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P05106

- ITB3_HUMAN

UniProt

P05106 - ITB3_HUMAN

Protein

Integrin beta-3

Gene

ITGB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 206 (01 Oct 2014)
      Sequence version 2 (06 Feb 2007)
      Previous versions | rss
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    Functioni

    Integrin alpha-V/beta-3 is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 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. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions.

    GO - Molecular functioni

    1. cell adhesion molecule binding Source: BHF-UCL
    2. identical protein binding Source: IntAct
    3. platelet-derived growth factor receptor binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. protein disulfide isomerase activity Source: UniProtKB
    6. receptor activity Source: InterPro
    7. vascular endothelial growth factor receptor 2 binding Source: BHF-UCL

    GO - Biological processi

    1. activation of protein kinase activity Source: BHF-UCL
    2. angiogenesis involved in wound healing Source: BHF-UCL
    3. axon guidance Source: Reactome
    4. blood coagulation Source: Reactome
    5. cell adhesion Source: ProtInc
    6. cell-matrix adhesion Source: InterPro
    7. cell-substrate adhesion Source: UniProtKB
    8. cell-substrate junction assembly Source: InterPro
    9. extracellular matrix organization Source: Reactome
    10. integrin-mediated signaling pathway Source: BHF-UCL
    11. leukocyte migration Source: Reactome
    12. negative regulation of lipid storage Source: BHF-UCL
    13. negative regulation of lipid transport Source: BHF-UCL
    14. negative regulation of lipoprotein metabolic process Source: BHF-UCL
    15. negative regulation of low-density lipoprotein particle receptor biosynthetic process Source: BHF-UCL
    16. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
    17. platelet activation Source: UniProtKB
    18. platelet aggregation Source: UniProtKB
    19. platelet degranulation Source: Reactome
    20. positive regulation of endothelial cell migration Source: BHF-UCL
    21. positive regulation of endothelial cell proliferation Source: BHF-UCL
    22. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    23. positive regulation of protein phosphorylation Source: BHF-UCL
    24. positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
    25. protein folding Source: GOC
    26. regulation of bone resorption Source: BHF-UCL
    27. smooth muscle cell migration Source: BHF-UCL
    28. tube development Source: BHF-UCL
    29. viral process Source: UniProtKB-KW
    30. wound healing Source: BHF-UCL

    Keywords - Molecular functioni

    Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_12519. PECAM1 interactions.
    REACT_13552. Integrin cell surface interactions.
    REACT_150331. Molecules associated with elastic fibres.
    REACT_150366. Elastic fibre formation.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.
    REACT_22272. Signal transduction by L1.
    SignaLinkiP05106.

    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
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:6156. ITGB3.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell projectionlamellipodium membrane 1 Publication. Cell junctionfocal adhesion 1 Publication

