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Integrin beta-3 (Platelet membrane glycoprotein IIIa) (GPIIIa) (CD antigen CD61)

 ITB3_HUMAN              Reviewed;         788 AA.
P05106; A0PJW2; D3DXJ8; O15495; Q12806; Q13413; Q14648; Q16499;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 2.
22-NOV-2017, entry version 242.
RecName: Full=Integrin beta-3;
AltName: Full=Platelet membrane glycoprotein IIIa;
Short=GPIIIa;
AltName: CD_antigen=CD61;
Flags: Precursor;
Name=ITGB3; Synonyms=GP3A;
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 BETA-3A).
PubMed=3494014;
Fitzgerald L.A., Steiner B., Rall S.C. Jr., Lo S., Phillips D.R.;
"Protein sequence of endothelial glycoprotein IIIa derived from a cDNA
clone. Identity with platelet glycoprotein IIIa and similarity to
'integrin'.";
J. Biol. Chem. 262:3936-3939(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A).
PubMed=2452834; DOI=10.1172/JCI113478;
Zimrin A.B., Eisman R., Vilaire G., Schwartz E., Bennett J.S.,
Poncz M.;
"Structure of platelet glycoprotein IIIa. A common subunit for two
different membrane receptors.";
J. Clin. Invest. 81:1470-1475(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A).
PubMed=2345548; DOI=10.1007/BF00422712;
Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H.,
Marguerie G.;
"GPIIb and GPIIIa amino acid sequences deduced from human
megakaryocyte cDNAs.";
Mol. Biol. Rep. 14:27-33(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3C), FUNCTION, AND
SUBCELLULAR LOCATION.
TISSUE=Osteoclastoma;
PubMed=9195946; DOI=10.1074/jbc.272.26.16390;
Kumar C.S., James I.E., Wong A., Mwangi V., Feild J.A.,
Nuthulaganti P., Connor J.R., Eichman C., Ali F., Hwang S.M.,
Rieman D.J., Drake F.H., Gowen M.;
"Cloning and characterization of a novel integrin beta3 subunit.";
J. Biol. Chem. 272:16390-16397(1997).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-3A).
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 1-26.
TISSUE=Blood;
PubMed=8298129;
Villa-Garcia M., Li L., Riely G., Bray P.F.;
"Isolation and characterization of a TATA-less promoter for the human
beta 3 integrin gene.";
Blood 83:668-676(1994).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-788.
TISSUE=Erythroleukemia;
PubMed=3165296;
Rosa J.P., Bray P.F., Gayet O., Johnston G.I., Cook R.G.,
Jackson K.W., Shuman M.A., McEver R.P.;
"Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells
and localization of the gene to chromosome 17.";
Blood 72:593-600(1988).
[9]
PROTEIN SEQUENCE OF 27-37.
TISSUE=Platelet;
PubMed=1953640; DOI=10.1042/bj2790419;
Catimel B., Parmentier S., Leung L.L., McGregor J.L.;
"Separation of important new platelet glycoproteins (GPIa, GPIc,
GPIc*, GPIIa and GMP-140) by F.P.L.C. Characterization by monoclonal
antibodies and gas-phase sequencing.";
Biochem. J. 279:419-425(1991).
[10]
PROTEIN SEQUENCE OF 27-34.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-788.
PubMed=2341395;
Zimrin A.B., Gidwitz S., Lord S., Schwartz E., Bennett J.S.,
White G.C. II, Poncz M.;
"The genomic organization of platelet glycoprotein IIIa.";
J. Biol. Chem. 265:8590-8595(1990).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-788.
PubMed=2145280;
Lanza F., Kieffer N., Phillips D.R., Fitzgerald L.A.;
"Characterization of the human platelet glycoprotein IIIa gene.
Comparison with the fibronectin receptor beta-subunit gene.";
J. Biol. Chem. 265:18098-18103(1990).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-120, AND VARIANTS PRO-59 AND
ARG-66.
TISSUE=Blood;
Pascual C., Balas A., Garcia-Sanchez F., Rodriguez de la Rua A.,
Vicario J.L.;
"A new exon II polymorphism in the platelet glycoprotein IIIa.";
Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-204.
PubMed=1382574; DOI=10.1093/intimm/4.9.1031;
Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D.,
Krissansen G.W.;
"The gene organization of the human beta 7 subunit, the common beta
subunit of the leukocyte integrins HML-1 and LPAM-1.";
Int. Immunol. 4:1031-1040(1992).
[15]
PROTEIN SEQUENCE OF 218-234 AND 439-443.
PubMed=3801670;
Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.;
"Purification and partial amino acid sequence of human platelet
membrane glycoproteins IIb and IIIa.";
Blood 69:560-564(1987).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 707-788 (ISOFORM BETA-3B).
TISSUE=Placenta;
PubMed=2787511; DOI=10.1073/pnas.86.14.5415;
Van Kuppevelt T.H.M.S.M., Languino L.R., Gailit J.O., Suzuki S.,
Ruoslahti E.;
"An alternative cytoplasmic domain of the integrin beta 3 subunit.";
Proc. Natl. Acad. Sci. U.S.A. 86:5415-5418(1989).
[17]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=2001252; DOI=10.1042/bj2740063;
Calvete J.J., Henschen A., Gonzalez-Rodriguez J.;
"Assignment of disulphide bonds in human platelet GPIIIa. A disulphide
pattern for the beta-subunits of the integrin family.";
Biochem. J. 274:63-71(1991).
[18]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH COXSACKIEVIRUS A9
CAPSID PROTEINS.
PubMed=7519807; DOI=10.1006/viro.1994.1494;
Roivainen M., Piirainen L., Hovi T., Virtanen I., Riikonen T.,
Heino J., Hyypiae T.;
"Entry of coxsackievirus A9 into host cells: specific interactions
with alpha v beta 3 integrin, the vitronectin receptor.";
Virology 203:357-365(1994).
[19]
PHOSPHORYLATION AT TYR-773 AND TYR-785 (ISOFORM BETA-3A).
PubMed=8631894; DOI=10.1074/jbc.271.18.10811;
Law D.A., Nannizzi-Alaimo L., Phillips D.R.;
"Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb
IIIa) tyrosine phosphorylation induced by platelet aggregation.";
J. Biol. Chem. 271:10811-10815(1996).
[20]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HANTAAN
GLYCOPROTEIN G.
PubMed=9618541; DOI=10.1073/pnas.95.12.7074;
Gavrilovskaya I.N., Shepley M., Shaw R., Ginsberg M.H., Mackow E.R.;
"beta3 Integrins mediate the cellular entry of hantaviruses that cause
respiratory failure.";
Proc. Natl. Acad. Sci. U.S.A. 95:7074-7079(1998).
[21]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 TAT.
PubMed=10397733;
Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S.,
Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.;
"The Tat protein of human immunodeficiency virus type-1 promotes
vascular cell growth and locomotion by engaging the alpha5beta1 and
alphavbeta3 integrins and by mobilizing sequestered basic fibroblast
growth factor.";
Blood 94:663-672(1999).
[22]
PHOSPHORYLATION AT THR-779.
PubMed=10896934; DOI=10.1074/jbc.M001908200;
Kirk R.I., Sanderson M.R., Lerea K.M.;
"Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at
a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc
binding.";
J. Biol. Chem. 275:30901-30906(2000).
[23]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
PARECHOVIRUS 1 CAPSID PROTEINS.
PubMed=11160695; DOI=10.1128/JVI.75.4.1958-1967.2001;
Joki-Korpela P., Marjomaki V., Krogerus C., Heino J., Hyypia T.;
"Entry of human parechovirus 1.";
J. Virol. 75:1958-1967(2001).
[24]
INTERACTION WITH SYK.
PubMed=11940607; DOI=10.1083/jcb.200112113;
Obergfell A., Eto K., Mocsai A., Buensuceso C., Moores S.L.,
Brugge J.S., Lowell C.A., Shattil S.J.;
"Coordinate interactions of Csk, Src, and Syk kinases with
[alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton.";
J. Cell Biol. 157:265-275(2002).
[25]
INTERACTION WITH FLNB.
TISSUE=Keratinocyte, and Skeletal muscle;
PubMed=11807098; DOI=10.1083/jcb.200103037;
van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
Takafuta T., Shapiro S.S., Sonnenberg A.;
"Different splice variants of filamin-B affect myogenesis, subcellular
distribution, and determine binding to integrin (beta) subunits.";
J. Cell Biol. 156:361-376(2002).
[26]
INTERACTION WITH NOV.
PubMed=12695522; DOI=10.1074/jbc.M302028200;
Lin C.G., Leu S.J., Chen N., Tebeau C.M., Lin S.X., Yeung C.Y.,
Lau L.F.;
"CCN3 (NOV) is a novel angiogenic regulator of the CCN protein
family.";
J. Biol. Chem. 278:24200-24208(2003).
[27]
FUNCTION, AND INTERACTION WITH FBN1.
PubMed=12807887; DOI=10.1074/jbc.M303159200;
Bax D.V., Bernard S.E., Lomas A., Morgan A., Humphries J.,
Shuttleworth C.A., Humphries M.J., Kielty C.M.;
"Cell adhesion to fibrillin-1 molecules and microfibrils is mediated
by alpha 5 beta 1 and alpha v beta 3 integrins.";
J. Biol. Chem. 278:34605-34616(2003).
[28]
INTERACTION WITH MYO10.
PubMed=15156152; DOI=10.1038/ncb1136;
Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A.,
Cheney R.E., Stromblad S.;
"Myosin-X provides a motor-based link between integrins and the
cytoskeleton.";
Nat. Cell Biol. 6:523-531(2004).
