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P04626 (ERBB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ERBB2
Synonyms:HER2, MLN19, NEU, NGL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

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

General annotation (Comments)

Function

Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Ref.11 Ref.14 Ref.19 Ref.25 Ref.26 Ref.29

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. Ref.11 Ref.14 Ref.19 Ref.25 Ref.26 Ref.29

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.39

Enzyme regulation

Activated by dimerization. Not activated by EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity. Ref.24

Subunit structure

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 ERBB2IP. Interacts with KPNB1, RANBP2, EEA1, CRM1, CLTC, PTK6, RPA94 and ACTB. Interacts with SRC By similarity. Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.20 Ref.24 Ref.29 Ref.30 Ref.33 Ref.34 Ref.36 Ref.39

Subcellular location

Isoform 1: Cell membrane; Single-pass type I membrane protein. Cytoplasm › perinuclear region. Nucleus Ref.14 Ref.17 Ref.19 Ref.29. Note: Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Ref.14 Ref.17 Ref.19 Ref.29

Isoform 2: Cytoplasm. Nucleus Ref.14 Ref.17 Ref.19 Ref.29.

Isoform 3: Cytoplasm. Nucleus Ref.14 Ref.17 Ref.19 Ref.29.

Tissue specificity

Expressed in a variety of tumor tissues including primary breast tumors and tumors from small bowel, esophagus, kidney and mouth. Ref.14

Post-translational modification

Autophosphorylated. Ligand-binding increases phosphorylation on tyrosine residues. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Signaling via SEMA4C promotes phosphorylation at Tyr-1248. Ref.20 Ref.21

Polymorphism

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.

Involvement in disease

Hereditary diffuse gastric cancer (HDGC) [MIM:137215]: A 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.
Note: The gene represented in this entry is involved in disease pathogenesis.

Glioma (GLM) [MIM:137800]: Gliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
Note: The gene represented in this entry is involved in disease pathogenesis.

Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.
Note: The gene represented in this entry is involved in disease pathogenesis.

Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease.
Note: The gene represented in this entry is involved in disease pathogenesis.

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.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative initiation
Alternative splicing
Chromosomal rearrangement
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cell proliferation

Traceable author statement PubMed 10851066. Source: ProtInc

heart development

Traceable author statement PubMed 15504738. Source: UniProtKB

mammary gland development

Traceable author statement PubMed 15504738. Source: UniProtKB

motor neuron axon guidance

Inferred from electronic annotation. Source: Compara

myelination

Inferred from electronic annotation. Source: Compara

negative regulation of immature T cell proliferation in thymus

Inferred from electronic annotation. Source: Compara

neuromuscular junction development

Inferred from electronic annotation. Source: Compara

peripheral nervous system development

Inferred from electronic annotation. Source: Compara

phosphatidylinositol 3-kinase cascade

Inferred from direct assay PubMed 7556068. Source: BHF-UCL

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 10572067. Source: UniProtKB

positive regulation of Rho GTPase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell adhesion

Inferred from direct assay PubMed 7556068. Source: BHF-UCL

positive regulation of cell growth

Inferred from mutant phenotype Ref.29. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from direct assay PubMed 10572067. Source: UniProtKB

positive regulation of transcription from RNA polymerase I promoter

Inferred from mutant phenotype Ref.29. Source: UniProtKB

positive regulation of transcription from RNA polymerase III promoter

Inferred from direct assay Ref.25. Source: UniProtKB

positive regulation of translation

Inferred from mutant phenotype Ref.29. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay PubMed 7556068. Source: BHF-UCL

regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of angiogenesis

Non-traceable author statement PubMed 15609325. Source: UniProtKB

regulation of microtubule-based process

Inferred from direct assay Ref.26. Source: UniProtKB

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

wound healing

Inferred from direct assay PubMed 12646923. Source: BHF-UCL

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Compara

basolateral plasma membrane

Inferred from direct assay PubMed 12646923. Source: BHF-UCL

endosome membrane

Inferred from direct assay Ref.17. Source: UniProtKB

integral to membrane

Non-traceable author statement PubMed 15609325. Source: UniProtKB

nucleus

Inferred from direct assay Ref.17Ref.29. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

receptor complex

Inferred from direct assay PubMed 7514177. Source: BHF-UCL

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ErbB-3 class receptor binding

