[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1038/319230a0; PubMed=3003577 [NCBI, ExPASy, EBI, Israel, Japan] Yamamoto T., Ikawa S., Akiyama T., Semba K., Nomura N., Miyajima N., Saito T., Toyoshima K.; "Similarity of protein encoded by the human c-erb-B-2 gene to epidermal growth factor receptor."; Nature 319:230-234(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ALA-1170. DOI=10.1126/science.2999974; PubMed=2999974 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Tyrosine kinase receptor with extensive homology to EGF receptor shares chromosomal location with neu oncogene."; Science 230:1132-1139(1985).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-452; VAL-655 AND ALA-1170. NIEHS SNPs program; Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-191. PubMed=3039351 [NCBI, ExPASy, EBI, Israel, Japan] Tal M., King C.R., Kraus M.H., Ullrich A., Schlessinger J., Givol D.; "Human HER2 (neu) promoter: evidence for multiple mechanisms for transcriptional initiation."; Mol. Cell. Biol. 7:2597-2601(1987).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 737-1031. DOI=10.1073/pnas.82.19.6497; PubMed=2995967 [NCBI, ExPASy, EBI, Israel, Japan] Semba K., Kamata N., Toyoshima K., Yamamoto T.; "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."; Proc. Natl. Acad. Sci. U.S.A. 82:6497-6501(1985).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 832-909. TISSUE=Mammary carcinoma; DOI=10.1126/science.2992089; PubMed=2992089 [NCBI, ExPASy, EBI, Israel, Japan] King C.R., Kraus M.H., Aaronson S.A.; "Amplification of a novel v-erbB-related gene in a human mammary carcinoma."; Science 229:974-976(1985).
[7]	NUCLEOTIDE SEQUENCE OF 1081-1245, AND VARIANT ALA-1170. DOI=10.1089/dna.1993.12.611; PubMed=8104414 [NCBI, ExPASy, EBI, Israel, Japan] Sarkar F.H., Ball D.E., Li Y.W., Crissman J.D.; "Molecular cloning and sequencing of an intron of Her-2/neu (ERBB2) gene."; DNA Cell Biol. 12:611-615(1993).
[8]	IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND EGFR, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND EGFR, AND INTERACTION WITH PIK3C2B. DOI=10.1128/MCB.20.11.3817-3830.2000; PubMed=10805725 [NCBI, ExPASy, EBI, Israel, Japan] Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.; "Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors."; Mol. Cell. Biol. 20:3817-3830(2000).
[9]	INTERACTION WITH MUC1. PubMed=12939402 [NCBI, ExPASy, EBI, Israel, Japan] Li Y., Yu W.-H., Ren J., Chen W., Huang L., Kharbanda S., Loda M., Kufe D.; "Heregulin targets gamma-catenin to the nucleolus by a mechanism dependent on the DF3/MUC1 oncoprotein."; Mol. Cancer Res. 1:765-775(2003).
[10]	INTERACTION WITH PLXNB1. DOI=10.1083/jcb.200312094; PubMed=15210733 [NCBI, ExPASy, EBI, Israel, Japan] Swiercz J.M., Kuner R., Offermanns S.; "Plexin-B1/RhoGEF-mediated RhoA activation involves the receptor tyrosine kinase ErbB-2."; J. Cell Biol. 165:869-880(2004).
[11]	INTERACTION WITH MEMO. DOI=10.1038/ncb1134; PubMed=15156151 [NCBI, ExPASy, EBI, Israel, Japan] Marone R., Hess D., Dankort D., Muller W.J., Hynes N.E., Badache A.; "Memo mediates ErbB2-driven cell motility."; Nat. Cell Biol. 6:515-522(2004).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1248, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[13]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-735, AND MASS SPECTROMETRY. TISSUE=Lung; DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND MASS SPECTROMETRY. DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan] Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.; "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."; Mol. Cell 31:438-448(2008).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 654-662 IN COMPLEX WITH HLA AND BETA-2 MICROGLOBULIN. DOI=10.1074/jbc.274.51.36422; PubMed=10593938 [NCBI, ExPASy, EBI, Israel, Japan] Kuhns J.J., Batalia M.A., Yan S., Collins E.J.; "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."; J. Biol. Chem. 274:36422-36427(1999).
[17]	X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 23-629 IN COMPLEX WITH FAB. DOI=10.1038/nature01392; PubMed=12610629 [NCBI, ExPASy, EBI, Israel, Japan] Cho H.-S., Mason K., Ramyar K.X., Stanley A.M., Gabelli S.B., Denney D.W. Jr., Leahy D.J.; "Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab."; Nature 421:756-760(2003).
[18]	VARIANTS VAL-654 AND VAL-655. DOI=10.1006/geno.1993.1081; PubMed=8095488 [NCBI, ExPASy, EBI, Israel, Japan] Ehsani A., Low J., Wallace R.B., Wu A.M.; "Characterization of a new allele of the human ERBB2 gene by allele-specific competition hybridization."; Genomics 15:426-429(1993).
[19]	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, AND VARIANT GLIOBLASTOMA LYS-914. 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., 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.; "Intragenic ERBB2 kinase mutations in tumours."; Nature 431:525-526(2004).
[20]	VARIANTS [LARGE SCALE ANALYSIS] VAL-654; VAL-655; SER-768; SER-776; SER-857; ALA-1170 AND ASP-1216. DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan] Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; "Patterns of somatic mutation in human cancer genomes."; Nature 446:153-158(2007).

