P05106 · ITB3_HUMAN
- ProteinIntegrin beta-3
- GeneITGB3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids788 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 FGF2 and this binding is essential for FGF2 signaling (PubMed:28302677).
ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119).
ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464).
ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (PubMed:29030430).
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).
In brain, plays a role in synaptic transmission and plasticity. Involved in the regulation of the serotonin neurotransmission, is required to localize to specific compartments within the synapse the serotonin receptor SLC6A4 and for an appropriate reuptake of serotonin. Controls excitatory synaptic strength by regulating GRIA2-containing AMPAR endocytosis, which affects AMPAR abundance and composition (By similarity).
ITGAV:ITGB3 act as a receptor for CD40LG (PubMed:31331973).
ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and migration to IBSP (PubMed:10640428).
Miscellaneous
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 147 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 149 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 149 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: S | ||||||
Binding site | 152 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: D | ||||||
Binding site | 153 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site | ||||
Sequence: D | ||||||
Binding site | 184 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: D | ||||||
Binding site | 241 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: N | ||||||
Binding site | 243 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: D | ||||||
Binding site | 245 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: P | ||||||
Binding site | 246 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: E | ||||||
Binding site | 246 | Mg2+ (UniProtKB | ChEBI); in MIDAS binding site | ||||
Sequence: E | ||||||
Binding site | 277 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site and liganded-open conformation | ||||
Sequence: D | ||||||
Binding site | 277 | Ca2+ 2 (UniProtKB | ChEBI); in LIMBS binding site | ||||
Sequence: D | ||||||
Binding site | 361 | Ca2+ 1 (UniProtKB | ChEBI); in ADMIDAS binding site and unliganded-closed conformation | ||||
Sequence: M |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIntegrin beta-3
- Alternative names
- CD Antigen Name
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP05106
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 27-718 | Extracellular | ||||
Sequence: GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPD | ||||||
Transmembrane | 719-741 | Helical | ||||
Sequence: ILVVLLSVMGAILLIGLAALLIW | ||||||
Topological domain | 742-788 | Cytoplasmic | ||||
Sequence: KLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Glanzmann thrombasthenia 2 (GT2)
- Note
- DescriptionA form of Glanzmann thrombasthenia, a disorder characterized by failure of platelet aggregation, absent or diminished clot retraction, and mucocutaneous bleeding of mild-to-moderate severity. Glanzmann thrombasthenia has been classified into clinical types I and II. In type I, platelets show absence of glycoprotein IIb-IIIa complexes at their surface and lack fibrinogen and clot retraction capability. In type II, the platelets express glycoprotein IIb-IIIa complexes at reduced levels, have detectable amounts of fibrinogen, and have low or moderate clot retraction capability.
- See alsoMIM:619267
Natural variants in GT2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_069920 | 64 | C>Y | in GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression; dbSNP:rs74554539 | |
VAR_030473 | 119 | R>W | in GT2; dbSNP:rs781062792 | |
VAR_030474 | 141 | Y>C | in GT2; dbSNP:rs1739770567 | |
VAR_010649 | 143 | L>W | in GT2; dbSNP:rs121918452 | |
VAR_069921 | 144 | M>R | in GT2; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; dbSNP:rs77963874 | |
