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Receptor tyrosine-protein kinase erbB-3 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-3) (Tyrosine kinase-type cell surface receptor HER3)

 ERBB3_HUMAN             Reviewed;        1342 AA.
P21860; A8K6L6; B4DIK7; B4DV32; E9PDT8; Q9BUD7;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
20-DEC-2017, entry version 206.
RecName: Full=Receptor tyrosine-protein kinase erbB-3;
EC=2.7.10.1;
AltName: Full=Proto-oncogene-like protein c-ErbB-3;
AltName: Full=Tyrosine kinase-type cell surface receptor HER3;
Flags: Precursor;
Name=ERBB3; Synonyms=HER3;
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=2687875; DOI=10.1073/pnas.86.23.9193;
Kraus M.H., Issing W., Miki T., Popescu N.C., Aaronson S.A.;
"Isolation and characterization of ERBB3, a third member of the
ERBB/epidermal growth factor receptor family: evidence for
overexpression in a subset of human mammary tumors.";
Proc. Natl. Acad. Sci. U.S.A. 86:9193-9197(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2164210; DOI=10.1073/pnas.87.13.4905;
Plowman G.D., Whitney G.S., Neubauer M.G., Green J.M., McDonald V.L.,
Todaro G.J., Shoyab M.;
"Molecular cloning and expression of an additional epidermal growth
factor receptor-related gene.";
Proc. Natl. Acad. Sci. U.S.A. 87:4905-4909(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=7685162; DOI=10.1006/bbrc.1993.1542;
Katoh M., Yazaki Y., Sugimura T., Terada M.;
"c-erbB3 gene encodes secreted as well as transmembrane receptor
tyrosine kinase.";
Biochem. Biophys. Res. Commun. 192:1189-1197(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
TISSUE=Hippocampus, Placenta, and Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Skin;
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).
[8]
INTERACTION WITH GRB7.
PubMed=9516479; DOI=10.1074/jbc.273.13.7717;
Fiddes R.J., Campbell D.H., Janes P.W., Sivertsen S.P., Sasaki H.,
Wallasch C., Daly R.J.;
"Analysis of Grb7 recruitment by heregulin-activated erbB receptors
reveals a novel target selectivity for erbB3.";
J. Biol. Chem. 273:7717-7724(1998).
[9]
INTERACTION WITH PA2G4.
PubMed=11325528; DOI=10.1016/S0303-7207(01)00387-2;
Lessor T.J., Hamburger A.W.;
"Regulation of the ErbB3 binding protein Ebp1 by protein kinase C.";
Mol. Cell. Endocrinol. 175:185-191(2001).
[10]
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).
[11]
INTERACTION WITH CSPG5, AND FUNCTION.
PubMed=15358134; DOI=10.1016/j.bbrc.2004.07.066;
Kinugasa Y., Ishiguro H., Tokita Y., Oohira A., Ohmoto H.,
Higashiyama S.;
"Neuroglycan C, a novel member of the neuregulin family.";
Biochem. Biophys. Res. Commun. 321:1045-1049(2004).
[12]
INTERACTION WITH PA2G4.
PubMed=16832058; DOI=10.1073/pnas.0602923103;
Liu Z., Ahn J.Y., Liu X., Ye K.;
"Ebp1 isoforms distinctively regulate cell survival and
differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 103:10917-10922(2006).
[13]
INVOLVEMENT IN LCCS2.
PubMed=17701904; DOI=10.1086/520770;
Narkis G., Ofir R., Manor E., Landau D., Elbedour K., Birk O.S.;
"Lethal congenital contractural syndrome type 2 (LCCS2) is caused by a
mutation in ERBB3 (Her3), a modulator of the phosphatidylinositol-3-
kinase/Akt pathway.";
Am. J. Hum. Genet. 81:589-595(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[15]
FUNCTION, BINDING TO NRG1, IDENTIFICATION IN A COMPLEX WITH NRG1 AND
INTEGRINS, AND PHOSPHORYLATION.
PubMed=20682778; DOI=10.1074/jbc.M110.113878;
Ieguchi K., Fujita M., Ma Z., Davari P., Taniguchi Y., Sekiguchi K.,
Wang B., Takada Y.K., Takada Y.;
"Direct binding of the EGF-like domain of neuregulin-1 to integrins
({alpha}v{beta}3 and {alpha}6{beta}4) is involved in neuregulin-1/ErbB
signaling.";
J. Biol. Chem. 285:31388-31398(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-982, 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).
