPRVPGSGRASVNQKAKSAEALMCPQGAGKA

Source isoform notes & selection

Alternative splicing · Alternative initiation

Complete source annotation

{
  "commentType": "ALTERNATIVE PRODUCTS",
  "events": [
    "Alternative splicing",
    "Alternative initiation"
  ],
  "isoforms": [
    {
      "name": {
        "value": "1"
      },
      "synonyms": [
        {
          "value": "ERBB2"
        },
        {
          "value": "HER2"
        }
      ],
      "isoformIds": [
        "P04626-1"
      ],
      "isoformSequenceStatus": "Displayed"
    },
    {
      "name": {
        "value": "2"
      },
      "synonyms": [
        {
          "value": "CTF-611"
        }
      ],
      "isoformIds": [
        "P04626-2"
      ],
      "sequenceIds": [
        "VSP_039249"
      ],
      "isoformSequenceStatus": "Described"
    },
    {
      "name": {
        "value": "3"
      },
      "synonyms": [
        {
          "value": "CTF-687"
        }
      ],
      "isoformIds": [
        "P04626-3"
      ],
      "sequenceIds": [
        "VSP_039250"
      ],
      "isoformSequenceStatus": "Described"
    },
    {
      "name": {
        "value": "4"
      },
      "isoformIds": [
        "P04626-4"
      ],
      "sequenceIds": [
        "VSP_039248"
      ],
      "isoformSequenceStatus": "Described"
    },
    {
      "name": {
        "value": "5"
      },
      "isoformIds": [
        "P04626-5"
      ],
      "sequenceIds": [
        "VSP_054787"
      ],
      "isoformSequenceStatus": "Described"
    },
    {
      "name": {
        "value": "6"
      },
      "synonyms": [
        {
          "value": "B"
        }
      ],
      "isoformIds": [
        "P04626-6"
      ],
      "sequenceIds": [
        "VSP_055902",
        "VSP_055903",
        "VSP_055904"
      ],
      "isoformSequenceStatus": "Described"
    }
  ]
}

P04626-1 · 1 · Displayed · ERBB2, HER2

Complete source annotation

{
  "name": {
    "value": "1"
  },
  "synonyms": [
    {
      "value": "ERBB2"
    },
    {
      "value": "HER2"
    }
  ],
  "isoformIds": [
    "P04626-1"
  ],
  "isoformSequenceStatus": "Displayed"
}

P04626-2 · 2 · Described · CTF-611 · VSP_039249

Complete source annotation

{
  "name": {
    "value": "2"
  },
  "synonyms": [
    {
      "value": "CTF-611"
    }
  ],
  "isoformIds": [
    "P04626-2"
  ],
  "sequenceIds": [
    "VSP_039249"
  ],
  "isoformSequenceStatus": "Described"
}

P04626-3 · 3 · Described · CTF-687 · VSP_039250

Complete source annotation

{
  "name": {
    "value": "3"
  },
  "synonyms": [
    {
      "value": "CTF-687"
    }
  ],
  "isoformIds": [
    "P04626-3"
  ],
  "sequenceIds": [
    "VSP_039250"
  ],
  "isoformSequenceStatus": "Described"
}

P04626-4 · 4 · Described · VSP_039248

Complete source annotation

{
  "name": {
    "value": "4"
  },
  "isoformIds": [
    "P04626-4"
  ],
  "sequenceIds": [
    "VSP_039248"
  ],
  "isoformSequenceStatus": "Described"
}

P04626-5 · 5 · Described · VSP_054787

Complete source annotation

{
  "name": {
    "value": "5"
  },
  "isoformIds": [
    "P04626-5"
  ],
  "sequenceIds": [
    "VSP_054787"
  ],
  "isoformSequenceStatus": "Described"
}

P04626-6 · 6 · Described · B · VSP_055902, VSP_055903, VSP_055904

Complete source annotation

{
  "name": {
    "value": "6"
  },
  "synonyms": [
    {
      "value": "B"
    }
  ],
  "isoformIds": [
    "P04626-6"
  ],
  "sequenceIds": [
    "VSP_055902",
    "VSP_055903",
    "VSP_055904"
  ],
  "isoformSequenceStatus": "Described"
}

Isoform sequence differences 7

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7 recorded rows

Feature	Position	Description	Evidence	Inspect
Alternative sequenceVSP_039250	1–686	in isoform 3	Curator inference Evidence & references ECO:0000305	No verified residues in this structure
Alternative sequenceVSP_039249	1–610	in isoform 2	Curator inference Evidence & references ECO:0000305	No verified residues in this structure
Alternative sequenceVSP_054787	1–30	in isoform 5	Curator inference Evidence & references ECO:0000305	No verified residues in this structure
Alternative sequenceVSP_039248	1–23	in isoform 4 MELAALCRWGLLLALLPPGAAST → MPRGSWKP	Published statement Evidence & references ECO:0000303 Reference:Ref.4	No verified residues in this structure
Alternative sequenceVSP_055902	633–648	in isoform 6	Published statement 1 publication Evidence & references ECO:0000303 PubMed:24722188 ↗	No verified residues in this structure
Alternative sequenceVSP_055903	771–883	in isoform 6 AYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGK → TISNLFSNFAPRGPSACCEPTCWCHSGKGQDSLPREEWGRQRRFCLWGCRGEPRVLDTPGRSCPSAPPSSCLQPSLRQPLLLGPGPTRAGGSTQHLQRDTYGREPRVPGSGRASVNQKAKSAEALMCPQGAGKA	Published statement 1 publication Evidence & references ECO:0000303 PubMed:24722188 ↗	No verified residues in this structure
Alternative sequenceVSP_055904	884–1255	in isoform 6	Published statement 1 publication Evidence & references ECO:0000303 PubMed:24722188 ↗	No verified residues in this structure

Sequence conflicts & cautions 0

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No annotation is recorded in this UniProt entry.