[29]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH
CYTOMEGALOVIRUS/HHV-5 GH:GL PROTEINS.
PubMed=15834425; DOI=10.1038/nm1236;
Wang X., Huang D.Y., Huong S.M., Huang E.S.;
"Integrin alphavbeta3 is a coreceptor for human cytomegalovirus.";
Nat. Med. 11:515-521(2005).
[30]
INTERACTION WITH PDIA6.
PubMed=15466936; DOI=10.1182/blood-2004-02-0608;
Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T.,
Authi K.S., Gibbins J.M.;
"A role for the thiol isomerase protein ERP5 in platelet function.";
Blood 105:1500-1507(2005).
[31]
INTERACTION WITH EMP2.
PubMed=16216233; DOI=10.1016/j.ydbio.2005.09.003;
Wadehra M., Forbes A., Pushkarna N., Goodglick L., Gordon L.K.,
Williams C.J., Braun J.;
"Epithelial membrane protein-2 regulates surface expression of
alphavbeta3 integrin in the endometrium.";
Dev. Biol. 287:336-345(2005).
[32]
INTERACTION WITH COMP.
PubMed=16051604; DOI=10.1074/jbc.M504778200;
Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.;
"Cartilage oligomeric matrix protein/thrombospondin 5 supports
chondrocyte attachment through interaction with integrins.";
J. Biol. Chem. 280:32655-32661(2005).
[33]
REVIEW.
PubMed=16322781; DOI=10.1172/JCI26989;
Bennett J.S.;
"Structure and function of the platelet integrin alphaIIbbeta3.";
J. Clin. Invest. 115:3363-3369(2005).
[34]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[35]
INTERACTION WITH ADGRA2.
PubMed=16982628; DOI=10.1074/jbc.M605291200;
Vallon M., Essler M.;
"Proteolytically processed soluble tumor endothelial marker (TEM) 5
mediates endothelial cell survival during angiogenesis by linking
integrin alpha(v)beta3 to glycosaminoglycans.";
J. Biol. Chem. 281:34179-34188(2006).
[36]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[37]
REVIEW.
PubMed=17635696; DOI=10.1111/j.1538-7836.2007.02537.x;
Ma Y.Q., Qin J., Plow E.F.;
"Platelet integrin alpha(IIb)beta(3): activation mechanisms.";
J. Thromb. Haemost. 5:1345-1352(2007).
[38]
FUNCTION, BINDING TO FGF1, AND IDENTIFICATION IN A COMPLEX WITH FGF1
AND FGFR1.
PubMed=18441324; DOI=10.1074/jbc.M801213200;
Mori S., Wu C.Y., Yamaji S., Saegusa J., Shi B., Ma Z., Kuwabara Y.,
Lam K.S., Isseroff R.R., Takada Y.K., Takada Y.;
"Direct binding of integrin alphavbeta3 to FGF1 plays a role in FGF1
signaling.";
J. Biol. Chem. 283:18066-18075(2008).
[39]
FUNCTION.
PubMed=18635536; DOI=10.1074/jbc.M804835200;
Saegusa J., Akakura N., Wu C.Y., Hoogland C., Ma Z., Lam K.S.,
Liu F.T., Takada Y.K., Takada Y.;
"Pro-inflammatory secretory phospholipase A2 type IIA binds to
integrins alphavbeta3 and alpha4beta1 and induces proliferation of
monocytic cells in an integrin-dependent manner.";
J. Biol. Chem. 283:26107-26115(2008).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-773, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[41]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HHV-8
GLYCOPROTEIN B.
PubMed=18045938; DOI=10.1128/JVI.01673-07;
Garrigues H.J., Rubinchikova Y.E., Dipersio C.M., Rose T.M.;
"Integrin alphaVbeta3 Binds to the RGD motif of glycoprotein B of
Kaposi's sarcoma-associated herpesvirus and functions as an RGD-
dependent entry receptor.";
J. Virol. 82:1570-1580(2008).
[42]
IDENTIFICATION OF ALLOANTIGEN HPA-1A BY MASS SPECTROMETRY, AND
ASSOCIATION TO ALLELE HLA-DRB3*01:01.
PubMed=19494351; DOI=10.1182/blood-2009-04-211839;
Anani Sarab G., Moss M., Barker R.N., Urbaniak S.J.;
"Naturally processed peptides spanning the HPA-1a polymorphism are
efficiently generated and displayed from platelet glycoprotein by HLA-
DRB3*0101-positive antigen-presenting cells.";
Blood 114:1954-1957(2009).
[43]
FUNCTION, BINDING TO IGF1, AND IDENTIFICATION IN A COMPLEX WITH IGF1
AND IGF1R.
PubMed=19578119; DOI=10.1074/jbc.M109.013201;
Saegusa J., Yamaji S., Ieguchi K., Wu C.Y., Lam K.S., Liu F.T.,
Takada Y.K., Takada Y.;
"The direct binding of insulin-like growth factor-1 (IGF-1) to
integrin alphavbeta3 is involved in IGF-1 signaling.";
J. Biol. Chem. 284:24106-24114(2009).
[44]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-680.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[45]
INTERACTION WITH FERMT2, AND SUBCELLULAR LOCATION.
PubMed=20702409; DOI=10.1074/jbc.C110.134247;
Bledzka K., Bialkowska K., Nie H., Qin J., Byzova T., Wu C.,
Plow E.F., Ma Y.Q.;
"Tyrosine phosphorylation of integrin beta3 regulates kindlin-2
binding and integrin activation.";
J. Biol. Chem. 285:30370-30374(2010).
[46]
FUNCTION, BINDING TO NRG1, AND IDENTIFICATION IN A COMPLEX WITH NRG1
AND ERBB3.
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).
[47]
FUNCTION, BINDING TO CX3CL1, IDENTIFICATION IN A COMPLEX WITH CX3CR1
AND CX3CL1, AND CX3CL1-BINDING REGION.
PubMed=23125415; DOI=10.4049/jimmunol.1200889;
Fujita M., Takada Y.K., Takada Y.;
"Integrins alphavbeta3 and alpha4beta1 act as coreceptors for
fractalkine, and the integrin-binding defective mutant of fractalkine
is an antagonist of CX3CR1.";
J. Immunol. 189:5809-5819(2012).
[48]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH WEST NILE VIRUS
ENVELOPE PROTEIN E.
PubMed=23658209; DOI=10.1099/vir.0.052613-0;
Schmidt K., Keller M., Bader B.L., Korytar T., Finke S., Ziegler U.,
Groschup M.H.;
"Integrins modulate the infection efficiency of West Nile virus into
cells.";
J. Gen. Virol. 94:1723-1733(2013).
[49]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
METAPNEUMOVIRUS FUSION PROTEIN.
PubMed=24478423; DOI=10.1128/JVI.03491-13;
Wei Y., Zhang Y., Cai H., Mirza A.M., Iorio R.M., Peeples M.E.,
Niewiesk S., Li J.;
"Roles of the putative integrin-binding motif of the human
metapneumovirus fusion (f) protein in cell-cell fusion, viral
infectivity, and pathogenesis.";
J. Virol. 88:4338-4352(2014).
[50]
BINDING TO CX3CL1, AND CX3CL1-BINDING REGION.
PubMed=24789099; DOI=10.1371/journal.pone.0096372;
Fujita M., Takada Y.K., Takada Y.;
"The chemokine fractalkine can activate integrins without CX3CR1
through direct binding to a ligand-binding site distinct from the
classical RGD-binding site.";
PLoS ONE 9:E96372-E96372(2014).
[51]
FUNCTION.
PubMed=25398877; DOI=10.1074/jbc.M114.579946;
Fujita M., Zhu K., Fujita C.K., Zhao M., Lam K.S., Kurth M.J.,
Takada Y.K., Takada Y.;
"Proinflammatory secreted phospholipase A2 type IIA (sPLA-IIA) induces
integrin activation through direct binding to a newly identified
binding site (site 2) in integrins alphavbeta3, alpha4beta1, and
alpha5beta1.";
J. Biol. Chem. 290:259-271(2015).
[52]
X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 27-718, AND GLYCOSYLATION AT
ASN-346; ASN-397; ASN-585 AND ASN-680.
PubMed=11546839; DOI=10.1126/science.1064535;
Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L.,
Joachimiak A., Goodman S.L., Arnaout M.A.;
"Crystal structure of the extracellular segment of integrin alpha
Vbeta3.";
Science 294:339-345(2001).
[53]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 50-61 (ALLOANTIGEN HPA-1A)
IN COMPLEX WITH HLA-DRA/HLA-DRB3 HETERODIMER.
PubMed=17583734; DOI=10.1016/j.jmb.2007.05.025;
Parry C.S., Gorski J., Stern L.J.;
"Crystallographic structure of the human leukocyte antigen DRA,
DRB3*0101: models of a directional alloimmune response and
autoimmunity.";
J. Mol. Biol. 371:435-446(2007).
[54]
REVIEW ON GT VARIANTS.
PubMed=7878622;
Bray P.F.;
"Inherited diseases of platelet glycoproteins: considerations for
rapid molecular characterization.";
Thromb. Haemost. 72:492-502(1994).
[55]
VARIANT HPA-1B PRO-59, AND DESCRIPTION OF ALLOANTIGEN SYSTEM PL(A).