VAR_030475 | 145 | D>N | in GT2; dbSNP:rs121918445 | |
VAR_003998 | 145 | D>Y | in GT2; type B; dbSNP:rs121918445 | |
VAR_030476 | 150 | M>V | in GT2; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor; dbSNP:rs767548512 | |
VAR_010651 | 188 | S>L | in GT2; type II; dbSNP:rs143146734 | |
VAR_030478 | 222 | L>P | in GT2; variant form; dbSNP:rs79208797 | |
VAR_003999 | 240 | R>Q | in GT2; type B; dbSNP:rs121918444 | |
VAR_004000 | 240 | R>W | in GT2; variant Strasbourg-1; dbSNP:rs121918446 | |
VAR_030479 | 242 | R>Q | in GT2; dbSNP:rs377162158 | |
VAR_030480 | 243 | D>V | in GT2; dbSNP:rs2143097053 | |
VAR_069922 | 247 | G>D | in GT2; 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 | |
VAR_069923 | 279 | K>M | in GT2; 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 | |
VAR_030481 | 288 | L>P | in GT2 | |
VAR_004001 | 306 | H>P | in GT2; dbSNP:rs13306476 | |
VAR_030482 | 321 | M>L | in GT2 | |
VAR_030483 | 330 | I>N | in GT2; not expressed on the surface and absent inside the transfected cells; dbSNP:rs2143105830 | |
VAR_004002 | 400 | C>Y | in GT2; dbSNP:rs121918449 | |
VAR_030484 | 532 | C>Y | in GT2; dbSNP:rs2065130922 | |
VAR_010671 | 568 | C>R | in GT2; type I; dbSNP:rs2065157102 | |
VAR_004003 | 586 | C>F | in GT2; dbSNP:rs2143129874 | |
VAR_030485 | 586 | C>R | in GT2; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1 | |
VAR_004004 | 598 | G>S | in GT2 | |
VAR_030486 | 601 | C>R | in GT2; dbSNP:rs747534508 | |
VAR_010672 | 605 | G>S | in GT2; type II; dbSNP:rs144884023 | |
VAR_004005 | 778 | S>P | in GT2; variant Strasbourg-1; dbSNP:rs121918447 |
Bleeding disorder, platelet-type, 24 (BDPLT24)
- Note
- DescriptionAn autosomal dominant disorder of platelet production characterized by congenital macrothrombocytopenia and platelet anisocytosis. Affected individuals may have no or only mildly increased bleeding tendency.
- See alsoMIM:619271
Natural variants in BDPLT24
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081732 | 746 | missing | in BDPLT24; the mutant protein is constitutively active; decreased platelet surface expression; spontaneous FAK phosphosphorylation; abnormal cell shape | |
VAR_069924 | 749 | D>H | in BDPLT24; the mutant protein is constitutively active; spontaneous FAK phosphosphorylation; abnormal cell shape; dbSNP:rs398122372 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_003993 | 59 | in alloantigen HPA-1B; dbSNP:rs5918 | |||
Sequence: L → P | ||||||
Natural variant | VAR_069920 | 64 | in GT2; severe type 1 phenotype; the mutation prevents normal ITGA2B/ITGB3 complex expression; dbSNP:rs74554539 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_049633 | 66 | in dbSNP:rs36080296 | |||
Sequence: L → R | ||||||
Natural variant | VAR_030473 | 119 | in GT2; dbSNP:rs781062792 | |||
Sequence: R → W | ||||||
Natural variant | VAR_030474 | 141 | in GT2; dbSNP:rs1739770567 | |||
Sequence: Y → C | ||||||
Natural variant | VAR_010649 | 143 | in GT2; dbSNP:rs121918452 | |||
Sequence: L → W | ||||||
Natural variant | VAR_069921 | 144 | in GT2; severe type 1 phenotype; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface; dbSNP:rs77963874 | |||
Sequence: M → R | ||||||
Natural variant | VAR_030475 | 145 | in GT2; dbSNP:rs121918445 | |||
Sequence: D → N | ||||||
Natural variant | VAR_003998 | 145 | in GT2; type B; dbSNP:rs121918445 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_030476 | 150 | in GT2; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor; dbSNP:rs767548512 | |||
Sequence: M → V | ||||||
Natural variant | VAR_030477 | 166 | probable risk factor for neonatal thrombocytopenia; alloantigen Duv(a+); does not affect significantly the integrin function; dbSNP:rs74708909 | |||
Sequence: T → I | ||||||
Natural variant | VAR_003994 | 169 | in alloantigen HPA-4B; dbSNP:rs5917 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_010651 | 188 | in GT2; type II; dbSNP:rs143146734 | |||
Sequence: S → L | ||||||
Natural variant | VAR_030478 | 222 | in GT2; variant form; dbSNP:rs79208797 | |||