Traceable author statement PubMed 9590694. Source: ProtInc

RNA polymerase I core binding

Inferred from direct assay Ref.29. Source: UniProtKB

epidermal growth factor-activated receptor activity

Non-traceable author statement PubMed 15504738. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay PubMed 10572067. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Traceable author statement PubMed 10851066. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform 1 (identifier: P04626-1)

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.
Isoform 2 (identifier: P04626-2)

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.
Isoform 3 (identifier: P04626-3)

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.
Isoform 4 (identifier: P04626-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MELAALCRWGLLLALLPPGAAST → MPRGSWKP
Note: Produced by alternative splicing of isoform 1.

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 – 67523Helical; Potential
Topological domain676 – 1255580Cytoplasmic Potential
Domain720 – 987268Protein kinase
Nucleotide binding726 – 7349ATP By similarity
Region676 – 68914Nuclear localization signal
Region676 – 68914Required for interaction with KPNB1 and EEA1
Region1195 – 11973Interaction with PIK3C2B Probable

Sites

Active site8451Proton acceptor By similarity
Binding site7531ATP By similarity

Amino acid modifications

Modified residue10541Phosphoserine Ref.22 Ref.23 Ref.31
Modified residue11071Phosphoserine Ref.27
Modified residue11391Phosphotyrosine; by autocatalysis By similarity
Modified residue11961Phosphotyrosine Potential
Modified residue12481Phosphotyrosine; by autocatalysis Ref.18 Ref.21
Glycosylation681N-linked (GlcNAc...) Ref.38
Glycosylation1241N-linked (GlcNAc...) Potential
Glycosylation1871N-linked (GlcNAc...) Potential
Glycosylation2591N-linked (GlcNAc...) Ref.36 Ref.37 Ref.38
Glycosylation5301N-linked (GlcNAc...) Ref.36 Ref.37
Glycosylation5711N-linked (GlcNAc...) Ref.38
Glycosylation6291N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 53 Ref.36 Ref.37 Ref.38
Disulfide bond162 ↔ 192 Ref.36 Ref.37 Ref.38
Disulfide bond195 ↔ 204 Ref.36 Ref.37 Ref.38
Disulfide bond199 ↔ 212 Ref.36 Ref.37 Ref.38
Disulfide bond220 ↔ 227 Ref.36 Ref.37 Ref.38
Disulfide bond224 ↔ 235 Ref.36 Ref.37 Ref.38
Disulfide bond236 ↔ 244 Ref.36 Ref.37 Ref.38
Disulfide bond240 ↔ 252 Ref.36 Ref.37 Ref.38
Disulfide bond255 ↔ 264 Ref.36 Ref.37 Ref.38
Disulfide bond268 ↔ 295 Ref.36 Ref.37 Ref.38
Disulfide bond299 ↔ 311 Ref.36 Ref.37 Ref.38
Disulfide bond315 ↔ 331 Ref.36 Ref.37 Ref.38
Disulfide bond334 ↔ 338 Ref.36 Ref.37 Ref.38
Disulfide bond342 ↔ 367 Ref.36 Ref.37 Ref.38
Disulfide bond475 ↔ 504 Ref.36 Ref.37 Ref.38
Disulfide bond511 ↔ 520 Ref.36 Ref.37 Ref.38
Disulfide bond515 ↔ 528 Ref.36 Ref.37 Ref.38
Disulfide bond531 ↔ 540 Ref.36 Ref.37 Ref.38
Disulfide bond544 ↔ 560 Ref.36 Ref.37 Ref.38
Disulfide bond563 ↔ 576 Ref.36 Ref.37 Ref.38
Disulfide bond567 ↔ 584 Ref.36 Ref.37 Ref.38
Disulfide bond587 ↔ 596 Ref.36 Ref.37 Ref.38
Disulfide bond600 ↔ 623 Ref.36 Ref.37 Ref.38
Disulfide bond626 ↔ 634 By similarity
Disulfide bond630 ↔ 642 By similarity

