ERBB2
entrez
2064
canonical
uniprot
P04626
canonical
ensembl
ENSG00000141736
resolver
ensp
ENSP00000269571
resolver
ensp
ENSP00000404047
resolver
ensp
ENSP00000462438
resolver
ensp
ENSP00000462808
resolver
ensp
ENSP00000463714
resolver
ensp
ENSP00000464420
resolver
ensp
ENSP00000521134
resolver
ensp
ENSP00000533155
resolver
ensp
ENSP00000533157
resolver
ensp
ENSP00000533158
resolver
ensp
ENSP00000533159
resolver
ensp
ENSP00000533160
resolver
ensp
ENSP00000533161
resolver
ensp
ENSP00000533162
resolver
ensp
ENSP00000608982
resolver
ensp
ENSP00000608983
resolver
ensp
ENSP00000736607
resolver
enst
ENST00000445658
resolver
enst
ENST00000578199
resolver
enst
ENST00000584014
resolver
enst
ENST00000584450
resolver
genesymbol
ERBB2
resolver
genesymbol_syn
HER2
resolver
genesymbol_syn
MLN19
resolver
genesymbol_syn
NEU
resolver
genesymbol_syn
NGL
resolver
hgnc
HGNC:3430
resolver
uniprot
B2RZG3
resolver
uniprot
B4DHN3
resolver
uniprot
B4DTR1
resolver
uniprot
F5H1T4
resolver
uniprot
F6QU44
resolver
uniprot
J3QLU9
resolver
uniprot
Q14256
resolver
uniprot
Q6LDV1
resolver
uniprot
Q9UMK4
resolver
uniprot
X5D2V5
resolver
uniprot
X5DNK3
resolver
uniprot_entry
B4DTR1_HUMAN
resolver
uniprot_entry
ERBB2_HUMAN
resolver
uniprot_entry
F5H1T4_HUMAN
resolver
uniprot_entry
F6QU44_HUMAN
resolver
uniprot_entry
J3QLU9_HUMAN
resolver
uniprot_entry
X5DNK3_HUMAN
resolver
uniprot_sec
B2RZG3
resolver
uniprot_sec
B4DHN3
resolver
uniprot_sec
Q14256
resolver
uniprot_sec
Q6LDV1
resolver
uniprot_sec
Q9UMK4
resolver
uniprot_sec
X5D2V5
resolver
activity_regulation
ACTIVITY REGULATION: Activated by dimerization. Not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity. {ECO:0000269|PubMed:18719096, ECO:0000269|PubMed:21454582}.
uniprot
proteins
amino_acid_sequence
MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLQVFETLEEITGYLYISAWPDSLPDLSVFQNLQVIRGRILHNGAYSLTLQGLGISWLGLRSLRELGSGLALIHHNTHLCFVHTVPWDQLFRNPHQALLHTANRPEDECVGEGLACHQLCARGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVNARHCLPCHPECQPQNGSVTCFGPEADQCVACAHYKDPPFCVARCPSGVKPDLSYMPIWKFPDEEGACQPCPINCTHSCVDLDDKGCPAEQRASPLTSIISAVVGILLVVVLGVVFGILIKRRQQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPDPAPGAGGMVHHRHRSSSTRSGGGDLTLGLEPSEEEAPRSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPTHDPSPLQRYSEDPTVPLPSETDGYVAPLTCSPQPEYVNQPDVRPQPPSPREGPLPAARPAGATLERPKTLSPGKNGVVKDVFAFGGAVENPEYLTPQGGAAPQPHPPPAFSPAFDNLYYWDQDPPERGAPPSTFKGTPTAENPEYLGLDVPV
uniprot
proteins
disease_involvement
DISEASE: Glioma (GLM) [MIM:137800]: 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. {ECO:0000269|PubMed:15457249}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Ovarian cancer (OC) [MIM:167000]: 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. {ECO:0000269|PubMed:15457249, ECO:0000269|PubMed:17344846}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Lung cancer (LNCR) [MIM:211980]: 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. {ECO:0000269|PubMed:15457249}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Gastric cancer (GASC) [MIM:613659]: 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. {ECO:0000269|PubMed:15457249, ECO:0000269|PubMed:17344846}. Note=The protein represented in this entry is involved in disease pathogenesis.; DISEASE: Note=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. {ECO:0000269|PubMed:21097718}.; DISEASE: Visceral neuropathy, familial, 2, autosomal recessive (VSCN2) [MIM:619465]: 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. {ECO:0000269|PubMed:33497358}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
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. {ECO:0000305}.; 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. {ECO:0000269|PubMed:10358079, ECO:0000269|PubMed:15380516, ECO:0000269|PubMed:21555369}.