Sequence: L → P | ||||||
Natural variant | VAR_003999 | 240 | in GT2; type B; dbSNP:rs121918444 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_004000 | 240 | in GT2; variant Strasbourg-1; dbSNP:rs121918446 | |||
Sequence: R → W | ||||||
Natural variant | VAR_030479 | 242 | in GT2; dbSNP:rs377162158 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_030480 | 243 | in GT2; dbSNP:rs2143097053 | |||
Sequence: D → V | ||||||
Natural variant | VAR_069922 | 247 | in GT2; 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 | |||
Sequence: G → D | ||||||
Natural variant | VAR_069923 | 279 | in GT2; 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 | |||
Sequence: K → M | ||||||
Natural variant | VAR_030481 | 288 | in GT2 | |||
Sequence: L → P | ||||||
Natural variant | VAR_004001 | 306 | in GT2; dbSNP:rs13306476 | |||
Sequence: H → P | ||||||
Natural variant | VAR_030482 | 321 | in GT2 | |||
Sequence: M → L | ||||||
Natural variant | VAR_030483 | 330 | in GT2; not expressed on the surface and absent inside the transfected cells; dbSNP:rs2143105830 | |||
Sequence: I → N | ||||||
Natural variant | VAR_004002 | 400 | in GT2; dbSNP:rs121918449 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_003995 | 433 | in alloantigen MO+; in a case of neonatal alloimmune thrombocytopenia; dbSNP:rs121918448 | |||
Sequence: P → A | ||||||
Natural variant | VAR_014178 | 453 | in dbSNP:rs5921 | |||
Sequence: V → I | ||||||
Mutagenesis | 502-508 | Increases ligand-binding activity. | ||||
Sequence: Missing | ||||||
Natural variant | VAR_003996 | 515 | in alloantigen CA+/TU+; dbSNP:rs13306487 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_030484 | 532 | in GT2; dbSNP:rs2065130922 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_010671 | 568 | in GT2; type I; dbSNP:rs2065157102 | |||
Sequence: C → R | ||||||
Natural variant | VAR_004003 | 586 | in GT2; dbSNP:rs2143129874 | |||
Sequence: C → F | ||||||
Natural variant | VAR_030485 | 586 | in GT2; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1 | |||
Sequence: C → R | ||||||
Natural variant | VAR_004004 | 598 | in GT2 | |||
Sequence: G → S | ||||||
Natural variant | VAR_030486 | 601 | in GT2; dbSNP:rs747534508 | |||
Sequence: C → R | ||||||
Natural variant | VAR_010672 | 605 | in GT2; type II; dbSNP:rs144884023 | |||
Sequence: G → S | ||||||
Mutagenesis | 659 | Slight increase in ligand-binding activity; when associated with 698-D--K-702 del. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_003997 | 662 | in alloantigen SR(A); dbSNP:rs151219882 | |||
Sequence: R → C | ||||||
Mutagenesis | 698-702 | Slight increase in ligand-binding activity; when associated with A-659. | ||||
Sequence: Missing | ||||||
Natural variant | VAR_081732 | 746 | in BDPLT24; the mutant protein is constitutively active; decreased platelet surface expression; spontaneous FAK phosphosphorylation; abnormal cell shape | |||
Sequence: Missing | ||||||
Natural variant | VAR_069924 | 749 | in BDPLT24; the mutant protein is constitutively active; spontaneous FAK phosphosphorylation; abnormal cell shape; dbSNP:rs398122372 | |||
Sequence: D → H | ||||||
Mutagenesis | 773 | No effect on cell surface location but impairs interaction with TNS3 and PEAK1. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_004005 | 778 | in GT2; variant Strasbourg-1; dbSNP:rs121918447 | |||
Sequence: S → P | ||||||
Mutagenesis | 785 | No effect on cell surface location but impairs interaction with TNS3 and PEAK1. | ||||
Sequence: Y → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 907 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-26 | UniProt | |||||
Sequence: MRARPRPRPLWATVLALGALAGVGVG | |||||||
Chain | PRO_0000016344 | 27-788 | UniProt | Integrin beta-3 | |||
Sequence: GPNICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCECSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCECDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCNCTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPTCPDACTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNCTYKNEDDCVVRFQYYEDSSGKSILYVVEEPECPKGPDILVVLLSVMGAILLIGLAALLIWKLLITIHDRKEFAKFEEERARAKWDTANNPLYKEATSTFTNITYRGT | |||||||