PubMed=2565345; DOI=10.1172/JCI114082;
Newman P.J., Derbes R.S., Aster R.H.;
"The human platelet alloantigens, PlA1 and PlA2, are associated with a
leucine33/proline33 amino acid polymorphism in membrane glycoprotein
IIIa, and are distinguishable by DNA typing.";
J. Clin. Invest. 83:1778-1781(1989).
[56]
VARIANT HPA-4B GLN-169, AND DESCRIPTION OF ALLOANTIGEN SYSTEM PEN.
PubMed=1430225; DOI=10.1172/JCI116084;
Wang R., Furihata K., McFarland J.G., Friedman K., Aster R.H.,
Newman P.J.;
"An amino acid polymorphism within the RGD binding domain of platelet
membrane glycoprotein IIIa is responsible for the formation of the
Pena/Penb alloantigen system.";
J. Clin. Invest. 90:2038-2043(1992).
[57]
VARIANT MO(+) ALA-433.
PubMed=8093349;
Kuijpers R.W.A.M., Simsek S., Faber N.M., Goldschmeding R.,
van Wermerkerken R.K.V., von Dem Borne A.E.G.K.;
"Single point mutation in human glycoprotein IIIa is associated with a
new platelet-specific alloantigen (Mo) involved in neonatal alloimmune
thrombocytopenia.";
Blood 81:70-76(1993).
[58]
VARIANT CA(+)/TU(+) GLN-515, AND DESCRIPTION OF ALLOANTIGEN SYSTEM
CA/TU.
PubMed=7694683;
Wang R., McFarland J.G., Kekomaki R., Newman P.J.;
"Amino acid 489 is encoded by a mutational 'hot spot' on the beta 3
integrin chain: the CA/TU human platelet alloantigen system.";
Blood 82:3386-3391(1993).
[59]
VARIANT SR(A) CYS-662, AND DESCRIPTION OF ALLOANTIGEN SYSTEM SR(A).
PubMed=8132570;
Santoso S., Kalb R., Kroll H., Walka M., Kiefel V.,
Mueller-Eckhardt C., Newman P.J.;
"A point mutation leads to an unpaired cysteine residue and a
molecular weight polymorphism of a functional platelet beta 3 integrin
subunit. The Sra alloantigen system of GPIIIa.";
J. Biol. Chem. 269:8439-8444(1994).
[60]
VARIANT GT TYR-145.
PubMed=2392682; DOI=10.1126/science.2392682;
Loftus J.C., O'Toole T.E., Plow E.F., Glass A., Frelinger A.L. III,
Ginsberg M.H.;
"A beta 3 integrin mutation abolishes ligand binding and alters
divalent cation-dependent conformation.";
Science 249:915-918(1990).
[61]
VARIANT GT GLN-240.
PubMed=1371279;
Bajt M.L., Ginsberg M.H., Frelinger A.L. III, Berndt M.C.,
Loftus J.C.;
"A spontaneous mutation of integrin alpha IIb beta 3 (platelet
glycoprotein IIb-IIIa) helps define a ligand binding site.";
J. Biol. Chem. 267:3789-3794(1992).
[62]
VARIANT GT TRP-240.
PubMed=1602006; DOI=10.1172/JCI115808;
Lanza F., Stierle A., Fournier D., Morales M., Andre G., Nurden A.T.,
Cazenave J.-P.;
"A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets
with functionally defective glycoprotein IIb-IIIa complexes and a
glycoprotein IIIa 214Arg-->214Trp mutation.";
J. Clin. Invest. 89:1995-2004(1992).
[63]
VARIANT GT PRO-778.
PubMed=1438206; DOI=10.1073/pnas.89.21.10169;
Chen Y.-P., Djaffar I., Pidard D., Steiner B., Cieutat A.-M.,
Caen J.P., Rosa J.-P.;
"Ser-752-->Pro mutation in the cytoplasmic domain of integrin beta 3
subunit and defective activation of platelet integrin alpha IIb beta 3
(glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia.";
Proc. Natl. Acad. Sci. U.S.A. 89:10169-10173(1992).
[64]
VARIANT GT TYR-400.
PubMed=8781422;
Grimaldi C.M., Chen F., Scudder L.E., Coller B.S., French D.L.;
"A Cys374Tyr homozygous mutation of platelet glycoprotein IIIa (beta
3) in a Chinese patient with Glanzmann's thrombasthenia.";
Blood 88:1666-1675(1996).
[65]
VARIANT GT TRP-143.
PubMed=9376589;
Basani R.B., Brown D.L., Vilaire G., Bennett J.S., Poncz M.;
"A Leu117-->Trp mutation within the RGD-peptide cross-linking region
of beta3 results in Glanzmann thrombasthenia by preventing alphaIIb
beta3 export to the platelet surface.";
Blood 90:3082-3088(1997).
[66]
VARIANTS GT ASN-145; GLN-242 AND PRO-288.
PubMed=9215749; DOI=10.1006/bcmd.1997.0117;
French D.L., Coller B.S.;
"Hematologically important mutations: Glanzmann thrombasthenia.";
Blood Cells Mol. Dis. 23:39-51(1997).
[67]
VARIANTS GT PRO-306; PHE-586; SER-598 AND SER-605.
PubMed=9790984; DOI=10.1006/bbrc.1998.9526;
Ambo H., Kamata T., Handa M., Taki M., Kuwajima M., Kawai Y., Oda A.,
Murata M., Takada Y., Watanabe K., Ikeda Y.;
"Three novel integrin beta3 subunit missense mutations (H280P, C560F,
and G579S) in thrombasthenia, including one (H280P) prevalent in
Japanese patients.";
Biochem. Biophys. Res. Commun. 251:763-768(1998).
[68]
VARIANT GT LEU-188.
PubMed=9684783;
Jackson D.E., White M.M., Jennings L.K., Newman P.J.;
"A Ser162-->Leu mutation within glycoprotein (GP) IIIa (integrin
beta3) results in an unstable alphaIIbbeta3 complex that retains
partial function in a novel form of type II Glanzmann
thrombasthenia.";
Thromb. Haemost. 80:42-48(1998).
[69]
VARIANT GT ARG-568.
PubMed=10233432; DOI=10.1111/j.1365-2141.1999.01376.x;
Ruan J., Schmugge M., Clemetson K.J., Cazes E., Combrie R., Bourre F.,
Nurden A.T.;
"Homozygous Cys542-->Arg substitution in GPIIIa in a Swiss patient
with type I Glanzmann's thrombasthenia.";
Br. J. Haematol. 105:523-531(1999).
[70]
VARIANTS PRO-59; GLN-169 AND ILE-453.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[71]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[72]
VARIANT GT ARG-586, AND CHARACTERIZATION OF VARIANT GT ARG-586.
PubMed=11588040; DOI=10.1182/blood.V98.8.2432;
Ruiz C., Liu C.-Y., Sun Q.-H., Sigaud-Fiks M., Fressinaud E.,
Muller J.-Y., Nurden P., Nurden A.T., Newman P.J., Valentin N.;
"A point mutation in the cysteine-rich domain of glycoprotein (GP)
IIIa results in the expression of a GPIIb-IIIa (alphaIIbbeta3)
integrin receptor locked in a high-affinity state and a Glanzmann
thrombasthenia-like phenotype.";
Blood 98:2432-2441(2001).
[73]
VARIANT ILE-166, AND CHARACTERIZATION OF VARIANT ILE-166.
PubMed=12036875; DOI=10.1182/blood.V99.12.4449;
Jallu V., Meunier M., Brement M., Kaplan C.;
"A new platelet polymorphism Duv(a+), localized within the RGD binding
domain of glycoprotein IIIa, is associated with neonatal
thrombocytopenia.";
Blood 99:4449-4456(2002).
[74]
VARIANT GT PRO-222.
PubMed=11897046; DOI=10.1080/09537100220122466;
Nurden A.T., Ruan J., Pasquet J.-M., Gauthier B., Combrie R.,
Kunicki T., Nurden P.;
"A novel 196Leu to Pro substitution in the beta3 subunit of the
alphaIIbbeta3 integrin in a patient with a variant form of Glanzmann
thrombasthenia.";
Platelets 13:101-111(2002).
[75]
VARIANTS GT TRP-119; VAL-243 AND ARG-601.
PubMed=12083483;
D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G.,
Margaglione M.;
"Glanzmann's thrombasthenia: identification of 19 new mutations in 30
patients.";
Thromb. Haemost. 87:1034-1042(2002).
[76]
VARIANT GT TYR-532.
PubMed=12353082; DOI=10.1267/THRO88030503;
Nair S., Li J., Mitchell W.B., Mohanty D., Coller B.S., French D.L.;
"Two new beta3 integrin mutations in Indian patients with Glanzmann
thrombasthenia: localization of mutations affecting cysteine residues
in integrin beta3.";
Thromb. Haemost. 88:503-509(2002).
[77]
VARIANT GT VAL-150, AND CHARACTERIZATION OF VARIANT GT VAL-150.
PubMed=15583747; DOI=10.1267/THRO04061377;
Gonzalez-Manchon C., Butta N., Larrucea S., Arias-Salgado E.G.,
Alonso S., Lopez A., Parrilla R.;
"A variant thrombasthenic phenotype associated with compound
heterozygosity of integrin beta3-subunit: (Met124Val)beta3 alters the
subunit dimerization rendering a decreased number of constitutive
active alphaIIbbeta3 receptors.";
Thromb. Haemost. 92:1377-1386(2004).
[78]
VARIANTS GT PRO-306 AND ASN-330, AND CHARACTERIZATION OF VARIANT GT
ASN-330.