    GO - Cellular componenti

    1. alphav-beta3 integrin-vitronectin complex Source: BHF-UCL
    2. cell surface Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. focal adhesion Source: UniProtKB-SubCell
    5. integral component of plasma membrane Source: ProtInc
    6. integrin complex Source: BHF-UCL
    7. lamellipodium membrane Source: UniProtKB-SubCell
    8. melanosome Source: UniProtKB
    9. nucleus Source: MGI
    10. plasma membrane Source: UniProtKB
    11. platelet alpha granule membrane Source: Reactome
    12. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.18 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti64 – 641C → Y in GT; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. 1 Publication
    VAR_069920
    Natural varianti119 – 1191R → W in GT. 1 Publication
    VAR_030473
    Natural varianti141 – 1411Y → C in GT. 1 Publication
    VAR_030474
    Natural varianti143 – 1431L → W in GT. 1 Publication
    VAR_010649
    Natural varianti144 – 1441M → R in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. 1 Publication
    VAR_069921
    Natural varianti145 – 1451D → N in GT. 1 Publication
    VAR_030475
    Natural varianti145 – 1451D → Y in GT; type B. 1 Publication
    VAR_003998
    Natural varianti150 – 1501M → V in GT; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor. 1 Publication
    VAR_030476
    Natural varianti188 – 1881S → L in GT; type II. 1 Publication
    VAR_010651
    Natural varianti222 – 2221L → P in GT; variant form. 2 Publications
    VAR_030478
    Natural varianti240 – 2401R → Q in GT; type B. 1 Publication
    VAR_003999
    Natural varianti240 – 2401R → W in GT; variant Strasbourg-1. 1 Publication
    VAR_004000
    Natural varianti242 – 2421R → Q in GT. 1 Publication
    VAR_030479
    Natural varianti243 – 2431D → V in GT. 1 Publication
    VAR_030480
    Natural varianti247 – 2471G → D in GT; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation may interfere with correct folding of the protein. 1 Publication
    VAR_069922
    Natural varianti279 – 2791K → M in GT; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation interupts the interaction of the ITGA2B/ITGB3 complex. 1 Publication
    VAR_069923
    Natural varianti288 – 2881L → P in GT. 1 Publication
    VAR_030481
    Natural varianti306 – 3061H → P in GT. 2 Publications
    Corresponds to variant rs13306476 [ dbSNP | Ensembl ].
    VAR_004001
    Natural varianti321 – 3211M → L in GT. 1 Publication
    VAR_030482
    Natural varianti330 – 3301I → N in GT; not expressed on the surface and absent inside the transfected cells. 1 Publication
    VAR_030483
    Natural varianti400 – 4001C → Y in GT. 1 Publication
    VAR_004002
    Natural varianti532 – 5321C → Y in GT. 1 Publication
    VAR_030484
    Natural varianti568 – 5681C → R in GT; type I. 1 Publication
    VAR_010671
    Natural varianti586 – 5861C → F in GT. 1 Publication
    VAR_004003
    Natural varianti586 – 5861C → R in GT; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1. 1 Publication
    VAR_030485
    Natural varianti598 – 5981G → S in GT. 1 Publication
    VAR_004004
    Natural varianti601 – 6011C → R in GT. 1 Publication
    VAR_030486
    Natural varianti605 – 6051G → S in GT; type II. 1 Publication
    VAR_010672
    Natural varianti778 – 7781S → P in GT; variant Strasbourg-1. 1 Publication
    VAR_004005
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti749 – 7491D → H in BDPLT16; the mutant protein is constitutively active. 1 Publication
    VAR_069924

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 788762Integrin beta-3PRO_0000016344Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 4611 Publication
    Disulfide bondi39 ↔ 491 Publication
    Disulfide bondi42 ↔ 751 Publication
    Disulfide bondi52 ↔ 641 Publication
    Glycosylationi125 – 1251N-linked (GlcNAc...)2 Publications
    Disulfide bondi203 ↔ 2101 Publication
    Disulfide bondi258 ↔ 2991 Publication
    Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi400 ↔ 4121 Publication
    Disulfide bondi432 ↔ 6811 Publication
    Disulfide bondi459 ↔ 4631 Publication
    Disulfide bondi474 ↔ 4861 Publication
    Glycosylationi478 – 4781N-linked (GlcNAc...)
    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
    Glycosylationi585 – 5851N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi680 – 6801N-linked (GlcNAc...)1 Publication
    Modified residuei773 – 7731Phosphotyrosine1 Publication
    Modified residuei779 – 7791Phosphothreonine; by PDPK1 and PKB/AKT1; in vitro1 Publication
    Modified residuei785 – 7851Phosphotyrosine

    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.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP05106.
    PaxDbiP05106.
    PRIDEiP05106.

    PTM databases

    PhosphoSiteiP05106.

    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

    ArrayExpressiP05106.
    BgeeiP05106.
    CleanExiHS_ITGB3.
    GenevestigatoriP05106.

    Organism-specific databases

    HPAiCAB002501.
    HPA027852.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. Beta-3 associates with either alpha-IIb or alpha-V. Isoform Beta-3C interacts with FLNB. Interacts with COMP. Interacts with HIV-1 Tat. 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. Alpha-V/beta-3 interacts with herpes virus 8/HHV-8 glycoprotein B and acts as a receptor for the virus.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-702847,EBI-702847
    P069354EBI-702847,EBI-981051From a different organism.
    ACTN1P050942EBI-702847,EBI-5847257From a different organism.
    ITGA2BP0851411EBI-702847,EBI-702693
    ITGAVP0675611EBI-702847,EBI-298282
    ORF8F5HB812EBI-702847,EBI-9027696From a different organism.
    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.

