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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)DescriptionActionsGraphical viewLength
Binding sitei753ATPPROSITE-ProRule annotation1
Active sitei845Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi726 – 734ATPPROSITE-ProRule annotation9

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

BioCyciZFISH:HS06866-MONOMER.
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.
R-HSA-8863795. Downregulation of ERBB2 signaling.
R-HSA-8866910. TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
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)DescriptionActionsGraphical viewLength
Topological domaini23 – 652ExtracellularSequence analysisAdd BLAST630
Transmembranei653 – 675HelicalSequence analysisAdd BLAST23
Topological domaini676 – 1255CytoplasmicSequence analysisAdd BLAST580

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)DescriptionActionsGraphical viewLength
Mutagenesisi317 – 318LH → AA: Reduces dimerization with ERBB3. 1 Publication2
Mutagenesisi611M → A: Prevents synthesis of isoform 2. 1 Publication1
Mutagenesisi687M → A: Prevents synthesis of isoform 3. 1 Publication1
Mutagenesisi706M → A: No effect on isoform production. 1 Publication1
Mutagenesisi712M → A: No effect on isoform production. 1 Publication1

Organism-specific databases

DisGeNETi2064.
MalaCardsiERBB2.
MIMi137215. phenotype.
137800. phenotype.
167000. phenotype.
211980. phenotype.
613659. phenotype.
OpenTargetsiENSG00000141736.
PharmGKBiPA27844.

Chemistry databases

ChEMBLiCHEMBL1824.
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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001666923 – 1255Receptor tyrosine-protein kinase erbB-2Add BLAST1233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi26 ↔ 53Combined sources
Glycosylationi68N-linked (GlcNAc...)Combined sources1 Publication1
Glycosylationi124N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi162 ↔ 192Combined sources
Modified residuei182PhosphothreonineCombined sources1
Glycosylationi187N-linked (GlcNAc...)Sequence analysisCombined sources1
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
Glycosylationi259N-linked (GlcNAc...)Combined sources3 Publications1
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
Glycosylationi530N-linked (GlcNAc...)Combined sources2 Publications1
Disulfide bondi531 ↔ 540Combined sources
Disulfide bondi544 ↔ 560Combined sources
Disulfide bondi563 ↔ 576Combined sources
Disulfide bondi567 ↔ 584Combined sources
Glycosylationi571N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi587 ↔ 596Combined sources
Disulfide bondi600 ↔ 623Combined sources
Disulfide bondi626 ↔ 634Combined sources
Glycosylationi629N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi630 ↔ 642Combined sources
Modified residuei1054PhosphoserineCombined sources1
Modified residuei1078PhosphoserineBy similarity1
Modified residuei1083PhosphoserineCombined sources1
Modified residuei1107PhosphoserineCombined sources1
Modified residuei1112Phosphotyrosine1 Publication1
Modified residuei1139Phosphotyrosine1 Publication1
Modified residuei1151PhosphoserineCombined sources1
Modified residuei1166PhosphothreonineCombined sources1
Modified residuei1196Phosphotyrosine1 Publication1
Modified residuei1248Phosphotyrosine; by autocatalysisCombined sources2 Publications1

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.
PhosphoSitePlusiP04626.

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 interactors.
DIPiDIP-8N.
IntActiP04626. 246 interactors.
MINTiMINT-158636.
STRINGi9606.ENSP00000269571.

Chemistry databases

BindingDBiP04626.

Structurei

Secondary structure

11255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 27Combined sources3
Helixi39 – 50Combined sources12
Beta strandi54 – 58Combined sources5
Beta strandi60 – 64Combined sources5
Helixi72 – 74Combined sources3
Beta strandi79 – 82Combined sources4
Beta strandi84 – 88Combined sources5
Beta strandi92 – 95Combined sources4
Turni109 – 111Combined sources3
Beta strandi112 – 117Combined sources6
Turni130 – 132Combined sources3
Beta strandi139 – 141Combined sources3
Beta strandi150 – 156Combined sources7
Turni164 – 166Combined sources3
Helixi169 – 172Combined sources4
Helixi175 – 177Combined sources3
Beta strandi182 – 184Combined sources3
Beta strandi199 – 202Combined sources4
Beta strandi204 – 208Combined sources5
Helixi209 – 211Combined sources3
Beta strandi217 – 219Combined sources3
Beta strandi221 – 223Combined sources3
Beta strandi227 – 231Combined sources5
Helixi232 – 234Combined sources3
Beta strandi240 – 248Combined sources9
Beta strandi251 – 260Combined sources10
Beta strandi263 – 267Combined sources5
Beta strandi271 – 274Combined sources4
Turni276 – 278Combined sources3
Beta strandi281 – 283Combined sources3
Beta strandi289 – 291Combined sources3
Beta strandi294 – 298Combined sources5
Beta strandi303 – 305Combined sources3
Beta strandi309 – 314Combined sources6
Beta strandi320 – 323Combined sources4
Beta strandi325 – 327Combined sources3
Beta strandi329 – 332Combined sources4
Beta strandi335 – 337Combined sources3
Helixi348 – 352Combined sources5
Turni358 – 360Combined sources3
Helixi361 – 364Combined sources4
Beta strandi368 – 376Combined sources9
Helixi378 – 382Combined sources5
Helixi385 – 387Combined sources3
Helixi396 – 402Combined sources7
Beta strandi405 – 408Combined sources4
Beta strandi410 – 413Combined sources4
Helixi423 – 425Combined sources3
Beta strandi430 – 435Combined sources6
Turni438 – 440Combined sources3
Beta strandi441 – 447Combined sources7
Beta strandi463 – 469Combined sources7
Turni477 – 479Combined sources3
Helixi482 – 485Combined sources4
Beta strandi486 – 488Combined sources3
Beta strandi493 – 499Combined sources7
Helixi501 – 506Combined sources6
Turni507 – 509Combined sources3
Helixi516 – 518Combined sources3
Beta strandi520 – 524Combined sources5
Helixi525 – 527Combined sources3
Beta strandi528 – 536Combined sources9
Beta strandi539 – 542Combined sources4
Beta strandi545 – 551Combined sources7
Beta strandi553 – 556Combined sources4
Beta strandi559 – 562Combined sources4
Beta strandi565 – 567Combined sources3
Beta strandi571 – 573Combined sources3
Beta strandi575 – 580Combined sources6
Beta strandi583 – 592Combined sources10
Beta strandi595 – 599Combined sources5
Beta strandi602 – 604Combined sources3
Beta strandi615 – 617Combined sources3
Beta strandi621 – 625Combined sources5
Beta strandi628 – 632Combined sources5
Beta strandi635 – 637Combined sources3
Helixi651 – 678Combined sources28
Helixi684 – 690Combined sources7
Helixi691 – 697Combined sources7
Helixi717 – 719Combined sources3
Beta strandi720 – 728Combined sources9
Beta strandi730 – 739Combined sources10
Beta strandi748 – 755Combined sources8
Helixi761 – 774Combined sources14
Beta strandi785 – 799Combined sources15
Helixi806 – 812Combined sources7
Turni814 – 816Combined sources3
Helixi819 – 838Combined sources20
Helixi848 – 850Combined sources3
Beta strandi851 – 855Combined sources5
Beta strandi858 – 861Combined sources4
Helixi886 – 888Combined sources3
Helixi891 – 896Combined sources6
Helixi901 – 916Combined sources16
Turni922 – 925Combined sources4
Helixi928 – 930Combined sources3
Helixi931 – 936Combined sources6
Helixi949 – 958Combined sources10
Helixi963 – 965Combined sources3
Helixi969 – 980Combined sources12
Helixi983 – 986Combined sources4
Helixi989 – 992Combined sources4
Helixi1003 – 1007Combined sources5
Beta strandi1140 – 1142Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04626.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini720 – 987Protein kinasePROSITE-ProRule annotationAdd BLAST268

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni676 – 689Required for interaction with KPNB1 and EEA11 PublicationAdd BLAST14
Regioni1195 – 1197Interaction with PIK3C2BCurated3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi676 – 689Nuclear localization signalAdd BLAST14

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_016317452W → C.1 PublicationCorresponds to variant rs4252633dbSNPEnsembl.1
Natural variantiVAR_004077654I → V in allele B3. 2 PublicationsCorresponds to variant rs1801201dbSNPEnsembl.1
Natural variantiVAR_004078655I → V in allele B2 and allele B3. 3 PublicationsCorresponds to variant rs1136201dbSNPEnsembl.1
Natural variantiVAR_055432755L → P in a lung adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs121913469dbSNPEnsembl.1
Natural variantiVAR_042097768L → S.1 PublicationCorresponds to variant rs56366519dbSNPEnsembl.1
Natural variantiVAR_055433774M → MAYVM in a lung adenocarcinoma sample; somatic mutation. 1
Natural variantiVAR_042098776G → S in a gastric adenocarcinoma sample; somatic mutation. 2 PublicationsCorresponds to variant rs28933369dbSNPEnsembl.1
Natural variantiVAR_055434779S → SVGS in a lung adenocarcinoma sample; somatic mutation. 1
Natural variantiVAR_042099857N → S in an ovarian cancer sample; somatic mutation. 2 PublicationsCorresponds to variant rs28933370dbSNPEnsembl.1
Natural variantiVAR_055435914E → K in a glioblastoma sample; somatic mutation. 1 PublicationCorresponds to variant rs28933368dbSNPEnsembl.1
Natural variantiVAR_0163181170P → A.4 PublicationsCorresponds to variant rs61552325dbSNPEnsembl.1
Natural variantiVAR_0421001216A → D.1 PublicationCorresponds to variant rs55943169dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0392501 – 686Missing in isoform 3. CuratedAdd BLAST686
Alternative sequenceiVSP_0392491 – 610Missing in isoform 2. CuratedAdd BLAST610
Alternative sequenceiVSP_0547871 – 30Missing in isoform 5. CuratedAdd BLAST30
Alternative sequenceiVSP_0392481 – 23MELAA…GAAST → MPRGSWKP in isoform 4. 1 PublicationAdd BLAST23
Alternative sequenceiVSP_055902633 – 648Missing in isoform 6. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_055903771 – 883AYVMA…ADGGK → TISNLFSNFAPRGPSACCEP TCWCHSGKGQDSLPREEWGR QRRFCLWGCRGEPRVLDTPG RSCPSAPPSSCLQPSLRQPL LLGPGPTRAGGSTQHLQRDT YGREPRVPGSGRASVNQKAK SAEALMCPQGAGKA in isoform 6. 1 PublicationAdd BLAST113
Alternative sequenceiVSP_055904884 – 1255Missing in isoform 6. 1 PublicationAdd BLAST372

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry databases

BindingDBiP04626.
ChEMBLiCHEMBL1824.
DrugBankiDB05773. ado-trastuzumab emtansine.
DB08916. Afatinib.
DB01259. Lapatinib.
DB06366. Pertuzumab.
DB00072. Trastuzumab.
GuidetoPHARMACOLOGYi2019.

PTM databases

iPTMnetiP04626.
PhosphoSitePlusiP04626.

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.
DisGeNETi2064.
GeneCardsiERBB2.
HGNCiHGNC:3430. ERBB2.
HPAiCAB000043.
CAB020416.
CAB062555.
HPA001338.
HPA001383.
MalaCardsiERBB2.
MIMi137215. phenotype.
137800. phenotype.
164870. gene.
167000. phenotype.
211980. phenotype.
613659. phenotype.
neXtProtiNX_P04626.
OpenTargetsiENSG00000141736.
PharmGKBiPA27844.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS06866-MONOMER.
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.
R-HSA-8863795. Downregulation of ERBB2 signaling.
R-HSA-8866910. TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
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: November 30, 2016
This is version 219 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.