Recorded secondary structure 119

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119 recorded rows

Feature	Position	Description	Evidence	Inspect
Beta strand	25–27	Beta strand	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	39–50	Helix	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Beta strand	55–64	Beta strand	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	72–74	Helix	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Beta strand	79–82	Beta strand	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Beta strand	84–88	Beta strand	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Beta strand	92–95	Beta strand	Evidence & references ECO:0007829 PDB:3H3B	No verified residues in this structure
Turn	109–111	Turn	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Beta strand	112–117	Beta strand	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Beta strand	123–125	Beta strand	Evidence & references ECO:0007829 PDB:8PWH	No verified residues in this structure
Turn	130–132	Turn	Evidence & references ECO:0007829 PDB:3H3B	No verified residues in this structure
Beta strand	139–141	Beta strand	Evidence & references ECO:0007829 PDB:3H3B	No verified residues in this structure
Beta strand	147–150	Beta strand	Evidence & references ECO:0007829 PDB:2A91	No verified residues in this structure
Beta strand	152–156	Beta strand	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	164–166	Helix	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	169–171	Helix	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	175–177	Helix	Evidence & references ECO:0007829 PDB:1N8Z	No verified residues in this structure
Beta strand	182–184	Beta strand	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	191–196	Helix	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	200–202	Helix	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Beta strand	204–208	Beta strand	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	209–211	Helix	Evidence & references ECO:0007829 PDB:8JYR	No verified residues in this structure
Helix	212–215	Helix	Evidence & references ECO:0007829 PDB:1S78	No verified residues in this structure
Beta strand	217–219	Beta strand	Evidence & references ECO:0007829 PDB:1N8Z	No verified residues in this structure
Helix	221–223	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	227–231	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Helix	232–234	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	240–248	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	251–260	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	263–267	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	271–274	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Turn	276–278	Turn	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	281–283	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Turn	284–286	Turn	Evidence & references ECO:0007829 PDB:6J71	No verified residues in this structure
Beta strand	289–291	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	294–298	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	303–305	Beta strand	Evidence & references ECO:0007829 PDB:1N8Z	No verified residues in this structure
Beta strand	309–314	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	319–323	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	325–327	Beta strand	Evidence & references ECO:0007829 PDB:8VQD	No verified residues in this structure
Beta strand	329–333	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	335–337	Beta strand	Evidence & references ECO:0007829 PDB:2A91	No verified residues in this structure
Helix	348–350	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Turn	358–360	Turn	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Helix	361–364	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	368–376	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Helix	378–382	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Helix	385–387	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Helix	390–393	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Helix	394–400	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	405–408	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	410–413	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	417–421	Beta strand	Evidence & references ECO:0007829 PDB:8PWH	No verified residues in this structure
Helix	423–425	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	430–435	Beta strand	Evidence & references ECO:0007829 PDB:3WLW	No verified residues in this structure
Turn	438–440	Turn	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	441–447	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	463–469	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Turn	476–479	Turn	Evidence & references ECO:0007829 PDB:8VQE	No verified residues in this structure
Helix	482–485	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	488–490	Beta strand	Evidence & references ECO:0007829 PDB:8VQD	No verified residues in this structure
Beta strand	493–499	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Helix	501–506	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Turn	507–509	Turn	Evidence & references ECO:0007829 PDB:3N85	No verified residues in this structure
Helix	516–518	Helix	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Beta strand	520–524	Beta strand	Evidence & references ECO:0007829 PDB:5MY6	No verified residues in this structure
Helix	525–527	Helix	Evidence & references ECO:0007829 PDB:2A91	No verified residues in this structure
Beta strand	532–536	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	539–542	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	545–551	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	553–556	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	559–562	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	565–567	Beta strand	Evidence & references ECO:0007829 PDB:3WSQ	No verified residues in this structure
Beta strand	571–573	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	575–580	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	583–592	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	595–599	Beta strand	Evidence & references ECO:0007829 PDB:6LBX	No verified residues in this structure
Beta strand	602–604	Beta strand	Evidence & references ECO:0007829 PDB:6J71	No verified residues in this structure
Beta strand	605–608	Beta strand	Evidence & references ECO:0007829 PDB:8PWH	No verified residues in this structure
Beta strand	613–616	Beta strand	Evidence & references ECO:0007829 PDB:8JYQ	No verified residues in this structure
Beta strand	621–625	Beta strand	Evidence & references ECO:0007829 PDB:1N8Z	No verified residues in this structure
Beta strand	630–632	Beta strand	Evidence & references ECO:0007829 PDB:6J71	No verified residues in this structure
Beta strand	635–637	Beta strand	Evidence & references ECO:0007829 PDB:6J71	No verified residues in this structure
Beta strand	641–643	Beta strand	Evidence & references ECO:0007829 PDB:8Q6J	No verified residues in this structure
Helix	651–678	Helix	Evidence & references ECO:0007829 PDB:2JWA	No verified residues in this structure
Helix	684–690	Helix	Evidence & references ECO:0007829 PDB:2N2A	No verified residues in this structure
Helix	693–697	Helix	Evidence & references ECO:0007829 PDB:2N2A	No verified residues in this structure
Helix	717–719	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Beta strand	720–729	Beta strand	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Beta strand	732–739	Beta strand	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Beta strand	748–755	Beta strand	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	761–774	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Beta strand	775–777	Beta strand	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Beta strand	785–799	Beta strand	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	806–812	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Turn	813–816	Turn	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	819–838	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	848–850	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Beta strand	851–855	Beta strand	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Beta strand	858–861	Beta strand	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	866–870	Helix	Evidence & references ECO:0007829 PDB:8U8X	No verified residues in this structure
Beta strand	874–877	Beta strand	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	878–880	Helix	Evidence & references ECO:0007829 PDB:8U8X	No verified residues in this structure
Helix	886–888	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	891–896	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	901–916	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Turn	922–925	Turn	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	928–930	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	931–937	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	941–944	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	949–958	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	963–965	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	969–981	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	983–985	Helix	Evidence & references ECO:0007829 PDB:8VB5	No verified residues in this structure
Helix	989–992	Helix	Evidence & references ECO:0007829 PDB:3PP0	No verified residues in this structure
Helix	1003–1007	Helix	Evidence & references ECO:0007829 PDB:3PP0	No verified residues in this structure
Turn	1008–1011	Turn	Evidence & references ECO:0007829 PDB:8U8X	No verified residues in this structure
Helix	1020–1022	Helix	Evidence & references ECO:0007829 PDB:8U8X	No verified residues in this structure
Beta strand	1140–1142	Beta strand	Evidence & references ECO:0007829 PDB:1MW4	No verified residues in this structure