    Protein-protein interaction databases

    BioGridi109896. 17 interactions.
    DIPiDIP-304N.
    IntActiP05106. 18 interactions.
    MINTiMINT-209501.
    STRINGi9606.ENSP00000262017.

    Structurei

    Secondary structure

    1
    788
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 334
    Helixi35 – 373
    Helixi39 – 457
    Beta strandi50 – 523
    Beta strandi54 – 574
    Beta strandi59 – 613
    Beta strandi63 – 653
    Helixi67 – 726
    Helixi77 – 793
    Beta strandi86 – 916
    Beta strandi99 – 1013
    Helixi103 – 1053
    Beta strandi109 – 1113
    Beta strandi113 – 1186
    Beta strandi123 – 1319
    Beta strandi138 – 1458
    Helixi148 – 1503
    Helixi151 – 1566
    Turni157 – 1593
    Helixi160 – 1689
    Turni169 – 1713
    Beta strandi175 – 1828
    Turni188 – 1903
    Helixi196 – 2005
    Turni202 – 2076
    Beta strandi215 – 22410
    Helixi226 – 23510
    Beta strandi242 – 2465
    Helixi248 – 25710
    Helixi259 – 2624
    Beta strandi266 – 27813
    Helixi285 – 2895
    Beta strandi305 – 3073
    Turni308 – 3125
    Helixi318 – 32710
    Beta strandi331 – 3366
    Helixi338 – 3403
    Helixi341 – 3499
    Beta strandi355 – 3584
    Turni361 – 3633
    Helixi366 – 37712
    Beta strandi381 – 3877
    Beta strandi392 – 4009
    Turni401 – 4033
    Beta strandi404 – 4074
    Beta strandi411 – 4155
    Beta strandi420 – 42910
    Beta strandi434 – 44411
    Beta strandi451 – 4577
    Helixi462 – 4665
    Beta strandi468 – 4703
    Turni472 – 4787
    Beta strandi479 – 4824
    Beta strandi485 – 4884
    Beta strandi489 – 4913
    Turni494 – 4974
    Beta strandi500 – 5045
    Beta strandi513 – 5186
    Helixi520 – 5234
    Beta strandi524 – 5274
    Beta strandi529 – 5346
    Beta strandi538 – 5403
    Beta strandi542 – 5443
    Beta strandi549 – 5524
    Beta strandi556 – 5616
    Helixi562 – 5643
    Beta strandi565 – 5695
    Beta strandi572 – 5754
    Beta strandi579 – 5846
    Turni591 – 5933
    Beta strandi598 – 6003
    Beta strandi602 – 6043
    Beta strandi606 – 6083
    Beta strandi611 – 6133
    Turni616 – 6183
    Beta strandi620 – 6245
    Beta strandi628 – 6303
    Turni633 – 6353
    Helixi639 – 6413
    Turni642 – 6465
    Beta strandi649 – 6557
    Turni658 – 6603
    Beta strandi664 – 6663
    Beta strandi669 – 6713
    Beta strandi674 – 6785
    Beta strandi680 – 6845
    Beta strandi688 – 6947
    Beta strandi698 – 7003
    Beta strandi704 – 7063
    Beta strandi707 – 7104
    Beta strandi715 – 7173
    Turni743 – 75917
    Turni761 – 7655
    Beta strandi767 – 7704
    Helixi771 – 7744
    Helixi776 – 7794
    Turni782 – 7865

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    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[»]
    ProteinModelPortaliP05106.
    SMRiP05106. Positions 27-788.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05106.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 718692ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini742 – 78847CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei719 – 74123HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini135 – 377243VWFAAdd
    BLAST
    Repeati463 – 51149IAdd
    BLAST
    Repeati512 – 55342IIAdd
    BLAST
    Repeati554 – 59239IIIAdd
    BLAST
    Repeati593 – 62937IVAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni463 – 629167Cysteine-rich tandem repeatsAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG287997.
    HOVERGENiHBG006190.
    InParanoidiP05106.
    KOiK06493.
    OMAiGHGQCSC.
    OrthoDBiEOG7T7GSB.
    PhylomeDBiP05106.
    TreeFamiTF105392.