[18]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 20-640, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-250; ASN-353; ASN-408; ASN-414; ASN-437; ASN-469;
ASN-522 AND ASN-566.
PubMed=12154198; DOI=10.1126/science.1074611;
Cho H.S., Leahy D.J.;
"Structure of the extracellular region of HER3 reveals an interdomain
tether.";
Science 297:1330-1333(2002).
[19]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 698-1019 IN COMPLEX WITH
AMP-PNP, AND SUBUNIT.
PubMed=20007378; DOI=10.1073/pnas.0912101106;
Jura N., Shan Y., Cao X., Shaw D.E., Kuriyan J.;
"Structural analysis of the catalytically inactive kinase domain of
the human EGF receptor 3.";
Proc. Natl. Acad. Sci. U.S.A. 106:21608-21613(2009).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 684-1020 IN COMPLEX WITH
AMP-PNP, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-742 AND TYR-868,
AUTOPHOSPHORYLATION, AND SUBUNIT.
PubMed=20351256; DOI=10.1073/pnas.1002753107;
Shi F., Telesco S.E., Liu Y., Radhakrishnan R., Lemmon M.A.;
"ErbB3/HER3 intracellular domain is competent to bind ATP and catalyze
autophosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 107:7692-7697(2010).
[21]
STRUCTURE BY NMR OF 640-670, AND SUBUNIT.
PubMed=21575594; DOI=10.1016/j.bbamem.2011.04.017;
Mineev K.S., Khabibullina N.F., Lyukmanova E.N., Dolgikh D.A.,
Kirpichnikov M.P., Arseniev A.S.;
"Spatial structure and dimer-monomer equilibrium of the ErbB3
transmembrane domain in DPC micelles.";
Biochim. Biophys. Acta 1808:2081-2088(2011).
[22]
VARIANTS [LARGE SCALE ANALYSIS] TYR-20; LEU-30; MET-104; ILE-204;
TRP-683; LEU-717; THR-744; ARG-998; CYS-1119; HIS-1127; ILE-1177 AND
LYS-1254.
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: Tyrosine-protein kinase that plays an essential role as
cell surface receptor for neuregulins. Binds to neuregulin-1
(NRG1) and is activated by it; ligand-binding increases
phosphorylation on tyrosine residues and promotes its association
with the p85 subunit of phosphatidylinositol 3-kinase
(PubMed:20682778). May also be activated by CSPG5
(PubMed:15358134). {ECO:0000269|PubMed:15358134,
ECO:0000269|PubMed:20682778}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000269|PubMed:20351256}.
-!- SUBUNIT: Monomer and homodimer. Heterodimer with each of the other
ERBB receptors (Potential). Interacts with CSPG5
(PubMed:15358134). Interacts with GRB7 (PubMed:9516479). Interacts
with MUC1 (PubMed:12939402). Interacts with MYOC (By similarity).
Interacts with isoform 2 of PA2G4 (PubMed:11325528,
PubMed:16832058). Found in a ternary complex with NRG1 and
ITGAV:ITGB3 or ITGA6:ITGB4 (PubMed:20682778).