PubMed=15634267; DOI=10.1111/j.1538-7836.2004.00990.x;
Tanaka S., Hayashi T., Yoshimura K., Nakayama M., Fujita T., Amano T.,
Tani Y.;
"Double heterozygosity for a novel missense mutation of Ile304 to Asn
in addition to the missense mutation His280 to Pro in the integrin
beta3 gene as a cause of the absence of platelet alphaIIbbeta3 in
Glanzmann's thrombasthenia.";
J. Thromb. Haemost. 3:68-73(2005).
[79]
VARIANTS GT CYS-141 AND LEU-321.
PubMed=15748237; DOI=10.1111/j.1538-7836.2005.01159.x;
Nair S., Ghosh K., Shetty S., Mohanty D.;
"Mutations in GPIIIa molecule as a cause for Glanzmann thrombasthenia
in Indian patients.";
J. Thromb. Haemost. 3:482-488(2005).
[80]
VARIANT BDPLT16 HIS-749, AND CHARACTERIZATION OF VARIANT BDPLT16
HIS-749.
PubMed=18065693; DOI=10.1182/blood-2007-09-112615;
Ghevaert C., Salsmann A., Watkins N.A., Schaffner-Reckinger E.,
Rankin A., Garner S.F., Stephens J., Smith G.A., Debili N.,
Vainchenker W., de Groot P.G., Huntington J.A., Laffan M., Kieffer N.,
Ouwehand W.H.;
"A nonsynonymous SNP in the ITGB3 gene disrupts the conserved
membrane-proximal cytoplasmic salt bridge in the alphaIIbbeta3
integrin and cosegregates dominantly with abnormal proplatelet
formation and macrothrombocytopenia.";
Blood 111:3407-3414(2008).
[81]
VARIANTS GT TYR-64; ARG-144; PRO-222; ASP-247 AND MET-279,
CHARACTERIZATION OF VARIANTS TYR-64; PRO-222; ASP-247 AND MET-279, AND
SUBCELLULAR LOCATION.
PubMed=20020534; DOI=10.1002/humu.21179;
Jallu V., Dusseaux M., Panzer S., Torchet M.F., Hezard N.,
Goudemand J., de Brevern A.G., Kaplan C.;
"AlphaIIbbeta3 integrin: new allelic variants in Glanzmann
thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression,
and structure-function.";
Hum. Mutat. 31:237-246(2010).
-!- FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for
cytotactin, fibronectin, laminin, matrix metalloproteinase-2,
osteopontin, osteomodulin, prothrombin, thrombospondin,
vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3
(ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen,
plasminogen, prothrombin, thrombospondin and vitronectin.
Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the
sequence R-G-D in a wide array of ligands. Integrin alpha-
IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in
fibrinogen gamma chain. Following activation integrin alpha-
IIb/beta-3 brings about platelet/platelet interaction through
binding of soluble fibrinogen. This step leads to rapid platelet
aggregation which physically plugs ruptured endothelial surface.
Fibrinogen binding enhances SELP expression in activated platelets
(By similarity). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and
acts as its coreceptor in CX3CR1-dependent fractalkine signaling
(PubMed:23125415, PubMed:24789099). ITGAV:ITGB3 binds to NRG1 (via
EGF domain) and this binding is essential for NRG1-ERBB signaling
(PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is
essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds
to IGF1 and this binding is essential for IGF1 signaling
(PubMed:19578119). ITGAV:ITGB3 binds to PLA2G2A via a site (site
2) which is distinct from the classical ligand-binding site (site
1) and this induces integrin conformational changes and enhanced
ligand binding to site 1 (PubMed:18635536, PubMed:25398877).
ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates
R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887).
{ECO:0000250|UniProtKB:O54890, ECO:0000269|PubMed:12807887,
ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:18635536,
ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20682778,
ECO:0000269|PubMed:23125415, ECO:0000269|PubMed:24789099,
ECO:0000269|PubMed:25398877, ECO:0000269|PubMed:9195946,
ECO:0000303|PubMed:16322781, ECO:0000303|PubMed:17635696}.
-!- FUNCTION: (Microbial infection) Integrin ITGAV:ITGB3 acts as a
receptor for herpes virus 8/HHV-8 (PubMed:18045938). Integrin
ITGAV:ITGB3 acts as a receptor for coxsackievirus A9
(PubMed:7519807). Acts as a receptor for Hantaan virus
(PubMed:9618541). Integrin ITGAV:ITGB3 acts as a receptor for
cytomegalovirus/HHV-5 (PubMed:15834425). Integrin ITGA5:ITGB3 acts
as a receptor for human metapneumovirus (PubMed:24478423).
Integrin ITGAV:ITGB3 acts aP05556s a receptor for human
parechovirus 1 (PubMed:11160695). Integrin ITGAV:ITGB3 acts as a
receptor for west nile virus (PubMed:23658209). In case of HIV-1
infection, the interaction with extracellular viral Tat protein
seems to enhance angiogenesis in Kaposi's sarcoma lesions
(PubMed:10397733). {ECO:0000269|PubMed:10397733,
ECO:0000269|PubMed:11160695, ECO:0000269|PubMed:15834425,
ECO:0000269|PubMed:18045938, ECO:0000269|PubMed:23658209,
ECO:0000269|PubMed:24478423, ECO:0000269|PubMed:7519807,
ECO:0000269|PubMed:9618541}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-3
(ITGB3) associates with either alpha-IIb (ITGA2B) or alpha-V
(ITGAV). Isoform Beta-3C interacts with FLNB. Interacts with COMP.
Interacts with PDIA6 following platelet stimulation. Interacts
with SYK; upon activation by ITGB3 promotes platelet adhesion.
Interacts with MYO10. Interacts with DAB2. Interacts with FERMT2.
Interacts with EMP2; regulates the levels of the heterodimer
ITGA5:ITGB3 integrin expression on the plasma membrane
(PubMed:16216233). Integrin ITGAV:ITGB3 interacts with FBLN5 (via
N-terminus) (By similarity). ITGAV:ITGB3 interacts with NOV
(PubMed:12695522). ITGAV:ITGB3 is found in a ternary complex with
CX3CR1 and CX3CL1 (PubMed:23125415). ITGAV:ITGB3 is found in a
ternary complex with NRG1 and ERBB3 (PubMed:20682778). ITGAV:ITGB3
is found in a ternary complex with FGF1 and FGFR1
(PubMed:18441324). ITGAV:ITGB3 is found in a ternary complex with
IGF1 and IGF1R (PubMed:19578119). ITGAV:ITGB3 interacts with FBN1
(PubMed:12807887). {ECO:0000250|UniProtKB:O54890,
ECO:0000269|PubMed:11807098, ECO:0000269|PubMed:11940607,
ECO:0000269|PubMed:12695522, ECO:0000269|PubMed:12807887,
ECO:0000269|PubMed:15156152, ECO:0000269|PubMed:15466936,
ECO:0000269|PubMed:16051604, ECO:0000269|PubMed:16216233,
ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:18441324,
ECO:0000269|PubMed:19578119, ECO:0000269|PubMed:20682778,
ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:23125415}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
herpes virus 8/HHV-8 glycoprotein B.
{ECO:0000269|PubMed:18045938}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
coxsackievirus A9 capsid proteins. {ECO:0000269|PubMed:7519807}.
-!- SUBUNIT: (Microbial infection) Interacts with Hantaan virus
glycoprotein G. {ECO:0000269|PubMed:9618541}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
cytomegalovirus/HHV-5 gH:gL proteins.
{ECO:0000269|PubMed:15834425}.
-!- SUBUNIT: (Microbial infection) Integrin ITGA5:ITGB3 interacts with
human metapneumovirus fusion protein.
{ECO:0000269|PubMed:24478423}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
human parechovirus 1 capsid proteins.
{ECO:0000269|PubMed:11160695}.
-!- SUBUNIT: (Microbial infection) Integrin ITGAV:ITGB3 interacts with
west nile virus envelope protein E. {ECO:0000269|PubMed:23658209}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat
(PubMed:10397733). ITGAV:ITGB3 interacts with AGRA2
(PubMed:16982628). {ECO:0000269|PubMed:10397733,
ECO:0000269|PubMed:16982628}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-702847, EBI-702847;
P06935:- (xeno); NbExp=4; IntAct=EBI-702847, EBI-981051;
P05094:ACTN1 (xeno); NbExp=2; IntAct=EBI-702847, EBI-5847257;
P78423:CX3CL1; NbExp=2; IntAct=EBI-702847, EBI-15188013;
P21333:FLNA; NbExp=3; IntAct=EBI-702847, EBI-350432;
F5HB81:gB (xeno); NbExp=2; IntAct=EBI-702847, EBI-9027696;
P08514:ITGA2B; NbExp=11; IntAct=EBI-702847, EBI-702693;
P08514-1:ITGA2B; NbExp=4; IntAct=EBI-702847, EBI-15805658;
P06756:ITGAV; NbExp=13; IntAct=EBI-702847, EBI-298282;
Q62101:Prkd1 (xeno); NbExp=2; IntAct=EBI-702847, EBI-6903636;
P18031:PTPN1; NbExp=4; IntAct=EBI-702847, EBI-968788;
P05480:Src (xeno); NbExp=5; IntAct=EBI-702847, EBI-298680;
P54939:TLN1 (xeno); NbExp=2; IntAct=EBI-702847, EBI-1035421;
Q9Y490:TLN1; NbExp=4; IntAct=EBI-702847, EBI-2462036;
P26039:Tln1 (xeno); NbExp=7; IntAct=EBI-702847, EBI-1039593;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20020534,
ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}; Single-
pass type I membrane protein {ECO:0000269|PubMed:20020534,
ECO:0000269|PubMed:20702409, ECO:0000269|PubMed:9195946}. Cell
projection, lamellipodium membrane {ECO:0000269|PubMed:20702409}.