    Family and domain databases

    Gene3Di1.20.5.630. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR027068. Integrin_beta-3.
    IPR015812. Integrin_bsu.
    IPR014836. Integrin_bsu_cyt_dom.
    IPR002369. Integrin_bsu_N.
    IPR012896. Integrin_bsu_tail.
    IPR016201. Plexin-like_fold.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR10082. PTHR10082. 1 hit.
    PTHR10082:SF25. PTHR10082:SF25. 1 hit.
    PfamiPF08725. Integrin_b_cyt. 1 hit.
    PF07965. Integrin_B_tail. 1 hit.
    PF00362. Integrin_beta. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002512. Integrin_B. 1 hit.
    PRINTSiPR01186. INTEGRINB.
    SMARTiSM00187. INB. 1 hit.
    SM00423. PSI. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF103575. SSF103575. 1 hit.
    SSF53300. SSF53300. 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. Align

    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

    MRARPRPRPL WATVLALGAL AGVGVGGPNI CTTRGVSSCQ QCLAVSPMCA    50
    WCSDEALPLG SPRCDLKENL LKDNCAPESI EFPVSEARVL EDRPLSDKGS 100
    GDSSQVTQVS PQRIALRLRP DDSKNFSIQV RQVEDYPVDI YYLMDLSYSM 150
    KDDLWSIQNL GTKLATQMRK LTSNLRIGFG AFVDKPVSPY MYISPPEALE 200
    NPCYDMKTTC LPMFGYKHVL TLTDQVTRFN EEVKKQSVSR NRDAPEGGFD 250
    AIMQATVCDE KIGWRNDASH LLVFTTDAKT HIALDGRLAG IVQPNDGQCH 300
    VGSDNHYSAS TTMDYPSLGL MTEKLSQKNI NLIFAVTENV VNLYQNYSEL 350
    IPGTTVGVLS MDSSNVLQLI VDAYGKIRSK VELEVRDLPE ELSLSFNATC 400
    LNNEVIPGLK SCMGLKIGDT VSFSIEAKVR GCPQEKEKSF TIKPVGFKDS 450
    LIVQVTFDCD CACQAQAEPN SHRCNNGNGT FECGVCRCGP GWLGSQCECS 500
    EEDYRPSQQD ECSPREGQPV CSQRGECLCG QCVCHSSDFG KITGKYCECD 550
    DFSCVRYKGE MCSGHGQCSC GDCLCDSDWT GYYCNCTTRT DTCMSSNGLL 600
    CSGRGKCECG SCVCIQPGSY GDTCEKCPTC PDACTFKKEC VECKKFDRGA 650
    LHDENTCNRY CRDEIESVKE LKDTGKDAVN CTYKNEDDCV VRFQYYEDSS 700
    GKSILYVVEE PECPKGPDIL VVLLSVMGAI LLIGLAALLI WKLLITIHDR 750
    KEFAKFEEER ARAKWDTANN PLYKEATSTF TNITYRGT 788
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121A → V in AAA52589. (PubMed:3494014)Curated
    Sequence conflicti12 – 121A → V in AAA35927. (PubMed:2345548)Curated
    Sequence conflicti151 – 1511K → P in AAA67537. (PubMed:2341395)Curated
    Sequence conflicti151 – 1511K → P in AAB23689. (PubMed:1382574)Curated
    Sequence conflicti205 – 2051D → EY in AAA67537. (PubMed:2341395)Curated
    Sequence conflicti649 – 6535GALHD → EPYMT in AAA52589. (PubMed:3494014)Curated
    Sequence conflicti649 – 6535GALHD → EPYMT in AAA60122. (PubMed:2452834)Curated
    Sequence conflicti649 – 6535GALHD → EPYMT in AAB71380. (PubMed:9195946)Curated
    Sequence conflicti716 – 7161G → H(PubMed:3165296)Curated
    Sequence conflicti737 – 7415ALLIW → PCSSG in AAA67537. (PubMed:2341395)Curated