{ECO:0000250|UniProtKB:Q61526, ECO:0000269|PubMed:11325528,
ECO:0000269|PubMed:12939402, ECO:0000269|PubMed:15358134,
ECO:0000269|PubMed:16832058, ECO:0000269|PubMed:20682778,
ECO:0000269|PubMed:9516479, ECO:0000305}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-720706, EBI-720706;
P42684:ABL2; NbExp=10; IntAct=EBI-720706, EBI-1102694;
P46108:CRK; NbExp=2; IntAct=EBI-720706, EBI-886;
P46109:CRKL; NbExp=3; IntAct=EBI-720706, EBI-910;
P00533:EGFR; NbExp=13; IntAct=EBI-720706, EBI-297353;
P04626:ERBB2; NbExp=29; IntAct=EBI-720706, EBI-641062;
Q15303:ERBB4; NbExp=4; IntAct=EBI-720706, EBI-80371;
P62993:GRB2; NbExp=3; IntAct=EBI-720706, EBI-401755;
Q14451:GRB7; NbExp=7; IntAct=EBI-720706, EBI-970191;
P08631:HCK; NbExp=2; IntAct=EBI-720706, EBI-346340;
P08238:HSP90AB1; NbExp=3; IntAct=EBI-720706, EBI-352572;
O43639:NCK2; NbExp=2; IntAct=EBI-720706, EBI-713635;
Q02297-7:NRG1; NbExp=3; IntAct=EBI-720706, EBI-2460927;
P42336:PIK3CA; NbExp=3; IntAct=EBI-720706, EBI-2116585;
P27986:PIK3R1; NbExp=41; IntAct=EBI-720706, EBI-79464;
O00459:PIK3R2; NbExp=16; IntAct=EBI-720706, EBI-346930;
Q92569:PIK3R3; NbExp=22; IntAct=EBI-720706, EBI-79893;
P19174:PLCG1; NbExp=4; IntAct=EBI-720706, EBI-79387;
P20936:RASA1; NbExp=6; IntAct=EBI-720706, EBI-1026476;
Q9UQQ2:SH2B3; NbExp=2; IntAct=EBI-720706, EBI-7879749;
P29353:SHC1; NbExp=5; IntAct=EBI-720706, EBI-78835;
Q92529:SHC3; NbExp=2; IntAct=EBI-720706, EBI-79084;
P12931:SRC; NbExp=2; IntAct=EBI-720706, EBI-621482;
P43405:SYK; NbExp=6; IntAct=EBI-720706, EBI-78302;
Q63HR2:TNS2; NbExp=3; IntAct=EBI-720706, EBI-949753;
Q68CZ2:TNS3; NbExp=2; IntAct=EBI-720706, EBI-1220488;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=long form;
IsoId=P21860-1; Sequence=Displayed;
Name=2; Synonyms=short form;
IsoId=P21860-2; Sequence=VSP_002893, VSP_002894;
Name=3;
IsoId=P21860-3; Sequence=VSP_041663, VSP_041664;
Name=4;
IsoId=P21860-4; Sequence=VSP_041662;
Name=5;
IsoId=P21860-5; Sequence=VSP_041661;
-!- TISSUE SPECIFICITY: Epithelial tissues and brain.
-!- DEVELOPMENTAL STAGE: Overexpressed in a subset of human mammary
tumors.
-!- DOMAIN: The cytoplasmic part of the receptor may interact with the
SH2 or SH3 domains of many signal-transducing proteins.
-!- PTM: Autophosphorylated (PubMed:20351256). Ligand-binding
increases phosphorylation on tyrosine residues and promotes its
association with the p85 subunit of phosphatidylinositol 3-kinase
(PubMed:20682778). {ECO:0000269|PubMed:20351256,
ECO:0000269|PubMed:20682778}.
-!- DISEASE: Lethal congenital contracture syndrome 2 (LCCS2)
[MIM:607598]: A form of lethal congenital contracture syndrome, an
autosomal recessive disorder characterized by degeneration of
anterior horn neurons, extreme skeletal muscle atrophy, and
congenital non-progressive joint contractures (arthrogryposis).
The contractures can involve the upper or lower limbs and/or the
vertebral column, leading to various degrees of flexion or
extension limitations evident at birth. LCCS2 patients manifest
craniofacial/ocular findings, lack of hydrops, multiple pterygia,
and fractures, as well as a normal duration of pregnancy and a
unique feature of a markedly distended urinary bladder (neurogenic
bladder defect). The phenotype suggests a spinal cord neuropathic
etiology. {ECO:0000269|PubMed:17701904}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- 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/ERBB3ID40479ch12q13.html";
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EMBL; M29366; AAA35790.1; -; mRNA.
EMBL; M34309; AAA35979.1; -; mRNA.
EMBL; S61953; AAB26935.1; -; mRNA.
EMBL; BT007226; AAP35890.1; -; mRNA.
EMBL; AK291681; BAF84370.1; -; mRNA.
EMBL; AK295650; BAG58519.1; -; mRNA.
EMBL; AK300909; BAG62544.1; -; mRNA.
EMBL; AC034102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002706; AAH02706.1; -; mRNA.
EMBL; BC082992; AAH82992.1; -; mRNA.
CCDS; CCDS31833.1; -. [P21860-1]
CCDS; CCDS44918.1; -. [P21860-2]
PIR; A36223; A36223.
PIR; JH0803; JH0803.
RefSeq; NP_001005915.1; NM_001005915.1. [P21860-2]
RefSeq; NP_001973.2; NM_001982.3. [P21860-1]
UniGene; Hs.118681; -.
UniGene; Hs.622058; -.
PDB; 1M6B; X-ray; 2.60 A; A/B=20-640.
PDB; 2L9U; NMR; -; A/B=639-670.
PDB; 3KEX; X-ray; 2.80 A; A/B=698-1019.
PDB; 3LMG; X-ray; 2.80 A; A/B=684-1020.
PDB; 3P11; X-ray; 3.70 A; A=20-532.
PDB; 4LEO; X-ray; 2.64 A; C=20-631.
PDB; 4OTW; X-ray; 2.51 A; A=698-1020.
PDB; 4P59; X-ray; 3.40 A; A=20-640.
PDB; 4RIW; X-ray; 3.10 A; A/C=698-1020.
PDB; 4RIX; X-ray; 3.10 A; A/C=698-1020.
PDB; 4RIY; X-ray; 2.98 A; A/C=698-1020.
PDB; 5CUS; X-ray; 3.20 A; A/B/C/D=20-641.
PDBsum; 1M6B; -.
PDBsum; 2L9U; -.
PDBsum; 3KEX; -.
PDBsum; 3LMG; -.
PDBsum; 3P11; -.
PDBsum; 4LEO; -.
PDBsum; 4OTW; -.
PDBsum; 4P59; -.
PDBsum; 4RIW; -.
PDBsum; 4RIX; -.
PDBsum; 4RIY; -.
PDBsum; 5CUS; -.
ProteinModelPortal; P21860; -.
SMR; P21860; -.
BioGrid; 108377; 185.
CORUM; P21860; -.
DIP; DIP-36441N; -.
ELM; P21860; -.
IntAct; P21860; 94.
MINT; MINT-158484; -.
STRING; 9606.ENSP00000267101; -.
BindingDB; P21860; -.
ChEMBL; CHEMBL5838; -.
GuidetoPHARMACOLOGY; 1798; -.
iPTMnet; P21860; -.
PhosphoSitePlus; P21860; -.
BioMuta; ERBB3; -.
DMDM; 119534; -.
MaxQB; P21860; -.
PaxDb; P21860; -.
PeptideAtlas; P21860; -.
PRIDE; P21860; -.
DNASU; 2065; -.
Ensembl; ENST00000267101; ENSP00000267101; ENSG00000065361. [P21860-1]
Ensembl; ENST00000411731; ENSP00000415753; ENSG00000065361. [P21860-2]
Ensembl; ENST00000415288; ENSP00000408340; ENSG00000065361. [P21860-4]
Ensembl; ENST00000551242; ENSP00000447510; ENSG00000065361. [P21860-3]
GeneID; 2065; -.
KEGG; hsa:2065; -.
UCSC; uc001sjg.4; human. [P21860-1]
CTD; 2065; -.
DisGeNET; 2065; -.
EuPathDB; HostDB:ENSG00000065361.14; -.
GeneCards; ERBB3; -.
HGNC; HGNC:3431; ERBB3.
HPA; CAB025331; -.
HPA; HPA045396; -.
MalaCards; ERBB3; -.
MIM; 190151; gene.
MIM; 607598; phenotype.
neXtProt; NX_P21860; -.
OpenTargets; ENSG00000065361; -.
Orphanet; 137776; Lethal congenital contracture syndrome type 2.
PharmGKB; PA27846; -.
eggNOG; KOG1025; Eukaryota.
eggNOG; ENOG410XNSR; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000230982; -.
HOVERGEN; HBG000490; -.
InParanoid; P21860; -.
KO; K05084; -.
OMA; CYHHSLN; -.
OrthoDB; EOG091G00IX; -.
PhylomeDB; P21860; -.
TreeFam; TF106002; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-1236394; Signaling by ERBB4.
Reactome; R-HSA-1250196; SHC1 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-1963642; PI3K events in ERBB2 signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
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.
SignaLink; P21860; -.
SIGNOR; P21860; -.
ChiTaRS; ERBB3; human.
EvolutionaryTrace; P21860; -.
GeneWiki; ERBB3; -.
GenomeRNAi; 2065; -.
PRO; PR:P21860; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000065361; -.
CleanEx; HS_ERBB3; -.