Disulfide bond | 31↔49 | UniProt | |||||
Sequence: CTTRGVSSCQQCLAVSPMC | |||||||
Disulfide bond | 39↔461 | UniProt | |||||
Sequence: CQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCAPESIEFPVSEARVLEDRPLSDKGSGDSSQVTQVSPQRIALRLRPDDSKNFSIQVRQVEDYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKIRSKVELEVRDLPEELSLSFNATCLNNEVIPGLKSCMGLKIGDTVSFSIEAKVRGCPQEKEKSFTIKPVGFKDSLIVQVTFDCDC | |||||||
Disulfide bond | 42↔64 | UniProt | |||||
Sequence: CLAVSPMCAWCSDEALPLGSPRC | |||||||
Disulfide bond | 52↔75 | UniProt | |||||
Sequence: CSDEALPLGSPRCDLKENLLKDNC | |||||||
Glycosylation | 125 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 203↔210 | UniProt | |||||
Sequence: CYDMKTTC | |||||||
Modified residue (large scale data) | 221 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Disulfide bond | 258↔299 | UniProt | |||||
Sequence: CDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQC | |||||||
Glycosylation | 346 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 397 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 400↔412 | UniProt | |||||
Sequence: CLNNEVIPGLKSC | |||||||
Disulfide bond | 432↔459 | UniProt | |||||
Sequence: CPQEKEKSFTIKPVGFKDSLIVQVTFDC | |||||||
Disulfide bond | 463↔483 | UniProt | |||||
Sequence: CQAQAEPNSHRCNNGNGTFEC | |||||||
Disulfide bond | 474↔486 | UniProt | |||||
Sequence: CNNGNGTFECGVC | |||||||
Glycosylation | 478 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 488↔497 | UniProt | |||||
Sequence: CGPGWLGSQC | |||||||
Disulfide bond | 499↔529 | UniProt | |||||
Sequence: CSEEDYRPSQQDECSPREGQPVCSQRGECLC | |||||||
Disulfide bond | 512↔527 | UniProt | |||||
Sequence: CSPREGQPVCSQRGEC | |||||||
Disulfide bond | 521↔532 | UniProt | |||||
Sequence: CSQRGECLCGQC | |||||||
Disulfide bond | 534↔547 | UniProt | |||||
Sequence: CHSSDFGKITGKYC | |||||||
Disulfide bond | 549↔570 | UniProt | |||||
Sequence: CDDFSCVRYKGEMCSGHGQCSC | |||||||
Disulfide bond | 554↔568 | UniProt | |||||
Sequence: CVRYKGEMCSGHGQC | |||||||
Disulfide bond | 562↔573 | UniProt | |||||
Sequence: CSGHGQCSCGDC | |||||||
Disulfide bond | 575↔584 | UniProt | |||||
Sequence: CDSDWTGYYC | |||||||
Glycosylation | 585 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 586↔609 | UniProt | |||||
Sequence: CTTRTDTCMSSNGLLCSGRGKCEC | |||||||
Disulfide bond | 593↔607 | UniProt | |||||
Sequence: CMSSNGLLCSGRGKC | |||||||
Disulfide bond | 601↔612 | UniProt | |||||
Sequence: CSGRGKCECGSC | |||||||
Disulfide bond | 614↔624 | UniProt | |||||
Sequence: CIQPGSYGDTC | |||||||
Disulfide bond | 627↔630 | UniProt | |||||
Sequence: CPTC | |||||||
Disulfide bond | 634↔681 | UniProt | |||||
Sequence: CTFKKECVECKKFDRGALHDENTCNRYCRDEIESVKELKDTGKDAVNC | |||||||
Disulfide bond | 640↔661 | UniProt | |||||
Sequence: CVECKKFDRGALHDENTCNRYC | |||||||
Disulfide bond | 643↔657 | UniProt | |||||
Sequence: CKKFDRGALHDENTC | |||||||
Glycosylation | 680 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 689↔713 | UniProt | |||||
Sequence: CVVRFQYYEDSSGKSILYVVEEPEC | |||||||
Modified residue | 767 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 767 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 773 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 777 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 778 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 779 | UniProt | Phosphothreonine; by PDPK1 and PKB/AKT1; in vitro | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 779 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 781 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 784 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 785 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 785 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 788 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Integrin ITGAV:ITGB3 interacts with FBLN5 (via N-terminus) (By similarity).
ITGAV:ITGB3 interacts with CCN3 (PubMed:12695522).