Similar proteins · UniRef

These are sequence clusters. A cluster threshold is not a measured pairwise identity to this protein, and does not establish shared function.

UniRef100_P04626 5 members

Cluster: Receptor tyrosine-protein kinase erbB-2

Recorded preview: 5 members. See UniRef for the complete cluster.

Receptor tyrosine-protein kinase erbB-2 · Homo sapiens (Human)
P04626 ↗
Receptor tyrosine-protein kinase erbB-2 (Fragment) · Homo sapiens (Human)
X5DNK3 ↗
Isoform 5 of Receptor tyrosine-protein kinase erbB-2 · Homo sapiens (Human)
P04626-5 ↗
Erb-b2 receptor tyrosine kinase 2 · Homo sapiens (Human)
A0ACP2CN92 ↗
Erb-b2 receptor tyrosine kinase 2 · Homo sapiens (Human)
A0ACP2CN50 ↗

Full cluster ↗

UniRef90_P04626 247 members

Cluster: Receptor tyrosine-protein kinase erbB-2

Recorded preview: 10 members. See UniRef for the complete cluster.

Receptor tyrosine-protein kinase erbB-2 · Homo sapiens (Human)
P04626 ↗
Receptor tyrosine-protein kinase erbB-2 (Fragment) · Homo sapiens (Human)
X5DNK3 ↗
Isoform 5 of Receptor tyrosine-protein kinase erbB-2 · Homo sapiens (Human)
P04626-5 ↗
Erb-b2 receptor tyrosine kinase 2 · Homo sapiens (Human)
A0ACP2CN92 ↗
Erb-b2 receptor tyrosine kinase 2 · Homo sapiens (Human)
A0ACP2CN50 ↗
Receptor protein-tyrosine kinase · Macaca mulatta (Rhesus macaque)
F7D6W7 ↗
Receptor protein-tyrosine kinase · Macaca mulatta (Rhesus macaque)
F7D6W0 ↗
Receptor tyrosine-protein kinase erbB-2 isoform b (Fragment) · Macaca mulatta (Rhesus macaque)
H9FK98 ↗
Receptor protein-tyrosine kinase · Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys)
A0A2K5L507 ↗
Receptor protein-tyrosine kinase · Mandrillus leucophaeus (Drill) (Papio leucophaeus)
A0A2K5YM50 ↗

Full cluster ↗

UniRef50_P04626 356 members

Cluster: Receptor tyrosine-protein kinase erbB-2

Recorded preview: 10 members. See UniRef for the complete cluster.

Receptor tyrosine-protein kinase erbB-2 · Homo sapiens (Human)
P04626 ↗
Growth factor receptor-bound protein 7 · Bos taurus (Bovine)
Q1RMW5 ↗
Receptor tyrosine-protein kinase erbB-2 (Fragment) · Homo sapiens (Human)
X5DNK3 ↗
Isoform 5 of Receptor tyrosine-protein kinase erbB-2 · Homo sapiens (Human)
P04626-5 ↗
Erb-b2 receptor tyrosine kinase 2 · Homo sapiens (Human)
A0ACP2CN92 ↗
Erb-b2 receptor tyrosine kinase 2 · Homo sapiens (Human)
A0ACP2CN50 ↗
Receptor protein-tyrosine kinase · Macaca mulatta (Rhesus macaque)
F7D6W7 ↗
Receptor protein-tyrosine kinase · Macaca mulatta (Rhesus macaque)
F7D6W0 ↗
Receptor tyrosine-protein kinase erbB-2 isoform b (Fragment) · Macaca mulatta (Rhesus macaque)
H9FK98 ↗
Receptor protein-tyrosine kinase · Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys)
A0A2K5L507 ↗

Full cluster ↗

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.