ExpressionAtlas; P21860; baseline and differential.
Genevisible; P21860; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:BHF-UCL.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0038132; F:neuregulin binding; IDA:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; NAS:BHF-UCL.
GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:BHF-UCL.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:CAFA.
GO; GO:0021545; P:cranial nerve development; ISS:BHF-UCL.
GO; GO:0003197; P:endocardial cushion development; IEA:Ensembl.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0007162; P:negative regulation of cell adhesion; IDA:BHF-UCL.
GO; GO:1901185; P:negative regulation of ERBB signaling pathway; TAS:Reactome.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:BHF-UCL.
GO; GO:0051048; P:negative regulation of secretion; IDA:BHF-UCL.
GO; GO:0009968; P:negative regulation of signal transduction; IDA:BHF-UCL.
GO; GO:0051402; P:neuron apoptotic process; IMP:BHF-UCL.
GO; GO:0007422; P:peripheral nervous system development; ISS:BHF-UCL.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IEA:Ensembl.
GO; GO:0055025; P:positive regulation of cardiac muscle tissue development; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; TAS:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IMP:BHF-UCL.
GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
GO; GO:0042127; P:regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0014037; P:Schwann cell differentiation; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISS:BHF-UCL.
GO; GO:0042060; P:wound healing; NAS:BHF-UCL.
Gene3D; 3.80.20.20; -; 3.
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; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/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; 5.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Secreted; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1342 Receptor tyrosine-protein kinase erbB-3.
/FTId=PRO_0000016672.
TOPO_DOM 20 643 Extracellular. {ECO:0000255}.
TRANSMEM 644 664 Helical. {ECO:0000255}.
TOPO_DOM 665 1342 Cytoplasmic. {ECO:0000255}.
DOMAIN 709 966 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 715 723 ATP.
NP_BIND 788 790 ATP.
NP_BIND 834 839 ATP.
ACT_SITE 834 834 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 742 742 ATP.
MOD_RES 686 686 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 982 982 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12154198}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12154198}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12154198}.
CARBOHYD 414 414 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12154198}.
CARBOHYD 437 437 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12154198}.
CARBOHYD 469 469 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12154198}.
CARBOHYD 522 522 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12154198}.
CARBOHYD 566 566 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12154198}.
CARBOHYD 616 616 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 29 56 {ECO:0000269|PubMed:12154198}.
DISULFID 156 183 {ECO:0000269|PubMed:12154198}.
DISULFID 186 194 {ECO:0000269|PubMed:12154198}.
DISULFID 190 202 {ECO:0000269|PubMed:12154198}.
DISULFID 210 218 {ECO:0000269|PubMed:12154198}.
DISULFID 214 226 {ECO:0000269|PubMed:12154198}.
DISULFID 227 235 {ECO:0000269|PubMed:12154198}.
DISULFID 231 243 {ECO:0000269|PubMed:12154198}.
DISULFID 246 255 {ECO:0000269|PubMed:12154198}.
DISULFID 259 286 {ECO:0000269|PubMed:12154198}.
DISULFID 290 301 {ECO:0000269|PubMed:12154198}.
DISULFID 305 320 {ECO:0000269|PubMed:12154198}.
DISULFID 323 327 {ECO:0000269|PubMed:12154198}.
DISULFID 500 509 {ECO:0000269|PubMed:12154198}.
DISULFID 504 517 {ECO:0000269|PubMed:12154198}.
DISULFID 520 529 {ECO:0000269|PubMed:12154198}.
DISULFID 533 549 {ECO:0000269|PubMed:12154198}.
DISULFID 552 565 {ECO:0000269|PubMed:12154198}.
DISULFID 556 573 {ECO:0000269|PubMed:12154198}.
DISULFID 576 585 {ECO:0000269|PubMed:12154198}.
DISULFID 589 610 {ECO:0000250}.
DISULFID 613 621 {ECO:0000250}.
DISULFID 617 629 {ECO:0000250}.
VAR_SEQ 1 643 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041661.
VAR_SEQ 1 59 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041662.
VAR_SEQ 141 183 EILSGGVYIEKNDKLCHMDTIDWRDIVRDRDAEIVVKDNGR
SC -> GQFPMVPSGLTPQPAQDWYLLDDDPRLLTLSASSK
VPVTLAAV (in isoform 2).
