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Protein

Integrin beta-3

Gene

ITGB3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).2 PublicationsBy similarity9 Publications
(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).8 Publications

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • coreceptor activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • extracellular matrix binding Source: UniProtKB
  • fibronectin binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protease binding Source: UniProtKB
  • protein disulfide isomerase activity Source: UniProtKB
  • vascular endothelial growth factor receptor 2 binding Source: BHF-UCL
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • activation of protein kinase activity Source: BHF-UCL
  • angiogenesis involved in wound healing Source: BHF-UCL
  • apolipoprotein A-I-mediated signaling pathway Source: UniProtKB
  • blood coagulation Source: ProtInc
  • cell adhesion Source: ProtInc
  • cell adhesion mediated by integrin Source: UniProtKB
  • cell growth Source: UniProtKB
  • cell-matrix adhesion Source: UniProtKB
  • cell migration Source: UniProtKB
  • cell-substrate adhesion Source: UniProtKB
  • cell-substrate junction assembly Source: InterPro
  • extracellular matrix organization Source: Reactome
  • heterotypic cell-cell adhesion Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • leukocyte migration Source: Reactome
  • mesodermal cell differentiation Source: UniProtKB
  • negative chemotaxis Source: UniProtKB
  • negative regulation of lipid storage Source: BHF-UCL
  • negative regulation of lipid transport Source: BHF-UCL
  • negative regulation of lipoprotein metabolic process Source: BHF-UCL
  • negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
  • negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  • platelet activation Source: UniProtKB
  • platelet aggregation Source: UniProtKB
  • platelet degranulation Source: Reactome
  • positive regulation of endothelial cell migration Source: BHF-UCL
  • positive regulation of endothelial cell proliferation Source: BHF-UCL
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • regulation of bone resorption Source: BHF-UCL
  • smooth muscle cell migration Source: BHF-UCL
  • substrate adhesion-dependent cell spreading Source: UniProtKB
  • tube development Source: BHF-UCL
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
  • viral entry into host cell Source: UniProtKB
  • wound healing Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Integrin, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000056345-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1566948. Elastic fibre formation.
R-HSA-210990. PECAM1 interactions.
R-HSA-2129379. Molecules associated with elastic fibres.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445144. Signal transduction by L1.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SignaLinkiP05106.
SIGNORiP05106.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta-3
Alternative name(s):
Platelet membrane glycoprotein IIIa
Short name:
GPIIIa
CD_antigen: CD61
Gene namesi
Name:ITGB3
Synonyms:GP3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:6156. ITGB3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 718ExtracellularSequence analysisAdd BLAST692
Transmembranei719 – 741HelicalSequence analysisAdd BLAST23
Topological domaini742 – 788CytoplasmicSequence analysisAdd BLAST47

GO - Cellular componenti

  • alphav-beta3 integrin-IGF-1-IGF1R complex Source: UniProtKB
  • alphav-beta3 integrin-vitronectin complex Source: BHF-UCL
  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • filopodium membrane Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • integrin alphav-beta3 complex Source: UniProtKB
  • integrin complex Source: BHF-UCL
  • lamellipodium membrane Source: UniProtKB
  • melanosome Source: UniProtKB
  • microvillus membrane Source: UniProtKB
  • nucleus Source: MGI
  • plasma membrane Source: UniProtKB
  • platelet alpha granule membrane Source: Reactome
  • receptor complex Source: MGI
  • ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Involvement in diseasei