UniProt ↗QuickGO ↗InterPro ↗PDB / PDBe ↗Complex Portal ↗UniRef ↗OMA ↗

Source dates & provenance

UniProt / The UniProt Consortium ↗ · 2026-11-09T11:39:42.856735+00:00
InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:39:42.900417+00:00
AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:39:44.445580+00:00
UniProt / The UniProt Consortium ↗ · 2026-11-09T11:39:42.856735+00:00
InterPro / EMBL-EBI and the member sources identified in the annotations ↗ · 2026-11-09T11:39:42.900417+00:00
AlphaFold DB / DeepMind Technologies Limited / EMBL-EBI ↗ · 2026-11-09T11:39:44.445580+00:00
UniProt overview ↗ · 2026-11-10T20:42:44.947498+00:00
www.ebi.ac.uk ↗ · 2026-11-10T21:11:27.619245+00:00
omabrowser.org ↗ · 2026-11-10T21:11:27.806964+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:28.147253+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:28.258761+00:00
omabrowser.org ↗ · 2026-11-10T21:11:28.954304+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:29.182571+00:00
www.ebi.ac.uk ↗ · 2026-11-10T21:11:29.945036+00:00
www.ebi.ac.uk ↗ · 2026-11-10T21:11:29.971915+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:30.255037+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:30.275801+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:30.362954+00:00
www.ebi.ac.uk ↗ · 2026-11-10T21:11:30.565324+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:31.491724+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:32.263960+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:33.284714+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:33.287633+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:33.290487+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:34.207883+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:34.250985+00:00
rest.uniprot.org ↗ · 2026-11-10T21:11:34.428762+00:00

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

Publications in this UniProt entry

1 · Similarity of protein encoded by the human c-erb-B-2 gene to epidermal growth factor receptor.

1986 · Nature

PubMed 3003577 ↗

Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)

Yamamoto T., Ikawa S., Akiyama T., Semba K., Nomura N., Miyajima N., Saito T., Toyoshima K.

2 · Tyrosine kinase receptor with extensive homology to EGF receptor shares chromosomal location with neu oncogene.

1985 · Science

PubMed 2999974 ↗

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1); VARIANT ALA-1170

Coussens L., Yang-Feng T.L., Liao Y.C., Chen E., Gray A., McGrath J., Seeburg P.H., Libermann T.A., Schlessinger J., Francke U., Levinson A., Ullrich A.

· Reference

DEC-2002 ·

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS CYS-452; VAL-655 AND ALA-1170

· NEDO human cDNA sequencing project focused on splicing variants.

OCT-2007 ·

Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4)

Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.

All source publications (53)

· Reference

JUL-2005 ·

Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]

Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.

6 · The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

2004 · Genome Res.

PubMed 15489334 ↗

Scope & authors

NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)

7 · Human HER2 (neu) promoter: evidence for multiple mechanisms for transcriptional initiation.

1987 · Mol. Cell. Biol.

PubMed 3039351 ↗

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-191 (ISOFORM 1)

Tal M., King C.R., Kraus M.H., Ullrich A., Schlessinger J., Givol D.

8 · Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism.

2014 · Nat. Commun.

PubMed 24722188 ↗

Scope & authors

NUCLEOTIDE SEQUENCE [MRNA] OF 1-867 (ISOFORM 6)

Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.

9 · A v-erbB-related protooncogene, c-erbB-2, is distinct from the c-erbB-1/epidermal growth factor-receptor gene and is amplified in a human salivary gland adenocarcinoma.

1985 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 2995967 ↗

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 737-1031

Semba K., Kamata N., Toyoshima K., Yamamoto T.

10 · Amplification of a novel v-erbB-related gene in a human mammary carcinoma.

1985 · Science

PubMed 2992089 ↗

Scope & authors

NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 832-909

King C.R., Kraus M.H., Aaronson S.A.

11 · Molecular cloning and sequencing of an intron of Her-2/neu (ERBB2) gene.

1993 · DNA Cell Biol.

PubMed 8104414 ↗

Scope & authors

NUCLEOTIDE SEQUENCE OF 1081-1245; VARIANT ALA-1170

Sarkar F.H., Ball D.E., Li Y.W., Crissman J.D.

12 · ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases.

1999 · J. Biol. Chem.

PubMed 10358079 ↗

Scope & authors

INTERACTION WITH ERBB4; FUNCTION IN ACTIVATION OF STAT5A

Olayioye M.A., Beuvink I., Horsch K., Daly J.M., Hynes N.E.

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

2000 · Mol. Cell. Biol.

PubMed 10805725 ↗

Scope & authors

IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND EGFR; IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND EGFR; INTERACTION WITH PIK3C2B

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

14 · Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein.

2003 · Mol. Cancer Res.

PubMed 12939402 ↗

Scope & authors

INTERACTION WITH MUC1

Li Y., Yu W.-H., Ren J., Chen W., Huang L., Kharbanda S., Loda M., Kufe D.

15 · Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2.

2004 · Cancer Cell

PubMed 15380516 ↗

Scope & authors

FUNCTION; SUBCELLULAR LOCATION; TISSUE SPECIFICITY

Wang S.C., Lien H.C., Xia W., Chen I.F., Lo H.W., Wang Z., Ali-Seyed M., Lee D.F., Bartholomeusz G., Ou-Yang F., Giri D.K., Hung M.C.

16 · Plexin-B1/RhoGEF-mediated RhoA activation involves the receptor tyrosine kinase ErbB-2.

2004 · J. Cell Biol.

PubMed 15210733 ↗

Scope & authors

INTERACTION WITH PLXNB1

Swiercz J.M., Kuner R., Offermanns S.

17 · Memo mediates ErbB2-driven cell motility.

2004 · Nat. Cell Biol.

PubMed 15156151 ↗

Scope & authors

INTERACTION WITH MEMO1

Marone R., Hess D., Dankort D., Muller W.J., Hynes N.E., Badache A.

18 · Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor.

2005 · Mol. Cell. Biol.

PubMed 16314522 ↗

Scope & authors

SUBCELLULAR LOCATION; NUCLEAR LOCALIZATION SIGNAL; INTERACTION WITH KPNB1; RANBP2; CRM1; EEA1 AND CLTC

Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., Wang S.C., Hung M.C.

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

2006 · Cell

PubMed 17081983 ↗

Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1248; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

20 · Biosynthesis of tumorigenic HER2 C-terminal fragments by alternative initiation of translation.

2006 · EMBO J.

PubMed 16794579 ↗

Scope & authors

FUNCTION; ALTERNATIVE INITIATION (ISOFORMS 2 AND 3); SUBCELLULAR LOCATION; MUTAGENESIS OF MET-611; MET-687; MET-706 AND MET-712

Anido J., Scaltriti M., Bech Serra J.J., Santiago Josefat B., Todo F.R., Baselga J., Arribas J.

21 · Neuregulin-1 only induces trans-phosphorylation between ErbB receptor heterodimer partners.

2007 · Cell. Signal.

PubMed 16978839 ↗

Scope & authors

INTERACTION WITH ERBB4; AUTOPHOSPHORYLATION IN TRANS

Li Z., Mei Y., Liu X., Zhou M.

22 · Plexin-B2, but not Plexin-B1, critically modulates neuronal migration and patterning of the developing nervous system in vivo.

2007 · J. Neurosci.

PubMed 17554007 ↗

Scope & authors

PHOSPHORYLATION AT TYR-1248

Deng S., Hirschberg A., Worzfeld T., Penachioni J.Y., Korostylev A., Swiercz J.M., Vodrazka P., Mauti O., Stoeckli E.T., Tamagnone L., Offermanns S., Kuner R.

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

2008 · Mol. Cell

PubMed 18691976 ↗

Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054; 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.

24 · A quantitative atlas of mitotic phosphorylation.

2008 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 18669648 ↗

Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054; 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.

25 · Brk is coamplified with ErbB2 to promote proliferation in breast cancer.

2008 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 18719096 ↗

Scope & authors

INTERACTION WITH PTK6; ACTIVITY REGULATION

Xiang B., Chatti K., Qiu H., Lakshmi B., Krasnitz A., Hicks J., Yu M., Miller W.T., Muthuswamy S.K.

26 · ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells.

2009 · Mol. Cancer Res.

PubMed 19372587 ↗

Scope & authors

FUNCTION IN NUCLEUS

Hawthorne V.S., Huang W.C., Neal C.L., Tseng L.M., Hung M.C., Yu D.

27 · Copine-III interacts with ErbB2 and promotes tumor cell migration.

2010 · Oncogene

PubMed 20010870 ↗

Scope & authors

INTERACTION WITH CPNE3

Heinrich C., Keller C., Boulay A., Vecchi M., Bianchi M., Sack R., Lienhard S., Duss S., Hofsteenge J., Hynes N.E.

28 · ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells.

2010 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 20937854 ↗

Scope & authors

FUNCTION

Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.

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

2010 · Sci. Signal.

PubMed 20068231 ↗

Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107; 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.

30 · Genetic and structural variation in the gastric cancer kinome revealed through targeted deep sequencing.

2011 · Cancer Res.

PubMed 21097718 ↗

Scope & authors

CHROMOSOMAL REARRANGEMENT WITH CDK12

Zang Z.J., Ong C.K., Cutcutache I., Yu W., Zhang S.L., Huang D., Ler L.D., Dykema K., Gan A., Tao J., Lim S., Liu Y., Futreal P.A., Grabsch H., Furge K.A., Goh L.K., Rozen S., Teh B.T., Tan P.

31 · Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes.

2011 · Cancer Res.

PubMed 21555369 ↗

Scope & authors

FUNCTION IN NUCLEUS; INTERACTION WITH ACTB AND RPA194; SUBCELLULAR LOCATION

Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H., Chen H.Y., Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P., Lien H.C., Tsai C.H., Hung M.C.

32 · Dissociation of epidermal growth factor receptor and ErbB2 heterodimers in the presence of somatostatin receptor 5 modulate signaling pathways.

2011 · Endocrinology

PubMed 21190959 ↗

Scope & authors

INTERACTION WITH EGFR

Kharmate G., Rajput P.S., Watt H.L., Somvanshi R.K., Chaudhari N., Qiu X., Kumar U.

33 · System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

2011 · Sci. Signal.

PubMed 21406692 ↗

Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.

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

2013 · J. Proteome Res.

PubMed 23186163 ↗

Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182; SER-1054; SER-1083 AND THR-1166; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]

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

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

2014 · J. Proteomics

PubMed 24275569 ↗

Scope & authors

PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054 AND SER-1151; 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.

36 · Client proteins and small molecule inhibitors display distinct binding preferences for constitutive and stress-induced HSP90 isoforms and their conformationally restricted mutants.

2015 · PLoS ONE

PubMed 26517842 ↗

Scope & authors

INTERACTION WITH HSP90AA1 AND HSP90AB1

Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K., Rivas C., Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T., Beebe K., Trepel J.B., Neckers L.

37 · Crystal structure and substrate specificity of PTPN12.

2016 · Cell Rep.

PubMed 27134172 ↗

Scope & authors

PHOSPHORYLATION AT TYR-1112; TYR-1139; TYR-1196 AND TYR-1248; DEPHOSPHORYLATION BY PTPN12

Li H., Yang F., Liu C., Xiao P., Xu Y., Liang Z., Liu C., Wang H., Wang W., Zheng W., Zhang W., Ma X., He D., Song X., Cui F., Xu Z., Yi F., Sun J.P., Yu X.

38 · SORLA regulates endosomal trafficking and oncogenic fitness of HER2.

2019 · Nat. Commun.

PubMed 31138794 ↗

Scope & authors

INTERACTION WITH SORL1; SUBCELLULAR LOCATION

Pietilae M., Sahgal P., Peuhu E., Jaentti N.Z., Paatero I., Naervae E., Al-Akhrass H., Lilja J., Georgiadou M., Andersen O.M., Padzik A., Sihto H., Joensuu H., Blomqvist M., Saarinen I., Bostroem P.J., Taimen P., Ivaska J.

39 · SH3BGRL confers innate drug resistance in breast cancer by stabilizing HER2 activation on cell membrane.

2020 · J. Exp. Clin. Cancer Res.

PubMed 32381043 ↗

Scope & authors

INTERACTION WITH SH3BGRL; SUBCELLULAR LOCATION; PHOSPHORYLATION AT TYR-877 AND TYR-1196

Li H., Zhang M., Wei Y., Haider F., Lin Y., Guan W., Liu Y., Zhang S., Yuan R., Yang X., Yang S., Wang H.

40 · SH3BGRL3 binds to myosin 1c in a calcium dependent manner and modulates migration in the MDA-MB-231 cell line.

2021 · BMC Mol. Cell Biol.

PubMed 34380438 ↗

Scope & authors

SUBCELLULAR LOCATION

Di Pisa F., Pesenti E., Bono M., Mazzarello A.N., Bernardi C., Lisanti M.P., Renzone G., Scaloni A., Ciccone E., Fais F., Bruno S., Scartezzini P., Ghiotto F.

41 · IGFBP5 is an ROR1 ligand promoting glioblastoma invasion via ROR1/HER2-CREB signaling axis.

2023 · Nat. Commun.

PubMed 36949068 ↗

Scope & authors

INTERACTION WITH ROR1

Lin W., Niu R., Park S.M., Zou Y., Kim S.S., Xia X., Xing S., Yang Q., Sun X., Yuan Z., Zhou S., Zhang D., Kwon H.J., Park S., Il Kim C., Koo H., Liu Y., Wu H., Zheng M., Yoo H., Shi B., Park J.B., Yin J.

42 · Poor binding of a HER-2/neu epitope (GP2) to HLA-A2.1 is due to a lack of interactions with the center of the peptide.

1999 · J. Biol. Chem.

PubMed 10593938 ↗

Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH HLA AND BETA-2 MICROGLOBULIN

Kuhns J.J., Batalia M.A., Yan S., Collins E.J.

43 · Novel mode of ligand recognition by the Erbin PDZ domain.

2003 · J. Biol. Chem.

PubMed 12444095 ↗

Scope & authors

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

Birrane G., Chung J., Ladias J.A.

44 · Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2.

2003 · J. Biomol. NMR

PubMed 12975581 ↗

Scope & authors

STRUCTURE BY NMR OF 1135-1144 IN COMPLEX WITH GRB7; INTERACTION WITH GRB7

Ivancic M., Daly R.J., Lyons B.A.

45 · Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab.

2003 · Nature

PubMed 12610629 ↗

Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH THE ANTIBODY HERCEPTIN

Cho H.-S., Mason K., Ramyar K.X., Stanley A.M., Gabelli S.B., Denney D.W. Jr., Leahy D.J.

46 · Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex.

2004 · Cancer Cell

PubMed 15093539 ↗

Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH THE ANTIBODY PERTUZUMAB; INTERACTION WITH ERBB3; MUTAGENESIS OF 317-LEU-HIS-318; DISULFIDE BONDS; GLYCOSYLATION AT ASN-187; ASN-259 AND ASN-530

Franklin M.C., Carey K.D., Vajdos F.F., Leahy D.J., de Vos A.M., Sliwkowski M.X.

47 · Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site.

2009 · Science

PubMed 19299620 ↗

Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH THE ANTIBODY HERCEPTIN; DISULFIDE BONDS; GLYCOSYLATION AT ASN-259 AND ASN-530

Bostrom J., Yu S.F., Kan D., Appleton B.A., Lee C.V., Billeci K., Man W., Peale F., Ross S., Wiesmann C., Fuh G.

48 · Structural basis for high-affinity HER2 receptor binding by an engineered protein.

2010 · Proc. Natl. Acad. Sci. U.S.A.

PubMed 20696930 ↗

Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ENGINEERED ANTIBODY ZHER2; DISULFIDE BONDS; GLYCOSYLATION AT ASN-68; ASN-259 AND ASN-571

Eigenbrot C., Ultsch M., Dubnovitsky A., Abrahmsen L., Hard T.

49 · Structural analysis of the mechanism of inhibition and allosteric activation of the kinase domain of HER2 protein.

2011 · J. Biol. Chem.

PubMed 21454582 ↗

Scope & authors

X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH INHIBITOR SYR127063; CATALYTIC ACTIVITY; SUBUNIT; ACTIVITY REGULATION

Aertgeerts K., Skene R., Yano J., Sang B.C., Zou H., Snell G., Jennings A., Iwamoto K., Habuka N., Hirokawa A., Ishikawa T., Tanaka T., Miki H., Ohta Y., Sogabe S.

50 · Characterization of a new allele of the human ERBB2 gene by allele-specific competition hybridization.

1993 · Genomics

PubMed 8095488 ↗

Scope & authors

VARIANTS VAL-654 AND VAL-655

Ehsani A., Low J., Wallace R.B., Wu A.M.

51 · Lung cancer: intragenic ERBB2 kinase mutations in tumours.

2004 · Nature

PubMed 15457249 ↗

Scope & authors

INVOLVEMENT IN CANCER; VARIANT GASC SER-776; VARIANT OC SER-857; VARIANT GLM LYS-914; VARIANTS LNCR PRO-755; ALA-TYR-VAL-MET-774 INS AND VAL-GLY-SER-779 INS

Stephens P., Hunter C., Bignell G., Edkins S., Davies H., Teague J., Stevens C., O'Meara S., Smith R., Parker A., Barthorpe A., Blow M., Brackenbury L., Butler A., Clarke O., Cole J., Dicks E., Dike A., Drozd A., Edwards K., Forbes S., Foster R., Gray K., Greenman C., Halliday K., Hills K., Kosmidou V., Lugg R., Menzies A., Perry J., Petty R., Raine K., Ratford L., Shepherd R., Small A., Stephens Y., Tofts C., Varian J., West S., Widaa S., Yates A., Brasseur F., Cooper C.S., Flanagan A.M., Knowles M., Leung S.Y., Louis D.N., Looijenga L.H., Malkowicz B., Pierotti M.A., Teh B., Chenevix-Trench G., Weber B.L., Yuen S.T., Harris G., Goldstraw P., Nicholson A.G., Futreal P.A., Wooster R., Stratton M.R.