{ECO:0000303|PubMed:7685162}.
/FTId=VSP_002893.
VAR_SEQ 184 1342 Missing (in isoform 2).
{ECO:0000303|PubMed:7685162}.
/FTId=VSP_002894.
VAR_SEQ 331 331 C -> F (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_041663.
VAR_SEQ 332 1342 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_041664.
VARIANT 20 20 S -> Y (in dbSNP:rs34379766).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042101.
VARIANT 30 30 P -> L (in dbSNP:rs56017157).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042102.
VARIANT 104 104 V -> M (in an ovarian mucinous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042103.
VARIANT 204 204 T -> I (in dbSNP:rs56107455).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042104.
VARIANT 385 385 N -> S (in dbSNP:rs12320176).
/FTId=VAR_049710.
VARIANT 683 683 R -> W (in dbSNP:rs56387488).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042105.
VARIANT 717 717 S -> L (in dbSNP:rs35961836).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042106.
VARIANT 744 744 I -> T (in dbSNP:rs55787439).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042107.
VARIANT 998 998 K -> R (in dbSNP:rs56259600).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042108.
VARIANT 1119 1119 S -> C (in dbSNP:rs773123).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042109.
VARIANT 1127 1127 R -> H (in dbSNP:rs2271188).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042110.
VARIANT 1177 1177 L -> I (in dbSNP:rs55699040).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042111.
VARIANT 1254 1254 T -> K (in dbSNP:rs55709407).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042112.
VARIANT 1271 1271 G -> S (in dbSNP:rs11171743).
/FTId=VAR_049711.
MUTAGEN 742 742 K->M: Strongly reduced
autophosphorylation.
{ECO:0000269|PubMed:20351256}.
MUTAGEN 868 868 Y->E: Strongly reduced tyrosine
phosphorylation.
{ECO:0000269|PubMed:20351256}.
CONFLICT 560 560 E -> G (in Ref. 2; AAA35979).
{ECO:0000305}.
CONFLICT 684 684 G -> S (in Ref. 5; BAF84370).
{ECO:0000305}.
CONFLICT 1064 1064 E -> G (in Ref. 2; AAA35979).
{ECO:0000305}.
CONFLICT 1078 1078 C -> S (in Ref. 5; BAG62544).
{ECO:0000305}.
CONFLICT 1163 1163 D -> G (in Ref. 5; BAF84370).
{ECO:0000305}.
STRAND 28 30 {ECO:0000244|PDB:4LEO}.
HELIX 43 53 {ECO:0000244|PDB:4LEO}.
STRAND 58 61 {ECO:0000244|PDB:1M6B}.
STRAND 63 67 {ECO:0000244|PDB:1M6B}.
HELIX 75 79 {ECO:0000244|PDB:1M6B}.
STRAND 82 85 {ECO:0000244|PDB:1M6B}.
STRAND 87 91 {ECO:0000244|PDB:1M6B}.
STRAND 95 98 {ECO:0000244|PDB:1M6B}.
TURN 112 114 {ECO:0000244|PDB:1M6B}.
STRAND 115 120 {ECO:0000244|PDB:1M6B}.
STRAND 125 128 {ECO:0000244|PDB:4LEO}.
STRAND 133 135 {ECO:0000244|PDB:1M6B}.
STRAND 141 144 {ECO:0000244|PDB:5CUS}.
STRAND 146 150 {ECO:0000244|PDB:1M6B}.
TURN 158 160 {ECO:0000244|PDB:1M6B}.
HELIX 163 166 {ECO:0000244|PDB:1M6B}.
STRAND 174 178 {ECO:0000244|PDB:1M6B}.
HELIX 188 190 {ECO:0000244|PDB:4LEO}.
STRAND 194 198 {ECO:0000244|PDB:1M6B}.
STRAND 214 216 {ECO:0000244|PDB:1M6B}.
STRAND 218 222 {ECO:0000244|PDB:1M6B}.
HELIX 223 225 {ECO:0000244|PDB:5CUS}.
STRAND 231 233 {ECO:0000244|PDB:1M6B}.
STRAND 235 239 {ECO:0000244|PDB:1M6B}.
HELIX 240 242 {ECO:0000244|PDB:1M6B}.
STRAND 243 251 {ECO:0000244|PDB:1M6B}.
STRAND 254 258 {ECO:0000244|PDB:1M6B}.