Cell junction, focal adhesion {ECO:0000269|PubMed:20702409}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Beta-3A;
IsoId=P05106-1; Sequence=Displayed;
Name=Beta-3B;
IsoId=P05106-2; Sequence=VSP_002745;
Name=Beta-3C;
IsoId=P05106-3; Sequence=VSP_002746;
-!- TISSUE SPECIFICITY: Isoform beta-3A and isoform beta-3C are widely
expressed. Isoform beta-3A is specifically expressed in osteoblast
cells; isoform beta-3C is specifically expressed in prostate and
testis.
-!- PTM: Phosphorylated on tyrosine residues in response to thrombin-
induced platelet aggregation. Probably involved in outside-in
signaling. A peptide (AA 740-762) is capable of binding GRB2 only
when both Tyr-773 and Tyr-785 are phosphorylated. Phosphorylation
of Thr-779 inhibits SHC binding. {ECO:0000269|PubMed:10896934}.
-!- POLYMORPHISM: Position 59 is associated with platelet-specific
alloantigen HPA-1 (ZW or PL(A)). HPA-1A/ZW(A)/PL(A1) has Leu-59
and HPA-1B/ZW(B)/PL(A2) has Pro-59. HPA-1A is involved in fetal-
maternal alloimmune thromobocytopenia (FMAIT) as well as in
neonatal alloimmune thrombocytopenia (NAIT).
-!- POLYMORPHISM: Position 169 is associated with platelet-specific
alloantigen HPA-4 (PEN or YUK). HPA-4A/PEN(A)/YUK(A) has Arg-169
and HPA-4B/PEN(B)/YUK(B) has Gln-169. HPA-4B is involved in
neonatal alloimmune thrombocytopenia (NAIT or NATP).
-!- POLYMORPHISM: Position 433 is associated with platelet-specific
alloantigen MO. MO(-) has Pro-433 and MO(+) has Ala-433. MO(+) is
involved in NAIT.
-!- POLYMORPHISM: Position 515 is associated with platelet-specific
alloantigen CA/TU. CA(-)/TU(-) has Arg-515 and CA(+)/TU(+) has
Gln-515. CA(+) is involved in NAIT.
-!- POLYMORPHISM: Position 662 is associated with platelet-specific
alloantigen SR(A). SR(A)(-) has Arg-662 and SR(A)(+) has Cys-662.
-!- DISEASE: Glanzmann thrombasthenia (GT) [MIM:273800]: A common
inherited disease of platelet aggregation. It is characterized by
mucocutaneous bleeding of mild-to-moderate severity. GT has been
classified clinically into types I and II. In type I, platelets
show absence of the glycoprotein IIb-IIIa complexes at their
surface and lack fibrinogen and clot retraction capability. In
type II, the platelets express the GPIIb-IIIa complex at reduced
levels, have detectable amounts of fibrinogen, and have low or
moderate clot retraction capability. {ECO:0000269|PubMed:10233432,
ECO:0000269|PubMed:11588040, ECO:0000269|PubMed:11897046,
ECO:0000269|PubMed:12083483, ECO:0000269|PubMed:12353082,
ECO:0000269|PubMed:1371279, ECO:0000269|PubMed:1438206,
ECO:0000269|PubMed:15583747, ECO:0000269|PubMed:15634267,
ECO:0000269|PubMed:15748237, ECO:0000269|PubMed:1602006,
ECO:0000269|PubMed:20020534, ECO:0000269|PubMed:2392682,
ECO:0000269|PubMed:8781422, ECO:0000269|PubMed:9215749,
ECO:0000269|PubMed:9376589, ECO:0000269|PubMed:9684783,
ECO:0000269|PubMed:9790984}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Bleeding disorder, platelet-type 16 (BDPLT16)
[MIM:187800]: An autosomal dominant form of congenital
macrothrombocytopenia associated with platelet anisocytosis. It is
a disorder of platelet production. Affected individuals may have
no or only mildly increased bleeding tendency. In vitro studies
show mild platelet functional abnormalities.
{ECO:0000269|PubMed:18065693}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ITGB3";
-----------------------------------------------------------------------
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EMBL; J02703; AAA52589.1; -; mRNA.
EMBL; M20311; AAA60122.1; -; mRNA.
EMBL; M35999; AAA35927.1; -; mRNA.
EMBL; U95204; AAB71380.1; -; mRNA.
EMBL; CH471231; EAW57682.1; -; Genomic_DNA.
EMBL; BC127666; AAI27667.1; -; mRNA.
EMBL; BC127667; AAI27668.1; -; mRNA.
EMBL; L28832; AAA20880.2; -; Genomic_DNA.
EMBL; M32686; AAA67537.1; -; Genomic_DNA.
EMBL; M32667; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M32672; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M32673; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M32674; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M32675; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M32680; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M32681; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M32682; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M32685; AAA67537.1; JOINED; Genomic_DNA.
EMBL; M57494; AAA52600.1; -; Genomic_DNA.
EMBL; M57481; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57482; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57483; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57484; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57485; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57486; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57487; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57488; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57489; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57490; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57491; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57492; AAA52600.1; JOINED; Genomic_DNA.
EMBL; M57493; AAA52600.1; JOINED; Genomic_DNA.
EMBL; U03881; AAA16076.1; -; Genomic_DNA.
EMBL; S49379; AAB23689.2; -; Genomic_DNA.
EMBL; M25108; AAA36121.1; -; mRNA.
CCDS; CCDS11511.1; -. [P05106-1]
PIR; A26547; A26547.
PIR; A60798; A60798.
PIR; B36268; B36268.
PIR; I77349; I77349.
PIR; S14324; S14324.
RefSeq; NP_000203.2; NM_000212.2. [P05106-1]
UniGene; Hs.218040; -.
PDB; 1JV2; X-ray; 3.10 A; B=27-718.
PDB; 1KUP; NMR; -; B=742-766.
PDB; 1KUZ; NMR; -; B=742-766.
PDB; 1L5G; X-ray; 3.20 A; B=27-718.
PDB; 1M1X; X-ray; 3.30 A; B=27-718.
PDB; 1M8O; NMR; -; B=742-788.
PDB; 1MIZ; X-ray; 1.90 A; A=765-769.
PDB; 1MK7; X-ray; 2.20 A; A/C=765-775.
PDB; 1MK9; X-ray; 2.80 A; A/C/E/G=765-776.
PDB; 1RN0; Model; -; B=135-378.
PDB; 1S4X; NMR; -; A=742-788.
PDB; 1TYE; X-ray; 2.90 A; B/D/F=27-466.
PDB; 1U8C; X-ray; 3.10 A; B=27-718.
PDB; 2INI; Model; -; B=81-460, B=558-716.
PDB; 2K9J; NMR; -; B=711-753.
PDB; 2KNC; NMR; -; B=715-788.
PDB; 2KV9; NMR; -; B=739-788.
PDB; 2L1C; NMR; -; B=762-788.
PDB; 2L91; NMR; -; A=711-753.
PDB; 2LJD; NMR; -; A=742-788.
PDB; 2LJE; NMR; -; A=742-788.
PDB; 2LJF; NMR; -; A=742-788.
PDB; 2MTP; NMR; -; C=742-788.
PDB; 2N9Y; NMR; -; B=712-753.
PDB; 2Q6W; X-ray; 2.25 A; C/F=50-61.
PDB; 2RMZ; NMR; -; A=711-753.
PDB; 2RN0; NMR; -; A=711-753.
PDB; 2VC2; X-ray; 3.10 A; B=27-487.
PDB; 2VDK; X-ray; 2.80 A; B=27-487.
PDB; 2VDL; X-ray; 2.75 A; B=27-487.
PDB; 2VDM; X-ray; 2.90 A; B=27-487.
PDB; 2VDN; X-ray; 2.90 A; B=27-487.
PDB; 2VDO; X-ray; 2.51 A; B=27-487.
PDB; 2VDP; X-ray; 2.80 A; B=27-487.
PDB; 2VDQ; X-ray; 2.59 A; B=27-487.
PDB; 2VDR; X-ray; 2.40 A; B=27-487.
PDB; 3FCS; X-ray; 2.55 A; B/D=27-716.
PDB; 3FCU; X-ray; 2.90 A; B/D/F=27-487.
PDB; 3IJE; X-ray; 2.90 A; B=27-721.
PDB; 3NID; X-ray; 2.30 A; B/D=27-497.
PDB; 3NIF; X-ray; 2.40 A; B/D=27-497.
PDB; 3NIG; X-ray; 2.25 A; B/D=27-497.
PDB; 3T3M; X-ray; 2.60 A; B/D=27-498.
PDB; 3T3P; X-ray; 2.20 A; B/D=27-498.
PDB; 3ZDX; X-ray; 2.45 A; B/D=27-498.
PDB; 3ZDY; X-ray; 2.45 A; B/D=27-498.
PDB; 3ZDZ; X-ray; 2.75 A; B/D=27-498.
PDB; 3ZE0; X-ray; 2.95 A; B/D=27-498.
PDB; 3ZE1; X-ray; 3.00 A; B/D=27-498.
PDB; 3ZE2; X-ray; 2.35 A; B/D=27-498.
PDB; 4CAK; EM; 20.50 A; B=27-716.
PDB; 4G1E; X-ray; 3.00 A; B=27-717.
PDB; 4G1M; X-ray; 2.90 A; B=27-718.
PDB; 4MMX; X-ray; 3.32 A; B=27-718.