ITGAV:ITGB3 and ITGA2B:ITGB3 interact with SELP (via C-type lectin domain); the interaction mediates cell-cell interaction and adhesion (PubMed:37184585).
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 interacts with FGF2; it is likely that FGF2 can simultaneously bind ITGAV:ITGB3 and FGF receptors (PubMed:28302677).
ITGAV:ITGB3 binds to IL1B (PubMed:29030430).
ITGAV:ITGB3 is found in a ternary complex with IGF1 and IGF1R (PubMed:19578119).
ITGAV:ITGB3 interacts with IGF2 (PubMed:28873464).
ITGAV:ITGB3 interacts with FBN1 (PubMed:12807887).
ITGAV:ITGB3 interacts with CD9, CD81 and CD151 (via second extracellular domain) (PubMed:27993971).
Interacts (via the allosteric site (site 2)) with CXCL12 in a CXCR4-independent manner (PubMed:29301984).
Interacts with MXRA8/DICAM; the interaction inhibits ITGAV:ITGB3 heterodimer formation (PubMed:22492581).
ITGAV:ITGB3 interacts with PTN (PubMed:19141530).
Forms a complex with PTPRZ1 and PTN that stimulates endothelial cell migration through ITGB3 Tyr-773 phosphorylation (PubMed:19141530).
ITGAV:ITGB3 interacts with SLC6A4. Interacts with SLC6A4 (via C-terminus); this interaction regulates SLC6A4 trafficking (By similarity).
ITGA2B:ITGB3 interacts with PPIA/CYPA; the interaction is ROS and PPIase activity-dependent and is increased in the presence of thrombin (By similarity).
Interacts with tensin TNS3; TNS3 also interacts with PEAK1, thus acting as an adapter molecule to bridge the association of PEAK1 with ITGB3 (PubMed:35687021).
ITGAV:ITGB3 interacts with AGRA2 (PubMed:16982628).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P05106 | ACTN1 P05094 | 2 | EBI-702847, EBI-5847257 | |
BINARY | P05106 | CX3CL1 P78423 | 6 | EBI-702847, EBI-15188013 | |
BINARY | P05106 | FLNA P21333 | 3 | EBI-702847, EBI-350432 | |
XENO | P05106 | gB F5HB81 | 2 | EBI-702847, EBI-9027696 | |
BINARY | P05106 | ITGA2B P08514 | 12 | EBI-702847, EBI-702693 | |
BINARY | P05106 | ITGA2B P08514-1 | 4 | EBI-702847, EBI-15805658 | |
BINARY | P05106 | ITGAV P06756 | 13 | EBI-702847, EBI-298282 | |
BINARY | P05106 | ITGB3 P05106 | 5 | EBI-702847, EBI-702847 | |
XENO | P05106 | P06935 | 4 | EBI-702847, EBI-981051 | |
XENO | P05106 | Prkd1 Q62101 | 2 | EBI-702847, EBI-6903636 | |
BINARY | P05106 | PTPN1 P18031 | 4 | EBI-702847, EBI-968788 | |
XENO | P05106 | Src P05480-2 | 4 | EBI-702847, EBI-26656723 | |
BINARY | P05106 | TLN1 Q9Y490 | 5 | EBI-702847, EBI-2462036 | |
XENO | P05106 | Tln1 P26039 | 7 | EBI-702847, EBI-1039593 | |
XENO | P05106 | TLN1 P54939 | 2 | EBI-702847, EBI-1035421 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-76 | PSI | ||||
Sequence: ICTTRGVSSCQQCLAVSPMCAWCSDEALPLGSPRCDLKENLLKDNCA | ||||||
Domain | 135-377 | VWFA | ||||
Sequence: DYPVDIYYLMDLSYSMKDDLWSIQNLGTKLATQMRKLTSNLRIGFGAFVDKPVSPYMYISPPEALENPCYDMKTTCLPMFGYKHVLTLTDQVTRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVQPNDGQCHVGSDNHYSASTTMDYPSLGLMTEKLSQKNINLIFAVTENVVNLYQNYSELIPGTTVGVLSMDSSNVLQLIVDAYGKI | ||||||
Region | 203-210 | Involved in CX3CL1-, NRG1-, FGF1- and IGF1-binding | ||||
Sequence: CYDMKTTC | ||||||
Region | 293-313 | CX3CL1-binding | ||||
Sequence: QPNDGQCHVGSDNHYSASTTM | ||||||
Domain | 436-498 | EGF-like 1 | ||||
Sequence: KEKSFTIKPVGFKDSLIVQVTFDCDCACQAQAEPNSHRCNNGNGTFECGVCRCGPGWLGSQCE | ||||||
Domain | 499-548 | EGF-like 2 | ||||
Sequence: CSEEDYRPSQQDECSPREGQPVCSQRGECLCGQCVCHSSDFGKITGKYCE | ||||||
Domain | 549-585 | EGF-like 3 | ||||
Sequence: CDDFSCVRYKGEMCSGHGQCSCGDCLCDSDWTGYYCN | ||||||
Domain | 586-629 | EGF-like 4 | ||||
Sequence: CTTRTDTCMSSNGLLCSGRGKCECGSCVCIQPGSYGDTCEKCPT | ||||||
Motif | 777-783 | LIR | ||||
Sequence: TSTFTNI |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
P05106-1
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.