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: 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.
INTERACTION:
Self; NbExp=1; IntAct=EBI-641062, EBI-641062;
P62157:CALM (xeno); NbExp=1; IntAct=EBI-641062, EBI-397403;
P62161:Calm1 (xeno); NbExp=1; IntAct=EBI-641062, EBI-397530;
P00533:EGFR; NbExp=2; IntAct=EBI-641062, EBI-297353;
P21860:ERBB3; NbExp=4; IntAct=EBI-641062, EBI-720706;
Q15303:ERBB4; NbExp=2; IntAct=EBI-641062, EBI-80371;
Q05209:PTPN12; NbExp=1; IntAct=EBI-641062, EBI-2266035;
Q9Y2R2:PTPN22; NbExp=1; IntAct=EBI-641062, EBI-1211241;
P26045:PTPN3; NbExp=1; IntAct=EBI-641062, EBI-1047946;
P23467:PTPRB; NbExp=1; IntAct=EBI-641062, EBI-1265766;
P08575:PTPRC; NbExp=1; IntAct=EBI-641062, EBI-1341;
P23470:PTPRG; NbExp=1; IntAct=EBI-641062, EBI-2258115;
Q12913:PTPRJ; NbExp=1; IntAct=EBI-641062, EBI-2264500;
Q15262:PTPRK; NbExp=1; IntAct=EBI-641062, EBI-474052;
Q16827:PTPRO; NbExp=1; IntAct=EBI-641062, EBI-723739;
P23471:PTPRZ1; NbExp=1; IntAct=EBI-641062, EBI-2263175;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
PTM: 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.
DISEASE: Defects in ERBB2 are associated with gastric cancer [MIM:137215]; also known as hereditary familial diffuse gastric cancer (HDGC).
DISEASE: 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.
DISEASE: 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.
DISEASE: Defects in ERBB2 are associated with lung cancer [MIM:211980]; also called adenocarcinoma of lung.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.
SIMILARITY: Contains 1 protein kinase domain.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/ERBB2ID162ch17q11.html";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/erbb2/";.
WEB RESOURCE: Name=Wikipedia; Note=ERBB2 entry; URL="http://en.wikipedia.org/wiki/ERBB2";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M11767; AAA35808.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11761; AAA35808.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11762; AAA35808.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11763; AAA35808.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11764; AAA35808.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11765; AAA35808.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11766; AAA35808.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11730; AAA75493.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12036; AAA35978.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY208911; AAO18082.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03363; CAA27060.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M16792; AAA58637.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M16789; AAA58637.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M16790; AAA58637.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M16791; AAA58637.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L29395; AAA35809.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M95667; AAC37531.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00300384; -.

PIR

A24571; A24571.

RefSeq

NP_001005862.1; -.
NP_004439.2; -.