PDB; 4MMY; X-ray; 3.18 A; B=27-718.
PDB; 4MMZ; X-ray; 3.10 A; B=27-718.
PDB; 4O02; X-ray; 3.60 A; B=27-718.
PDB; 4Z7N; X-ray; 2.60 A; B/D=29-497.
PDB; 4Z7O; X-ray; 2.85 A; B/D=29-497.
PDB; 4Z7Q; X-ray; 2.70 A; B/D=27-497.
PDB; 5HDB; X-ray; 2.70 A; B/D=27-497.
PDBsum; 1JV2; -.
PDBsum; 1KUP; -.
PDBsum; 1KUZ; -.
PDBsum; 1L5G; -.
PDBsum; 1M1X; -.
PDBsum; 1M8O; -.
PDBsum; 1MIZ; -.
PDBsum; 1MK7; -.
PDBsum; 1MK9; -.
PDBsum; 1RN0; -.
PDBsum; 1S4X; -.
PDBsum; 1TYE; -.
PDBsum; 1U8C; -.
PDBsum; 2INI; -.
PDBsum; 2K9J; -.
PDBsum; 2KNC; -.
PDBsum; 2KV9; -.
PDBsum; 2L1C; -.
PDBsum; 2L91; -.
PDBsum; 2LJD; -.
PDBsum; 2LJE; -.
PDBsum; 2LJF; -.
PDBsum; 2MTP; -.
PDBsum; 2N9Y; -.
PDBsum; 2Q6W; -.
PDBsum; 2RMZ; -.
PDBsum; 2RN0; -.
PDBsum; 2VC2; -.
PDBsum; 2VDK; -.
PDBsum; 2VDL; -.
PDBsum; 2VDM; -.
PDBsum; 2VDN; -.
PDBsum; 2VDO; -.
PDBsum; 2VDP; -.
PDBsum; 2VDQ; -.
PDBsum; 2VDR; -.
PDBsum; 3FCS; -.
PDBsum; 3FCU; -.
PDBsum; 3IJE; -.
PDBsum; 3NID; -.
PDBsum; 3NIF; -.
PDBsum; 3NIG; -.
PDBsum; 3T3M; -.
PDBsum; 3T3P; -.
PDBsum; 3ZDX; -.
PDBsum; 3ZDY; -.
PDBsum; 3ZDZ; -.
PDBsum; 3ZE0; -.
PDBsum; 3ZE1; -.
PDBsum; 3ZE2; -.
PDBsum; 4CAK; -.
PDBsum; 4G1E; -.
PDBsum; 4G1M; -.
PDBsum; 4MMX; -.
PDBsum; 4MMY; -.
PDBsum; 4MMZ; -.
PDBsum; 4O02; -.
PDBsum; 4Z7N; -.
PDBsum; 4Z7O; -.
PDBsum; 4Z7Q; -.
PDBsum; 5HDB; -.
ProteinModelPortal; P05106; -.
SMR; P05106; -.
BioGrid; 109896; 30.
CORUM; P05106; -.
DIP; DIP-304N; -.
ELM; P05106; -.
IntAct; P05106; 27.
MINT; MINT-209501; -.
STRING; 9606.ENSP00000262017; -.
BindingDB; P05106; -.
ChEMBL; CHEMBL2111461; -.
DrugBank; DB00054; Abciximab.
DrugBank; DB00098; Anti-thymocyte Globulin (Rabbit).
DrugBank; DB00063; Eptifibatide.
DrugBank; DB04863; Lefradafiban.
DrugBank; DB05787; LM-609.
DrugBank; DB00775; Tirofiban.
GuidetoPHARMACOLOGY; 2457; -.
iPTMnet; P05106; -.
PhosphoSitePlus; P05106; -.
BioMuta; ITGB3; -.
DMDM; 125987835; -.
EPD; P05106; -.
MaxQB; P05106; -.
PaxDb; P05106; -.
PeptideAtlas; P05106; -.
PRIDE; P05106; -.
Ensembl; ENST00000559488; ENSP00000452786; ENSG00000259207. [P05106-1]
GeneID; 3690; -.
KEGG; hsa:3690; -.
UCSC; uc002ilj.4; human. [P05106-1]
CTD; 3690; -.
DisGeNET; 3690; -.
EuPathDB; HostDB:ENSG00000259207.7; -.
GeneCards; ITGB3; -.
HGNC; HGNC:6156; ITGB3.
HPA; HPA027852; -.
MalaCards; ITGB3; -.
MIM; 173470; gene+phenotype.
MIM; 187800; phenotype.
MIM; 273800; phenotype.
neXtProt; NX_P05106; -.
OpenTargets; ENSG00000259207; -.
Orphanet; 140957; Autosomal dominant macrothrombocytopenia.
Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia.
Orphanet; 849; Glanzmann thrombasthenia.
PharmGKB; PA205; -.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
GeneTree; ENSGT00760000119064; -.
HOVERGEN; HBG006190; -.
InParanoid; P05106; -.
KO; K06493; -.
OMA; CHSSDFG; -.
OrthoDB; EOG091G029W; -.
PhylomeDB; P05106; -.
TreeFam; TF105392; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1566948; Elastic fibre formation.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-HSA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
SignaLink; P05106; -.
SIGNOR; P05106; -.
ChiTaRS; ITGB3; human.
EvolutionaryTrace; P05106; -.
GeneWiki; CD61; -.
GenomeRNAi; 3690; -.
PMAP-CutDB; P05106; -.
PRO; PR:P05106; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000259207; -.
CleanEx; HS_ITGB3; -.
ExpressionAtlas; P05106; baseline and differential.
Genevisible; P05106; HS.
GO; GO:0035867; C:alphav-beta3 integrin-IGF-1-IGF1R complex; IDA:UniProtKB.
GO; GO:0071062; C:alphav-beta3 integrin-vitronectin complex; TAS:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0034683; C:integrin alphav-beta3 complex; IDA:UniProtKB.
GO; GO:0008305; C:integrin complex; IDA:BHF-UCL.
GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IDA:UniProtKB.
GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
GO; GO:0015026; F:coreceptor activity; TAS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0050840; F:extracellular matrix binding; IDA:UniProtKB.
GO; GO:0001968; F:fibronectin binding; IMP:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; TAS:BHF-UCL.
GO; GO:0002020; F:protease binding; IDA:UniProtKB.
GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB.
GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:BHF-UCL.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0032147; P:activation of protein kinase activity; IMP:BHF-UCL.
GO; GO:0060055; P:angiogenesis involved in wound healing; TAS:BHF-UCL.
GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007596; P:blood coagulation; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0016049; P:cell growth; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
GO; GO:0007044; P:cell-substrate junction assembly; IEA:InterPro.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0048333; P:mesodermal cell differentiation; IEP:UniProtKB.
GO; GO:0050919; P:negative chemotaxis; IMP:UniProtKB.
GO; GO:0010888; P:negative regulation of lipid storage; IMP:BHF-UCL.
GO; GO:0032369; P:negative regulation of lipid transport; IMP:BHF-UCL.
GO; GO:0050748; P:negative regulation of lipoprotein metabolic process; IMP:BHF-UCL.
GO; GO:0045715; P:negative regulation of low-density lipoprotein particle receptor biosynthetic process; IMP:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
GO; GO:0030168; P:platelet activation; IMP:UniProtKB.
GO; GO:0070527; P:platelet aggregation; IMP:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; TAS:BHF-UCL.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; TAS:BHF-UCL.
GO; GO:0045124; P:regulation of bone resorption; TAS:BHF-UCL.
GO; GO:0014909; P:smooth muscle cell migration; IMP:BHF-UCL.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0035295; P:tube development; TAS:BHF-UCL.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0046718; P:viral entry into host cell; IMP:UniProtKB.
GO; GO:0042060; P:wound healing; IC:BHF-UCL.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR027068; Integrin_beta-3.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR037076; Integrin_bsu_cyt_dom_sf.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR016201; PSI.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF25; PTHR10082:SF25; 1.
Pfam; PF07974; EGF_2; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS00243; INTEGRIN_BETA; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Integrin; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 788 Integrin beta-3.
/FTId=PRO_0000016344.
TOPO_DOM 27 718 Extracellular. {ECO:0000255}.
TRANSMEM 719 741 Helical. {ECO:0000255}.
TOPO_DOM 742 788 Cytoplasmic. {ECO:0000255}.
DOMAIN 135 377 VWFA.
REPEAT 463 511 I.
REPEAT 512 553 II.
REPEAT 554 592 III.
REPEAT 593 629 IV.
REGION 203 210 Involved in CX3CL1-, NRG1-, FGF1- and
IGF1-binding.
{ECO:0000269|PubMed:18441324,
ECO:0000269|PubMed:19578119,
ECO:0000269|PubMed:20682778,
ECO:0000269|PubMed:23125415}.
REGION 293 313 CX3CL1-binding.
{ECO:0000269|PubMed:24789099}.
REGION 463 629 Cysteine-rich tandem repeats.
MOD_RES 767 767 Phosphothreonine.
{ECO:0000250|UniProtKB:O54890}.
MOD_RES 773 773 Phosphotyrosine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 779 779 Phosphothreonine; by PDPK1 and PKB/AKT1;
in vitro. {ECO:0000269|PubMed:10896934}.
MOD_RES 785 785 Phosphotyrosine.
{ECO:0000269|PubMed:8631894}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:11546839}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:11546839}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
CARBOHYD 585 585 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:11546839}.
CARBOHYD 680 680 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11546839,
ECO:0000269|PubMed:19159218}.