STRAND 262 265 {ECO:0000244|PDB:1M6B}.
TURN 267 269 {ECO:0000244|PDB:1M6B}.
STRAND 270 274 {ECO:0000244|PDB:1M6B}.
STRAND 280 282 {ECO:0000244|PDB:1M6B}.
STRAND 285 289 {ECO:0000244|PDB:1M6B}.
STRAND 295 297 {ECO:0000244|PDB:1M6B}.
STRAND 300 304 {ECO:0000244|PDB:1M6B}.
STRAND 309 314 {ECO:0000244|PDB:1M6B}.
STRAND 317 322 {ECO:0000244|PDB:1M6B}.
STRAND 324 326 {ECO:0000244|PDB:4LEO}.
STRAND 330 332 {ECO:0000244|PDB:1M6B}.
STRAND 338 342 {ECO:0000244|PDB:5CUS}.
TURN 345 347 {ECO:0000244|PDB:1M6B}.
HELIX 348 351 {ECO:0000244|PDB:1M6B}.
STRAND 356 363 {ECO:0000244|PDB:1M6B}.
HELIX 365 369 {ECO:0000244|PDB:1M6B}.
TURN 372 375 {ECO:0000244|PDB:1M6B}.
HELIX 381 389 {ECO:0000244|PDB:1M6B}.
STRAND 392 395 {ECO:0000244|PDB:1M6B}.
STRAND 397 400 {ECO:0000244|PDB:1M6B}.
HELIX 410 412 {ECO:0000244|PDB:1M6B}.
STRAND 425 433 {ECO:0000244|PDB:1M6B}.
STRAND 451 457 {ECO:0000244|PDB:1M6B}.
HELIX 465 467 {ECO:0000244|PDB:4LEO}.
HELIX 470 473 {ECO:0000244|PDB:1M6B}.
STRAND 482 488 {ECO:0000244|PDB:1M6B}.
HELIX 490 493 {ECO:0000244|PDB:1M6B}.
TURN 494 497 {ECO:0000244|PDB:1M6B}.
STRAND 509 513 {ECO:0000244|PDB:1M6B}.
HELIX 514 516 {ECO:0000244|PDB:1M6B}.
STRAND 517 527 {ECO:0000244|PDB:1M6B}.
STRAND 529 531 {ECO:0000244|PDB:1M6B}.
STRAND 534 536 {ECO:0000244|PDB:1M6B}.
STRAND 538 540 {ECO:0000244|PDB:1M6B}.
STRAND 542 545 {ECO:0000244|PDB:1M6B}.
STRAND 548 551 {ECO:0000244|PDB:1M6B}.
STRAND 560 562 {ECO:0000244|PDB:5CUS}.
STRAND 564 570 {ECO:0000244|PDB:1M6B}.
STRAND 573 581 {ECO:0000244|PDB:1M6B}.
STRAND 584 588 {ECO:0000244|PDB:1M6B}.
STRAND 591 594 {ECO:0000244|PDB:4LEO}.
STRAND 600 604 {ECO:0000244|PDB:1M6B}.
STRAND 608 612 {ECO:0000244|PDB:1M6B}.
STRAND 622 625 {ECO:0000244|PDB:1M6B}.
HELIX 626 628 {ECO:0000244|PDB:4LEO}.
HELIX 641 670 {ECO:0000244|PDB:2L9U}.
HELIX 706 708 {ECO:0000244|PDB:4OTW}.
STRAND 709 716 {ECO:0000244|PDB:4OTW}.
STRAND 722 728 {ECO:0000244|PDB:4OTW}.
STRAND 731 733 {ECO:0000244|PDB:3LMG}.
STRAND 737 744 {ECO:0000244|PDB:4OTW}.
TURN 747 749 {ECO:0000244|PDB:4OTW}.
STRAND 753 755 {ECO:0000244|PDB:4RIY}.
HELIX 758 764 {ECO:0000244|PDB:4OTW}.
STRAND 774 778 {ECO:0000244|PDB:4OTW}.
STRAND 780 788 {ECO:0000244|PDB:4OTW}.
HELIX 795 802 {ECO:0000244|PDB:4OTW}.
HELIX 803 805 {ECO:0000244|PDB:4OTW}.
HELIX 808 827 {ECO:0000244|PDB:4OTW}.