UniGene

Hs.446352

3D structure databases

PDB

1MFG; X-ray; 1.25 A; B=1247-1255.	[ExPASy / RCSB / EBI]
1MFL; X-ray; 1.88 A; B=1247-1255.	[ExPASy / RCSB / EBI]
1MW4; NMR; -; B=1135-1144.	[ExPASy / RCSB / EBI]
1N8Z; X-ray; 2.52 A; C=23-629.	[ExPASy / RCSB / EBI]
1OVC; Model; -; A=737-1031.	[ExPASy / RCSB / EBI]
1QR1; X-ray; 2.40 A; C/F=654-662.	[ExPASy / RCSB / EBI]
1S78; X-ray; 3.25 A; A/B=23-646.	[ExPASy / RCSB / EBI]
2A91; X-ray; 2.50 A; A=22-530.	[ExPASy / RCSB / EBI]
2JWA; NMR; -; A/B=641-684.	[ExPASy / RCSB / EBI]
3BE1; X-ray; 2.90 A; A=23-646.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1MFG; -.
1MFL; -.
1MW4; -.
1N8Z; -.
1OVC; -.
1QR1; -.
1S78; -.
2A91; -.
2JWA; -.
3BE1; -.

SMR

P04626; 704-1026.

ModBase

P04626.

Protein-protein interaction databases

DIP

DIP:8N; -.

IntAct

P04626; 21.

PTM databases

PhosphoSite

P04626; -.

Enzyme and pathway databases

BRENDA

2.7.10.1; 247.

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.

Organism-specific databases

GC17P035109; -.

HIX0039027; -.

HGNC:3430; ERBB2.

CAB000043; -.
HPA001383; -.

MIM

137215; phenotype. [NCBI / EBI]
137800; phenotype. [NCBI / EBI]
164870; gene. [NCBI / EBI]
167000; phenotype. [NCBI / EBI]
211980; phenotype. [NCBI / EBI]

PharmGKB

PA27844; -.

Gene expression databases

P04626; -.

P04626; -.

HS_ERBB2; -.

ENSG00000141736; Homo sapiens.

Ontologies

GO:0016323;	Cellular component: basolateral plasma membrane (inferred from direct assay from UniProtKB).
GO:0016021;	Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0043235;	Cellular component: receptor complex (inferred from direct assay from UniProtKB).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005006;	Molecular function: epidermal growth factor receptor activity (non-traceable author statement from UniProtKB).
GO:0043125;	Molecular function: ErbB-3 class receptor binding (traceable author statement from ProtInc).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0008022;	Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0046982;	Molecular function: protein heterodimerization activity (inferred from direct assay from UniProtKB).
GO:0019903;	Molecular function: protein phosphatase binding (inferred from physical interaction from UniProtKB).
GO:0004716;	Molecular function: receptor signaling protein tyrosine kinase activity (traceable author statement from ProtInc).
GO:0008283;	Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0007507;	Biological process: heart development (traceable author statement from UniProtKB).
GO:0030879;	Biological process: mammary gland development (traceable author statement from UniProtKB).
GO:0014065;	Biological process: phosphoinositide 3-kinase cascade (inferred from direct assay from UniProtKB).
GO:0048015;	Biological process: phosphoinositide-mediated signaling (non-traceable author statement from UniProtKB).
GO:0045785;	Biological process: positive regulation of cell adhesion (inferred from direct assay from UniProtKB).
GO:0050679;	Biological process: positive regulation of epithelial cell proliferation (inferred from direct assay from UniProtKB).
GO:0043406;	Biological process: positive regulation of MAP kinase activity (inferred from direct assay from UniProtKB).
GO:0046777;	Biological process: protein amino acid autophosphorylation (inferred from direct assay from UniProtKB).
GO:0045765;	Biological process: regulation of angiogenesis (non-traceable author statement from UniProtKB).
GO:0007169;	Biological process: transmembrane receptor protein tyrosine kinase signaling pathway (non-traceable author statement from UniProtKB).
GO:0042060;	Biological process: wound healing (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000494; EGF_rcpt_L.
IPR006211; Furin-like.
IPR006212; Furin_repeat.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR016245; Tyr_kinase_rcpt_EGF/ERB/XmrK.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
IPR004019; YLP_motif.
Graphical view of domain structure.