DISULFID 31 461 {ECO:0000269|PubMed:2001252}.
DISULFID 39 49 {ECO:0000269|PubMed:2001252}.
DISULFID 42 75 {ECO:0000269|PubMed:2001252}.
DISULFID 52 64 {ECO:0000269|PubMed:2001252}.
DISULFID 203 210 {ECO:0000269|PubMed:2001252}.
DISULFID 258 299 {ECO:0000269|PubMed:2001252}.
DISULFID 400 412 {ECO:0000269|PubMed:2001252}.
DISULFID 432 681 {ECO:0000269|PubMed:2001252}.
DISULFID 459 463 {ECO:0000269|PubMed:2001252}.
DISULFID 474 486 {ECO:0000305|PubMed:2001252}.
DISULFID 483 521 {ECO:0000305|PubMed:2001252}.
DISULFID 488 497 {ECO:0000305|PubMed:2001252}.
DISULFID 499 512 {ECO:0000305|PubMed:2001252}.
DISULFID 527 532 {ECO:0000305|PubMed:2001252}.
DISULFID 529 562 {ECO:0000305|PubMed:2001252}.
DISULFID 534 547 {ECO:0000305|PubMed:2001252}.
DISULFID 549 554 {ECO:0000269|PubMed:2001252}.
DISULFID 568 573 {ECO:0000305|PubMed:2001252}.
DISULFID 570 601 {ECO:0000305|PubMed:2001252}.
DISULFID 575 584 {ECO:0000305|PubMed:2001252}.
DISULFID 586 593 {ECO:0000305|PubMed:2001252}.
DISULFID 607 612 {ECO:0000305|PubMed:2001252}.
DISULFID 609 657 {ECO:0000305|PubMed:2001252}.
DISULFID 614 624 {ECO:0000305|PubMed:2001252}.
DISULFID 627 630 {ECO:0000305|PubMed:2001252}.
DISULFID 634 643 {ECO:0000305|PubMed:2001252}.
DISULFID 640 713 {ECO:0000305|PubMed:2001252}.
DISULFID 661 689 {ECO:0000269|PubMed:2001252}.
VAR_SEQ 768 788 ANNPLYKEATSTFTNITYRGT -> VRDGAGRFLKSLV
(in isoform Beta-3B).
{ECO:0000303|PubMed:2787511}.
/FTId=VSP_002745.
VAR_SEQ 768 788 ANNPLYKEATSTFTNITYRGT -> HYAQSLRKWNQPVSID
G (in isoform Beta-3C).
{ECO:0000303|PubMed:9195946}.
/FTId=VSP_002746.
VARIANT 59 59 L -> P (in alloantigen HPA-1B;
dbSNP:rs5918).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:2565345,
ECO:0000269|Ref.13}.
/FTId=VAR_003993.
VARIANT 64 64 C -> Y (in GT; severe type 1 phenotype;
the mutation prevents normal ITGA2B/ITGB3
complex expression; dbSNP:rs74554539).
{ECO:0000269|PubMed:20020534}.
/FTId=VAR_069920.
VARIANT 66 66 L -> R (in dbSNP:rs36080296).
{ECO:0000269|Ref.13}.
/FTId=VAR_049633.
VARIANT 119 119 R -> W (in GT; dbSNP:rs781062792).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030473.
VARIANT 141 141 Y -> C (in GT).
{ECO:0000269|PubMed:15748237}.
/FTId=VAR_030474.
VARIANT 143 143 L -> W (in GT; dbSNP:rs121918452).
{ECO:0000269|PubMed:9376589}.
/FTId=VAR_010649.
VARIANT 144 144 M -> R (in GT; severe type 1 phenotype;
the mutation prevented normal ITGA2B/
ITGB3 complex expression on the cell
surface; dbSNP:rs77963874).
{ECO:0000269|PubMed:20020534}.
/FTId=VAR_069921.
VARIANT 145 145 D -> N (in GT).
{ECO:0000269|PubMed:9215749}.
/FTId=VAR_030475.
VARIANT 145 145 D -> Y (in GT; type B;
dbSNP:rs121918445).
{ECO:0000269|PubMed:2392682}.
/FTId=VAR_003998.
VARIANT 150 150 M -> V (in GT; may confer constitutive
activity to the alpha-IIb/(mutated)beta-3
receptor; dbSNP:rs767548512).
{ECO:0000269|PubMed:15583747}.
/FTId=VAR_030476.
VARIANT 166 166 T -> I (associated with neonatal
thrombocytopenia; alloantigen Duv(a+);
does not affect significantly the
integrin function; dbSNP:rs74708909).
{ECO:0000269|PubMed:12036875}.
/FTId=VAR_030477.
VARIANT 169 169 R -> Q (in alloantigen HPA-4B;
dbSNP:rs5917).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:1430225}.
/FTId=VAR_003994.
VARIANT 188 188 S -> L (in GT; type II;
dbSNP:rs143146734).
{ECO:0000269|PubMed:9684783}.
/FTId=VAR_010651.
VARIANT 222 222 L -> P (in GT; variant form;
dbSNP:rs79208797).
{ECO:0000269|PubMed:11897046,
ECO:0000269|PubMed:20020534}.
/FTId=VAR_030478.
VARIANT 240 240 R -> Q (in GT; type B;
dbSNP:rs121918444).
{ECO:0000269|PubMed:1371279}.
/FTId=VAR_003999.
VARIANT 240 240 R -> W (in GT; variant Strasbourg-1;
dbSNP:rs121918446).
{ECO:0000269|PubMed:1602006}.
/FTId=VAR_004000.
VARIANT 242 242 R -> Q (in GT; dbSNP:rs377162158).
{ECO:0000269|PubMed:9215749}.
/FTId=VAR_030479.
VARIANT 243 243 D -> V (in GT).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030480.
VARIANT 247 247 G -> D (in GT; severe type 1 phenotype;
the mutation prevents normal ITGA2B/ITGB3
complex expression on the cell surface;
the mutation may interfere with correct
folding of the protein;
dbSNP:rs79560904).
{ECO:0000269|PubMed:20020534}.
/FTId=VAR_069922.
VARIANT 279 279 K -> M (in GT; severe type 1 phenotype;
the mutation prevents normal ITGA2B/ITGB3
complex expression on the cell surface;
the mutation interupts the interaction of
the ITGA2B/ITGB3 complex;
dbSNP:rs79775494).
{ECO:0000269|PubMed:20020534}.
/FTId=VAR_069923.
VARIANT 288 288 L -> P (in GT).
{ECO:0000269|PubMed:9215749}.
/FTId=VAR_030481.
VARIANT 306 306 H -> P (in GT; dbSNP:rs13306476).
{ECO:0000269|PubMed:15634267,
ECO:0000269|PubMed:9790984}.
/FTId=VAR_004001.
VARIANT 321 321 M -> L (in GT).
{ECO:0000269|PubMed:15748237}.
/FTId=VAR_030482.
VARIANT 330 330 I -> N (in GT; not expressed on the
surface and absent inside the transfected
cells). {ECO:0000269|PubMed:15634267}.
/FTId=VAR_030483.
VARIANT 400 400 C -> Y (in GT; dbSNP:rs121918449).
{ECO:0000269|PubMed:8781422}.
/FTId=VAR_004002.
VARIANT 433 433 P -> A (in alloantigen MO(+); in a case
of neonatal alloimmune thrombocytopenia;
dbSNP:rs121918448).
{ECO:0000269|PubMed:8093349}.
/FTId=VAR_003995.
VARIANT 453 453 V -> I (in dbSNP:rs5921).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_014178.
VARIANT 515 515 R -> Q (in alloantigen CA(+)/TU(+);
dbSNP:rs13306487).
{ECO:0000269|PubMed:7694683}.
/FTId=VAR_003996.
VARIANT 532 532 C -> Y (in GT).
{ECO:0000269|PubMed:12353082}.
/FTId=VAR_030484.
VARIANT 568 568 C -> R (in GT; type I).
{ECO:0000269|PubMed:10233432}.
/FTId=VAR_010671.
VARIANT 586 586 C -> F (in GT).
{ECO:0000269|PubMed:9790984}.
/FTId=VAR_004003.
VARIANT 586 586 C -> R (in GT; gain-of-function mutation;
constitutively binds ligand-induced
binding sites antibodies and the
fibrinogen-mimetic antibody PAC-1).
{ECO:0000269|PubMed:11588040}.
/FTId=VAR_030485.
VARIANT 598 598 G -> S (in GT).
{ECO:0000269|PubMed:9790984}.
/FTId=VAR_004004.
VARIANT 601 601 C -> R (in GT; dbSNP:rs747534508).
{ECO:0000269|PubMed:12083483}.
/FTId=VAR_030486.
VARIANT 605 605 G -> S (in GT; type II;
dbSNP:rs144884023).
{ECO:0000269|PubMed:9790984}.
/FTId=VAR_010672.
VARIANT 662 662 R -> C (in alloantigen SR(A);
dbSNP:rs151219882).
{ECO:0000269|PubMed:8132570}.
/FTId=VAR_003997.
VARIANT 749 749 D -> H (in BDPLT16; the mutant protein is
constitutively active;
dbSNP:rs398122372).
{ECO:0000269|PubMed:18065693}.
/FTId=VAR_069924.
VARIANT 778 778 S -> P (in GT; variant Strasbourg-1;
dbSNP:rs121918447).
{ECO:0000269|PubMed:1438206}.
/FTId=VAR_004005.
CONFLICT 12 12 A -> V (in Ref. 1; AAA52589 and 3;
AAA35927). {ECO:0000305}.