Glanzmann thrombasthenia (GT)18 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:273800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06992064C → Y in GT; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression. 1 PublicationCorresponds to variant rs74554539dbSNPEnsembl.1
Natural variantiVAR_030473119R → W in GT. 1 PublicationCorresponds to variant rs781062792dbSNPEnsembl.1
Natural variantiVAR_030474141Y → C in GT. 1 Publication1
Natural variantiVAR_010649143L → W in GT. 1 PublicationCorresponds to variant rs121918452dbSNPEnsembl.1
Natural variantiVAR_069921144M → R in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface. 1 PublicationCorresponds to variant rs77963874dbSNPEnsembl.1
Natural variantiVAR_030475145D → N in GT. 1 Publication1
Natural variantiVAR_003998145D → Y in GT; type B. 1 PublicationCorresponds to variant rs121918445dbSNPEnsembl.1
Natural variantiVAR_030476150M → V in GT; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor. 1 PublicationCorresponds to variant rs767548512dbSNPEnsembl.1
Natural variantiVAR_010651188S → L in GT; type II. 1 PublicationCorresponds to variant rs143146734dbSNPEnsembl.1
Natural variantiVAR_030478222L → P in GT; variant form. 2 PublicationsCorresponds to variant rs79208797dbSNPEnsembl.1
Natural variantiVAR_003999240R → Q in GT; type B. 1 PublicationCorresponds to variant rs121918444dbSNPEnsembl.1
Natural variantiVAR_004000240R → W in GT; variant Strasbourg-1. 1 PublicationCorresponds to variant rs121918446dbSNPEnsembl.1
Natural variantiVAR_030479242R → Q in GT. 1 PublicationCorresponds to variant rs377162158dbSNPEnsembl.1
Natural variantiVAR_030480243D → V in GT. 1 Publication1
Natural variantiVAR_069922247G → 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. 1 PublicationCorresponds to variant rs79560904dbSNPEnsembl.1
Natural variantiVAR_069923279K → 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. 1 PublicationCorresponds to variant rs79775494dbSNPEnsembl.1
Natural variantiVAR_030481288L → P in GT. 1 Publication1
Natural variantiVAR_004001306H → P in GT. 2 PublicationsCorresponds to variant rs13306476dbSNPEnsembl.1
Natural variantiVAR_030482321M → L in GT. 1 Publication1
Natural variantiVAR_030483330I → N in GT; not expressed on the surface and absent inside the transfected cells. 1 Publication1
Natural variantiVAR_004002400C → Y in GT. 1 PublicationCorresponds to variant rs121918449dbSNPEnsembl.1
Natural variantiVAR_030484532C → Y in GT. 1 Publication1
Natural variantiVAR_010671568C → R in GT; type I. 1 Publication1
Natural variantiVAR_004003586C → F in GT. 1 Publication1
Natural variantiVAR_030485586C → R in GT; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1. 1 Publication1
Natural variantiVAR_004004598G → S in GT. 1 Publication1
Natural variantiVAR_030486601C → R in GT. 1 PublicationCorresponds to variant rs747534508dbSNPEnsembl.1
Natural variantiVAR_010672605G → S in GT; type II. 1 PublicationCorresponds to variant rs144884023dbSNPEnsembl.1
Natural variantiVAR_004005778S → P in GT; variant Strasbourg-1. 1 PublicationCorresponds to variant rs121918447dbSNPEnsembl.1
Bleeding disorder, platelet-type 16 (BDPLT16)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:187800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069924749D → H in BDPLT16; the mutant protein is constitutively active. 1 PublicationCorresponds to variant rs398122372dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3690.
MalaCardsiITGB3.
MIMi173470. gene+phenotype.
187800. phenotype.
273800. phenotype.
OpenTargetsiENSG00000259207.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBiPA205.

Chemistry databases

ChEMBLiCHEMBL2093869.
DrugBankiDB00054. Abciximab.
DB00098. Anti-thymocyte Globulin (Rabbit).
DB00063. Eptifibatide.
DB00775. Tirofiban.

Polymorphism and mutation databases

BioMutaiITGB3.
DMDMi125987835.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001634427 – 788Integrin beta-3Add BLAST762

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi31 ↔ 4611 Publication
Disulfide bondi39 ↔ 491 Publication
Disulfide bondi42 ↔ 751 Publication
Disulfide bondi52 ↔ 641 Publication
Glycosylationi125N-linked (GlcNAc...)2 Publications1
Disulfide bondi203 ↔ 2101 Publication
Disulfide bondi258 ↔ 2991 Publication
Glycosylationi346N-linked (GlcNAc...)Sequence analysis1 Publication1
Glycosylationi397N-linked (GlcNAc...)Sequence analysis1 Publication1
Disulfide bondi400 ↔ 4121 Publication
Disulfide bondi432 ↔ 6811 Publication
Disulfide bondi459 ↔ 4631 Publication
Disulfide bondi474 ↔ 4861 Publication
Glycosylationi478N-linked (GlcNAc...)1
Disulfide bondi483 ↔ 5211 Publication
Disulfide bondi488 ↔ 4971 Publication
Disulfide bondi499 ↔ 5121 Publication
Disulfide bondi527 ↔ 5321 Publication
Disulfide bondi529 ↔ 5621 Publication
Disulfide bondi534 ↔ 5471 Publication
Disulfide bondi549 ↔ 5541 Publication
Disulfide bondi568 ↔ 5731 Publication
Disulfide bondi570 ↔ 6011 Publication
Disulfide bondi575 ↔ 5841 Publication
Glycosylationi585N-linked (GlcNAc...)Sequence analysis1 Publication1
Disulfide bondi586 ↔ 5931 Publication
Disulfide bondi607 ↔ 6121 Publication
Disulfide bondi609 ↔ 6571 Publication
Disulfide bondi614 ↔ 6241 Publication
Disulfide bondi627 ↔ 6301 Publication
Disulfide bondi634 ↔ 6431 Publication
Disulfide bondi640 ↔ 7131 Publication
Disulfide bondi661 ↔ 6891 Publication
Glycosylationi680N-linked (GlcNAc...)2 Publications1
Modified residuei767PhosphothreonineBy similarity1
Modified residuei773PhosphotyrosineCombined sources1
Modified residuei779Phosphothreonine; by PDPK1 and PKB/AKT1; in vitro1 Publication1
Modified residuei785Phosphotyrosine1 Publication1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP05106.
MaxQBiP05106.
PaxDbiP05106.
PeptideAtlasiP05106.
PRIDEiP05106.