- NameBeta-3A
- Length788
- Mass (Da)87,058
- Last updated2007-02-06 v2
- ChecksumF246623608E05F9E
P05106-2
- NameBeta-3B
- Differences from canonical
- 768-788: ANNPLYKEATSTFTNITYRGT → VRDGAGRFLKSLV
P05106-3
- NameBeta-3C
- Differences from canonical
- 768-788: ANNPLYKEATSTFTNITYRGT → HYAQSLRKWNQPVSIDG
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 12 | in Ref. 1; AAA52589 and 3; AAA35927 | ||||
Sequence: A → V | ||||||
Sequence conflict | 151 | in Ref. 11; AAA67537 and 14; AAB23689 | ||||
Sequence: K → P | ||||||
Sequence conflict | 205 | in Ref. 11; AAA67537 | ||||
Sequence: D → EY | ||||||
Sequence conflict | 649-653 | in Ref. 1; AAA52589, 2; AAA60122 and 4; AAB71380 | ||||
Sequence: GALHD → EPYMT | ||||||
Sequence conflict | 716 | in Ref. 8 | ||||
Sequence: G → H | ||||||
Sequence conflict | 737-741 | in Ref. 11; AAA67537 | ||||
Sequence: ALLIW → PCSSG | ||||||
Alternative sequence | VSP_002745 | 768-788 | in isoform Beta-3B | |||
Sequence: ANNPLYKEATSTFTNITYRGT → VRDGAGRFLKSLV | ||||||
Alternative sequence | VSP_002746 | 768-788 | in isoform Beta-3C | |||
Sequence: ANNPLYKEATSTFTNITYRGT → HYAQSLRKWNQPVSIDG |
Polymorphism
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J02703 EMBL· GenBank· DDBJ | AAA52589.1 EMBL· GenBank· DDBJ | mRNA | ||
M20311 EMBL· GenBank· DDBJ | AAA60122.1 EMBL· GenBank· DDBJ | mRNA | ||
M35999 EMBL· GenBank· DDBJ | AAA35927.1 EMBL· GenBank· DDBJ | mRNA | ||
U95204 EMBL· GenBank· DDBJ | AAB71380.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471231 EMBL· GenBank· DDBJ | EAW57682.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC127666 EMBL· GenBank· DDBJ | AAI27667.1 EMBL· GenBank· DDBJ | mRNA | ||
BC127667 EMBL· GenBank· DDBJ | AAI27668.1 EMBL· GenBank· DDBJ | mRNA | ||
L28832 EMBL· GenBank· DDBJ | AAA20880.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32686 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32667 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32672 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32673 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32674 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32675 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32680 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32681 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32682 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M32685 EMBL· GenBank· DDBJ | AAA67537.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57494 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57481 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57482 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57483 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57484 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57485 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57486 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57487 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57488 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57489 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57490 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57491 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57492 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M57493 EMBL· GenBank· DDBJ | AAA52600.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U03881 EMBL· GenBank· DDBJ | AAA16076.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
S49379 EMBL· GenBank· DDBJ | AAB23689.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
M25108 EMBL· GenBank· DDBJ | AAA36121.1 EMBL· GenBank· DDBJ | mRNA |