Pfam

PF00757; Furin-like; 1.
PF07714; Pkinase_Tyr; 1.
PF01030; Recep_L_domain; 2.
PF02757; YLP; 2.
Pfam graphical view of domain structure.

PIRSF

PIRSF000619; TyrPK_EGF-R; 1.

PRINTS

PR00109; TYRKINASE.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00261; FU; 3.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P04626; -.

Genome annotation databases

Ensembl

ENSG00000141736; Homo sapiens. [Contig view]

GeneID

2064; -.

KEGG

hsa:2064; -.

Phylogenomic databases

HOGENOM

P04626; -.

HOVERGEN

P04626; -.

OMA

P04626; ACYPLCA.

Other

DrugBank

DB01259; Lapatinib.
DB01006; Letrozole.
DB00072; Trastuzumab.

8385; -.

P04626; -.

ERBB2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Signal; Transferase; Transmembrane; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`	`Potential.`
`CHAIN`	`23 1255`	`1233`	`Receptor tyrosine-protein kinase erbB-2.`	`PRO_0000016669`
`TOPO_DOM`	`23 652`	`630`	`Extracellular (Potential).`
`TRANSMEM`	`653 675`	`23`	`Potential.`
`TOPO_DOM`	`676 1255`	`580`	`Cytoplasmic (Potential).`
`DOMAIN`	`720 987`	`268`	`Protein kinase.`
`NP_BIND`	`726 734`	`9`	`ATP (By similarity).`
`REGION`	`1195 1197`	`3`	`Interaction with PIK3C2B (Probable).`
`ACT_SITE`	`845 845`		`Proton acceptor (By similarity).`
`BINDING`	`753 753`		`ATP (By similarity).`
`MOD_RES`	`735 735`		`Phosphotyrosine.`
`MOD_RES`	`1054 1054`		`Phosphoserine.`
`MOD_RES`	`1139 1139`		`Phosphotyrosine; by autocatalysis (By similarity).`
`MOD_RES`	`1196 1196`		`Phosphotyrosine (Potential).`
`MOD_RES`	`1248 1248`		`Phosphotyrosine; by autocatalysis (By similarity).`
`CARBOHYD`	`68 68`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`124 124`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`187 187`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`259 259`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`530 530`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`571 571`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`629 629`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`195 204`		`By similarity.`
`DISULFID`	`199 212`		`By similarity.`
`DISULFID`	`220 227`		`By similarity.`
`DISULFID`	`224 235`		`By similarity.`
`DISULFID`	`236 244`		`By similarity.`
`DISULFID`	`240 252`		`By similarity.`
`DISULFID`	`255 264`		`By similarity.`
`DISULFID`	`268 295`		`By similarity.`
`DISULFID`	`299 311`		`By similarity.`
`DISULFID`	`315 331`		`By similarity.`
`DISULFID`	`334 338`		`By similarity.`
`DISULFID`	`511 520`		`By similarity.`
`DISULFID`	`515 528`		`By similarity.`
`DISULFID`	`531 540`		`By similarity.`
`DISULFID`	`544 560`		`By similarity.`
`DISULFID`	`563 576`		`By similarity.`
`DISULFID`	`567 584`		`By similarity.`
`DISULFID`	`587 596`		`By similarity.`
`DISULFID`	`600 623`		`By similarity.`
`DISULFID`	`626 634`		`By similarity.`
`DISULFID`	`630 642`		`By similarity.`