CONFLICT 151 151 K -> P (in Ref. 11; AAA67537 and 14;
AAB23689). {ECO:0000305}.
CONFLICT 205 205 D -> EY (in Ref. 11; AAA67537).
{ECO:0000305}.
CONFLICT 649 653 GALHD -> EPYMT (in Ref. 1; AAA52589, 2;
AAA60122 and 4; AAB71380). {ECO:0000305}.
CONFLICT 716 716 G -> H (in Ref. 8). {ECO:0000305}.
CONFLICT 737 741 ALLIW -> PCSSG (in Ref. 11; AAA67537).
{ECO:0000305}.
HELIX 30 33 {ECO:0000244|PDB:3T3P}.
HELIX 35 37 {ECO:0000244|PDB:4MMX}.
HELIX 39 45 {ECO:0000244|PDB:3T3P}.
STRAND 50 52 {ECO:0000244|PDB:3T3P}.
STRAND 54 57 {ECO:0000244|PDB:3IJE}.
STRAND 59 61 {ECO:0000244|PDB:2VDO}.
STRAND 63 65 {ECO:0000244|PDB:3T3P}.
HELIX 67 72 {ECO:0000244|PDB:3T3P}.
HELIX 77 79 {ECO:0000244|PDB:3T3P}.
STRAND 86 91 {ECO:0000244|PDB:3T3P}.
STRAND 99 101 {ECO:0000244|PDB:3T3P}.
HELIX 103 105 {ECO:0000244|PDB:3ZE2}.
STRAND 109 111 {ECO:0000244|PDB:3NID}.
STRAND 113 118 {ECO:0000244|PDB:3T3P}.
STRAND 123 131 {ECO:0000244|PDB:3T3P}.
STRAND 138 145 {ECO:0000244|PDB:3T3P}.
HELIX 148 150 {ECO:0000244|PDB:3T3P}.
HELIX 151 156 {ECO:0000244|PDB:3T3P}.
TURN 157 159 {ECO:0000244|PDB:3T3P}.
HELIX 160 168 {ECO:0000244|PDB:3T3P}.
TURN 169 171 {ECO:0000244|PDB:3T3P}.
STRAND 175 182 {ECO:0000244|PDB:3T3P}.
TURN 188 190 {ECO:0000244|PDB:3T3P}.
HELIX 196 200 {ECO:0000244|PDB:3T3P}.
TURN 202 207 {ECO:0000244|PDB:3T3P}.
STRAND 215 224 {ECO:0000244|PDB:3T3P}.
HELIX 226 235 {ECO:0000244|PDB:3T3P}.
STRAND 242 246 {ECO:0000244|PDB:3T3P}.
HELIX 248 257 {ECO:0000244|PDB:3T3P}.
HELIX 259 262 {ECO:0000244|PDB:3T3P}.
STRAND 266 278 {ECO:0000244|PDB:3T3P}.
HELIX 285 289 {ECO:0000244|PDB:3T3P}.
STRAND 305 307 {ECO:0000244|PDB:5HDB}.
TURN 308 312 {ECO:0000244|PDB:3T3P}.
HELIX 318 327 {ECO:0000244|PDB:3T3P}.
STRAND 331 336 {ECO:0000244|PDB:3T3P}.
HELIX 338 340 {ECO:0000244|PDB:3T3P}.
HELIX 341 349 {ECO:0000244|PDB:3T3P}.
STRAND 355 358 {ECO:0000244|PDB:3T3P}.
TURN 361 363 {ECO:0000244|PDB:3ZE2}.
HELIX 366 377 {ECO:0000244|PDB:3T3P}.
STRAND 381 387 {ECO:0000244|PDB:3T3P}.
STRAND 392 400 {ECO:0000244|PDB:3T3P}.
TURN 401 403 {ECO:0000244|PDB:3T3P}.
STRAND 404 407 {ECO:0000244|PDB:3T3P}.
STRAND 411 415 {ECO:0000244|PDB:2VDR}.
STRAND 420 429 {ECO:0000244|PDB:3T3P}.
STRAND 434 444 {ECO:0000244|PDB:3T3P}.
STRAND 451 457 {ECO:0000244|PDB:3T3P}.
HELIX 462 466 {ECO:0000244|PDB:3T3P}.
STRAND 468 470 {ECO:0000244|PDB:3NID}.
TURN 472 478 {ECO:0000244|PDB:3T3P}.
STRAND 479 482 {ECO:0000244|PDB:3T3P}.
STRAND 485 488 {ECO:0000244|PDB:3T3P}.
STRAND 489 491 {ECO:0000244|PDB:3IJE}.
TURN 494 497 {ECO:0000244|PDB:3FCS}.
STRAND 500 504 {ECO:0000244|PDB:3IJE}.
STRAND 513 518 {ECO:0000244|PDB:3FCS}.
HELIX 520 523 {ECO:0000244|PDB:3FCS}.
STRAND 524 527 {ECO:0000244|PDB:3FCS}.
STRAND 529 534 {ECO:0000244|PDB:3FCS}.
STRAND 538 540 {ECO:0000244|PDB:4G1M}.
STRAND 542 544 {ECO:0000244|PDB:3IJE}.
STRAND 549 552 {ECO:0000244|PDB:3IJE}.
STRAND 556 561 {ECO:0000244|PDB:3FCS}.
HELIX 562 564 {ECO:0000244|PDB:3FCS}.
STRAND 565 569 {ECO:0000244|PDB:3FCS}.
STRAND 572 575 {ECO:0000244|PDB:3FCS}.
STRAND 579 584 {ECO:0000244|PDB:3FCS}.
TURN 591 593 {ECO:0000244|PDB:3FCS}.
STRAND 598 600 {ECO:0000244|PDB:3FCS}.
STRAND 602 604 {ECO:0000244|PDB:3FCS}.
STRAND 606 608 {ECO:0000244|PDB:3FCS}.
STRAND 611 613 {ECO:0000244|PDB:3FCS}.
TURN 616 618 {ECO:0000244|PDB:3IJE}.
STRAND 620 624 {ECO:0000244|PDB:1U8C}.
STRAND 628 630 {ECO:0000244|PDB:4G1E}.
TURN 633 635 {ECO:0000244|PDB:3FCS}.
HELIX 639 641 {ECO:0000244|PDB:3FCS}.
TURN 642 646 {ECO:0000244|PDB:3FCS}.
STRAND 649 655 {ECO:0000244|PDB:3FCS}.
TURN 658 660 {ECO:0000244|PDB:3FCS}.
STRAND 664 666 {ECO:0000244|PDB:3FCS}.
STRAND 669 671 {ECO:0000244|PDB:1M1X}.
STRAND 674 678 {ECO:0000244|PDB:3FCS}.
STRAND 680 684 {ECO:0000244|PDB:3FCS}.
STRAND 688 694 {ECO:0000244|PDB:3FCS}.
STRAND 698 700 {ECO:0000244|PDB:3FCS}.
STRAND 704 706 {ECO:0000244|PDB:3FCS}.
STRAND 707 710 {ECO:0000244|PDB:1U8C}.
STRAND 715 717 {ECO:0000244|PDB:2KNC}.
TURN 743 759 {ECO:0000244|PDB:1KUP}.
TURN 761 765 {ECO:0000244|PDB:1KUP}.
STRAND 767 770 {ECO:0000244|PDB:1S4X}.
HELIX 771 774 {ECO:0000244|PDB:1MK7}.
HELIX 776 779 {ECO:0000244|PDB:2LJD}.
TURN 782 786 {ECO:0000244|PDB:1S4X}.
SEQUENCE 788 AA; 87058 MW; F246623608E05F9E CRC64;
MRARPRPRPL WATVLALGAL AGVGVGGPNI CTTRGVSSCQ QCLAVSPMCA WCSDEALPLG
SPRCDLKENL LKDNCAPESI EFPVSEARVL EDRPLSDKGS GDSSQVTQVS PQRIALRLRP
DDSKNFSIQV RQVEDYPVDI YYLMDLSYSM KDDLWSIQNL GTKLATQMRK LTSNLRIGFG
AFVDKPVSPY MYISPPEALE NPCYDMKTTC LPMFGYKHVL TLTDQVTRFN EEVKKQSVSR
NRDAPEGGFD AIMQATVCDE KIGWRNDASH LLVFTTDAKT HIALDGRLAG IVQPNDGQCH
VGSDNHYSAS TTMDYPSLGL MTEKLSQKNI NLIFAVTENV VNLYQNYSEL IPGTTVGVLS
MDSSNVLQLI VDAYGKIRSK VELEVRDLPE ELSLSFNATC LNNEVIPGLK SCMGLKIGDT
VSFSIEAKVR GCPQEKEKSF TIKPVGFKDS LIVQVTFDCD CACQAQAEPN SHRCNNGNGT
FECGVCRCGP GWLGSQCECS EEDYRPSQQD ECSPREGQPV CSQRGECLCG QCVCHSSDFG
KITGKYCECD DFSCVRYKGE MCSGHGQCSC GDCLCDSDWT GYYCNCTTRT DTCMSSNGLL
CSGRGKCECG SCVCIQPGSY GDTCEKCPTC PDACTFKKEC VECKKFDRGA LHDENTCNRY
CRDEIESVKE LKDTGKDAVN CTYKNEDDCV VRFQYYEDSS GKSILYVVEE PECPKGPDIL
VVLLSVMGAI LLIGLAALLI WKLLITIHDR KEFAKFEEER ARAKWDTANN PLYKEATSTF
TNITYRGT


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