HELIX 837 839 {ECO:0000244|PDB:4OTW}.
STRAND 840 846 {ECO:0000244|PDB:4OTW}.
STRAND 848 850 {ECO:0000244|PDB:4OTW}.
HELIX 855 858 {ECO:0000244|PDB:4OTW}.
HELIX 865 868 {ECO:0000244|PDB:4RIY}.
TURN 870 872 {ECO:0000244|PDB:4RIY}.
HELIX 875 877 {ECO:0000244|PDB:4OTW}.
HELIX 880 885 {ECO:0000244|PDB:4OTW}.
HELIX 890 905 {ECO:0000244|PDB:4OTW}.
TURN 911 914 {ECO:0000244|PDB:4OTW}.
HELIX 917 919 {ECO:0000244|PDB:4OTW}.
HELIX 920 925 {ECO:0000244|PDB:4OTW}.
HELIX 938 947 {ECO:0000244|PDB:4OTW}.
TURN 952 954 {ECO:0000244|PDB:4OTW}.
HELIX 958 968 {ECO:0000244|PDB:4OTW}.
HELIX 972 975 {ECO:0000244|PDB:4OTW}.
STRAND 980 983 {ECO:0000244|PDB:3KEX}.
SEQUENCE 1342 AA; 148098 MW; 7201E7F66CA374BD CRC64;
MRANDALQVL GLLFSLARGS EVGNSQAVCP GTLNGLSVTG DAENQYQTLY KLYERCEVVM
GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSTLPLP NLRVVRGTQV YDGKFAIFVM
LNYNTNSSHA LRQLRLTQLT EILSGGVYIE KNDKLCHMDT IDWRDIVRDR DAEIVVKDNG
RSCPPCHEVC KGRCWGPGSE DCQTLTKTIC APQCNGHCFG PNPNQCCHDE CAGGCSGPQD
TDCFACRHFN DSGACVPRCP QPLVYNKLTF QLEPNPHTKY QYGGVCVASC PHNFVVDQTS
CVRACPPDKM EVDKNGLKMC EPCGGLCPKA CEGTGSGSRF QTVDSSNIDG FVNCTKILGN
LDFLITGLNG DPWHKIPALD PEKLNVFRTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG
RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRIYISANR QLCYHHSLNW TKVLRGPTEE
RLDIKHNRPR RDCVAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSRGGVCV THCNFLNGEP
REFAHEAECF SCHPECQPME GTATCNGSGS DTCAQCAHFR DGPHCVSSCP HGVLGAKGPI
YKYPDVQNEC RPCHENCTQG CKGPELQDCL GQTLVLIGKT HLTMALTVIA GLVVIFMMLG
GTFLYWRGRR IQNKRAMRRY LERGESIEPL DPSEKANKVL ARIFKETELR KLKVLGSGVF
GTVHKGVWIP EGESIKIPVC IKVIEDKSGR QSFQAVTDHM LAIGSLDHAH IVRLLGLCPG
SSLQLVTQYL PLGSLLDHVR QHRGALGPQL LLNWGVQIAK GMYYLEEHGM VHRNLAARNV
LLKSPSQVQV ADFGVADLLP PDDKQLLYSE AKTPIKWMAL ESIHFGKYTH QSDVWSYGVT
VWELMTFGAE PYAGLRLAEV PDLLEKGERL AQPQICTIDV YMVMVKCWMI DENIRPTFKE
LANEFTRMAR DPPRYLVIKR ESGPGIAPGP EPHGLTNKKL EEVELEPELD LDLDLEAEED
NLATTTLGSA LSLPVGTLNR PRGSQSLLSP SSGYMPMNQG NLGESCQESA VSGSSERCPR
PVSLHPMPRG CLASESSEGH VTGSEAELQE KVSMCRSRSR SRSPRPRGDS AYHSQRHSLL
TPVTPLSPPG LEEEDVNGYV MPDTHLKGTP SSREGTLSSV GLSSVLGTEE EDEDEEYEYM
NRRRRHSPPH PPRPSSLEEL GYEYMDVGSD LSASLGSTQS CPLHPVPIMP TAGTTPDEDY
EYMNRQRDGG GPGGDYAAMG ACPASEQGYE EMRAFQGPGH QAPHVHYARL KTLRSLEATD
SAFDNPDYWH SRLFPKANAQ RT


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