Natural variations

Alternative sequence1 – 686686Missing in isoform 3.
VSP_039250
Alternative sequence1 – 610610Missing in isoform 2.
VSP_039249
Alternative sequence1 – 2323MELAA…GAAST → MPRGSWKP in isoform 4.
VSP_039248
Natural variant4521W → C. Ref.3
Corresponds to variant rs4252633 [ dbSNP | Ensembl ].
VAR_016317
Natural variant6541I → V in allele B3. Ref.40 Ref.42
Corresponds to variant rs1801201 [ dbSNP | Ensembl ].
VAR_004077
Natural variant6551I → V in allele B2 and allele B3. Ref.3 Ref.40 Ref.42
Corresponds to variant rs1136201 [ dbSNP | Ensembl ].
VAR_004078
Natural variant7551L → P in a lung adenocarcinoma sample; somatic mutation. Ref.41
VAR_055432
Natural variant7681L → S. Ref.42
Corresponds to variant rs56366519 [ dbSNP | Ensembl ].
VAR_042097
Natural variant7741M → MAYVM in a lung adenocarcinoma sample; somatic mutation.
VAR_055433
Natural variant7761G → S in a gastric adenocarcinoma sample; somatic mutation. Ref.41 Ref.42
Corresponds to variant rs28933369 [ dbSNP | Ensembl ].
VAR_042098
Natural variant7791S → SVGS in a lung adenocarcinoma sample; somatic mutation.
VAR_055434
Natural variant8571N → S in an ovarian cancer sample; somatic mutation. Ref.41 Ref.42
Corresponds to variant rs28933370 [ dbSNP | Ensembl ].
VAR_042099
Natural variant9141E → K in a glioblastoma sample; somatic mutation. Ref.41
Corresponds to variant rs28933368 [ dbSNP | Ensembl ].
VAR_055435
Natural variant11701P → A. Ref.2 Ref.3 Ref.10 Ref.42
Corresponds to variant rs61552325 [ dbSNP | Ensembl ].
VAR_016318
Natural variant12161A → D. Ref.42
Corresponds to variant rs55943169 [ dbSNP | Ensembl ].
VAR_042100

Experimental info

Mutagenesis317 – 3182LH → AA: Reduces dimerization with ERBB3. Ref.36
Mutagenesis6111M → A: Prevents synthesis of isoform 2. Ref.19 Ref.36
Mutagenesis6871M → A: Prevents synthesis of isoform 3. Ref.19 Ref.36
Mutagenesis7061M → A: No effect on isoform production. Ref.19 Ref.36
Mutagenesis7121M → A: No effect on isoform production. Ref.19 Ref.36

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ERBB2) (HER2) [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

Isoform 2 (CTF-611) [UniParc].

Checksum: 288AFEFB6D101A34
Show »

FASTA64570,917
Isoform 3 (CTF-687) [UniParc].

Checksum: 090ABCB192CE1E73
Show »

FASTA56962,568
Isoform 4 [UniParc].

Checksum: 1C679DD67798C0DE
Show »

FASTA1,240136,501

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), 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]"NEDO human cDNA sequencing project focused on splicing variants."
Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T. expand/collapse author list , Sugano S., Nomura N., Isogai T.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Brain.
[5]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].
[6]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-191 (ISOFORM 1).
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 737-1031.
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 832-909.
Tissue: Mammary carcinoma.
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1081-1245, VARIANT ALA-1170.
[11]"ErbB receptor-induced activation of stat transcription factors is mediated by Src tyrosine kinases."
Olayioye M.A., Beuvink I., Horsch K., Daly J.M., Hynes N.E.
J. Biol. Chem. 274:17209-17218(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4, FUNCTION IN ACTIVATION OF STAT5A.
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND EGFR, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND EGFR, INTERACTION WITH PIK3C2B.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUC1.
[14]"Binding at and transactivation of the COX-2 promoter by nuclear tyrosine kinase receptor ErbB-2."
Wang S.C., Lien H.C., Xia W., Chen I.F., Lo H.W., Wang Z., Ali-Seyed M., Lee D.F., Bartholomeusz G., Ou-Yang F., Giri D.K., Hung M.C.
Cancer Cell 6:251-261(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB1.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEMO1.
[17]"Endosomal transport of ErbB-2: mechanism for nuclear entry of the cell surface receptor."
Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G., Wang S.C., Hung M.C.
Mol. Cell. Biol. 25:11005-11018(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, INTERACTION WITH KPNB1; RANBP2; CRM1; EEA1 AND CLTC.
[18]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1248, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[19]"Biosynthesis of tumorigenic HER2 C-terminal fragments by alternative initiation of translation."
Anido J., Scaltriti M., Bech Serra J.J., Santiago Josefat B., Todo F.R., Baselga J., Arribas J.
EMBO J. 25:3234-3244(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ALTERNATIVE INITIATION (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, MUTAGENESIS OF MET-611; MET-687; MET-706 AND MET-712.
[20]"Neuregulin-1 only induces trans-phosphorylation between ErbB receptor heterodimer partners."
Li Z., Mei Y., Liu X., Zhou M.
Cell. Signal. 19:466-471(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ERBB4, AUTOPHOSPHORYLATION IN TRANS.
[21]"Plexin-B2, but not Plexin-B1, critically modulates neuronal migration and patterning of the developing nervous system in vivo."
Deng S., Hirschberg A., Worzfeld T., Penachioni J.Y., Korostylev A., Swiercz J.M., Vodrazka P., Mauti O., Stoeckli E.T., Tamagnone L., Offermanns S., Kuner R.
J. Neurosci. 27:6333-6347(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-1248.
[22]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[23]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[24]"Brk is coamplified with ErbB2 to promote proliferation in breast cancer."
Xiang B., Chatti K., Qiu H., Lakshmi B., Krasnitz A., Hicks J., Yu M., Miller W.T., Muthuswamy S.K.
Proc. Natl. Acad. Sci. U.S.A. 105:12463-12468(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK6, ENZYME REGULATION.
[25]"ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells."
Hawthorne V.S., Huang W.C., Neal C.L., Tseng L.M., Hung M.C., Yu D.
Mol. Cancer Res. 7:592-600(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEUS.
[26]"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells."
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[27]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[28]"Genetic and structural variation in the gastric cancer kinome revealed through targeted deep sequencing."
Zang Z.J., Ong C.K., Cutcutache I., Yu W., Zhang S.L., Huang D., Ler L.D., Dykema K., Gan A., Tao J., Lim S., Liu Y., Futreal P.A., Grabsch H., Furge K.A., Goh L.K., Rozen S., Teh B.T., Tan P.
Cancer Res. 71:29-39(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL REARRANGEMENT WITH CDK12.
[29]"Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes."
Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H., Chen H.Y., Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P., Lien H.C., Tsai C.H., Hung M.C.
Cancer Res. 71:4269-4279(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NUCLEUS, INTERACTION WITH ACTB AND RPA194, SUBCELLULAR LOCATION.
[30]"Dissociation of epidermal growth factor receptor and ErbB2 heterodimers in the presence of somatostatin receptor 5 modulate signaling pathways."
Kharmate G., Rajput P.S., Watt H.L., Somvanshi R.K., Chaudhari N., Qiu X., Kumar U.
Endocrinology 152:931-945(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EGFR.
[31]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, MASS SPECTROMETRY.
[32]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 654-662 IN COMPLEX WITH HLA AND BETA-2 MICROGLOBULIN.
[33]"Novel mode of ligand recognition by the Erbin PDZ domain."
Birrane G., Chung J., Ladias J.A.
J. Biol. Chem. 278:1399-1402(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1247-1255 IN COMPLEX WITH ERBB2IP, INTERACTION WITH ERBB2IP.
[34]"Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex and structural basis for Grb7 binding to ErbB2."
Ivancic M., Daly R.J., Lyons B.A.
J. Biomol. NMR 27:205-219(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1135-1144 IN COMPLEX WITH GRB7, INTERACTION WITH GRB7.
[35]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 23-629 IN COMPLEX WITH THE ANTIBODY HERCEPTIN.
[36]"Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex."
Franklin M.C., Carey K.D., Vajdos F.F., Leahy D.J., de Vos A.M., Sliwkowski M.X.
Cancer Cell 5:317-328(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-646 IN COMPLEX WITH THE ANTIBODY PERTUZUMAB, INTERACTION WITH ERBB3, MUTAGENESIS OF 317-LEU-HIS-318, DISULFIDE BONDS, GLYCOSYLATION AT ASN-187; ASN-259 AND ASN-530.
[37]"Variants of the antibody herceptin that interact with HER2 and VEGF at the antigen binding site."
Bostrom J., Yu S.F., Kan D., Appleton B.A., Lee C.V., Billeci K., Man W., Peale F., Ross S., Wiesmann C., Fuh G.
Science 323:1610-1614(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 23-646 IN COMPLEX WITH THE ANTIBODY HERCEPTIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-259 AND ASN-530.
[38]"Structural basis for high-affinity HER2 receptor binding by an engineered protein."
Eigenbrot C., Ultsch M., Dubnovitsky A., Abrahmsen L., Hard T.
Proc. Natl. Acad. Sci. U.S.A. 107:15039-15044(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 23-646 IN COMPLEX WITH ENGINEERED ANTIBODY ZHER2, DISULFIDE BONDS, GLYCOSYLATION AT ASN-68; ASN-259 AND ASN-571.
[39]"Structural analysis of the mechanism of inhibition and allosteric activation of the kinase domain of HER2 protein."
Aertgeerts K., Skene R., Yano J., Sang B.C., Zou H., Snell G., Jennings A., Iwamoto K., Habuka N., Hirokawa A., Ishikawa T., Tanaka T., Miki H., Ohta Y., Sogabe S.
J. Biol. Chem. 286:18756-18765(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 703-1029 IN COMPLEX WITH INHIBITOR SYR127063, CATALYTIC ACTIVITY, SUBUNIT, ENYZME REGULATION.
[40]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-654 AND VAL-655.
[41]"Lung cancer: 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., 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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PRO-755; SER-776; ALA-TYR-VAL-MET-774 INS AND VAL-GLY-SER-779 INS; SER-857 AND LYS-914, INVOLVEMENT IN CANCER.
[42]"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] [Europe PMC] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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 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.
IPI00845478.
IPI00941360.
IPI00964086.
PIRA24571.
RefSeqNP_001005862.1. NM_001005862.1.
NP_004439.2. NM_004448.2.
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[»]
2KS1NMR-A641-684[»]
2L4KNMR-B1135-1144[»]
3BE1X-ray2.90A23-646[»]
3H3BX-ray2.45A/B22-214[»]
3MZWX-ray2.90A23-646[»]
3N85X-ray3.20A23-646[»]
3PP0X-ray2.25A/B703-1029[»]
3RCDX-ray3.21A/B/C/D703-1029[»]
ProteinModelPortalP04626.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-8N.
IntActP04626. 42 interactions.
MINTMINT-158636.
STRING9606.ENSP00000269571.

PTM databases

PhosphoSiteP04626.

Polymorphism databases

DMDM119533.

Proteomic databases

PaxDbP04626.
PRIDEP04626.

Protocols and materials databases

DNASU2064.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269571; ENSP00000269571; ENSG00000141736.
ENST00000541774; ENSP00000446466; ENSG00000141736.
GeneID2064.
KEGGhsa:2064.
UCSCuc002hsm.3. human.
uc010cwa.3. human.

Organism-specific databases

CTD2064.
GeneCardsGC17P037844.
HGNCHGNC:3430. ERBB2.
HPACAB000043.
CAB020416.
HPA001383.
MIM137215. phenotype.
137800. phenotype.
164870. gene.
167000. phenotype.
211980. phenotype.
613659. phenotype.
neXtProtNX_P04626.
PharmGKBPA27844.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000230982.
HOVERGENHBG000490.
InParanoidP04626.
KOK05083.
OMAGGCARCK.
OrthoDBEOG461434.
PhylomeDBP04626.

Enzyme and pathway databases

Pathway_Interaction_DBa6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

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.
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]
PfamPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00261. FU. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF57184. Grow_fac_recept. 2 hits.
SSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP04626.
ChEMBLCHEMBL1824.
ChiTaRSERBB2. human.
DrugBankDB01259. Lapatinib.
DB01006. Letrozole.
DB00072. Trastuzumab.
EvolutionaryTraceP04626.
GenomeRNAi2064.
NextBio8385.
PMAP-CutDBP04626.
SOURCESearch...

Entry information

Entry nameERBB2_HUMAN
AccessionPrimary (citable) accession number: P04626
Secondary accession number(s): B2RZG3 expand/collapse secondary AC list , B4DHN3, Q14256, Q6LDV1, Q9UMK4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: May 1, 2013
This is version 178 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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