PTM databases

iPTMnetiP05106.
PhosphoSitePlusiP05106.

Miscellaneous databases

PMAP-CutDBP05106.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiENSG00000259207.
CleanExiHS_ITGB3.
ExpressionAtlasiP05106. baseline and differential.
GenevisibleiP05106. HS.

Organism-specific databases

HPAiHPA027852.

Interactioni

Subunit structurei

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).By similarity14 Publications
(Microbial infection) Integrin ITGAV:ITGB3 interacts with herpes virus 8/HHV-8 glycoprotein B.1 Publication
(Microbial infection) Integrin ITGAV:ITGB3 interacts with coxsackievirus A9 capsid proteins.1 Publication
(Microbial infection) Interacts with Hantaan virus glycoprotein G.1 Publication
(Microbial infection) Integrin ITGAV:ITGB3 interacts with cytomegalovirus/HHV-5 gH:gL proteins.1 Publication
(Microbial infection) Integrin ITGA5:ITGB3 interacts with human metapneumovirus fusion protein.1 Publication
(Microbial infection) Integrin ITGAV:ITGB3 interacts with human parechovirus 1 capsid proteins.1 Publication
(Microbial infection) Integrin ITGAV:ITGB3 interacts with west nile virus envelope protein E.1 Publication
(Microbial infection) Interacts with HIV-1 Tat (PubMed:10397733). ITGAV:ITGB3 interacts with AGRA2 (PubMed:16982628).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-702847,EBI-702847
P069354EBI-702847,EBI-981051From a different organism.
ACTN1P050942EBI-702847,EBI-5847257From a different organism.
gBF5HB812EBI-702847,EBI-9027696From a different organism.
ITGA2BP0851411EBI-702847,EBI-702693
ITGAVP0675611EBI-702847,EBI-298282
Prkd1Q621012EBI-702847,EBI-6903636From a different organism.
PTPN1P180314EBI-702847,EBI-968788
SrcP054805EBI-702847,EBI-298680From a different organism.
TLN1P549392EBI-702847,EBI-1035421From a different organism.
TLN1Q9Y4904EBI-702847,EBI-2462036
Tln1P260393EBI-702847,EBI-1039593From a different organism.

GO - Molecular functioni

  • cell adhesion molecule binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • fibronectin binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protease binding Source: UniProtKB
  • vascular endothelial growth factor receptor 2 binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi109896. 18 interactors.
DIPiDIP-304N.
IntActiP05106. 19 interactors.
MINTiMINT-209501.
STRINGi9606.ENSP00000262017.

Chemistry databases

BindingDBiP05106.

Structurei

Secondary structure

1788
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 33Combined sources4
Helixi35 – 37Combined sources3
Helixi39 – 45Combined sources7
Beta strandi50 – 52Combined sources3
Beta strandi54 – 57Combined sources4
Beta strandi59 – 61Combined sources3
Beta strandi63 – 65Combined sources3
Helixi67 – 72Combined sources6
Helixi77 – 79Combined sources3
Beta strandi86 – 91Combined sources6
Beta strandi99 – 101Combined sources3
Helixi103 – 105Combined sources3
Beta strandi109 – 111Combined sources3
Beta strandi113 – 118Combined sources6
Beta strandi123 – 131Combined sources9
Beta strandi138 – 145Combined sources8
Helixi148 – 150Combined sources3
Helixi151 – 156Combined sources6
Turni157 – 159Combined sources3
Helixi160 – 168Combined sources9
Turni169 – 171Combined sources3
Beta strandi175 – 182Combined sources8
Turni188 – 190Combined sources3
Helixi196 – 200Combined sources5
Turni202 – 207Combined sources6
Beta strandi215 – 224Combined sources10
Helixi226 – 235Combined sources10
Beta strandi242 – 246Combined sources5
Helixi248 – 257Combined sources10
Helixi259 – 262Combined sources4
Beta strandi266 – 278Combined sources13
Helixi285 – 289Combined sources5
Beta strandi305 – 307Combined sources3
Turni308 – 312Combined sources5
Helixi318 – 327Combined sources10
Beta strandi331 – 336Combined sources6
Helixi338 – 340Combined sources3
Helixi341 – 349Combined sources9
Beta strandi355 – 358Combined sources4
Turni361 – 363Combined sources3
Helixi366 – 377Combined sources12
Beta strandi381 – 387Combined sources7
Beta strandi392 – 400Combined sources9
Turni401 – 403Combined sources3
Beta strandi404 – 407Combined sources4
Beta strandi411 – 415Combined sources5
Beta strandi420 – 429Combined sources10
Beta strandi434 – 444Combined sources11
Beta strandi451 – 457Combined sources7
Helixi462 – 466Combined sources5
Beta strandi468 – 470Combined sources3
Turni472 – 478Combined sources7
Beta strandi479 – 482Combined sources4
Beta strandi485 – 488Combined sources4
Beta strandi489 – 491Combined sources3
Turni494 – 497Combined sources4
Beta strandi500 – 504Combined sources5
Beta strandi513 – 518Combined sources6
Helixi520 – 523Combined sources4
Beta strandi524 – 527Combined sources4
Beta strandi529 – 534Combined sources6
Beta strandi538 – 540Combined sources3
Beta strandi542 – 544Combined sources3
Beta strandi549 – 552Combined sources4
Beta strandi556 – 561Combined sources6
Helixi562 – 564Combined sources3
Beta strandi565 – 569Combined sources5
Beta strandi572 – 575Combined sources4
Beta strandi579 – 584Combined sources6
Turni591 – 593Combined sources3
Beta strandi598 – 600Combined sources3
Beta strandi602 – 604Combined sources3
Beta strandi606 – 608Combined sources3
Beta strandi611 – 613Combined sources3
Turni616 – 618Combined sources3
Beta strandi620 – 624Combined sources5
Beta strandi628 – 630Combined sources3
Turni633 – 635Combined sources3
Helixi639 – 641Combined sources3
Turni642 – 646Combined sources5
Beta strandi649 – 655Combined sources7
Turni658 – 660Combined sources3
Beta strandi664 – 666Combined sources3
Beta strandi669 – 671Combined sources3
Beta strandi674 – 678Combined sources5
Beta strandi680 – 684Combined sources5
Beta strandi688 – 694Combined sources7
Beta strandi698 – 700Combined sources3
Beta strandi704 – 706Combined sources3
Beta strandi707 – 710Combined sources4
Beta strandi715 – 717Combined sources3
Turni743 – 759Combined sources17
Turni761 – 765Combined sources5
Beta strandi767 – 770Combined sources4
Helixi771 – 774Combined sources4
Helixi776 – 779Combined sources4
Turni782 – 786Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JV2X-ray3.10B27-718[»]
1KUPNMR-B742-766[»]
1KUZNMR-B742-766[»]
1L5GX-ray3.20B27-718[»]
1M1XX-ray3.30B27-718[»]
1M8ONMR-B742-788[»]
1MIZX-ray1.90A765-769[»]
1MK7X-ray2.20A/C765-775[»]
1MK9X-ray2.80A/C/E/G765-776[»]
1RN0model-B135-378[»]
1S4XNMR-A742-788[»]
1TYEX-ray2.90B/D/F27-466[»]
1U8CX-ray3.10B27-718[»]
2INImodel-B81-460[»]
B558-716[»]
2K9JNMR-B711-753[»]
2KNCNMR-B715-788[»]
2KV9NMR-B739-788[»]
2L1CNMR-B762-788[»]
2L91NMR-A711-753[»]
2LJDNMR-A742-788[»]
2LJENMR-A742-788[»]
2LJFNMR-A742-788[»]
2MTPNMR-C742-788[»]
2N9YNMR-B712-753[»]
2Q6WX-ray2.25C/F50-61[»]
2RMZNMR-A711-753[»]
2RN0NMR-A711-753[»]
2VC2X-ray3.10B27-487[»]
2VDKX-ray2.80B27-487[»]
2VDLX-ray2.75B27-487[»]
2VDMX-ray2.90B27-487[»]
2VDNX-ray2.90B27-487[»]
2VDOX-ray2.51B27-487[»]
2VDPX-ray2.80B27-487[»]
2VDQX-ray2.59B27-487[»]
2VDRX-ray2.40B27-487[»]
3FCSX-ray2.55B/D27-716[»]
3FCUX-ray2.90B/D/F27-487[»]
3IJEX-ray2.90B27-721[»]
3NIDX-ray2.30B/D27-497[»]
3NIFX-ray2.40B/D27-497[»]
3NIGX-ray2.25B/D27-497[»]
3T3MX-ray2.60B/D27-498[»]
3T3PX-ray2.20B/D27-498[»]
3ZDXX-ray2.45B/D27-498[»]
3ZDYX-ray2.45B/D27-498[»]
3ZDZX-ray2.75B/D27-498[»]
3ZE0X-ray2.95B/D27-498[»]
3ZE1X-ray3.00B/D27-498[»]
3ZE2X-ray2.35B/D27-498[»]
4CAKelectron microscopy20.50B27-716[»]
4G1EX-ray3.00B27-717[»]
4G1MX-ray2.90B27-718[»]
4MMXX-ray3.32B27-718[»]
4MMYX-ray3.18B27-718[»]
4MMZX-ray3.10B27-718[»]
4O02X-ray3.60B27-718[»]
4Z7NX-ray2.60B/D29-497[»]
4Z7OX-ray2.85B/D29-497[»]
4Z7QX-ray2.70B/D27-497[»]
5HDBX-ray2.70B/D27-497[»]
ProteinModelPortaliP05106.
SMRiP05106.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05106.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini135 – 377VWFAAdd BLAST243
Repeati463 – 511IAdd BLAST49
Repeati512 – 553IIAdd BLAST42
Repeati554 – 592IIIAdd BLAST39
Repeati593 – 629IVAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni203 – 210Involved in CX3CL1-, NRG1-, FGF1- and IGF1-binding4 Publications8
Regioni293 – 313CX3CL1-binding1 PublicationAdd BLAST21
Regioni463 – 629Cysteine-rich tandem repeatsAdd BLAST167

Sequence similaritiesi

Belongs to the integrin beta chain family.Curated
Contains 1 VWFA domain.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOVERGENiHBG006190.
InParanoidiP05106.
KOiK06493.
OMAiGHGQCSC.
OrthoDBiEOG091G029W.
PhylomeDBiP05106.
TreeFamiTF105392.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR033760. Integin_beta_N.
IPR027068. Integrin_beta-3.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR016201. PSI.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF25. PTHR10082:SF25. 1 hit.
PfamiPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
PF17205. PSI_integrin. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Beta-3A (identifier: P05106-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRARPRPRPL WATVLALGAL AGVGVGGPNI CTTRGVSSCQ QCLAVSPMCA
60 70 80 90 100
WCSDEALPLG SPRCDLKENL LKDNCAPESI EFPVSEARVL EDRPLSDKGS
110 120 130 140 150
GDSSQVTQVS PQRIALRLRP DDSKNFSIQV RQVEDYPVDI YYLMDLSYSM
160 170 180 190 200
KDDLWSIQNL GTKLATQMRK LTSNLRIGFG AFVDKPVSPY MYISPPEALE
210 220 230 240 250
NPCYDMKTTC LPMFGYKHVL TLTDQVTRFN EEVKKQSVSR NRDAPEGGFD
260 270 280 290 300
AIMQATVCDE KIGWRNDASH LLVFTTDAKT HIALDGRLAG IVQPNDGQCH
310 320 330 340 350
VGSDNHYSAS TTMDYPSLGL MTEKLSQKNI NLIFAVTENV VNLYQNYSEL
360 370 380 390 400
IPGTTVGVLS MDSSNVLQLI VDAYGKIRSK VELEVRDLPE ELSLSFNATC
410 420 430 440 450
LNNEVIPGLK SCMGLKIGDT VSFSIEAKVR GCPQEKEKSF TIKPVGFKDS
460 470 480 490 500
LIVQVTFDCD CACQAQAEPN SHRCNNGNGT FECGVCRCGP GWLGSQCECS
510 520 530 540 550
EEDYRPSQQD ECSPREGQPV CSQRGECLCG QCVCHSSDFG KITGKYCECD
560 570 580 590 600
DFSCVRYKGE MCSGHGQCSC GDCLCDSDWT GYYCNCTTRT DTCMSSNGLL
610 620 630 640 650
CSGRGKCECG SCVCIQPGSY GDTCEKCPTC PDACTFKKEC VECKKFDRGA
660 670 680 690 700
LHDENTCNRY CRDEIESVKE LKDTGKDAVN CTYKNEDDCV VRFQYYEDSS
710 720 730 740 750
GKSILYVVEE PECPKGPDIL VVLLSVMGAI LLIGLAALLI WKLLITIHDR
760 770 780
KEFAKFEEER ARAKWDTANN PLYKEATSTF TNITYRGT
Length:788
Mass (Da):87,058
Last modified:February 6, 2007 - v2
Checksum:iF246623608E05F9E
GO
Isoform Beta-3B (identifier: P05106-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     768-788: ANNPLYKEATSTFTNITYRGT → VRDGAGRFLKSLV

Show »
Length:780
Mass (Da):86,113
Checksum:iC21A1B7814080CD7
GO
Isoform Beta-3C (identifier: P05106-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     768-788: ANNPLYKEATSTFTNITYRGT → HYAQSLRKWNQPVSIDG

Show »
Length:784
Mass (Da):86,694
Checksum:iB8A9F2A7F3C39247
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12A → V in AAA52589 (PubMed:3494014).Curated1
Sequence conflicti12A → V in AAA35927 (PubMed:2345548).Curated1
Sequence conflicti151K → P in AAA67537 (PubMed:2341395).Curated1
Sequence conflicti151K → P in AAB23689 (PubMed:1382574).Curated1
Sequence conflicti205D → EY in AAA67537 (PubMed:2341395).Curated1
Sequence conflicti649 – 653GALHD → EPYMT in AAA52589 (PubMed:3494014).Curated5
Sequence conflicti649 – 653GALHD → EPYMT in AAA60122 (PubMed:2452834).Curated5
Sequence conflicti649 – 653GALHD → EPYMT in AAB71380 (PubMed:9195946).Curated5
Sequence conflicti716G → H (PubMed:3165296).Curated1
Sequence conflicti737 – 741ALLIW → PCSSG in AAA67537 (PubMed:2341395).Curated5

Polymorphismi

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).
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).
Position 433 is associated with platelet-specific alloantigen MO. MO- has Pro-433 and MO+ has Ala-433. MO+ is involved in NAIT.
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.
Position 662 is associated with platelet-specific alloantigen SR(A). SR(A)- has Arg-662 and SR(A)+ has Cys-662.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00399359L → P in alloantigen HPA-1B. 3 PublicationsCorresponds to variant rs5918dbSNPEnsembl.1
Natural variantiVAR_06992064C → Y in GT; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression. 1 PublicationCorresponds to variant rs74554539dbSNPEnsembl.1
Natural variantiVAR_04963366L → R.1 PublicationCorresponds to variant rs36080296dbSNPEnsembl.1
Natural variantiVAR_030473119R → W in GT. 1 PublicationCorresponds to variant rs781062792dbSNPEnsembl.1
Natural variantiVAR_030474141Y → C in GT. 1 Publication1
Natural variantiVAR_010649143L → W in GT. 1 PublicationCorresponds to variant rs121918452dbSNPEnsembl.1
Natural variantiVAR_069921144M → R in GT; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface. 1 PublicationCorresponds to variant rs77963874dbSNPEnsembl.1
Natural variantiVAR_030475145D → N in GT. 1 Publication1
Natural variantiVAR_003998145D → Y in GT; type B. 1 PublicationCorresponds to variant rs121918445dbSNPEnsembl.1
Natural variantiVAR_030476150M → V in GT; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor. 1 PublicationCorresponds to variant rs767548512dbSNPEnsembl.1
Natural variantiVAR_030477166T → I Associated with neonatal thrombocytopenia; alloantigen Duv(a+); does not affect significantly the integrin function. 1 PublicationCorresponds to variant rs74708909dbSNPEnsembl.1
Natural variantiVAR_003994169R → Q in alloantigen HPA-4B. 2 PublicationsCorresponds to variant rs5917dbSNPEnsembl.1
Natural variantiVAR_010651188S → L in GT; type II. 1 PublicationCorresponds to variant rs143146734dbSNPEnsembl.1
Natural variantiVAR_030478222L → P in GT; variant form. 2 PublicationsCorresponds to variant rs79208797dbSNPEnsembl.1
Natural variantiVAR_003999240R → Q in GT; type B. 1 PublicationCorresponds to variant rs121918444dbSNPEnsembl.1
Natural variantiVAR_004000240R → W in GT; variant Strasbourg-1. 1 PublicationCorresponds to variant rs121918446dbSNPEnsembl.1
Natural variantiVAR_030479242R → Q in GT. 1 PublicationCorresponds to variant rs377162158dbSNPEnsembl.1
Natural variantiVAR_030480243D → V in GT. 1 Publication1
Natural variantiVAR_069922247G → 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. 1 PublicationCorresponds to variant rs79560904dbSNPEnsembl.1
Natural variantiVAR_069923279K → 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. 1 PublicationCorresponds to variant rs79775494dbSNPEnsembl.1
Natural variantiVAR_030481288L → P in GT. 1 Publication1
Natural variantiVAR_004001306H → P in GT. 2 PublicationsCorresponds to variant rs13306476dbSNPEnsembl.1
Natural variantiVAR_030482321M → L in GT. 1 Publication1
Natural variantiVAR_030483330I → N in GT; not expressed on the surface and absent inside the transfected cells. 1 Publication1
Natural variantiVAR_004002400C → Y in GT. 1 PublicationCorresponds to variant rs121918449dbSNPEnsembl.1
Natural variantiVAR_003995433P → A in alloantigen MO(+); in a case of neonatal alloimmune thrombocytopenia. 1 PublicationCorresponds to variant rs121918448dbSNPEnsembl.1
Natural variantiVAR_014178453V → I.1 PublicationCorresponds to variant rs5921dbSNPEnsembl.1
Natural variantiVAR_003996515R → Q in alloantigen CA(+)/TU(+). 1 PublicationCorresponds to variant rs13306487dbSNPEnsembl.1
Natural variantiVAR_030484532C → Y in GT. 1 Publication1
Natural variantiVAR_010671568C → R in GT; type I. 1 Publication1
Natural variantiVAR_004003586C → F in GT. 1 Publication1
Natural variantiVAR_030485586C → R in GT; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1. 1 Publication1
Natural variantiVAR_004004598G → S in GT. 1 Publication1
Natural variantiVAR_030486601C → R in GT. 1 PublicationCorresponds to variant rs747534508dbSNPEnsembl.1
Natural variantiVAR_010672605G → S in GT; type II. 1 PublicationCorresponds to variant rs144884023dbSNPEnsembl.1
Natural variantiVAR_003997662R → C in alloantigen SR(A). 1 PublicationCorresponds to variant rs151219882dbSNPEnsembl.1
Natural variantiVAR_069924749D → H in BDPLT16; the mutant protein is constitutively active. 1 PublicationCorresponds to variant rs398122372dbSNPEnsembl.1
Natural variantiVAR_004005778S → P in GT; variant Strasbourg-1. 1 PublicationCorresponds to variant rs121918447dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002745768 – 788ANNPL…TYRGT → VRDGAGRFLKSLV in isoform Beta-3B. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_002746768 – 788ANNPL…TYRGT → HYAQSLRKWNQPVSIDG in isoform Beta-3C. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02703 mRNA. Translation: AAA52589.1.
M20311 mRNA. Translation: AAA60122.1.
M35999 mRNA. Translation: AAA35927.1.
U95204 mRNA. Translation: AAB71380.1.
CH471231 Genomic DNA. Translation: EAW57682.1.
BC127666 mRNA. Translation: AAI27667.1.
BC127667 mRNA. Translation: AAI27668.1.
L28832 Genomic DNA. Translation: AAA20880.2.
M32686
, M32667, M32672, M32673, M32674, M32675, M32680, M32681, M32682, M32685 Genomic DNA. Translation: AAA67537.1.
M57494
, M57481, M57482, M57483, M57484, M57485, M57486, M57487, M57488, M57489, M57490, M57491, M57492, M57493 Genomic DNA. Translation: AAA52600.1.
U03881 Genomic DNA. Translation: AAA16076.1.
S49379 Genomic DNA. Translation: AAB23689.2.
M25108 mRNA. Translation: AAA36121.1.
CCDSiCCDS11511.1. [P05106-1]
PIRiA26547.
A60798.
B36268.
I77349.
S14324.
RefSeqiNP_000203.2. NM_000212.2. [P05106-1]
UniGeneiHs.218040.

Genome annotation databases

EnsembliENST00000559488; ENSP00000452786; ENSG00000259207. [P05106-1]
GeneIDi3690.
KEGGihsa:3690.
UCSCiuc002ilj.4. human. [P05106-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02703 mRNA. Translation: AAA52589.1.
M20311 mRNA. Translation: AAA60122.1.
M35999 mRNA. Translation: AAA35927.1.
U95204 mRNA. Translation: AAB71380.1.
CH471231 Genomic DNA. Translation: EAW57682.1.
BC127666 mRNA. Translation: AAI27667.1.
BC127667 mRNA. Translation: AAI27668.1.
L28832 Genomic DNA. Translation: AAA20880.2.
M32686
, M32667, M32672, M32673, M32674, M32675, M32680, M32681, M32682, M32685 Genomic DNA. Translation: AAA67537.1.
M57494
, M57481, M57482, M57483, M57484, M57485, M57486, M57487, M57488, M57489, M57490, M57491, M57492, M57493 Genomic DNA. Translation: AAA52600.1.
U03881 Genomic DNA. Translation: AAA16076.1.
S49379 Genomic DNA. Translation: AAB23689.2.
M25108 mRNA. Translation: AAA36121.1.
CCDSiCCDS11511.1. [P05106-1]
PIRiA26547.
A60798.
B36268.
I77349.
S14324.
RefSeqiNP_000203.2. NM_000212.2. [P05106-1]
UniGeneiHs.218040.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JV2X-ray3.10B27-718[»]
1KUPNMR-B742-766[»]
1KUZNMR-B742-766[»]
1L5GX-ray3.20B27-718[»]
1M1XX-ray3.30B27-718[»]
1M8ONMR-B742-788[»]
1MIZX-ray1.90A765-769[»]
1MK7X-ray2.20A/C765-775[»]
1MK9X-ray2.80A/C/E/G765-776[»]
1RN0model-B135-378[»]
1S4XNMR-A742-788[»]
1TYEX-ray2.90B/D/F27-466[»]
1U8CX-ray3.10B27-718[»]
2INImodel-B81-460[»]
B558-716[»]
2K9JNMR-B711-753[»]
2KNCNMR-B715-788[»]
2KV9NMR-B739-788[»]
2L1CNMR-B762-788[»]
2L91NMR-A711-753[»]
2LJDNMR-A742-788[»]
2LJENMR-A742-788[»]
2LJFNMR-A742-788[»]
2MTPNMR-C742-788[»]
2N9YNMR-B712-753[»]
2Q6WX-ray2.25C/F50-61[»]
2RMZNMR-A711-753[»]
2RN0NMR-A711-753[»]
2VC2X-ray3.10B27-487[»]
2VDKX-ray2.80B27-487[»]
2VDLX-ray2.75B27-487[»]
2VDMX-ray2.90B27-487[»]
2VDNX-ray2.90B27-487[»]
2VDOX-ray2.51B27-487[»]
2VDPX-ray2.80B27-487[»]
2VDQX-ray2.59B27-487[»]
2VDRX-ray2.40B27-487[»]
3FCSX-ray2.55B/D27-716[»]
3FCUX-ray2.90B/D/F27-487[»]
3IJEX-ray2.90B27-721[»]
3NIDX-ray2.30B/D27-497[»]
3NIFX-ray2.40B/D27-497[»]
3NIGX-ray2.25B/D27-497[»]
3T3MX-ray2.60B/D27-498[»]
3T3PX-ray2.20B/D27-498[»]
3ZDXX-ray2.45B/D27-498[»]
3ZDYX-ray2.45B/D27-498[»]
3ZDZX-ray2.75B/D27-498[»]
3ZE0X-ray2.95B/D27-498[»]
3ZE1X-ray3.00B/D27-498[»]
3ZE2X-ray2.35B/D27-498[»]
4CAKelectron microscopy20.50B27-716[»]
4G1EX-ray3.00B27-717[»]
4G1MX-ray2.90B27-718[»]
4MMXX-ray3.32B27-718[»]
4MMYX-ray3.18B27-718[»]
4MMZX-ray3.10B27-718[»]
4O02X-ray3.60B27-718[»]
4Z7NX-ray2.60B/D29-497[»]
4Z7OX-ray2.85B/D29-497[»]
4Z7QX-ray2.70B/D27-497[»]
5HDBX-ray2.70B/D27-497[»]
ProteinModelPortaliP05106.
SMRiP05106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109896. 18 interactors.
DIPiDIP-304N.
IntActiP05106. 19 interactors.
MINTiMINT-209501.
STRINGi9606.ENSP00000262017.

Chemistry databases

BindingDBiP05106.
ChEMBLiCHEMBL2093869.
DrugBankiDB00054. Abciximab.
DB00098. Anti-thymocyte Globulin (Rabbit).
DB00063. Eptifibatide.
DB00775. Tirofiban.

PTM databases

iPTMnetiP05106.
PhosphoSitePlusiP05106.

Polymorphism and mutation databases

BioMutaiITGB3.
DMDMi125987835.

Proteomic databases

EPDiP05106.
MaxQBiP05106.
PaxDbiP05106.
PeptideAtlasiP05106.
PRIDEiP05106.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000559488; ENSP00000452786; ENSG00000259207. [P05106-1]
GeneIDi3690.
KEGGihsa:3690.
UCSCiuc002ilj.4. human. [P05106-1]

Organism-specific databases

CTDi3690.
DisGeNETi3690.
GeneCardsiITGB3.
HGNCiHGNC:6156. ITGB3.
HPAiHPA027852.
MalaCardsiITGB3.
MIMi173470. gene+phenotype.
187800. phenotype.
273800. phenotype.
neXtProtiNX_P05106.
OpenTargetsiENSG00000259207.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
853. Fetal and neonatal alloimmune thrombocytopenia.
849. Glanzmann thrombasthenia.
PharmGKBiPA205.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOVERGENiHBG006190.
InParanoidiP05106.
KOiK06493.
OMAiGHGQCSC.
OrthoDBiEOG091G029W.
PhylomeDBiP05106.
TreeFamiTF105392.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000056345-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-1566948. Elastic fibre formation.
R-HSA-210990. PECAM1 interactions.
R-HSA-2129379. Molecules associated with elastic fibres.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-354194. GRB2:SOS provides linkage to MAPK signaling for Integrins.
R-HSA-372708. p130Cas linkage to MAPK signaling for integrins.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445144. Signal transduction by L1.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
SignaLinkiP05106.
SIGNORiP05106.

Miscellaneous databases

ChiTaRSiITGB3. human.
EvolutionaryTraceiP05106.
GeneWikiiCD61.
GenomeRNAii3690.
PMAP-CutDBP05106.
PROiP05106.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000259207.
CleanExiHS_ITGB3.
ExpressionAtlasiP05106. baseline and differential.
GenevisibleiP05106. HS.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR033760. Integin_beta_N.
IPR027068. Integrin_beta-3.
IPR015812. Integrin_bsu.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR016201. PSI.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF25. PTHR10082:SF25. 1 hit.
PfamiPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
PF17205. PSI_integrin. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITB3_HUMAN
AccessioniPrimary (citable) accession number: P05106
Secondary accession number(s): A0PJW2
, D3DXJ8, O15495, Q12806, Q13413, Q14648, Q16499
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 6, 2007
Last modified: November 30, 2016
This is version 231 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Metallothioneins
    Classification of metallothioneins and list of entries
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.