uniprot
proteins
mass_dalton
137910
uniprot
proteins
mutagenesis
MUTAGEN 317..318; /note="LH->AA: Reduces dimerization with ERBB3."; /evidence="ECO:0000269|PubMed:15093539"; MUTAGEN 611; /note="M->A: Prevents synthesis of isoform 2."; /evidence="ECO:0000269|PubMed:16794579"; MUTAGEN 687; /note="M->A: Prevents synthesis of isoform 3."; /evidence="ECO:0000269|PubMed:16794579"; MUTAGEN 706; /note="M->A: No effect on isoform production."; /evidence="ECO:0000269|PubMed:16794579"; MUTAGEN 712; /note="M->A: No effect on isoform production."; /evidence="ECO:0000269|PubMed:16794579
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:27134172, ECO:0000269|PubMed:33497358, ECO:0000305}.
uniprot
proteins
protein_family
EGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10358079
uniprot
proteins
pubmed
10593938
uniprot
proteins
pubmed
10805725
uniprot
proteins
pubmed
12444095
uniprot
proteins
pubmed
12610629
uniprot
proteins
pubmed
12939402
uniprot
proteins
pubmed
12975581
uniprot
proteins
pubmed
15093539
uniprot
proteins
pubmed
15156151
uniprot
proteins
pubmed
15210733
uniprot
proteins
pubmed
15380516
uniprot
proteins
pubmed
15457249
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16314522
uniprot
proteins
pubmed
16794579
uniprot
proteins
pubmed
16978839
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17554007
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18719096
uniprot
proteins
pubmed
19299620
uniprot
proteins
pubmed
19372587
uniprot
proteins
pubmed
20010870
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20696930
uniprot
proteins
pubmed
20937854
uniprot
proteins
pubmed
21097718
uniprot
proteins
pubmed
21190959
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21454582
uniprot
proteins
pubmed
21555369
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24722188
uniprot
proteins
pubmed
26517842
uniprot
proteins
pubmed
27134172
uniprot
proteins
pubmed
2992089
uniprot
proteins
pubmed
2995967
uniprot
proteins
pubmed
2999974
uniprot
proteins
pubmed
3003577
uniprot
proteins
pubmed
3039351
uniprot
proteins
pubmed
31138794
uniprot
proteins
pubmed
32381043
uniprot
proteins
pubmed
33497358
uniprot
proteins
pubmed
34380438
uniprot
proteins
pubmed
36949068
uniprot
proteins
pubmed
8095488
uniprot
proteins
pubmed
8104414
uniprot
proteins
sequence_length
1255
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32381043}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:34380438}; Single-pass type I membrane protein {ECO:0000255}. Note=Internalized from the cell membrane in response to EGF stimulation. {ECO:0000269|PubMed:32381043}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:31138794, ECO:0000269|PubMed:33497358}; Single-pass type I membrane protein {ECO:0000255}. Early endosome {ECO:0000269|PubMed:31138794}. Cytoplasm, perinuclear region. Nucleus. Note=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 (PubMed:31138794). {ECO:0000269|PubMed:31138794}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.
uniprot
proteins
transmembrane_region
TRANSMEM 653..675; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins