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Reviewed, UniProtKB/Swiss-Prot P04626 (ERBB2_HUMAN)

Last modified February 9, 2010. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Receptor tyrosine-protein kinase erbB-2
    EC=2.7.10.1
Alternative name(s):
    p185erbB2
    c-erbB-2
    Proto-oncogene NEU
    Tyrosine kinase-type cell surface receptor HER2
    Metastatic lymph node gene 19 protein
      Short name=MLN 19
    CD_antigen=CD340
Gene names
Name: ERBB2
Synonyms: HER2, MLN19, NEU, NGL
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Not activated by EGF, TGF-alpha and amphiregulin.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Heterodimer with each of the other ERBB receptors Potential. Interacts with PRKCABP and PLXNB1. Part of a complex with EGFR and either PIK3C2A or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-1196. Interacts with MEMO when phosphorylated on Tyr-1248. Interacts with MUC1. Stimulation by heregulin (HRG) in breast cancer cell lines induces binding of MUC1 with gamma-catenin. Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Ligand-binding increases phosphorylation on tyrosine residues By similarity.

Polymorphism

There are fours 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.

Involvement in disease

Defects in ERBB2 are associated with gastric cancer [MIM:137215]; also known as hereditary familial diffuse gastric cancer (HDGC).

Defects in ERBB2 are associated with familial glioma of brain [MIM:137800]; also called glioblastoma multiforme. Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas, and ependymomas.

Defects in ERBB2 are associated with ovarian cancer [MIM:167000]. Ovarian cancer is the leading cause of death from gynecologic malignancy. It is characterized by advanced presentation with loco-regional dissemination in the peritoneal cavity and the rare incidence of visceral metastases. These typical features relate to the biology of the disease, which is a principal determinant of outcome.

Defects in ERBB2 are associated with lung cancer [MIM:211980]; also called adenocarcinoma of lung.

Sequence similarities

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

Contains 1 protein kinase domain.

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Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DomainSignal
Transmembrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcell proliferation

Traceable author statement. Source: ProtInc

heart development

Traceable author statement. Source: UniProtKB

phosphoinositide 3-kinase cascade

Inferred from direct assay. Source: UniProtKB

phosphoinositide-mediated signaling

Non-traceable author statement. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay. Source: UniProtKB

positive regulation of cell adhesion

Inferred from direct assay. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from direct assay. Source: UniProtKB

protein amino acid autophosphorylation

Inferred from direct assay. Source: UniProtKB

regulation of angiogenesis

Non-traceable author statement. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from direct assay. Source: UniProtKB

wound healing

Inferred from direct assay. Source: UniProtKB

   Cellular componentintegral to membrane

Non-traceable author statement. Source: UniProtKB

receptor complex

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ErbB-3 class receptor binding

Traceable author statement. Source: ProtInc

epidermal growth factor receptor activity

Non-traceable author statement. Source: UniProtKB

identical protein binding

Inferred from physical interaction. Source: IntAct

protein C-terminus binding

Inferred from physical interaction. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 12551233Receptor tyrosine-protein kinase erbB-2
PRO_0000016669

Regions

Topological domain23 – 652630Extracellular Potential
Transmembrane653 – 67523 Potential
Topological domain676 – 1255580Cytoplasmic Potential
Domain720 – 987268Protein kinase
Nucleotide binding726 – 7349ATP By similarity
Region1195 – 11973Interaction with PIK3C2B Probable

Sites

Active site8451Proton acceptor By similarity
Binding site7531ATP By similarity

Amino acid modifications

Modified residue7351Phosphotyrosine Ref.15
Modified residue10541Phosphoserine Ref.16 Ref.17
Modified residue11391Phosphotyrosine; by autocatalysis By similarity
Modified residue11961Phosphotyrosine Potential
Modified residue12481Phosphotyrosine; by autocatalysis By similarity
Glycosylation681N-linked (GlcNAc...) Potential
Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Potential
Glycosylation5301N-linked (GlcNAc...) Potential
Glycosylation5711N-linked (GlcNAc...) Potential
Glycosylation6291N-linked (GlcNAc...) Potential
Disulfide bond195 ↔ 204 By similarity
Disulfide bond199 ↔ 212 By similarity
Disulfide bond220 ↔ 227 By similarity
Disulfide bond224 ↔ 235 By similarity
Disulfide bond236 ↔ 244 By similarity
Disulfide bond240 ↔ 252 By similarity
Disulfide bond255 ↔ 264 By similarity
Disulfide bond268 ↔ 295 By similarity
Disulfide bond299 ↔ 311 By similarity
Disulfide bond315 ↔ 331 By similarity
Disulfide bond334 ↔ 338 By similarity
Disulfide bond511 ↔ 520 By similarity
Disulfide bond515 ↔ 528 By similarity
Disulfide bond531 ↔ 540 By similarity
Disulfide bond544 ↔ 560 By similarity
Disulfide bond563 ↔ 576 By similarity
Disulfide bond567 ↔ 584 By similarity
Disulfide bond587 ↔ 596 By similarity
Disulfide bond600 ↔ 623 By similarity
Disulfide bond626 ↔ 634 By similarity
Disulfide bond630 ↔ 642 By similarity

Natural variations

Natural variant4521W → C: dbSNP rs4252633. Ref.3
VAR_016317
Natural variant6541I → V in allele B3. dbSNP rs1801201. Ref.20 Ref.22
VAR_004077
Natural variant6551I → V in allele B2 and allele B3. dbSNP rs1136201. Ref.3 Ref.20 Ref.22
VAR_004078
Natural variant7551L → P in adenocarcinoma of lung; somatic mutation. Ref.21
VAR_055432
Natural variant7681L → S: dbSNP rs56366519. Ref.22
VAR_042097
Natural variant7741M → MAYVM in adenocarcinoma of lung; somatic mutationa.
VAR_055433
Natural variant7761G → S in a gastric adenocarcinoma sample; somatic mutation. dbSNP rs28933369. Ref.22 Ref.21
VAR_042098
Natural variant7791S → SVGS in adenocarcinoma of lung; somatic mutation.
VAR_055434
Natural variant8571N → S in ovarian cancer; somatic mutation. dbSNP rs28933370. Ref.22 Ref.21
VAR_042099
Natural variant9141E → K in glioblastoma; somatic mutation. dbSNP rs28933368. Ref.21
VAR_055435
Natural variant11701P → A: dbSNP rs1058808 and dbSNP rs61552325. Ref.3 Ref.22 Ref.2 Ref.9
VAR_016318
Natural variant12161A → D: dbSNP rs55943169. Ref.22
VAR_042100

Secondary structure

1 ......................................................................................................................... 1255
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P04626-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 39E9DFDA04DCF962

FASTA1,255137,910
        10         20         30         40         50         60 
MELAALCRWG LLLALLPPGA ASTQVCTGTD MKLRLPASPE THLDMLRHLY QGCQVVQGNL 

        70         80         90        100        110        120 
ELTYLPTNAS LSFLQDIQEV QGYVLIAHNQ VRQVPLQRLR IVRGTQLFED NYALAVLDNG 

       130        140        150        160        170        180 
DPLNNTTPVT GASPGGLREL QLRSLTEILK GGVLIQRNPQ LCYQDTILWK DIFHKNNQLA 

       190        200        210        220        230        240 
LTLIDTNRSR ACHPCSPMCK GSRCWGESSE DCQSLTRTVC AGGCARCKGP LPTDCCHEQC 

       250        260        270        280        290        300 
AAGCTGPKHS DCLACLHFNH SGICELHCPA LVTYNTDTFE SMPNPEGRYT FGASCVTACP 

       310        320        330        340        350        360 
YNYLSTDVGS CTLVCPLHNQ EVTAEDGTQR CEKCSKPCAR VCYGLGMEHL REVRAVTSAN 

       370        380        390        400        410        420 
IQEFAGCKKI FGSLAFLPES FDGDPASNTA PLQPEQLQVF ETLEEITGYL YISAWPDSLP 

       430        440        450        460        470        480 
DLSVFQNLQV IRGRILHNGA YSLTLQGLGI SWLGLRSLRE LGSGLALIHH NTHLCFVHTV 

       490        500        510        520        530        540 
PWDQLFRNPH QALLHTANRP EDECVGEGLA CHQLCARGHC WGPGPTQCVN CSQFLRGQEC 

       550        560        570        580        590        600 
VEECRVLQGL PREYVNARHC LPCHPECQPQ NGSVTCFGPE ADQCVACAHY KDPPFCVARC 

       610        620        630        640        650        660 
PSGVKPDLSY MPIWKFPDEE GACQPCPINC THSCVDLDDK GCPAEQRASP LTSIISAVVG 

       670        680        690        700        710        720 
ILLVVVLGVV FGILIKRRQQ KIRKYTMRRL LQETELVEPL TPSGAMPNQA QMRILKETEL 

       730        740        750        760        770        780 
RKVKVLGSGA FGTVYKGIWI PDGENVKIPV AIKVLRENTS PKANKEILDE AYVMAGVGSP 

       790        800        810        820        830        840 
YVSRLLGICL TSTVQLVTQL MPYGCLLDHV RENRGRLGSQ DLLNWCMQIA KGMSYLEDVR 

       850        860        870        880        890        900 
LVHRDLAARN VLVKSPNHVK ITDFGLARLL DIDETEYHAD GGKVPIKWMA LESILRRRFT 

       910        920        930        940        950        960 
HQSDVWSYGV TVWELMTFGA KPYDGIPARE IPDLLEKGER LPQPPICTID VYMIMVKCWM 

       970        980        990       1000       1010       1020 
IDSECRPRFR ELVSEFSRMA RDPQRFVVIQ NEDLGPASPL DSTFYRSLLE DDDMGDLVDA 

      1030       1040       1050       1060       1070       1080 
EEYLVPQQGF FCPDPAPGAG GMVHHRHRSS STRSGGGDLT LGLEPSEEEA PRSPLAPSEG 

      1090       1100       1110       1120       1130       1140 
AGSDVFDGDL GMGAAKGLQS LPTHDPSPLQ RYSEDPTVPL PSETDGYVAP LTCSPQPEYV 

      1150       1160       1170       1180       1190       1200 
NQPDVRPQPP SPREGPLPAA RPAGATLERP KTLSPGKNGV VKDVFAFGGA VENPEYLTPQ 

      1210       1220       1230       1240       1250 
GGAAPQPHPP PAFSPAFDNL YYWDQDPPER GAPPSTFKGT PTAENPEYLG LDVPV

« Hide

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References

« Hide 'large scale' references
[1]"Similarity of protein encoded by the human c-erb-B-2 gene to epidermal growth factor receptor."
Yamamoto T., Ikawa S., Akiyama T., Semba K., Nomura N., Miyajima N., Saito T., Toyoshima K.
Nature 319:230-234(1986) [PubMed: 3003577] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Tyrosine kinase receptor with extensive homology to EGF receptor shares chromosomal location with neu oncogene."
Coussens L., Yang-Feng T.L., Liao Y.C., Chen E., Gray A., McGrath J., Seeburg P.H., Libermann T.A., Schlessinger J., Francke U., Levinson A., Ullrich A.
Science 230:1132-1139(1985) [PubMed: 2999974] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ALA-1170.
[3]NIEHS SNPs program
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-452; VAL-655 AND ALA-1170.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Human HER2 (neu) promoter: evidence for multiple mechanisms for transcriptional initiation."
Tal M., King C.R., Kraus M.H., Ullrich A., Schlessinger J., Givol D.
Mol. Cell. Biol. 7:2597-2601(1987) [PubMed: 3039351] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-191.
[7]"A v-erbB-related protooncogene, c-erbB-2, is distinct from the c-erbB-1/epidermal growth factor-receptor gene and is amplified in a human salivary gland adenocarcinoma."
Semba K., Kamata N., Toyoshima K., Yamamoto T.
Proc. Natl. Acad. Sci. U.S.A. 82:6497-6501(1985) [PubMed: 2995967] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 737-1031.
[8]"Amplification of a novel v-erbB-related gene in a human mammary carcinoma."
King C.R., Kraus M.H., Aaronson S.A.
Science 229:974-976(1985) [PubMed: 2992089] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 832-909.
Tissue: Mammary carcinoma.
[9]"Molecular cloning and sequencing of an intron of Her-2/neu (ERBB2) gene."
Sarkar F.H., Ball D.E., Li Y.W., Crissman J.D.
DNA Cell Biol. 12:611-615(1993) [PubMed: 8104414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1081-1245, VARIANT ALA-1170.
[10]"Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors."
Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.
Mol. Cell. Biol. 20:3817-3830(2000) [PubMed: 10805725] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND EGFR, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND EGFR, INTERACTION WITH PIK3C2B.
[11]"Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein."
Li Y., Yu W.-H., Ren J., Chen W., Huang L., Kharbanda S., Loda M., Kufe D.
Mol. Cancer Res. 1:765-775(2003) [PubMed: 12939402] [Abstract]
Cited for: INTERACTION WITH MUC1.
[12]"Plexin-B1/RhoGEF-mediated RhoA activation involves the receptor tyrosine kinase ErbB-2."
Swiercz J.M., Kuner R., Offermanns S.
J. Cell Biol. 165:869-880(2004) [PubMed: 15210733] [Abstract]
Cited for: INTERACTION WITH PLXNB1.
[13]"Memo mediates ErbB2-driven cell motility."
Marone R., Hess D., Dankort D., Muller W.J., Hynes N.E., Badache A.
Nat. Cell Biol. 6:515-522(2004) [PubMed: 15156151] [Abstract]
Cited for: INTERACTION WITH MEMO.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1248, MASS SPECTROMETRY.
Tissue: Epithelium.
[15]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-735, MASS SPECTROMETRY.
Tissue: Lung.
[16]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, MASS SPECTROMETRY.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, MASS SPECTROMETRY.
[18]"Poor binding of a HER-2/neu epitope (GP2) to HLA-A2.1 is due to a lack of interactions with the center of the peptide."
Kuhns J.J., Batalia M.A., Yan S., Collins E.J.
J. Biol. Chem. 274:36422-36427(1999) [PubMed: 10593938] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 654-662 IN COMPLEX WITH HLA AND BETA-2 MICROGLOBULIN.
[19]"Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab."
Cho H.-S., Mason K., Ramyar K.X., Stanley A.M., Gabelli S.B., Denney D.W. Jr., Leahy D.J.
Nature 421:756-760(2003) [PubMed: 12610629] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 23-629 IN COMPLEX WITH FAB.
[20]"Characterization of a new allele of the human ERBB2 gene by allele-specific competition hybridization."
Ehsani A., Low J., Wallace R.B., Wu A.M.
Genomics 15:426-429(1993) [PubMed: 8095488] [Abstract]
Cited for: VARIANTS VAL-654 AND VAL-655.
[21]"Intragenic ERBB2 kinase mutations in tumours."
Cancer genome project and collaborative group
Stephens P., Hunter C., Bignell G., Edkins S., Davies H., Teague J., Stevens C., O'Meara S., Smith R., Parker A., Barthorpe A., Blow M., Brackenbury L., Butler A., Clarke O., Cole J., Dicks E., Dike A. expand/collapse author list , Drozd A., Edwards K., Forbes S., Foster R., Gray K., Greenman C., Halliday K., Hills K., Kosmidou V., Lugg R., Menzies A., Perry J., Petty R., Raine K., Ratford L., Shepherd R., Small A., Stephens Y., Tofts C., Varian J., West S., Widaa S., Yates A., Brasseur F., Cooper C.S., Flanagan A.M., Knowles M., Leung S.Y., Louis D.N., Looijenga L.H.J., Malkowicz B., Pierotti M.A., Teh B., Chenevix-Trench G., Weber B.L., Yuen S.T., Harris G., Goldstraw P., Nicholson A.G., Futreal P.A., Wooster R., Stratton M.R.
Nature 431:525-526(2004)
Cited for: VARIANTS ADENOCARCINOMA OF LUNG PRO-755; ALA-TYR-VAL-MET-774 INS AND VAL-GLY-SER-779 INS, VARIANT GASTRIC CANCER SER-776, VARIANT OVARIAN CANCER SER-857, VARIANT GLIOBLASTOMA LYS-914.
[22]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-654; VAL-655; SER-768; SER-776; SER-857; ALA-1170 AND ASP-1216.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M11767 expand/collapse EMBL AC list , M11761, M11762, M11763, M11764, M11765, M11766 Genomic DNA. Translation: AAA35808.1.
M11730 mRNA. Translation: AAA75493.1.
M12036 Genomic DNA. Translation: AAA35978.1.
AY208911 Genomic DNA. Translation: AAO18082.1.
X03363 mRNA. Translation: CAA27060.1.
CH471152 Genomic DNA. Translation: EAW60597.1.
BC167147 mRNA. Translation: AAI67147.1.
M16792 expand/collapse EMBL AC list , M16789, M16790, M16791 Genomic DNA. Translation: AAA58637.1.
L29395 Genomic DNA. Translation: AAA35809.1.
M95667 Genomic DNA. Translation: AAC37531.1.
IPIIPI00300384.
PIRA24571.
RefSeqNP_001005862.1.
NP_004439.2.
UniGeneHs.446352

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
3BE1X-ray2.90A23-646[»]
SMRP04626. Positions 677-729, 707-1025.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-8N.
IntActP04626. 21 interactions.
STRINGP04626.

PTM databases

PhosphoSiteP04626.

Proteomic databases

PRIDEP04626.

Genome annotation databases

EnsemblENST00000269571; ENSP00000269571; ENSG00000141736; Homo sapiens. [Genome view]
GeneID2064.
KEGGhsa:2064.
UCSCuc002hso.1. human.

Organism-specific databases

CTD2064.
GeneCardsGC17P035109.
H-InvDBHIX0039027.
HGNCHGNC:3430. ERBB2.
HPACAB000043.
CAB020416.
HPA001383.
MIM137215. phenotype.
137800. phenotype.
164870. gene.
167000. phenotype.
211980. phenotype.
PharmGKBPA27844.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06030.
HOGENOMHBG445128.
HOVERGENP04626.
InParanoidP04626.
OMAACYPLCA.
PhylomeDBP04626.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.
Pathway_Interaction_DBa6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
ReactomeREACT_18266. Axon guidance.

Gene expression databases

ArrayExpressP04626.
BgeeP04626.
CleanExHS_ERBB2.
GenevestigatorP04626.
GermOnlineENSG00000141736. Homo sapiens.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]
PANTHERPTHR23256. Tyr_prot_kinase. 1 hit.
PfamPF00757. Furin-like. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
SMARTSM00261. FU. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01259. Lapatinib.
DB01006. Letrozole.
DB00072. Trastuzumab.
NextBio8385.
PMAP-CutDBP04626.
SOURCESearch...

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Entry information

Entry nameERBB2_HUMAN
AccessionPrimary (citable) accession number: P04626
Secondary accession number(s): B2RZG3 expand/collapse secondary AC list , Q14256, Q6LDV1, Q9UMK4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: February 9, 2010
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents