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Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Metastatic lymph node gene 19 protein) (MLN 19) (Proto-oncogene Neu) (Proto-oncogene c-ErbB-2) (Tyrosine kinase-type cell surface receptor HER2) (p185erbB2) (CD antigen CD340)

 ERBB2_HUMAN             Reviewed;        1255 AA.
P04626; B2RZG3; B4DHN3; Q14256; Q6LDV1; Q9UMK4; X5D2V5;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
22-NOV-2017, entry version 230.
RecName: Full=Receptor tyrosine-protein kinase erbB-2;
EC=2.7.10.1;
AltName: Full=Metastatic lymph node gene 19 protein;
Short=MLN 19;
AltName: Full=Proto-oncogene Neu;
AltName: Full=Proto-oncogene c-ErbB-2;
AltName: Full=Tyrosine kinase-type cell surface receptor HER2;
AltName: Full=p185erbB2;
AltName: CD_antigen=CD340;
Flags: Precursor;
Name=ERBB2; Synonyms=HER2, MLN19, NEU, NGL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3003577; DOI=10.1038/319230a0;
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] (ISOFORM 1), AND VARIANT
ALA-1170.
PubMed=2999974; DOI=10.1126/science.2999974;
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 [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
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., Sugano S., Nomura N., Isogai T.;
"NEDO human cDNA sequencing project focused on splicing variants.";
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-191 (ISOFORM 1).
PubMed=3039351; DOI=10.1128/MCB.7.7.2597;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-867 (ISOFORM 6).
TISSUE=Fetal brain;
PubMed=24722188; DOI=10.1038/ncomms4650;
Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L.,
Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S.,
Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.,
Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S.,
Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M.,
Iakoucheva L.M.;
"Protein interaction network of alternatively spliced isoforms from
brain links genetic risk factors for autism.";
Nat. Commun. 5:3650-3650(2014).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 737-1031.
PubMed=2995967; DOI=10.1073/pnas.82.19.6497;
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 832-909.
TISSUE=Mammary carcinoma;
PubMed=2992089; DOI=10.1126/science.2992089;
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).
[11]
NUCLEOTIDE SEQUENCE OF 1081-1245, AND VARIANT ALA-1170.
PubMed=8104414; DOI=10.1089/dna.1993.12.611;
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).
[12]
INTERACTION WITH ERBB4, AND FUNCTION IN ACTIVATION OF STAT5A.
PubMed=10358079; DOI=10.1074/jbc.274.24.17209;
Olayioye M.A., Beuvink I., Horsch K., Daly J.M., Hynes N.E.;
"ErbB receptor-induced activation of stat transcription factors is
mediated by Src tyrosine kinases.";
J. Biol. Chem. 274:17209-17218(1999).
[13]
IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND EGFR, IDENTIFICATION IN A
COMPLEX WITH PIK3C2B AND EGFR, AND INTERACTION WITH PIK3C2B.
PubMed=10805725; DOI=10.1128/MCB.20.11.3817-3830.2000;
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).
[14]
INTERACTION WITH MUC1.
PubMed=12939402;
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).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15380516; DOI=10.1016/j.ccr.2004.07.012;
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.;
"Binding at and transactivation of the COX-2 promoter by nuclear
tyrosine kinase receptor ErbB-2.";
Cancer Cell 6:251-261(2004).
[16]
INTERACTION WITH PLXNB1.
PubMed=15210733; DOI=10.1083/jcb.200312094;
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).
[17]
INTERACTION WITH MEMO1.
PubMed=15156151; DOI=10.1038/ncb1134;
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).
[18]
SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND INTERACTION
WITH KPNB1; RANBP2; CRM1; EEA1 AND CLTC.
PubMed=16314522; DOI=10.1128/MCB.25.24.11005-11018.2005;
Giri D.K., Ali-Seyed M., Li L.Y., Lee D.F., Ling P., Bartholomeusz G.,
Wang S.C., Hung M.C.;
"Endosomal transport of ErbB-2: mechanism for nuclear entry of the
cell surface receptor.";
Mol. Cell. Biol. 25:11005-11018(2005).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1248, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
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).
[20]
FUNCTION, ALTERNATIVE INITIATION (ISOFORMS 2 AND 3), SUBCELLULAR
LOCATION, AND MUTAGENESIS OF MET-611; MET-687; MET-706 AND MET-712.
PubMed=16794579; DOI=10.1038/sj.emboj.7601191;
Anido J., Scaltriti M., Bech Serra J.J., Santiago Josefat B.,
Todo F.R., Baselga J., Arribas J.;
"Biosynthesis of tumorigenic HER2 C-terminal fragments by alternative
initiation of translation.";
EMBO J. 25:3234-3244(2006).
[21]
INTERACTION WITH ERBB4, AND AUTOPHOSPHORYLATION IN TRANS.
PubMed=16978839; DOI=10.1016/j.cellsig.2006.07.020;
Li Z., Mei Y., Liu X., Zhou M.;
"Neuregulin-1 only induces trans-phosphorylation between ErbB receptor
heterodimer partners.";
Cell. Signal. 19:466-471(2007).
[22]
PHOSPHORYLATION AT TYR-1248.
PubMed=17554007; DOI=10.1523/JNEUROSCI.5381-06.2007;
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.;
"Plexin-B2, but not Plexin-B1, critically modulates neuronal migration
and patterning of the developing nervous system in vivo.";
J. Neurosci. 27:6333-6347(2007).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[25]
INTERACTION WITH PTK6, AND ENZYME REGULATION.
PubMed=18719096; DOI=10.1073/pnas.0805009105;
Xiang B., Chatti K., Qiu H., Lakshmi B., Krasnitz A., Hicks J., Yu M.,
Miller W.T., Muthuswamy S.K.;
"Brk is coamplified with ErbB2 to promote proliferation in breast
cancer.";
Proc. Natl. Acad. Sci. U.S.A. 105:12463-12468(2008).
[26]
FUNCTION IN NUCLEUS.
PubMed=19372587; DOI=10.1158/1541-7786.MCR-08-0316;
Hawthorne V.S., Huang W.C., Neal C.L., Tseng L.M., Hung M.C., Yu D.;
"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.";
Mol. Cancer Res. 7:592-600(2009).
[27]
INTERACTION WITH CPNE3.
PubMed=20010870; DOI=10.1038/onc.2009.456;
Heinrich C., Keller C., Boulay A., Vecchi M., Bianchi M., Sack R.,
Lienhard S., Duss S., Hofsteenge J., Hynes N.E.;
"Copine-III interacts with ErbB2 and promotes tumor cell migration.";
Oncogene 29:1598-1610(2010).
[28]
FUNCTION.
PubMed=20937854; DOI=10.1073/pnas.1000975107;
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
plasma membrane of migrating cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
CHROMOSOMAL REARRANGEMENT WITH CDK12.
PubMed=21097718; DOI=10.1158/0008-5472.CAN-10-1749;
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.;
"Genetic and structural variation in the gastric cancer kinome
revealed through targeted deep sequencing.";
Cancer Res. 71:29-39(2011).
[31]
FUNCTION IN NUCLEUS, INTERACTION WITH ACTB AND RPA194, AND SUBCELLULAR
LOCATION.
PubMed=21555369; DOI=10.1158/0008-5472.CAN-10-3504;
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.;
"Nuclear ErbB2 enhances translation and cell growth by activating
transcription of ribosomal RNA genes.";
Cancer Res. 71:4269-4279(2011).
[32]
INTERACTION WITH EGFR.
PubMed=21190959; DOI=10.1210/en.2010-0940;
Kharmate G., Rajput P.S., Watt H.L., Somvanshi R.K., Chaudhari N.,
Qiu X., Kumar U.;
"Dissociation of epidermal growth factor receptor and ErbB2
heterodimers in the presence of somatostatin receptor 5 modulate
signaling pathways.";
Endocrinology 152:931-945(2011).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182; SER-1054; SER-1083
AND THR-1166, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054 AND SER-1151, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
INTERACTION WITH HSP90AA1 AND HSP90AB1.
PubMed=26517842; DOI=10.1371/journal.pone.0141786;
Prince T.L., Kijima T., Tatokoro M., Lee S., Tsutsumi S., Yim K.,
Rivas C., Alarcon S., Schwartz H., Khamit-Kush K., Scroggins B.T.,
Beebe K., Trepel J.B., Neckers L.;
"Client proteins and small molecule inhibitors display distinct
binding preferences for constitutive and stress-induced HSP90 isoforms
and their conformationally restricted mutants.";
PLoS ONE 10:E0141786-E0141786(2015).
[37]
PHOSPHORYLATION AT TYR-1112; TYR-1139; TYR-1196 AND TYR-1248, AND
DEPHOSPHORYLATION BY PTPN12.
PubMed=27134172; DOI=10.1016/j.celrep.2016.04.016;
Li H., Yang F., Liu C., Xiao P., Xu Y., Liang Z., Liu C., Wang H.,
Wang W., Zheng W., Zhang W., Ma X., He D., Song X., Cui F., Xu Z.,
Yi F., Sun J.P., Yu X.;
"Crystal structure and substrate specificity of PTPN12.";
Cell Rep. 15:1345-1358(2016).
[38]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 654-662 IN COMPLEX WITH HLA
AND BETA-2 MICROGLOBULIN.
PubMed=10593938; DOI=10.1074/jbc.274.51.36422;
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).
[39]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 1247-1255 IN COMPLEX WITH
ERBIN, AND INTERACTION WITH ERBIN.
PubMed=12444095; DOI=10.1074/jbc.C200571200;
Birrane G., Chung J., Ladias J.A.;
"Novel mode of ligand recognition by the Erbin PDZ domain.";
J. Biol. Chem. 278:1399-1402(2003).
[40]
STRUCTURE BY NMR OF 1135-1144 IN COMPLEX WITH GRB7, AND INTERACTION
WITH GRB7.
PubMed=12975581; DOI=10.1023/A:1025498409113;
Ivancic M., Daly R.J., Lyons B.A.;
"Solution structure of the human Grb7-SH2 domain/erbB2 peptide complex
and structural basis for Grb7 binding to ErbB2.";
J. Biomol. NMR 27:205-219(2003).
[41]
X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 23-629 IN COMPLEX WITH THE
ANTIBODY HERCEPTIN.
PubMed=12610629; DOI=10.1038/nature01392;
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).
[42]
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, AND GLYCOSYLATION AT ASN-187;
ASN-259 AND ASN-530.
PubMed=15093539; DOI=10.1016/S1535-6108(04)00083-2;
Franklin M.C., Carey K.D., Vajdos F.F., Leahy D.J., de Vos A.M.,
Sliwkowski M.X.;
"Insights into ErbB signaling from the structure of the ErbB2-
pertuzumab complex.";
Cancer Cell 5:317-328(2004).
[43]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 23-646 IN COMPLEX WITH THE
ANTIBODY HERCEPTIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-259 AND
ASN-530.
PubMed=19299620; DOI=10.1126/science.1165480;
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.;
"Variants of the antibody herceptin that interact with HER2 and VEGF
at the antigen binding site.";
Science 323:1610-1614(2009).
[44]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 23-646 IN COMPLEX WITH
ENGINEERED ANTIBODY ZHER2, DISULFIDE BONDS, AND GLYCOSYLATION AT
ASN-68; ASN-259 AND ASN-571.
PubMed=20696930; DOI=10.1073/pnas.1005025107;
Eigenbrot C., Ultsch M., Dubnovitsky A., Abrahmsen L., Hard T.;
"Structural basis for high-affinity HER2 receptor binding by an
engineered protein.";
Proc. Natl. Acad. Sci. U.S.A. 107:15039-15044(2010).
[45]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 703-1029 IN COMPLEX WITH
INHIBITOR SYR127063, CATALYTIC ACTIVITY, SUBUNIT, AND ENZYME
REGULATION.
PubMed=21454582; DOI=10.1074/jbc.M110.206193;
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.;
"Structural analysis of the mechanism of inhibition and allosteric
activation of the kinase domain of HER2 protein.";
J. Biol. Chem. 286:18756-18765(2011).
[46]
VARIANTS VAL-654 AND VAL-655.
PubMed=8095488; DOI=10.1006/geno.1993.1081;
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).
[47]
INVOLVEMENT IN CANCER, VARIANT GASC SER-776, VARIANT OC SER-857,
VARIANT GLM LYS-914, AND VARIANTS LNCR PRO-755; ALA-TYR-VAL-MET-774
INS AND VAL-GLY-SER-779 INS.
PubMed=15457249; DOI=10.1038/431525b;
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., 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.;
"Lung cancer: intragenic ERBB2 kinase mutations in tumours.";
Nature 431:525-526(2004).
[48]
VARIANTS [LARGE SCALE ANALYSIS] VAL-654; VAL-655; SER-768; ALA-1170
AND ASP-1216, VARIANT GASC SER-776, AND VARIANT OC SER-857.
PubMed=17344846; DOI=10.1038/nature05610;
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).
-!- 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. {ECO:0000305}.
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10358079, ECO:0000269|PubMed:15380516,
ECO:0000269|PubMed:21555369}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:21454582}.
-!- ENZYME REGULATION: Activated by dimerization. Not activated by
EGF, TGF-alpha and amphiregulin. Interaction with PTK6 increases
its intrinsic kinase activity. {ECO:0000269|PubMed:18719096,
ECO:0000269|PubMed:21454582}.
-!- SUBUNIT: Homodimer (PubMed:21454582). Heterodimer with EGFR, ERBB3
and ERBB4 (PubMed:10358079, PubMed:15093539, PubMed:21190959,
PubMed:16978839). Part of a complex with EGFR and either PIK3C2A
or PIK3C2B. May interact with PIK3C2B when phosphorylated on Tyr-
1196 (PubMed:10805725). Interacts with PLXNB1 (PubMed:15210733).
Interacts (when phosphorylated on Tyr-1248) with MEMO1
(PubMed:15156151). Interacts with MUC1; the interaction is
enhanced by heregulin (HRG) (PubMed:12939402). Interacts (when
phosphorylated on Tyr-1139) with GRB7 (via SH2 domain)
(PubMed:12975581). Interacts (when phosphorylated on Tyr-1248)
with ERBIN (PubMed:12444095). Interacts with KPNB1, RANBP2, EEA1,
CRM1 and CLTC (PubMed:16314522). Interacts with PTK6
(PubMed:18719096). Interacts with RPA194 and ACTB
(PubMed:21555369). Interacts with PRKCABP, SRC and MYOC (By
similarity). Interacts (preferentially with the tyrosine
phosphorylated form) with CPNE3; this interaction occurs at the
cell membrane and is increased in a growth factor heregulin-
dependent manner (PubMed:20010870). Interacts with HSP90AA1 and
HSP90AB1 in an ATP-dependent manner; the interaction suppresses
ERBB2 kinase activity (PubMed:26517842).
{ECO:0000250|UniProtKB:P70424, ECO:0000269|PubMed:10358079,
ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:12939402,
ECO:0000269|PubMed:12975581, ECO:0000269|PubMed:15093539,
ECO:0000269|PubMed:15156151, ECO:0000269|PubMed:15210733,
ECO:0000269|PubMed:16314522, ECO:0000269|PubMed:16978839,
ECO:0000269|PubMed:18719096, ECO:0000269|PubMed:20010870,
ECO:0000269|PubMed:21190959, ECO:0000269|PubMed:21454582,
ECO:0000269|PubMed:21555369, ECO:0000269|PubMed:26517842}.
-!- INTERACTION:
Self; NbExp=12; IntAct=EBI-641062, EBI-641062;
P00519:ABL1; NbExp=2; IntAct=EBI-641062, EBI-375543;
P42684:ABL2; NbExp=6; IntAct=EBI-641062, EBI-1102694;
P15309:ACPP; NbExp=3; IntAct=EBI-641062, EBI-1222012;
P60709:ACTB; NbExp=10; IntAct=EBI-641062, EBI-353944;
Q92625:ANKS1A; NbExp=2; IntAct=EBI-641062, EBI-1048612;
O00213:APBB1; NbExp=2; IntAct=EBI-641062, EBI-81694;
O75815:BCAR3; NbExp=2; IntAct=EBI-641062, EBI-702336;
Q16543:CDC37; NbExp=3; IntAct=EBI-641062, EBI-295634;
Q9NSE2:CISH; NbExp=4; IntAct=EBI-641062, EBI-617866;
Q7Z7G1:CLNK; NbExp=2; IntAct=EBI-641062, EBI-7878194;
P46109:CRKL; NbExp=2; IntAct=EBI-641062, EBI-910;
Q93034:CUL5; NbExp=2; IntAct=EBI-641062, EBI-1057139;
Q99704:DOK1; NbExp=2; IntAct=EBI-641062, EBI-1384360;
Q8TEW6:DOK4; NbExp=2; IntAct=EBI-641062, EBI-6918542;
Q15075:EEA1; NbExp=5; IntAct=EBI-641062, EBI-298113;
P98172:EFNB1; NbExp=11; IntAct=EBI-641062, EBI-538287;
P00533:EGFR; NbExp=25; IntAct=EBI-641062, EBI-297353;
P21860:ERBB3; NbExp=29; IntAct=EBI-641062, EBI-720706;
Q15303:ERBB4; NbExp=4; IntAct=EBI-641062, EBI-80371;
Q9UJM3:ERRFI1; NbExp=3; IntAct=EBI-641062, EBI-2941912;
P09769:FGR; NbExp=3; IntAct=EBI-641062, EBI-1383732;
P06241:FYN; NbExp=2; IntAct=EBI-641062, EBI-515315;
O75791:GRAP2; NbExp=2; IntAct=EBI-641062, EBI-740418;
P62993:GRB2; NbExp=4; IntAct=EBI-641062, EBI-401755;
Q14451:GRB7; NbExp=5; IntAct=EBI-641062, EBI-970191;
O75367:H2AFY; NbExp=6; IntAct=EBI-641062, EBI-2868511;
O75367-3:H2AFY; NbExp=3; IntAct=EBI-641062, EBI-6250866;
P07900:HSP90AA1; NbExp=5; IntAct=EBI-641062, EBI-296047;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-641062, EBI-352572;
P14625:HSP90B1; NbExp=2; IntAct=EBI-641062, EBI-359129;
P46940:IQGAP1; NbExp=5; IntAct=EBI-641062, EBI-297509;
P35568:IRS1; NbExp=2; IntAct=EBI-641062, EBI-517592;
Q08881:ITK; NbExp=2; IntAct=EBI-641062, EBI-968552;
P23458:JAK1; NbExp=2; IntAct=EBI-641062, EBI-1383438;
Q14974:KPNB1; NbExp=14; IntAct=EBI-641062, EBI-286758;
Q9UQF2:MAPK8IP1; NbExp=3; IntAct=EBI-641062, EBI-78404;
Q13387:MAPK8IP2; NbExp=3; IntAct=EBI-641062, EBI-722813;
P42679:MATK; NbExp=2; IntAct=EBI-641062, EBI-751664;
Q9Y316:MEMO1; NbExp=6; IntAct=EBI-641062, EBI-1104564;
O43639:NCK2; NbExp=2; IntAct=EBI-641062, EBI-713635;
Q02297-7:NRG1; NbExp=2; IntAct=EBI-641062, EBI-2460927;
O00750:PIK3C2B; NbExp=2; IntAct=EBI-641062, EBI-641107;
P27986:PIK3R1; NbExp=11; IntAct=EBI-641062, EBI-79464;
O00459:PIK3R2; NbExp=6; IntAct=EBI-641062, EBI-346930;
Q92569:PIK3R3; NbExp=9; IntAct=EBI-641062, EBI-79893;
P19174:PLCG1; NbExp=5; IntAct=EBI-641062, EBI-79387;
P16885:PLCG2; NbExp=3; IntAct=EBI-641062, EBI-617403;
O95602:POLR1A; NbExp=16; IntAct=EBI-641062, EBI-359472;
Q05397:PTK2; NbExp=2; IntAct=EBI-641062, EBI-702142;
Q13882:PTK6; NbExp=4; IntAct=EBI-641062, EBI-1383632;
Q06124:PTPN11; NbExp=2; IntAct=EBI-641062, EBI-297779;
Q05209:PTPN12; NbExp=4; IntAct=EBI-641062, EBI-2266035;
Q99952:PTPN18; NbExp=6; IntAct=EBI-641062, EBI-1384210;
Q99952-1:PTPN18; NbExp=5; IntAct=EBI-641062, EBI-12739708;
P23467:PTPRB; NbExp=2; IntAct=EBI-641062, EBI-1265766;
P08575:PTPRC; NbExp=2; IntAct=EBI-641062, EBI-1341;
Q12913:PTPRJ; NbExp=2; IntAct=EBI-641062, EBI-2264500;
Q15262:PTPRK; NbExp=2; IntAct=EBI-641062, EBI-474052;
Q16827:PTPRO; NbExp=2; IntAct=EBI-641062, EBI-723739;
P49792:RANBP2; NbExp=3; IntAct=EBI-641062, EBI-973138;
P20936:RASA1; NbExp=8; IntAct=EBI-641062, EBI-1026476;
O95980:RECK; NbExp=4; IntAct=EBI-641062, EBI-2823742;
Q9NP31:SH2D2A; NbExp=2; IntAct=EBI-641062, EBI-490630;
P29353:SHC1; NbExp=9; IntAct=EBI-641062, EBI-78835;
P98077:SHC2; NbExp=3; IntAct=EBI-641062, EBI-7256023;
Q92529:SHC3; NbExp=2; IntAct=EBI-641062, EBI-79084;
Q9H6Q3:SLA2; NbExp=2; IntAct=EBI-641062, EBI-1222854;
O15524:SOCS1; NbExp=2; IntAct=EBI-641062, EBI-968198;
P12931:SRC; NbExp=11; IntAct=EBI-641062, EBI-621482;
P42224:STAT1; NbExp=3; IntAct=EBI-641062, EBI-1057697;
P40763:STAT3; NbExp=9; IntAct=EBI-641062, EBI-518675;
Q7KZ85:SUPT6H; NbExp=2; IntAct=EBI-641062, EBI-2515547;
P43405:SYK; NbExp=7; IntAct=EBI-641062, EBI-78302;
Q9Y490:TLN1; NbExp=3; IntAct=EBI-641062, EBI-2462036;
Q63HR2:TNS2; NbExp=4; IntAct=EBI-641062, EBI-949753;
Q68CZ2:TNS3; NbExp=2; IntAct=EBI-641062, EBI-1220488;
Q96D37:VAV1; NbExp=2; IntAct=EBI-641062, EBI-7875353;
P52735:VAV2; NbExp=3; IntAct=EBI-641062, EBI-297549;
O14980:XPO1; NbExp=2; IntAct=EBI-641062, EBI-355867;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein. Cytoplasm, perinuclear region. Nucleus.
Note=Translocation to the nucleus requires endocytosis, probably
endosomal sorting and is mediated by importin beta-1/KPNB1.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=6;
Name=1; Synonyms=ERBB2, HER2;
IsoId=P04626-1; Sequence=Displayed;
Name=2; Synonyms=CTF-611;
IsoId=P04626-2; Sequence=VSP_039249;
Note=Produced by alternative initiation at Met-611 of isoform
1.;
Name=3; Synonyms=CTF-687;
IsoId=P04626-3; Sequence=VSP_039250;
Note=Produced by alternative initiation at Met-687 of isoform
1.;
Name=4;
IsoId=P04626-4; Sequence=VSP_039248;
Note=Produced by alternative splicing of isoform 1.;
Name=5;
IsoId=P04626-5; Sequence=VSP_054787;
Note=No experimental confirmation available. Gene prediction
based on partial mRNA and EST data.;
Name=6; Synonyms=B;
IsoId=P04626-6; Sequence=VSP_055902, VSP_055903, VSP_055904;
-!- TISSUE SPECIFICITY: Expressed in a variety of tumor tissues
including primary breast tumors and tumors from small bowel,
esophagus, kidney and mouth. {ECO:0000269|PubMed:15380516}.
-!- PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e.
one subunit of the dimeric receptor phosphorylates tyrosine
residues on the other subunit (Probable). Ligand-binding increases
phosphorylation on tyrosine residues (PubMed:27134172). Signaling
via SEMA4C promotes phosphorylation at Tyr-1248 (PubMed:17554007).
Dephosphorylated by PTPN12 (PubMed:27134172).
{ECO:0000269|PubMed:17554007, ECO:0000269|PubMed:27134172,
ECO:0000305}.
-!- 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.
-!- DISEASE: 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.
{ECO:0000269|PubMed:15457249}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: 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.
{ECO:0000269|PubMed:15457249, ECO:0000269|PubMed:17344846}.
Note=The gene represented in this entry is involved in disease
pathogenesis.
-!- DISEASE: 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.
{ECO:0000269|PubMed:15457249}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: 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. {ECO:0000269|PubMed:15457249,
ECO:0000269|PubMed:17344846}. Note=The protein represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Note=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.
{ECO:0000269|PubMed:21097718}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- 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="https://en.wikipedia.org/wiki/ERBB2";
-----------------------------------------------------------------------
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EMBL; AH001455; AAA35808.1; -; Genomic_DNA.
EMBL; X03363; CAA27060.1; -; mRNA.
EMBL; M11730; AAA75493.1; -; mRNA.
EMBL; M12036; AAA35978.1; -; Genomic_DNA.
EMBL; AY208911; AAO18082.1; -; Genomic_DNA.
EMBL; AK295195; BAG58195.1; -; mRNA.
EMBL; CH471152; EAW60597.1; -; Genomic_DNA.
EMBL; BC167147; AAI67147.1; -; mRNA.
EMBL; M16792; AAA58637.1; -; Genomic_DNA.
EMBL; M16789; AAA58637.1; JOINED; Genomic_DNA.
EMBL; M16790; AAA58637.1; JOINED; Genomic_DNA.
EMBL; M16791; AAA58637.1; JOINED; Genomic_DNA.
EMBL; KJ534964; AHW56604.1; -; mRNA.
EMBL; L29395; AAA35809.1; -; Genomic_DNA.
EMBL; M95667; AAC37531.1; -; Genomic_DNA.
CCDS; CCDS32642.1; -. [P04626-1]
CCDS; CCDS45667.1; -. [P04626-5]
CCDS; CCDS74052.1; -. [P04626-4]
PIR; A24571; A24571.
RefSeq; NP_001005862.1; NM_001005862.2. [P04626-5]
RefSeq; NP_001276865.1; NM_001289936.1. [P04626-4]
RefSeq; NP_001276867.1; NM_001289938.1.
RefSeq; NP_004439.2; NM_004448.3. [P04626-1]
UniGene; Hs.446352; -.
PDB; 1MFG; X-ray; 1.25 A; B=1247-1255.
PDB; 1MFL; X-ray; 1.88 A; B=1247-1255.
PDB; 1MW4; NMR; -; B=1135-1144.
PDB; 1N8Z; X-ray; 2.52 A; C=23-629.
PDB; 1OVC; Model; -; A=737-1031.
PDB; 1QR1; X-ray; 2.40 A; C/F=654-662.
PDB; 1S78; X-ray; 3.25 A; A/B=23-646.
PDB; 2A91; X-ray; 2.50 A; A=22-530.
PDB; 2JWA; NMR; -; A/B=641-684.
PDB; 2KS1; NMR; -; A=641-684.
PDB; 2L4K; NMR; -; B=1135-1144.
PDB; 2N2A; NMR; -; A/B=644-700.
PDB; 3BE1; X-ray; 2.90 A; A=23-646.
PDB; 3H3B; X-ray; 2.45 A; A/B=23-214.
PDB; 3MZW; X-ray; 2.90 A; A=23-646.
PDB; 3N85; X-ray; 3.20 A; A=23-646.
PDB; 3PP0; X-ray; 2.25 A; A/B=703-1009.
PDB; 3RCD; X-ray; 3.21 A; A/B/C/D=713-1028.
PDB; 3WLW; X-ray; 3.09 A; A/B=23-586.
PDB; 3WSQ; X-ray; 3.50 A; A=23-586.
PDB; 4GFU; X-ray; 2.00 A; F=1246-1252.
PDB; 4HRL; X-ray; 2.55 A; C=24-219.
PDB; 4HRM; X-ray; 3.20 A; A/C=24-219.
PDB; 4HRN; X-ray; 2.65 A; C/D=529-625.
PDB; 5K33; X-ray; 3.30 A; C=23-629.
PDB; 5KWG; X-ray; 4.30 A; C=23-653.
PDB; 5MY6; X-ray; 2.25 A; A=24-645.
PDB; 5TQS; X-ray; 1.88 A; E/F/G/H=1218-1228.
PDBsum; 1MFG; -.
PDBsum; 1MFL; -.
PDBsum; 1MW4; -.
PDBsum; 1N8Z; -.
PDBsum; 1OVC; -.
PDBsum; 1QR1; -.
PDBsum; 1S78; -.
PDBsum; 2A91; -.
PDBsum; 2JWA; -.
PDBsum; 2KS1; -.
PDBsum; 2L4K; -.
PDBsum; 2N2A; -.
PDBsum; 3BE1; -.
PDBsum; 3H3B; -.
PDBsum; 3MZW; -.
PDBsum; 3N85; -.
PDBsum; 3PP0; -.
PDBsum; 3RCD; -.
PDBsum; 3WLW; -.
PDBsum; 3WSQ; -.
PDBsum; 4GFU; -.
PDBsum; 4HRL; -.
PDBsum; 4HRM; -.
PDBsum; 4HRN; -.
PDBsum; 5K33; -.
PDBsum; 5KWG; -.
PDBsum; 5MY6; -.
PDBsum; 5TQS; -.
ProteinModelPortal; P04626; -.
SMR; P04626; -.
BioGrid; 108376; 200.
CORUM; P04626; -.
DIP; DIP-8N; -.
ELM; P04626; -.
IntAct; P04626; 250.
MINT; MINT-158636; -.
STRING; 9606.ENSP00000269571; -.
BindingDB; P04626; -.
ChEMBL; CHEMBL1824; -.
DrugBank; DB08916; Afatinib.
DrugBank; DB04988; IGN311.
DrugBank; DB01259; Lapatinib.
DrugBank; DB06366; Pertuzumab.
DrugBank; DB00072; Trastuzumab.
DrugBank; DB05773; Trastuzumab emtansine.
DrugBank; DB05007; XL647.
GuidetoPHARMACOLOGY; 2019; -.
iPTMnet; P04626; -.
PhosphoSitePlus; P04626; -.
BioMuta; ERBB2; -.
DMDM; 119533; -.
EPD; P04626; -.
PaxDb; P04626; -.
PeptideAtlas; P04626; -.
PRIDE; P04626; -.
DNASU; 2064; -.
Ensembl; ENST00000269571; ENSP00000269571; ENSG00000141736. [P04626-1]
Ensembl; ENST00000406381; ENSP00000385185; ENSG00000141736. [P04626-5]
Ensembl; ENST00000541774; ENSP00000446466; ENSG00000141736. [P04626-4]
Ensembl; ENST00000584601; ENSP00000462438; ENSG00000141736. [P04626-5]
GeneID; 2064; -.
KEGG; hsa:2064; -.
UCSC; uc060esv.1; human. [P04626-1]
CTD; 2064; -.
DisGeNET; 2064; -.
EuPathDB; HostDB:ENSG00000141736.13; -.
GeneCards; ERBB2; -.
HGNC; HGNC:3430; ERBB2.
HPA; CAB000043; -.
HPA; CAB020416; -.
HPA; CAB062555; -.
HPA; HPA001060; -.
HPA; HPA001338; -.
HPA; HPA001383; -.
MalaCards; ERBB2; -.
MIM; 137800; phenotype.
MIM; 164870; gene.
MIM; 167000; phenotype.
MIM; 211980; phenotype.
MIM; 613659; phenotype.
neXtProt; NX_P04626; -.
OpenTargets; ENSG00000141736; -.
PharmGKB; PA27844; -.
eggNOG; KOG1025; Eukaryota.
eggNOG; ENOG410XNSR; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000230982; -.
HOVERGEN; HBG000490; -.
InParanoid; P04626; -.
KO; K05083; -.
OMA; PINCTHS; -.
OrthoDB; EOG091G00NO; -.
PhylomeDB; P04626; -.
TreeFam; TF106002; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1251932; PLCG1 events in ERBB2 signaling.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1306955; GRB7 events in ERBB2 signaling.
Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLink; P04626; -.
SIGNOR; P04626; -.
ChiTaRS; ERBB2; human.
EvolutionaryTrace; P04626; -.
GeneWiki; HER2/neu; -.
GenomeRNAi; 2064; -.
PMAP-CutDB; P04626; -.
PRO; PR:P04626; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000141736; -.
CleanEx; HS_ERBB2; -.
ExpressionAtlas; P04626; baseline and differential.
Genevisible; P04626; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043125; F:ErbB-3 class receptor binding; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:BHF-UCL.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0001042; F:RNA polymerase I core binding; IDA:UniProtKB.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:BHF-UCL.
GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:BHF-UCL.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
GO; GO:0007167; P:enzyme linked receptor protein signaling pathway; TAS:ProtInc.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
GO; GO:0042552; P:myelination; IEA:Ensembl.
GO; GO:1901185; P:negative regulation of ERBB signaling pathway; TAS:Reactome.
GO; GO:0033088; P:negative regulation of immature T cell proliferation in thymus; IEA:Ensembl.
GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0007422; P:peripheral nervous system development; IEA:Ensembl.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; ISS:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:BHF-UCL.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; IMP:UniProtKB.
GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IDA:UniProtKB.
GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0045765; P:regulation of angiogenesis; NAS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0032886; P:regulation of microtubule-based process; IDA:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IDA:BHF-UCL.
GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 3.80.20.20; -; 3.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
Pfam; PF00757; Furin-like; 1.
Pfam; PF14843; GF_recep_IV; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00261; FU; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative initiation; Alternative splicing;
ATP-binding; Cell membrane; Chromosomal rearrangement;
Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein; Kinase;
Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Signal; Transcription;
Transcription regulation; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 1255 Receptor tyrosine-protein kinase erbB-2.
/FTId=PRO_0000016669.
TOPO_DOM 23 652 Extracellular. {ECO:0000255}.
TRANSMEM 653 675 Helical. {ECO:0000255}.
TOPO_DOM 676 1255 Cytoplasmic. {ECO:0000255}.
DOMAIN 720 987 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 726 734 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 676 689 Required for interaction with KPNB1 and
EEA1. {ECO:0000269|PubMed:16314522}.
REGION 1195 1197 Interaction with PIK3C2B. {ECO:0000305}.
MOTIF 676 689 Nuclear localization signal.
ACT_SITE 845 845 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 753 753 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1054 1054 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1078 1078 Phosphoserine.
{ECO:0000250|UniProtKB:P06494}.
MOD_RES 1083 1083 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1107 1107 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1112 1112 Phosphotyrosine.
{ECO:0000269|PubMed:27134172}.
MOD_RES 1139 1139 Phosphotyrosine.
{ECO:0000269|PubMed:27134172}.
MOD_RES 1151 1151 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1166 1166 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1196 1196 Phosphotyrosine.
{ECO:0000269|PubMed:27134172}.
MOD_RES 1248 1248 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:17081983,
ECO:0000269|PubMed:17554007,
ECO:0000269|PubMed:27134172}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3MZW,
ECO:0000269|PubMed:20696930}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3N85, ECO:0000255}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000269|PubMed:15093539,
ECO:0000269|PubMed:19299620,
ECO:0000269|PubMed:20696930}.
CARBOHYD 530 530 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1S78,
ECO:0000269|PubMed:15093539,
ECO:0000269|PubMed:19299620}.
CARBOHYD 571 571 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3MZW,
ECO:0000269|PubMed:20696930}.
CARBOHYD 629 629 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 26 53 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3H3B,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ,
ECO:0000244|PDB:4HRL,
ECO:0000244|PDB:4HRM}.
DISULFID 162 192 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3H3B,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ,
ECO:0000244|PDB:4HRL,
ECO:0000244|PDB:4HRM}.
DISULFID 195 204 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3H3B,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ,
ECO:0000244|PDB:4HRL,
ECO:0000244|PDB:4HRM}.
DISULFID 199 212 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3H3B,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ,
ECO:0000244|PDB:4HRL,
ECO:0000244|PDB:4HRM}.
DISULFID 220 227 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 224 235 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 236 244 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 240 252 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 255 264 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 268 295 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 299 311 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 315 331 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 334 338 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 342 367 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 475 504 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 511 520 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 515 528 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:2A91,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ}.
DISULFID 531 540 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ,
ECO:0000244|PDB:4HRN}.
DISULFID 544 560 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ,
ECO:0000244|PDB:4HRN}.
DISULFID 563 576 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ,
ECO:0000244|PDB:4HRN}.
DISULFID 567 584 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:3WLW,
ECO:0000244|PDB:3WSQ,
ECO:0000244|PDB:4HRN}.
DISULFID 587 596 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:1S78,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3MZW,
ECO:0000244|PDB:3N85,
ECO:0000244|PDB:4HRN}.
DISULFID 600 623 {ECO:0000244|PDB:1N8Z,
ECO:0000244|PDB:3BE1,
ECO:0000244|PDB:3N85}.
DISULFID 626 634 {ECO:0000244|PDB:3N85}.
DISULFID 630 642 {ECO:0000244|PDB:3N85}.
VAR_SEQ 1 686 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_039250.
VAR_SEQ 1 610 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_039249.
VAR_SEQ 1 30 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_054787.
VAR_SEQ 1 23 MELAALCRWGLLLALLPPGAAST -> MPRGSWKP (in
isoform 4). {ECO:0000303|Ref.4}.
/FTId=VSP_039248.
VAR_SEQ 633 648 Missing (in isoform 6).
{ECO:0000303|PubMed:24722188}.
/FTId=VSP_055902.
VAR_SEQ 771 883 AYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVR
ENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVL
VKSPNHVKITDFGLARLLDIDETEYHADGGK -> TISNLF
SNFAPRGPSACCEPTCWCHSGKGQDSLPREEWGRQRRFCLW
GCRGEPRVLDTPGRSCPSAPPSSCLQPSLRQPLLLGPGPTR
AGGSTQHLQRDTYGREPRVPGSGRASVNQKAKSAEALMCPQ
GAGKA (in isoform 6).
{ECO:0000303|PubMed:24722188}.
/FTId=VSP_055903.
VAR_SEQ 884 1255 Missing (in isoform 6).
{ECO:0000303|PubMed:24722188}.
/FTId=VSP_055904.
VARIANT 452 452 W -> C (in dbSNP:rs4252633).
{ECO:0000269|Ref.3}.
/FTId=VAR_016317.
VARIANT 654 654 I -> V (in allele B3; dbSNP:rs1801201).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8095488}.
/FTId=VAR_004077.
VARIANT 655 655 I -> V (in allele B2 and allele B3;
dbSNP:rs1136201).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8095488,
ECO:0000269|Ref.3}.
/FTId=VAR_004078.
VARIANT 755 755 L -> P (in LNCR; somatic mutation;
unknown pathological significance;
dbSNP:rs121913469).
{ECO:0000269|PubMed:15457249}.
/FTId=VAR_055432.
VARIANT 768 768 L -> S (in dbSNP:rs56366519).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042097.
VARIANT 774 774 M -> MAYVM (in LNCR; somatic mutation;
unknown pathological significance).
{ECO:0000269|PubMed:15457249}.
/FTId=VAR_055433.
VARIANT 776 776 G -> S (in GASC; somatic mutation;
unknown pathological significance;
dbSNP:rs28933369).
{ECO:0000269|PubMed:15457249,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_042098.
VARIANT 779 779 S -> SVGS (in LNCR; somatic mutation;
unknown pathological significance).
{ECO:0000269|PubMed:15457249}.
/FTId=VAR_055434.
VARIANT 857 857 N -> S (in OC; somatic mutation; unknown
pathological significance;
dbSNP:rs28933370).
{ECO:0000269|PubMed:15457249,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_042099.
VARIANT 914 914 E -> K (in GLM; somatic mutation; unknown
pathological significance;
dbSNP:rs28933368).
{ECO:0000269|PubMed:15457249}.
/FTId=VAR_055435.
VARIANT 1170 1170 P -> A (in dbSNP:rs61552325).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:2999974,
ECO:0000269|PubMed:8104414,
ECO:0000269|Ref.3}.
/FTId=VAR_016318.
VARIANT 1216 1216 A -> D (in dbSNP:rs55943169).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042100.
MUTAGEN 317 318 LH->AA: Reduces dimerization with ERBB3.
{ECO:0000269|PubMed:15093539}.
MUTAGEN 611 611 M->A: Prevents synthesis of isoform 2.
{ECO:0000269|PubMed:16794579}.
MUTAGEN 687 687 M->A: Prevents synthesis of isoform 3.
{ECO:0000269|PubMed:16794579}.
MUTAGEN 706 706 M->A: No effect on isoform production.
{ECO:0000269|PubMed:16794579}.
MUTAGEN 712 712 M->A: No effect on isoform production.
{ECO:0000269|PubMed:16794579}.
STRAND 25 27 {ECO:0000244|PDB:5MY6}.
HELIX 39 50 {ECO:0000244|PDB:5MY6}.
STRAND 55 64 {ECO:0000244|PDB:5MY6}.
HELIX 72 74 {ECO:0000244|PDB:5MY6}.
STRAND 79 82 {ECO:0000244|PDB:5MY6}.
STRAND 84 88 {ECO:0000244|PDB:5MY6}.
STRAND 92 95 {ECO:0000244|PDB:3H3B}.
TURN 109 111 {ECO:0000244|PDB:5MY6}.
STRAND 112 117 {ECO:0000244|PDB:5MY6}.
TURN 130 132 {ECO:0000244|PDB:3H3B}.
STRAND 139 141 {ECO:0000244|PDB:3H3B}.
STRAND 147 150 {ECO:0000244|PDB:2A91}.
STRAND 152 156 {ECO:0000244|PDB:5MY6}.
TURN 164 166 {ECO:0000244|PDB:3H3B}.
HELIX 169 172 {ECO:0000244|PDB:5MY6}.
HELIX 175 177 {ECO:0000244|PDB:1N8Z}.
STRAND 182 184 {ECO:0000244|PDB:3H3B}.
HELIX 200 202 {ECO:0000244|PDB:5MY6}.
STRAND 204 208 {ECO:0000244|PDB:5MY6}.
HELIX 209 211 {ECO:0000244|PDB:5MY6}.
STRAND 217 219 {ECO:0000244|PDB:1N8Z}.
HELIX 221 223 {ECO:0000244|PDB:5MY6}.
STRAND 227 231 {ECO:0000244|PDB:5MY6}.
HELIX 232 234 {ECO:0000244|PDB:5MY6}.
STRAND 240 248 {ECO:0000244|PDB:5MY6}.
STRAND 251 260 {ECO:0000244|PDB:5MY6}.
STRAND 263 267 {ECO:0000244|PDB:5MY6}.
STRAND 271 274 {ECO:0000244|PDB:5MY6}.
TURN 276 278 {ECO:0000244|PDB:5MY6}.
STRAND 281 283 {ECO:0000244|PDB:5MY6}.
STRAND 289 291 {ECO:0000244|PDB:5MY6}.
STRAND 294 298 {ECO:0000244|PDB:5MY6}.
STRAND 303 305 {ECO:0000244|PDB:1N8Z}.
STRAND 309 314 {ECO:0000244|PDB:5MY6}.
STRAND 319 323 {ECO:0000244|PDB:5MY6}.
STRAND 325 327 {ECO:0000244|PDB:3MZW}.
STRAND 329 333 {ECO:0000244|PDB:5MY6}.
STRAND 335 337 {ECO:0000244|PDB:2A91}.
HELIX 348 350 {ECO:0000244|PDB:5MY6}.
TURN 358 360 {ECO:0000244|PDB:5MY6}.
HELIX 361 364 {ECO:0000244|PDB:5MY6}.
STRAND 368 376 {ECO:0000244|PDB:5MY6}.
HELIX 378 382 {ECO:0000244|PDB:5MY6}.
HELIX 385 387 {ECO:0000244|PDB:5MY6}.
HELIX 394 400 {ECO:0000244|PDB:5MY6}.
STRAND 405 408 {ECO:0000244|PDB:5MY6}.
STRAND 410 413 {ECO:0000244|PDB:5MY6}.
HELIX 423 425 {ECO:0000244|PDB:5MY6}.
STRAND 430 435 {ECO:0000244|PDB:3WLW}.
TURN 438 440 {ECO:0000244|PDB:5MY6}.
STRAND 441 447 {ECO:0000244|PDB:5MY6}.
STRAND 463 469 {ECO:0000244|PDB:5MY6}.
TURN 477 479 {ECO:0000244|PDB:3WLW}.
HELIX 482 485 {ECO:0000244|PDB:5MY6}.
STRAND 486 488 {ECO:0000244|PDB:3N85}.
STRAND 493 499 {ECO:0000244|PDB:5MY6}.
HELIX 501 506 {ECO:0000244|PDB:5MY6}.
TURN 507 509 {ECO:0000244|PDB:3N85}.
HELIX 516 518 {ECO:0000244|PDB:5MY6}.
STRAND 520 524 {ECO:0000244|PDB:5MY6}.
STRAND 527 536 {ECO:0000244|PDB:5MY6}.
STRAND 539 542 {ECO:0000244|PDB:5MY6}.
STRAND 545 551 {ECO:0000244|PDB:5MY6}.
STRAND 553 562 {ECO:0000244|PDB:5MY6}.
STRAND 565 567 {ECO:0000244|PDB:3WSQ}.
STRAND 571 573 {ECO:0000244|PDB:5MY6}.
STRAND 576 580 {ECO:0000244|PDB:5MY6}.
STRAND 583 585 {ECO:0000244|PDB:5MY6}.
STRAND 587 590 {ECO:0000244|PDB:1S78}.
STRAND 595 599 {ECO:0000244|PDB:1N8Z}.
STRAND 602 604 {ECO:0000244|PDB:3N85}.
STRAND 615 617 {ECO:0000244|PDB:1N8Z}.
STRAND 621 625 {ECO:0000244|PDB:1N8Z}.
STRAND 628 632 {ECO:0000244|PDB:3N85}.
STRAND 635 637 {ECO:0000244|PDB:3N85}.
HELIX 651 678 {ECO:0000244|PDB:2JWA}.
HELIX 684 690 {ECO:0000244|PDB:2N2A}.
HELIX 691 697 {ECO:0000244|PDB:2N2A}.
HELIX 717 719 {ECO:0000244|PDB:3PP0}.
STRAND 720 728 {ECO:0000244|PDB:3PP0}.
STRAND 730 739 {ECO:0000244|PDB:3PP0}.
STRAND 748 755 {ECO:0000244|PDB:3PP0}.
HELIX 761 774 {ECO:0000244|PDB:3PP0}.
STRAND 785 799 {ECO:0000244|PDB:3PP0}.
HELIX 806 812 {ECO:0000244|PDB:3PP0}.
TURN 814 816 {ECO:0000244|PDB:3PP0}.
HELIX 819 838 {ECO:0000244|PDB:3PP0}.
HELIX 848 850 {ECO:0000244|PDB:3PP0}.
STRAND 851 855 {ECO:0000244|PDB:3PP0}.
STRAND 858 861 {ECO:0000244|PDB:3PP0}.
HELIX 886 888 {ECO:0000244|PDB:3PP0}.
HELIX 891 896 {ECO:0000244|PDB:3PP0}.
HELIX 901 916 {ECO:0000244|PDB:3PP0}.
TURN 922 925 {ECO:0000244|PDB:3PP0}.
HELIX 928 930 {ECO:0000244|PDB:3PP0}.
HELIX 931 936 {ECO:0000244|PDB:3PP0}.
HELIX 949 958 {ECO:0000244|PDB:3PP0}.
HELIX 963 965 {ECO:0000244|PDB:3PP0}.
HELIX 969 980 {ECO:0000244|PDB:3PP0}.
HELIX 983 986 {ECO:0000244|PDB:3PP0}.
HELIX 989 992 {ECO:0000244|PDB:3PP0}.
HELIX 1003 1007 {ECO:0000244|PDB:3PP0}.
STRAND 1140 1142 {ECO:0000244|PDB:1MW4}.
SEQUENCE 1255 AA; 137910 MW; 39E9DFDA04DCF962 CRC64;
MELAALCRWG LLLALLPPGA ASTQVCTGTD MKLRLPASPE THLDMLRHLY QGCQVVQGNL
ELTYLPTNAS LSFLQDIQEV QGYVLIAHNQ VRQVPLQRLR IVRGTQLFED NYALAVLDNG
DPLNNTTPVT GASPGGLREL QLRSLTEILK GGVLIQRNPQ LCYQDTILWK DIFHKNNQLA
LTLIDTNRSR ACHPCSPMCK GSRCWGESSE DCQSLTRTVC AGGCARCKGP LPTDCCHEQC
AAGCTGPKHS DCLACLHFNH SGICELHCPA LVTYNTDTFE SMPNPEGRYT FGASCVTACP
YNYLSTDVGS CTLVCPLHNQ EVTAEDGTQR CEKCSKPCAR VCYGLGMEHL REVRAVTSAN
IQEFAGCKKI FGSLAFLPES FDGDPASNTA PLQPEQLQVF ETLEEITGYL YISAWPDSLP
DLSVFQNLQV IRGRILHNGA YSLTLQGLGI SWLGLRSLRE LGSGLALIHH NTHLCFVHTV
PWDQLFRNPH QALLHTANRP EDECVGEGLA CHQLCARGHC WGPGPTQCVN CSQFLRGQEC
VEECRVLQGL PREYVNARHC LPCHPECQPQ NGSVTCFGPE ADQCVACAHY KDPPFCVARC
PSGVKPDLSY MPIWKFPDEE GACQPCPINC THSCVDLDDK GCPAEQRASP LTSIISAVVG
ILLVVVLGVV FGILIKRRQQ KIRKYTMRRL LQETELVEPL TPSGAMPNQA QMRILKETEL
RKVKVLGSGA FGTVYKGIWI PDGENVKIPV AIKVLRENTS PKANKEILDE AYVMAGVGSP
YVSRLLGICL TSTVQLVTQL MPYGCLLDHV RENRGRLGSQ DLLNWCMQIA KGMSYLEDVR
LVHRDLAARN VLVKSPNHVK ITDFGLARLL DIDETEYHAD GGKVPIKWMA LESILRRRFT
HQSDVWSYGV TVWELMTFGA KPYDGIPARE IPDLLEKGER LPQPPICTID VYMIMVKCWM
IDSECRPRFR ELVSEFSRMA RDPQRFVVIQ NEDLGPASPL DSTFYRSLLE DDDMGDLVDA
EEYLVPQQGF FCPDPAPGAG GMVHHRHRSS STRSGGGDLT LGLEPSEEEA PRSPLAPSEG
AGSDVFDGDL GMGAAKGLQS LPTHDPSPLQ RYSEDPTVPL PSETDGYVAP LTCSPQPEYV
NQPDVRPQPP SPREGPLPAA RPAGATLERP KTLSPGKNGV VKDVFAFGGA VENPEYLTPQ
GGAAPQPHPP PAFSPAFDNL YYWDQDPPER GAPPSTFKGT PTAENPEYLG LDVPV


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