`VARIANT`	`452 452`	`1`	`W -> C (in dbSNP:rs4252633 [NCBI]).`	`VAR_016317 [3D]`
`VARIANT`	`654 654`	`1`	`I -> V (in allele B3; dbSNP:rs1801201 [NCBI]).`	`VAR_004077`
`VARIANT`	`655 655`	`1`	`I -> V (in allele B2 and allele B3; dbSNP:rs1136201 [NCBI]).`	`VAR_004078`
`VARIANT`	`755 755`	`1`	`L -> P (in adenocarcinoma of lung; somatic mutation).`	`VAR_055432`
`VARIANT`	`768 768`	`1`	`L -> S (in dbSNP:rs56366519 [NCBI]).`	`VAR_042097`
`VARIANT`	`774 774`	`1`	`M -> MAYVM (in adenocarcinoma of lung; somatic mutationa).`	`VAR_055433`
`VARIANT`	`776 776`	`1`	`G -> S (in a gastric adenocarcinoma sample; somatic mutation).`	`VAR_042098`
`VARIANT`	`779 779`	`1`	`S -> SVGS (in adenocarcinoma of lung; somatic mutation).`	`VAR_055434`
`VARIANT`	`857 857`	`1`	`N -> S (in ovarian cancer; somatic mutation; dbSNP:rs28933370 [NCBI]).`	`VAR_042099`
`VARIANT`	`914 914`	`1`	`E -> K (in glioblastoma; somatic mutation).`	`VAR_055435`
`VARIANT`	`1170 1170`	`1`	`P -> A (in dbSNP:rs1058808 [NCBI] and dbSNP:rs61552325 [NCBI]).`	`VAR_016318`
`VARIANT`	`1216 1216`	`1`	`A -> D (in dbSNP:rs55943169 [NCBI]).`	`VAR_042100`
`STRAND`	`25 27`	`3`
`HELIX`	`39 50`	`12`
`STRAND`	`55 64`	`10`
`HELIX`	`72 74`	`3`
`STRAND`	`79 82`	`4`
`STRAND`	`84 88`	`5`
`TURN`	`109 111`	`3`
`STRAND`	`112 117`	`6`
`STRAND`	`152 157`	`6`
`TURN`	`164 166`	`3`
`HELIX`	`169 172`	`4`
`HELIX`	`175 177`	`3`
`STRAND`	`182 184`	`3`
`STRAND`	`199 202`	`4`
`STRAND`	`204 208`	`5`
`STRAND`	`217 219`	`3`
`STRAND`	`221 223`	`3`
`STRAND`	`227 231`	`5`
`HELIX`	`232 234`	`3`
`STRAND`	`240 242`	`3`
`STRAND`	`244 248`	`5`
`STRAND`	`251 260`	`10`
`STRAND`	`263 267`	`5`
`STRAND`	`271 274`	`4`
`TURN`	`276 278`	`3`
`STRAND`	`281 283`	`3`
`STRAND`	`289 291`	`3`
`STRAND`	`294 298`	`5`
`STRAND`	`303 305`	`3`
`STRAND`	`309 314`	`6`
`STRAND`	`319 323`	`5`
`STRAND`	`329 333`	`5`
`STRAND`	`335 337`	`3`
`HELIX`	`348 350`	`3`
`TURN`	`358 360`	`3`
`HELIX`	`361 364`	`4`
`STRAND`	`368 376`	`9`
`HELIX`	`378 380`	`3`
`HELIX`	`396 402`	`7`
`STRAND`	`405 408`	`4`
`STRAND`	`410 413`	`4`
`HELIX`	`423 425`	`3`
`TURN`	`438 440`	`3`
`STRAND`	`441 447`	`7`
`STRAND`	`463 469`	`7`
`HELIX`	`482 485`	`4`
`STRAND`	`493 498`	`6`
`HELIX`	`501 506`	`6`
`HELIX`	`516 518`	`3`
`STRAND`	`520 524`	`5`
`STRAND`	`528 536`	`9`
`STRAND`	`539 542`	`4`
`STRAND`	`545 551`	`7`
`STRAND`	`553 556`	`4`
`STRAND`	`559 562`	`4`
`STRAND`	`571 573`	`3`
`STRAND`	`575 580`	`6`
`STRAND`	`583 592`	`10`
`STRAND`	`595 599`	`5`
`STRAND`	`615 617`	`3`
`STRAND`	`621 625`	`5`
`HELIX`	`651 678`	`28`

Sequence information

Length: 1255 AA [This is the length of the unprocessed precursor]

Molecular weight: 137910 Da [This is the MW of the unprocessed precursor]

CRC64: 39E9DFDA04DCF962 [This is a checksum on the sequence]

        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

P04626 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools