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Protein

Receptor tyrosine-protein kinase erbB-2

Gene

ERBB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.Curated
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.3 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Activated by dimerization. Not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei753 – 7531ATPPROSITE-ProRule annotation
Active sitei845 – 8451Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi726 – 7349ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ErbB-3 class receptor binding Source: ProtInc
  • identical protein binding Source: IntAct
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
  • protein C-terminus binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • protein tyrosine kinase activity Source: BHF-UCL
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • receptor signaling protein tyrosine kinase activity Source: ProtInc
  • RNA polymerase I core binding Source: UniProtKB
  • transmembrane receptor protein tyrosine kinase activity Source: BHF-UCL
  • transmembrane signaling receptor activity Source: BHF-UCL

GO - Biological processi

  • cell proliferation Source: ProtInc
  • cell surface receptor signaling pathway Source: MGI
  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • cellular response to growth factor stimulus Source: UniProtKB
  • enzyme linked receptor protein signaling pathway Source: ProtInc
  • ERBB2 signaling pathway Source: Reactome
  • heart development Source: Ensembl
  • MAPK cascade Source: Reactome
  • motor neuron axon guidance Source: Ensembl
  • myelination Source: Ensembl
  • negative regulation of immature T cell proliferation in thymus Source: Ensembl
  • neuromuscular junction development Source: Ensembl
  • oligodendrocyte differentiation Source: Ensembl
  • peripheral nervous system development Source: Ensembl
  • phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of cell adhesion Source: BHF-UCL
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: UniProtKB
  • positive regulation of GTPase activity Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: UniProtKB
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of protein targeting to membrane Source: UniProtKB
  • positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase I promoter Source: UniProtKB
  • positive regulation of translation Source: UniProtKB
  • protein autophosphorylation Source: BHF-UCL
  • protein phosphorylation Source: ProtInc
  • regulation of angiogenesis Source: UniProtKB
  • regulation of cell motility Source: Reactome
  • regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • regulation of microtubule-based process Source: UniProtKB
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • signal transduction Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • transmembrane receptor protein tyrosine kinase signaling pathway Source: BHF-UCL
  • wound healing Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-1227986. Signaling by ERBB2.
R-HSA-1250196. SHC1 events in ERBB2 signaling.
R-HSA-1251932. PLCG1 events in ERBB2 signaling.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1306955. GRB7 events in ERBB2 signaling.
R-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-HSA-1963640. GRB2 events in ERBB2 signaling.
R-HSA-1963642. PI3K events in ERBB2 signaling.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6785631. ERBB2 Regulates Cell Motility.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8847993. ERBB2 Activates PTK6 Signaling.
SignaLinkiP04626.
SIGNORiP04626.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor tyrosine-protein kinase erbB-2 (EC:2.7.10.1)
Alternative name(s):
Metastatic lymph node gene 19 protein
Short name:
MLN 19
Proto-oncogene Neu
Proto-oncogene c-ErbB-2
Tyrosine kinase-type cell surface receptor HER2
p185erbB2
CD_antigen: CD340
Gene namesi
Name:ERBB2
Synonyms:HER2, MLN19, NEU, NGL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3430. ERBB2.

Subcellular locationi

Isoform 1 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 652630ExtracellularSequence analysisAdd
BLAST
Transmembranei653 – 67523HelicalSequence analysisAdd
BLAST
Topological domaini676 – 1255580CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: BHF-UCL
  • cytoplasm Source: HPA
  • cytoplasmic vesicle Source: Ensembl
  • endosome membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
  • receptor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Hereditary diffuse gastric cancer (HDGC)
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA cancer predisposition syndrome with increased susceptibility to diffuse gastric cancer. Diffuse gastric cancer is a malignant disease characterized by poorly differentiated infiltrating lesions resulting in thickening of the stomach. Malignant tumors start 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.
See also OMIM:137215
Glioma (GLM)
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionGliomas 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.
See also OMIM:137800
Ovarian cancer (OC)
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionThe 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.
See also OMIM:167000
Lung cancer (LNCR)
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA 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.
See also OMIM:211980
Gastric cancer (GASC)
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA 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.
See also OMIM:613659

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi317 – 3182LH → AA: Reduces dimerization with ERBB3. 1 Publication
Mutagenesisi611 – 6111M → A: Prevents synthesis of isoform 2. 1 Publication
Mutagenesisi687 – 6871M → A: Prevents synthesis of isoform 3. 1 Publication
Mutagenesisi706 – 7061M → A: No effect on isoform production. 1 Publication
Mutagenesisi712 – 7121M → A: No effect on isoform production. 1 Publication

Organism-specific databases

MalaCardsiERBB2.
MIMi137215. phenotype.
137800. phenotype.
167000. phenotype.
211980. phenotype.
613659. phenotype.
PharmGKBiPA27844.

Chemistry

ChEMBLiCHEMBL2363049.
DrugBankiDB05773. ado-trastuzumab emtansine.
DB08916. Afatinib.
DB01259. Lapatinib.
DB06366. Pertuzumab.
DB00072. Trastuzumab.
GuidetoPHARMACOLOGYi2019.

Polymorphism and mutation databases

BioMutaiERBB2.
DMDMi119533.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Chaini23 – 12551233Receptor tyrosine-protein kinase erbB-2PRO_0000016669Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 53Combined sources
Glycosylationi68 – 681N-linked (GlcNAc...)Combined sources1 Publication
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence analysis
Disulfide bondi162 ↔ 192Combined sources
Modified residuei182 – 1821PhosphothreonineCombined sources
Glycosylationi187 – 1871N-linked (GlcNAc...)Sequence analysisCombined sources
Disulfide bondi195 ↔ 204Combined sources
Disulfide bondi199 ↔ 212Combined sources
Disulfide bondi220 ↔ 227Combined sources
Disulfide bondi224 ↔ 235Combined sources
Disulfide bondi236 ↔ 244Combined sources
Disulfide bondi240 ↔ 252Combined sources
Disulfide bondi255 ↔ 264Combined sources
Glycosylationi259 – 2591N-linked (GlcNAc...)Combined sources3 Publications
Disulfide bondi268 ↔ 295Combined sources
Disulfide bondi299 ↔ 311Combined sources
Disulfide bondi315 ↔ 331Combined sources
Disulfide bondi334 ↔ 338Combined sources
Disulfide bondi342 ↔ 367Combined sources
Disulfide bondi475 ↔ 504Combined sources
Disulfide bondi511 ↔ 520Combined sources
Disulfide bondi515 ↔ 528Combined sources
Glycosylationi530 – 5301N-linked (GlcNAc...)Combined sources2 Publications
Disulfide bondi531 ↔ 540Combined sources
Disulfide bondi544 ↔ 560Combined sources
Disulfide bondi563 ↔ 576Combined sources
Disulfide bondi567 ↔ 584Combined sources
Glycosylationi571 – 5711N-linked (GlcNAc...)Combined sources1 Publication
Disulfide bondi587 ↔ 596Combined sources
Disulfide bondi600 ↔ 623Combined sources
Disulfide bondi626 ↔ 634Combined sources
Glycosylationi629 – 6291N-linked (GlcNAc...)Sequence analysis
Disulfide bondi630 ↔ 642Combined sources
Modified residuei1054 – 10541PhosphoserineCombined sources
Modified residuei1078 – 10781PhosphoserineBy similarity
Modified residuei1083 – 10831PhosphoserineCombined sources
Modified residuei1107 – 11071PhosphoserineCombined sources
Modified residuei1112 – 11121Phosphotyrosine1 Publication
Modified residuei1139 – 11391Phosphotyrosine1 Publication
Modified residuei1151 – 11511PhosphoserineCombined sources
Modified residuei1166 – 11661PhosphothreonineCombined sources
Modified residuei1196 – 11961Phosphotyrosine1 Publication
Modified residuei1248 – 12481Phosphotyrosine; by autocatalysisCombined sources2 Publications

Post-translational modificationi

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). Signaling via SEMA4C promotes phosphorylation at Tyr-1248 (PubMed:17554007). Dephosphorylated by PTPN12 (PubMed:27134172).Curated2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP04626.
PaxDbiP04626.
PeptideAtlasiP04626.
PRIDEiP04626.

PTM databases

iPTMnetiP04626.
PhosphoSiteiP04626.

Miscellaneous databases

PMAP-CutDBP04626.

Expressioni

Tissue specificityi

Expressed in a variety of tumor tissues including primary breast tumors and tumors from small bowel, esophagus, kidney and mouth.1 Publication

Gene expression databases

BgeeiENSG00000141736.
CleanExiHS_ERBB2.
ExpressionAtlasiP04626. baseline and differential.
GenevisibleiP04626. HS.

Organism-specific databases

HPAiCAB000043.
CAB020416.
CAB062555.
HPA001338.
HPA001383.

Interactioni

Subunit structurei

Homodimer. Heterodimer with EGFR, ERBB3 and ERBB4. Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1196. Interacts with PRKCABP and PLXNB1. Interacts (when phosphorylated on Tyr-1248) with MEMO1. Interacts with MUC1; the interaction is enhanced by heregulin (HRG). Interacts (when phosphorylated on Tyr-1139) with GRB7 (via SH2 domain). Interacts (when phosphorylated on Tyr-1248) with ERBIN. Interacts with KPNB1, RANBP2, EEA1, CRM1, CLTC, PTK6, RPA94 and ACTB. Interacts with 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).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-641062,EBI-641062
ABL1P005192EBI-641062,EBI-375543
ABL2P426846EBI-641062,EBI-1102694
ACTBP6070910EBI-641062,EBI-353944
ANKS1AQ926252EBI-641062,EBI-1048612
APBB1O002132EBI-641062,EBI-81694
BCAR3O758152EBI-641062,EBI-702336
CDC37Q165433EBI-641062,EBI-295634
CISHQ9NSE24EBI-641062,EBI-617866
CLNKQ7Z7G12EBI-641062,EBI-7878194
CRKLP461092EBI-641062,EBI-910
DOK1Q997042EBI-641062,EBI-1384360
DOK4Q8TEW62EBI-641062,EBI-6918542
EEA1Q150755EBI-641062,EBI-298113
EFNB1P9817211EBI-641062,EBI-538287
EGFRP0053321EBI-641062,EBI-297353
ERBB3P2186025EBI-641062,EBI-720706
ERBB4Q153033EBI-641062,EBI-80371
ERRFI1Q9UJM33EBI-641062,EBI-2941912
FGRP097693EBI-641062,EBI-1383732
FYNP062412EBI-641062,EBI-515315
GRAP2O757912EBI-641062,EBI-740418
GRB2P629934EBI-641062,EBI-401755
GRB7Q144515EBI-641062,EBI-970191
H2AFYO753676EBI-641062,EBI-2868511
H2AFYO75367-33EBI-641062,EBI-6250866
HSP90AA1P079004EBI-641062,EBI-296047
HSP90AB1P082383EBI-641062,EBI-352572
IQGAP1P469405EBI-641062,EBI-297509
IRS1P355682EBI-641062,EBI-517592
ITKQ088812EBI-641062,EBI-968552
JAK1P234582EBI-641062,EBI-1383438
KPNB1Q1497414EBI-641062,EBI-286758
MAPK8IP1Q9UQF23EBI-641062,EBI-78404
MAPK8IP2Q133873EBI-641062,EBI-722813
MATKP426792EBI-641062,EBI-751664
MEMO1Q9Y3166EBI-641062,EBI-1104564
NCK2O436392EBI-641062,EBI-713635
NRG1Q02297-72EBI-641062,EBI-2460927
PIK3C2BO007502EBI-641062,EBI-641107
PIK3R1P2798611EBI-641062,EBI-79464
PIK3R2O004596EBI-641062,EBI-346930
PIK3R3Q925699EBI-641062,EBI-79893
PLCG1P191745EBI-641062,EBI-79387
PLCG2P168853EBI-641062,EBI-617403
POLR1AO9560216EBI-641062,EBI-359472
PTK2Q053972EBI-641062,EBI-702142
PTK6Q138822EBI-641062,EBI-1383632
PTPN11Q061242EBI-641062,EBI-297779
PTPN12Q052094EBI-641062,EBI-2266035
PTPRBP234672EBI-641062,EBI-1265766
PTPRCP085752EBI-641062,EBI-1341
PTPRJQ129132EBI-641062,EBI-2264500
PTPRKQ152622EBI-641062,EBI-474052
PTPROQ168272EBI-641062,EBI-723739
RANBP2P497923EBI-641062,EBI-973138
RASA1P209368EBI-641062,EBI-1026476
RECKO959804EBI-641062,EBI-2823742
SH2D2AQ9NP312EBI-641062,EBI-490630
SHC1P293539EBI-641062,EBI-78835
SHC2P980773EBI-641062,EBI-7256023
SHC3Q925292EBI-641062,EBI-79084
SLA2Q9H6Q32EBI-641062,EBI-1222854
SOCS1O155242EBI-641062,EBI-968198
SRCP1293111EBI-641062,EBI-621482
STAT1P422243EBI-641062,EBI-1057697
STAT3P407639EBI-641062,EBI-518675
SUPT6HQ7KZ852EBI-641062,EBI-2515547
SYKP434057EBI-641062,EBI-78302
TLN1Q9Y4903EBI-641062,EBI-2462036
TNS2Q63HR24EBI-641062,EBI-949753
TNS3Q68CZ22EBI-641062,EBI-1220488
VAV1Q96D372EBI-641062,EBI-7875353
VAV2P527353EBI-641062,EBI-297549
XPO1O149802EBI-641062,EBI-355867

GO - Molecular functioni

  • ErbB-3 class receptor binding Source: ProtInc
  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: UniProtKB
  • protein dimerization activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein phosphatase binding Source: UniProtKB
  • RNA polymerase I core binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108376. 171 interactions.
DIPiDIP-8N.
IntActiP04626. 246 interactions.
MINTiMINT-158636.
STRINGi9606.ENSP00000269571.

Chemistry

BindingDBiP04626.

Structurei

Secondary structure

1
1255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 273Combined sources
Helixi39 – 5012Combined sources
Beta strandi54 – 585Combined sources
Beta strandi60 – 645Combined sources
Helixi72 – 743Combined sources
Beta strandi79 – 824Combined sources
Beta strandi84 – 885Combined sources
Beta strandi92 – 954Combined sources
Turni109 – 1113Combined sources
Beta strandi112 – 1176Combined sources
Turni130 – 1323Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi150 – 1567Combined sources
Turni164 – 1663Combined sources
Helixi169 – 1724Combined sources
Helixi175 – 1773Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi199 – 2024Combined sources
Beta strandi204 – 2085Combined sources
Helixi209 – 2113Combined sources
Beta strandi217 – 2193Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi227 – 2315Combined sources
Helixi232 – 2343Combined sources
Beta strandi240 – 2489Combined sources
Beta strandi251 – 26010Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi271 – 2744Combined sources
Turni276 – 2783Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi294 – 2985Combined sources
Beta strandi303 – 3053Combined sources
Beta strandi309 – 3146Combined sources
Beta strandi320 – 3234Combined sources
Beta strandi325 – 3273Combined sources
Beta strandi329 – 3324Combined sources
Beta strandi335 – 3373Combined sources
Helixi348 – 3525Combined sources
Turni358 – 3603Combined sources
Helixi361 – 3644Combined sources
Beta strandi368 – 3769Combined sources
Helixi378 – 3825Combined sources
Helixi385 – 3873Combined sources
Helixi396 – 4027Combined sources
Beta strandi405 – 4084Combined sources
Beta strandi410 – 4134Combined sources
Helixi423 – 4253Combined sources
Beta strandi430 – 4356Combined sources
Turni438 – 4403Combined sources
Beta strandi441 – 4477Combined sources
Beta strandi463 – 4697Combined sources
Turni477 – 4793Combined sources
Helixi482 – 4854Combined sources
Beta strandi486 – 4883Combined sources
Beta strandi493 – 4997Combined sources
Helixi501 – 5066Combined sources
Turni507 – 5093Combined sources
Helixi516 – 5183Combined sources
Beta strandi520 – 5245Combined sources
Helixi525 – 5273Combined sources
Beta strandi528 – 5369Combined sources
Beta strandi539 – 5424Combined sources
Beta strandi545 – 5517Combined sources
Beta strandi553 – 5564Combined sources
Beta strandi559 – 5624Combined sources
Beta strandi565 – 5673Combined sources
Beta strandi571 – 5733Combined sources
Beta strandi575 – 5806Combined sources
Beta strandi583 – 59210Combined sources
Beta strandi595 – 5995Combined sources
Beta strandi602 – 6043Combined sources
Beta strandi615 – 6173Combined sources
Beta strandi621 – 6255Combined sources
Beta strandi628 – 6325Combined sources
Beta strandi635 – 6373Combined sources
Helixi651 – 67828Combined sources
Helixi684 – 6907Combined sources
Helixi691 – 6977Combined sources
Helixi717 – 7193Combined sources
Beta strandi720 – 7289Combined sources
Beta strandi730 – 73910Combined sources
Beta strandi748 – 7558Combined sources
Helixi761 – 77414Combined sources
Beta strandi785 – 79915Combined sources
Helixi806 – 8127Combined sources
Turni814 – 8163Combined sources
Helixi819 – 83820Combined sources
Helixi848 – 8503Combined sources
Beta strandi851 – 8555Combined sources
Beta strandi858 – 8614Combined sources
Helixi886 – 8883Combined sources
Helixi891 – 8966Combined sources
Helixi901 – 91616Combined sources
Turni922 – 9254Combined sources
Helixi928 – 9303Combined sources
Helixi931 – 9366Combined sources
Helixi949 – 95810Combined sources
Helixi963 – 9653Combined sources
Helixi969 – 98012Combined sources
Helixi983 – 9864Combined sources
Helixi989 – 9924Combined sources
Helixi1003 – 10075Combined sources
Beta strandi1140 – 11423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFGX-ray1.25B1247-1255[»]
1MFLX-ray1.88B1247-1255[»]
1MW4NMR-B1135-1144[»]
1N8ZX-ray2.52C23-629[»]
1OVCmodel-A737-1031[»]
1QR1X-ray2.40C/F654-662[»]
1S78X-ray3.25A/B23-646[»]
2A91X-ray2.50A22-530[»]
2JWANMR-A/B641-684[»]
2KS1NMR-A641-684[»]
2L4KNMR-B1135-1144[»]
2N2ANMR-A/B644-700[»]
3BE1X-ray2.90A23-646[»]
3H3BX-ray2.45A/B23-214[»]
3MZWX-ray2.90A23-646[»]
3N85X-ray3.20A23-646[»]
3PP0X-ray2.25A/B703-1009[»]
3RCDX-ray3.21A/B/C/D713-1028[»]
3WLWX-ray3.09A/B23-586[»]
3WSQX-ray3.50A23-586[»]
4GFUX-ray2.00F1246-1252[»]
4HRLX-ray2.55C24-219[»]
4HRMX-ray3.20A/C24-219[»]
4HRNX-ray2.65C/D529-625[»]
ProteinModelPortaliP04626.
SMRiP04626. Positions 22-629, 641-1009.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04626.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini720 – 987268Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni676 – 68914Required for interaction with KPNB1 and EEA1Add
BLAST
Regioni1195 – 11973Interaction with PIK3C2BCurated

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi676 – 68914Nuclear localization signalAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1025. Eukaryota.
ENOG410XNSR. LUCA.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiP04626.
KOiK05083.
OMAiACYPLCA.
OrthoDBiEOG091G00NO.
PhylomeDBiP04626.
TreeFamiTF106002.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR032778. GF_recep_IV.
IPR009030. Growth_fac_rcpt_.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF14843. GF_recep_IV. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00261. FU. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 6 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P04626-1) [UniParc]FASTAAdd to basket
Also known as: ERBB2, HER2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELAALCRWG LLLALLPPGA ASTQVCTGTD MKLRLPASPE THLDMLRHLY
60 70 80 90 100
QGCQVVQGNL ELTYLPTNAS LSFLQDIQEV QGYVLIAHNQ VRQVPLQRLR
110 120 130 140 150
IVRGTQLFED NYALAVLDNG DPLNNTTPVT GASPGGLREL QLRSLTEILK
160 170 180 190 200
GGVLIQRNPQ LCYQDTILWK DIFHKNNQLA LTLIDTNRSR ACHPCSPMCK
210 220 230 240 250
GSRCWGESSE DCQSLTRTVC AGGCARCKGP LPTDCCHEQC AAGCTGPKHS
260 270 280 290 300
DCLACLHFNH SGICELHCPA LVTYNTDTFE SMPNPEGRYT FGASCVTACP
310 320 330 340 350
YNYLSTDVGS CTLVCPLHNQ EVTAEDGTQR CEKCSKPCAR VCYGLGMEHL
360 370 380 390 400
REVRAVTSAN IQEFAGCKKI FGSLAFLPES FDGDPASNTA PLQPEQLQVF
410 420 430 440 450
ETLEEITGYL YISAWPDSLP DLSVFQNLQV IRGRILHNGA YSLTLQGLGI
460 470 480 490 500
SWLGLRSLRE LGSGLALIHH NTHLCFVHTV PWDQLFRNPH QALLHTANRP
510 520 530 540 550
EDECVGEGLA CHQLCARGHC WGPGPTQCVN CSQFLRGQEC VEECRVLQGL
560 570 580 590 600
PREYVNARHC LPCHPECQPQ NGSVTCFGPE ADQCVACAHY KDPPFCVARC
610 620 630 640 650
PSGVKPDLSY MPIWKFPDEE GACQPCPINC THSCVDLDDK GCPAEQRASP
660 670 680 690 700
LTSIISAVVG ILLVVVLGVV FGILIKRRQQ KIRKYTMRRL LQETELVEPL
710 720 730 740 750
TPSGAMPNQA QMRILKETEL RKVKVLGSGA FGTVYKGIWI PDGENVKIPV
760 770 780 790 800
AIKVLRENTS PKANKEILDE AYVMAGVGSP YVSRLLGICL TSTVQLVTQL
810 820 830 840 850
MPYGCLLDHV RENRGRLGSQ DLLNWCMQIA KGMSYLEDVR LVHRDLAARN
860 870 880 890 900
VLVKSPNHVK ITDFGLARLL DIDETEYHAD GGKVPIKWMA LESILRRRFT
910 920 930 940 950
HQSDVWSYGV TVWELMTFGA KPYDGIPARE IPDLLEKGER LPQPPICTID
960 970 980 990 1000
VYMIMVKCWM IDSECRPRFR ELVSEFSRMA RDPQRFVVIQ NEDLGPASPL
1010 1020 1030 1040 1050
DSTFYRSLLE DDDMGDLVDA EEYLVPQQGF FCPDPAPGAG GMVHHRHRSS
1060 1070 1080 1090 1100
STRSGGGDLT LGLEPSEEEA PRSPLAPSEG AGSDVFDGDL GMGAAKGLQS
1110 1120 1130 1140 1150
LPTHDPSPLQ RYSEDPTVPL PSETDGYVAP LTCSPQPEYV NQPDVRPQPP
1160 1170 1180 1190 1200
SPREGPLPAA RPAGATLERP KTLSPGKNGV VKDVFAFGGA VENPEYLTPQ
1210 1220 1230 1240 1250
GGAAPQPHPP PAFSPAFDNL YYWDQDPPER GAPPSTFKGT PTAENPEYLG

LDVPV
Length:1,255
Mass (Da):137,910
Last modified:August 13, 1987 - v1
Checksum:i39E9DFDA04DCF962
GO
Isoform 2 (identifier: P04626-2) [UniParc]FASTAAdd to basket
Also known as: CTF-611

The sequence of this isoform differs from the canonical sequence as follows:
     1-610: Missing.

Note: Produced by alternative initiation at Met-611 of isoform 1.
Show »
Length:645
Mass (Da):70,917
Checksum:i288AFEFB6D101A34
GO
Isoform 3 (identifier: P04626-3) [UniParc]FASTAAdd to basket
Also known as: CTF-687

The sequence of this isoform differs from the canonical sequence as follows:
     1-686: Missing.

Note: Produced by alternative initiation at Met-687 of isoform 1.
Show »
Length:569
Mass (Da):62,568
Checksum:i090ABCB192CE1E73
GO
Isoform 4 (identifier: P04626-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MELAALCRWGLLLALLPPGAAST → MPRGSWKP

Note: Produced by alternative splicing of isoform 1.
Show »
Length:1,240
Mass (Da):136,501
Checksum:i1C679DD67798C0DE
GO
Isoform 5 (identifier: P04626-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Note: No experimental confirmation available. Gene prediction based on partial mRNA and EST data.
Show »
Length:1,225
Mass (Da):134,856
Checksum:i09B9238293C83D80
GO
Isoform 6 (identifier: P04626-6) [UniParc]FASTAAdd to basket
Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     633-648: Missing.
     771-883: AYVMAGVGSP...ETEYHADGGK → TISNLFSNFA...LMCPQGAGKA
     884-1255: Missing.

Show »
Length:888
Mass (Da):97,382
Checksum:iB2A5C268C58767E5
GO

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti452 – 4521W → C.1 Publication
Corresponds to variant rs4252633 [ dbSNP | Ensembl ].
VAR_016317
Natural varianti654 – 6541I → V in allele B3. 2 Publications
Corresponds to variant rs1801201 [ dbSNP | Ensembl ].
VAR_004077
Natural varianti655 – 6551I → V in allele B2 and allele B3. 3 Publications
Corresponds to variant rs1136201 [ dbSNP | Ensembl ].
VAR_004078
Natural varianti755 – 7551L → P in a lung adenocarcinoma sample; somatic mutation. 1 Publication
Corresponds to variant rs121913469 [ dbSNP | Ensembl ].
VAR_055432
Natural varianti768 – 7681L → S.1 Publication
Corresponds to variant rs56366519 [ dbSNP | Ensembl ].
VAR_042097
Natural varianti774 – 7741M → MAYVM in a lung adenocarcinoma sample; somatic mutation.
VAR_055433
Natural varianti776 – 7761G → S in a gastric adenocarcinoma sample; somatic mutation. 2 Publications
Corresponds to variant rs28933369 [ dbSNP | Ensembl ].
VAR_042098
Natural varianti779 – 7791S → SVGS in a lung adenocarcinoma sample; somatic mutation.
VAR_055434
Natural varianti857 – 8571N → S in an ovarian cancer sample; somatic mutation. 2 Publications
Corresponds to variant rs28933370 [ dbSNP | Ensembl ].
VAR_042099
Natural varianti914 – 9141E → K in a glioblastoma sample; somatic mutation. 1 Publication
Corresponds to variant rs28933368 [ dbSNP | Ensembl ].
VAR_055435
Natural varianti1170 – 11701P → A.4 Publications
Corresponds to variant rs61552325 [ dbSNP | Ensembl ].
VAR_016318
Natural varianti1216 – 12161A → D.1 Publication
Corresponds to variant rs55943169 [ dbSNP | Ensembl ].
VAR_042100

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 686686Missing in isoform 3. CuratedVSP_039250Add
BLAST
Alternative sequencei1 – 610610Missing in isoform 2. CuratedVSP_039249Add
BLAST
Alternative sequencei1 – 3030Missing in isoform 5. CuratedVSP_054787Add
BLAST
Alternative sequencei1 – 2323MELAA…GAAST → MPRGSWKP in isoform 4. 1 PublicationVSP_039248Add
BLAST
Alternative sequencei633 – 64816Missing in isoform 6. 1 PublicationVSP_055902Add
BLAST
Alternative sequencei771 – 883113AYVMA…ADGGK → TISNLFSNFAPRGPSACCEP TCWCHSGKGQDSLPREEWGR QRRFCLWGCRGEPRVLDTPG RSCPSAPPSSCLQPSLRQPL LLGPGPTRAGGSTQHLQRDT YGREPRVPGSGRASVNQKAK SAEALMCPQGAGKA in isoform 6. 1 PublicationVSP_055903Add
BLAST
Alternative sequencei884 – 1255372Missing in isoform 6. 1 PublicationVSP_055904Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AH001455 Genomic DNA. Translation: AAA35808.1.
X03363 mRNA. Translation: CAA27060.1.
M11730 mRNA. Translation: AAA75493.1.
M12036 Genomic DNA. Translation: AAA35978.1.
AY208911 Genomic DNA. Translation: AAO18082.1.
AK295195 mRNA. Translation: BAG58195.1.
CH471152 Genomic DNA. Translation: EAW60597.1.
BC167147 mRNA. Translation: AAI67147.1.
M16792
, M16789, M16790, M16791 Genomic DNA. Translation: AAA58637.1.
KJ534964 mRNA. Translation: AHW56604.1.
L29395 Genomic DNA. Translation: AAA35809.1.
M95667 Genomic DNA. Translation: AAC37531.1.
CCDSiCCDS32642.1. [P04626-1]
CCDS45667.1. [P04626-5]
CCDS74052.1. [P04626-4]
PIRiA24571.
RefSeqiNP_001005862.1. NM_001005862.2. [P04626-5]
NP_001276865.1. NM_001289936.1. [P04626-4]
NP_001276867.1. NM_001289938.1.
NP_004439.2. NM_004448.3. [P04626-1]
UniGeneiHs.446352.

Genome annotation databases

EnsembliENST00000269571; ENSP00000269571; ENSG00000141736. [P04626-1]
ENST00000406381; ENSP00000385185; ENSG00000141736. [P04626-5]
ENST00000541774; ENSP00000446466; ENSG00000141736. [P04626-4]
ENST00000584601; ENSP00000462438; ENSG00000141736. [P04626-5]
GeneIDi2064.
KEGGihsa:2064.
UCSCiuc060esv.1. human. [P04626-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Wikipedia

ERBB2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AH001455 Genomic DNA. Translation: AAA35808.1.
X03363 mRNA. Translation: CAA27060.1.
M11730 mRNA. Translation: AAA75493.1.
M12036 Genomic DNA. Translation: AAA35978.1.
AY208911 Genomic DNA. Translation: AAO18082.1.
AK295195 mRNA. Translation: BAG58195.1.
CH471152 Genomic DNA. Translation: EAW60597.1.
BC167147 mRNA. Translation: AAI67147.1.
M16792
, M16789, M16790, M16791 Genomic DNA. Translation: AAA58637.1.
KJ534964 mRNA. Translation: AHW56604.1.
L29395 Genomic DNA. Translation: AAA35809.1.
M95667 Genomic DNA. Translation: AAC37531.1.
CCDSiCCDS32642.1. [P04626-1]
CCDS45667.1. [P04626-5]
CCDS74052.1. [P04626-4]
PIRiA24571.
RefSeqiNP_001005862.1. NM_001005862.2. [P04626-5]
NP_001276865.1. NM_001289936.1. [P04626-4]
NP_001276867.1. NM_001289938.1.
NP_004439.2. NM_004448.3. [P04626-1]
UniGeneiHs.446352.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MFGX-ray1.25B1247-1255[»]
1MFLX-ray1.88B1247-1255[»]
1MW4NMR-B1135-1144[»]
1N8ZX-ray2.52C23-629[»]
1OVCmodel-A737-1031[»]
1QR1X-ray2.40C/F654-662[»]
1S78X-ray3.25A/B23-646[»]
2A91X-ray2.50A22-530[»]
2JWANMR-A/B641-684[»]
2KS1NMR-A641-684[»]
2L4KNMR-B1135-1144[»]
2N2ANMR-A/B644-700[»]
3BE1X-ray2.90A23-646[»]
3H3BX-ray2.45A/B23-214[»]
3MZWX-ray2.90A23-646[»]
3N85X-ray3.20A23-646[»]
3PP0X-ray2.25A/B703-1009[»]
3RCDX-ray3.21A/B/C/D713-1028[»]
3WLWX-ray3.09A/B23-586[»]
3WSQX-ray3.50A23-586[»]
4GFUX-ray2.00F1246-1252[»]
4HRLX-ray2.55C24-219[»]
4HRMX-ray3.20A/C24-219[»]
4HRNX-ray2.65C/D529-625[»]
ProteinModelPortaliP04626.
SMRiP04626. Positions 22-629, 641-1009.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108376. 171 interactions.
DIPiDIP-8N.
IntActiP04626. 246 interactions.
MINTiMINT-158636.
STRINGi9606.ENSP00000269571.

Chemistry

BindingDBiP04626.
ChEMBLiCHEMBL2363049.
DrugBankiDB05773. ado-trastuzumab emtansine.
DB08916. Afatinib.
DB01259. Lapatinib.
DB06366. Pertuzumab.
DB00072. Trastuzumab.
GuidetoPHARMACOLOGYi2019.

PTM databases

iPTMnetiP04626.
PhosphoSiteiP04626.

Polymorphism and mutation databases

BioMutaiERBB2.
DMDMi119533.

Proteomic databases

EPDiP04626.
PaxDbiP04626.
PeptideAtlasiP04626.
PRIDEiP04626.

Protocols and materials databases

DNASUi2064.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269571; ENSP00000269571; ENSG00000141736. [P04626-1]
ENST00000406381; ENSP00000385185; ENSG00000141736. [P04626-5]
ENST00000541774; ENSP00000446466; ENSG00000141736. [P04626-4]
ENST00000584601; ENSP00000462438; ENSG00000141736. [P04626-5]
GeneIDi2064.
KEGGihsa:2064.
UCSCiuc060esv.1. human. [P04626-1]

Organism-specific databases

CTDi2064.
GeneCardsiERBB2.
HGNCiHGNC:3430. ERBB2.
HPAiCAB000043.
CAB020416.
CAB062555.
HPA001338.
HPA001383.
MalaCardsiERBB2.
MIMi137215. phenotype.
137800. phenotype.
164870. gene.
167000. phenotype.
211980. phenotype.
613659. phenotype.
neXtProtiNX_P04626.
PharmGKBiPA27844.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1025. Eukaryota.
ENOG410XNSR. LUCA.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiP04626.
KOiK05083.
OMAiACYPLCA.
OrthoDBiEOG091G00NO.
PhylomeDBiP04626.
TreeFamiTF106002.

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-1227986. Signaling by ERBB2.
R-HSA-1250196. SHC1 events in ERBB2 signaling.
R-HSA-1251932. PLCG1 events in ERBB2 signaling.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1306955. GRB7 events in ERBB2 signaling.
R-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-HSA-1963640. GRB2 events in ERBB2 signaling.
R-HSA-1963642. PI3K events in ERBB2 signaling.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6785631. ERBB2 Regulates Cell Motility.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8847993. ERBB2 Activates PTK6 Signaling.
SignaLinkiP04626.
SIGNORiP04626.

Miscellaneous databases

ChiTaRSiERBB2. human.
EvolutionaryTraceiP04626.
GeneWikiiHER2/neu.
GenomeRNAii2064.
PMAP-CutDBP04626.
PROiP04626.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141736.
CleanExiHS_ERBB2.
ExpressionAtlasiP04626. baseline and differential.
GenevisibleiP04626. HS.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR032778. GF_recep_IV.
IPR009030. Growth_fac_rcpt_.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF14843. GF_recep_IV. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00261. FU. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERBB2_HUMAN
AccessioniPrimary (citable) accession number: P04626
Secondary accession number(s): B2RZG3
, B4DHN3, Q14256, Q6LDV1, Q9UMK4, X5D2V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: September 7, 2016
This is version 216 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  8. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.