52 · Patterns of somatic mutation in human cancer genomes.

2007 · Nature

PubMed 17344846 ↗

Scope & authors

VARIANTS [LARGE SCALE ANALYSIS] VAL-654; VAL-655; SER-768; ALA-1170 AND ASP-1216; VARIANT GASC SER-776; VARIANT OC SER-857

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.

53 · Dysregulation of the NRG1/ERBB pathway causes a developmental disorder with gastrointestinal dysmotility in humans.

2021 · J. Clin. Invest.

PubMed 33497358 ↗

Scope & authors

INVOLVEMENT IN VSCN2; VARIANT VSCN2 VAL-710; CHARACTERIZATION OF VARIANT VSCN2 VAL-710; SUBCELLULAR LOCATION; PHOSPHORYLATION

Le T.L., Galmiche L., Levy J., Suwannarat P., Hellebrekers D.M., Morarach K., Boismoreau F., Theunissen T.E., Lefebvre M., Pelet A., Martinovic J., Gelot A., Guimiot F., Calleroz A., Gitiaux C., Hully M., Goulet O., Chardot C., Drunat S., Capri Y., Bole-Feysot C., Nitschke P., Whalen S., Mouthon L., Babcock H.E., Hofstra R., de Coo I.F., Tabet A.C., Molina T.J., Keren B., Brooks A., Smeets H.J., Marklund U., Gordon C.T., Lyonnet S., Amiel J., Bondurand N.

Atlas of Genetics and Cytogenetics in Oncology and Haematology ↗

Wikipedia ↗

Annotation coverage audit

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

229 source comments and features accounted for.

View annotation inventory

Source record	Type	Section
FUNCTION:0	FUNCTION	function
FUNCTION:1	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
SUBCELLULAR LOCATION:2	SUBCELLULAR LOCATION	location
SUBCELLULAR LOCATION:3	SUBCELLULAR LOCATION	location
ALTERNATIVE PRODUCTS:0	ALTERNATIVE PRODUCTS	sequence
TISSUE SPECIFICITY:0	TISSUE SPECIFICITY	expression
PTM:0	PTM	processing
POLYMORPHISM:0	POLYMORPHISM	disease
DISEASE:0	DISEASE	disease
DISEASE:1	DISEASE	disease
DISEASE:2	DISEASE	disease
DISEASE:3	DISEASE	disease
DISEASE:4	DISEASE	disease
DISEASE:5	DISEASE	disease
MISCELLANEOUS:0	MISCELLANEOUS	function
MISCELLANEOUS:1	MISCELLANEOUS	function
MISCELLANEOUS:2	MISCELLANEOUS	function
SIMILARITY:0	SIMILARITY	domains
WEB RESOURCE:0	WEB RESOURCE	sources
WEB RESOURCE:1	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	Domain	domains
feature-6	Region	domains
feature-7	Region	domains
feature-8	Region	domains
feature-9	Region	domains
feature-10	Motif	domains
feature-11	Compositional bias	domains
feature-12	Active site	domains
feature-13	Binding site	domains
feature-14	Binding site	domains
feature-15	Modified residue	processing
feature-16	Modified residue	processing
feature-17	Modified residue	processing
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	Glycosylation	processing
feature-28	Glycosylation	processing
feature-29	Glycosylation	processing
feature-30	Glycosylation	processing
feature-31	Glycosylation	processing
feature-32	Glycosylation	processing
feature-33	Glycosylation	processing
feature-34	Disulfide bond	processing
feature-35	Disulfide bond	processing
feature-36	Disulfide bond	processing
feature-37	Disulfide bond	processing
feature-38	Disulfide bond	processing
feature-39	Disulfide bond	processing
feature-40	Disulfide bond	processing
feature-41	Disulfide bond	processing
feature-42	Disulfide bond	processing
feature-43	Disulfide bond	processing
feature-44	Disulfide bond	processing
feature-45	Disulfide bond	processing
feature-46	Disulfide bond	processing
feature-47	Disulfide bond	processing
feature-48	Disulfide bond	processing
feature-49	Disulfide bond	processing
feature-50	Disulfide bond	processing
feature-51	Disulfide bond	processing
feature-52	Disulfide bond	processing
feature-53	Disulfide bond	processing
feature-54	Disulfide bond	processing
feature-55	Disulfide bond	processing
feature-56	Disulfide bond	processing
feature-57	Disulfide bond	processing
feature-58	Disulfide bond	processing
feature-59	Alternative sequence	sequence
feature-60	Alternative sequence	sequence
feature-61	Alternative sequence	sequence
feature-62	Alternative sequence	sequence
feature-63	Alternative sequence	sequence
feature-64	Alternative sequence	sequence
feature-65	Alternative sequence	sequence
feature-66	Natural variant	disease
feature-67	Natural variant	disease
feature-68	Natural variant	disease
feature-69	Natural variant	disease
feature-70	Natural variant	disease
feature-71	Natural variant	disease
feature-72	Natural variant	disease
feature-73	Natural variant	disease
feature-74	Natural variant	disease
feature-75	Natural variant	disease
feature-76	Natural variant	disease
feature-77	Natural variant	disease
feature-78	Natural variant	disease
feature-79	Mutagenesis	disease
feature-80	Mutagenesis	disease
feature-81	Mutagenesis	disease
feature-82	Mutagenesis	disease
feature-83	Mutagenesis	disease
feature-84	Beta strand	sequence
feature-85	Helix	sequence
feature-86	Beta strand	sequence
feature-87	Helix	sequence
feature-88	Beta strand	sequence
feature-89	Beta strand	sequence
feature-90	Beta strand	sequence
feature-91	Turn	sequence
feature-92	Beta strand	sequence
feature-93	Beta strand	sequence
feature-94	Turn	sequence
feature-95	Beta strand	sequence
feature-96	Beta strand	sequence
feature-97	Beta strand	sequence
feature-98	Helix	sequence
feature-99	Helix	sequence
feature-100	Helix	sequence
feature-101	Beta strand	sequence
feature-102	Helix	sequence
feature-103	Helix	sequence
feature-104	Beta strand	sequence
feature-105	Helix	sequence
feature-106	Helix	sequence
feature-107	Beta strand	sequence
feature-108	Helix	sequence
feature-109	Beta strand	sequence
feature-110	Helix	sequence
feature-111	Beta strand	sequence
feature-112	Beta strand	sequence
feature-113	Beta strand	sequence
feature-114	Beta strand	sequence
feature-115	Turn	sequence
feature-116	Beta strand	sequence
feature-117	Turn	sequence
feature-118	Beta strand	sequence
feature-119	Beta strand	sequence
feature-120	Beta strand	sequence
feature-121	Beta strand	sequence
feature-122	Beta strand	sequence
feature-123	Beta strand	sequence
feature-124	Beta strand	sequence
feature-125	Beta strand	sequence
feature-126	Helix	sequence
feature-127	Turn	sequence
feature-128	Helix	sequence
feature-129	Beta strand	sequence
feature-130	Helix	sequence
feature-131	Helix	sequence
feature-132	Helix	sequence
feature-133	Helix	sequence
feature-134	Beta strand	sequence
feature-135	Beta strand	sequence
feature-136	Beta strand	sequence
feature-137	Helix	sequence
feature-138	Beta strand	sequence
feature-139	Turn	sequence
feature-140	Beta strand	sequence
feature-141	Beta strand	sequence
feature-142	Turn	sequence
feature-143	Helix	sequence
feature-144	Beta strand	sequence
feature-145	Beta strand	sequence
feature-146	Helix	sequence
feature-147	Turn	sequence
feature-148	Helix	sequence
feature-149	Beta strand	sequence
feature-150	Helix	sequence
feature-151	Beta strand	sequence
feature-152	Beta strand	sequence
feature-153	Beta strand	sequence
feature-154	Beta strand	sequence
feature-155	Beta strand	sequence
feature-156	Beta strand	sequence
feature-157	Beta strand	sequence
feature-158	Beta strand	sequence
feature-159	Beta strand	sequence
feature-160	Beta strand	sequence
feature-161	Beta strand	sequence
feature-162	Beta strand	sequence
feature-163	Beta strand	sequence
feature-164	Beta strand	sequence
feature-165	Beta strand	sequence
feature-166	Beta strand	sequence
feature-167	Beta strand	sequence
feature-168	Helix	sequence
feature-169	Helix	sequence
feature-170	Helix	sequence
feature-171	Helix	sequence
feature-172	Beta strand	sequence
feature-173	Beta strand	sequence
feature-174	Beta strand	sequence
feature-175	Helix	sequence
feature-176	Beta strand	sequence
feature-177	Beta strand	sequence
feature-178	Helix	sequence
feature-179	Turn	sequence
feature-180	Helix	sequence
feature-181	Helix	sequence
feature-182	Beta strand	sequence
feature-183	Beta strand	sequence
feature-184	Helix	sequence
feature-185	Beta strand	sequence
feature-186	Helix	sequence
feature-187	Helix	sequence
feature-188	Helix	sequence
feature-189	Helix	sequence
feature-190	Turn	sequence
feature-191	Helix	sequence
feature-192	Helix	sequence
feature-193	Helix	sequence
feature-194	Helix	sequence
feature-195	Helix	sequence
feature-196	Helix	sequence
feature-197	Helix	sequence
feature-198	Helix	sequence
feature-199	Helix	sequence
feature-200	Turn	sequence
feature-201	Helix	sequence
feature-202	Beta strand	sequence

ERBB2Receptor tyrosine-protein kinase erbB-2

Function

Additional functional context

Catalytic activity

Activity regulation

GO functions & biological processes

Names & Taxonomy

Subcellular Location

Membrane topology 3

Disease & Variants

Glioma GLM

Ovarian cancer OC

Lung cancer LNCR

Gastric cancer GASC

Visceral neuropathy, familial, 2, autosomal recessive VSCN2

Polymorphism notes

Natural variants 13

Laboratory mutagenesis 5

PTM/Processing

Processed chains & precursor regions 2

Modifications 44

Expression

Interaction

Documented interaction partners

Complex membership & assembly descriptions

UniProt subunit description

Other association resources

Structure

7MN5 · Structure of the HER2/HER3/NRG1b Heterodimer Extracellular Domain

Recorded components

Biological assemblies

Publication

Available structures 64

Family & Domains

Domain architecture

Atlas domains, motifs & repeats 9

UniProt domains, repeats & motifs 2

Functional sites 3

Sequence regions 5

Sequence & Isoforms

Sequence & isoforms

Isoform sequence differences 7

Sequence conflicts & cautions 0

Recorded secondary structure 119

Similar Proteins

Similar proteins · UniRef

Homologs

OMA orthologs

Sources & References

Publications in this UniProt entry

Annotation coverage audit