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591L → P in alloantigen HPA-1B. 3 Publications
    Corresponds to variant rs5918 [ dbSNP | Ensembl ].
    VAR_003993
    Natural varianti64 – 641C → Y in GT; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. 1 Publication
    VAR_069920
    Natural varianti66 – 661L → R.1 Publication
    Corresponds to variant rs36080296 [ dbSNP | Ensembl ].
    VAR_049633
    Natural varianti119 – 1191R → W in GT. 1 Publication
    VAR_030473
    Natural varianti141 – 1411Y → C in GT. 1 Publication
    VAR_030474
    Natural varianti143 – 1431L → W in GT. 1 Publication
    VAR_010649
    Natural varianti144 – 1441M → R in GT; the mutation prevented normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype. 1 Publication
    VAR_069921
    Natural varianti145 – 1451D → N in GT. 1 Publication
    VAR_030475
    Natural varianti145 – 1451D → Y in GT; type B. 1 Publication
    VAR_003998
    Natural varianti150 – 1501M → V in GT; may confer constitutive activity to the alpha-IIb/(mutated)beta-3 receptor. 1 Publication
    VAR_030476
    Natural varianti166 – 1661T → I Associated with neonatal thrombocytopenia; alloantigen Duv(a+); does not affect significantly the integrin function. 1 Publication
    VAR_030477
    Natural varianti169 – 1691R → Q in alloantigen HPA-4B. 2 Publications
    Corresponds to variant rs5917 [ dbSNP | Ensembl ].
    VAR_003994
    Natural varianti188 – 1881S → L in GT; type II. 1 Publication
    VAR_010651
    Natural varianti222 – 2221L → P in GT; variant form. 2 Publications
    VAR_030478
    Natural varianti240 – 2401R → Q in GT; type B. 1 Publication
    VAR_003999
    Natural varianti240 – 2401R → W in GT; variant Strasbourg-1. 1 Publication
    VAR_004000
    Natural varianti242 – 2421R → Q in GT. 1 Publication
    VAR_030479
    Natural varianti243 – 2431D → V in GT. 1 Publication
    VAR_030480
    Natural varianti247 – 2471G → D in GT; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation may interfere with correct folding of the protein. 1 Publication
    VAR_069922
    Natural varianti279 – 2791K → M in GT; the mutation prevents normal ITGA2B/ITGB3 complex expression on the cell surface consistent with a severe type 1 phenotype; the mutation interupts the interaction of the ITGA2B/ITGB3 complex. 1 Publication
    VAR_069923
    Natural varianti288 – 2881L → P in GT. 1 Publication
    VAR_030481
    Natural varianti306 – 3061H → P in GT. 2 Publications
    Corresponds to variant rs13306476 [ dbSNP | Ensembl ].
    VAR_004001
    Natural varianti321 – 3211M → L in GT. 1 Publication
    VAR_030482
    Natural varianti330 – 3301I → N in GT; not expressed on the surface and absent inside the transfected cells. 1 Publication
    VAR_030483
    Natural varianti400 – 4001C → Y in GT. 1 Publication
    VAR_004002
    Natural varianti433 – 4331P → A in alloantigen MO(+); in a case of neonatal alloimmune thrombocytopenia. 1 Publication
    Corresponds to variant rs121918448 [ dbSNP | Ensembl ].
    VAR_003995
    Natural varianti453 – 4531V → I.1 Publication
    Corresponds to variant rs5921 [ dbSNP | Ensembl ].
    VAR_014178
    Natural varianti515 – 5151R → Q in alloantigen CA(+)/TU(+). 1 Publication
    Corresponds to variant rs13306487 [ dbSNP | Ensembl ].
    VAR_003996
    Natural varianti532 – 5321C → Y in GT. 1 Publication
    VAR_030484
    Natural varianti568 – 5681C → R in GT; type I. 1 Publication
    VAR_010671
    Natural varianti586 – 5861C → F in GT. 1 Publication
    VAR_004003
    Natural varianti586 – 5861C → R in GT; gain-of-function mutation; constitutively binds ligand-induced binding sites antibodies and the fibrinogen-mimetic antibody PAC-1. 1 Publication
    VAR_030485
    Natural varianti598 – 5981G → S in GT. 1 Publication
    VAR_004004
    Natural varianti601 – 6011C → R in GT. 1 Publication
    VAR_030486
    Natural varianti605 – 6051G → S in GT; type II. 1 Publication
    VAR_010672
    Natural varianti662 – 6621R → C in alloantigen SR(A). 1 Publication
    Corresponds to variant rs151219882 [ dbSNP | Ensembl ].
    VAR_003997
    Natural varianti749 – 7491D → H in BDPLT16; the mutant protein is constitutively active. 1 Publication
    VAR_069924
    Natural varianti778 – 7781S → P in GT; variant Strasbourg-1. 1 Publication
    VAR_004005

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei768 – 78821ANNPL…TYRGT → VRDGAGRFLKSLV in isoform Beta-3B. 1 PublicationVSP_002745Add
    BLAST
    Alternative sequencei768 – 78821ANNPL…TYRGT → HYAQSLRKWNQPVSIDG in isoform Beta-3C. 1 PublicationVSP_002746Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human. [P05106-1]

    Polymorphism databases

    DMDMi125987835.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11511.1. [P05106-1 ]
    PIRi A26547.
    A60798.
    B36268.
    I77349.
    S14324.
    RefSeqi NP_000203.2. NM_000212.2. [P05106-1 ]
    UniGenei Hs.218040.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JV2 X-ray 3.10 B 27-718 [» ]
    1KUP NMR - B 742-766 [» ]
    1KUZ NMR - B 742-766 [» ]
    1L5G X-ray 3.20 B 27-718 [» ]
    1M1X X-ray 3.30 B 27-718 [» ]
    1M8O NMR - B 742-788 [» ]
    1MIZ X-ray 1.90 A 765-769 [» ]
    1MK7 X-ray 2.20 A/C 765-775 [» ]
    1MK9 X-ray 2.80 A/C/E/G 765-776 [» ]
    1RN0 model - B 135-378 [» ]
    1S4X NMR - A 742-788 [» ]
    1TYE X-ray 2.90 B/D/F 27-466 [» ]
    1U8C X-ray 3.10 B 27-718 [» ]
    2INI model - B 81-460 [» ]
    B 558-716 [» ]
    2K9J NMR - B 711-753 [» ]
    2KNC NMR - B 715-788 [» ]
    2KV9 NMR - B 739-788 [» ]
    2L1C NMR - B 762-788 [» ]
    2L91 NMR - A 711-753 [» ]
    2LJD NMR - A 742-788 [» ]
    2LJE NMR - A 742-788 [» ]
    2LJF NMR - A 742-788 [» ]
    2Q6W X-ray 2.25 C/F 50-61 [» ]
    2RMZ NMR - A 711-753 [» ]
    2RN0 NMR - A 711-753 [» ]
    2VC2 X-ray 3.10 B 27-487 [» ]
    2VDK X-ray 2.80 B 27-487 [» ]
    2VDL X-ray 2.75 B 27-487 [» ]
    2VDM X-ray 2.90 B 27-487 [» ]
    2VDN X-ray 2.90 B 27-487 [» ]
    2VDO X-ray 2.51 B 27-487 [» ]
    2VDP X-ray 2.80 B 27-487 [» ]
    2VDQ X-ray 2.59 B 27-487 [» ]
    2VDR X-ray 2.40 B 27-487 [» ]
    3FCS X-ray 2.55 B/D 27-716 [» ]
    3FCU X-ray 2.90 B/D/F 27-487 [» ]
    3IJE X-ray 2.90 B 27-721 [» ]
    3NID X-ray 2.30 B/D 27-497 [» ]
    3NIF X-ray 2.40 B/D 27-497 [» ]
    3NIG X-ray 2.25 B/D 27-497 [» ]
    3T3M X-ray 2.60 B/D 27-498 [» ]
    3T3P X-ray 2.20 B/D 27-498 [» ]
    3ZDX X-ray 2.45 B/D 27-498 [» ]
    3ZDY X-ray 2.45 B/D 27-498 [» ]
    3ZDZ X-ray 2.75 B/D 27-498 [» ]
    3ZE0 X-ray 2.95 B/D 27-498 [» ]
    3ZE1 X-ray 3.00 B/D 27-498 [» ]
    3ZE2 X-ray 2.35 B/D 27-498 [» ]
    4CAK electron microscopy 20.50 B 27-716 [» ]
    4G1E X-ray 3.00 B 27-717 [» ]
    4G1M X-ray 2.90 B 27-718 [» ]
    4MMX X-ray 3.32 B 27-718 [» ]
    4MMY X-ray 3.18 B 27-718 [» ]
    4MMZ X-ray 3.10 B 27-718 [» ]
    4O02 X-ray 3.60 B 27-718 [» ]
    ProteinModelPortali P05106.
    SMRi P05106. Positions 27-788.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109896. 17 interactions.
    DIPi DIP-304N.
    IntActi P05106. 18 interactions.
    MINTi MINT-209501.
    STRINGi 9606.ENSP00000262017.

    Chemistry

    BindingDBi P05106.
    ChEMBLi CHEMBL2111443.
    DrugBanki DB00054. Abciximab.
    DB00775. Tirofiban.

    PTM databases

    PhosphoSitei P05106.

    Polymorphism databases

    DMDMi 125987835.

    Proteomic databases

    MaxQBi P05106.
    PaxDbi P05106.
    PRIDEi P05106.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000559488 ; ENSP00000452786 ; ENSG00000259207 . [P05106-1 ]
    GeneIDi 3690.
    KEGGi hsa:3690.
    UCSCi uc002ilj.3. human. [P05106-1 ]

    Organism-specific databases

    CTDi 3690.
    GeneCardsi GC17P045331.
    HGNCi HGNC:6156. ITGB3.
    HPAi CAB002501.
    HPA027852.
    MIMi 173470. gene+phenotype.
    187800. phenotype.
    273800. phenotype.
    neXtProti NX_P05106.
    Orphaneti 140957. Autosomal dominant macrothrombocytopenia.
    853. Fetal and neonatal alloimmune thrombocytopenia.
    849. Glanzmann thrombasthenia.
    PharmGKBi PA205.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287997.
    HOVERGENi HBG006190.
    InParanoidi P05106.
    KOi K06493.
    OMAi GHGQCSC.
    OrthoDBi EOG7T7GSB.
    PhylomeDBi P05106.
    TreeFami TF105392.

    Enzyme and pathway databases

    Reactomei REACT_12519. PECAM1 interactions.
    REACT_13552. Integrin cell surface interactions.
    REACT_150331. Molecules associated with elastic fibres.
    REACT_150366. Elastic fibre formation.
    REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_15523. Integrin alphaIIb beta3 signaling.
    REACT_163906. ECM proteoglycans.
    REACT_163942. Syndecan interactions.
    REACT_22272. Signal transduction by L1.
    SignaLinki P05106.

    Miscellaneous databases

    ChiTaRSi ITGB3. human.
    EvolutionaryTracei P05106.
    GeneWikii CD61.
    GenomeRNAii 3690.
    NextBioi 14453.
    PMAP-CutDB P05106.
    PROi P05106.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05106.
    Bgeei P05106.
    CleanExi HS_ITGB3.
    Genevestigatori P05106.

    Family and domain databases

    Gene3Di 1.20.5.630. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR027068. Integrin_beta-3.
    IPR015812. Integrin_bsu.
    IPR014836. Integrin_bsu_cyt_dom.
    IPR002369. Integrin_bsu_N.
    IPR012896. Integrin_bsu_tail.
    IPR016201. Plexin-like_fold.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR10082. PTHR10082. 1 hit.
    PTHR10082:SF25. PTHR10082:SF25. 1 hit.
    Pfami PF08725. Integrin_b_cyt. 1 hit.
    PF07965. Integrin_B_tail. 1 hit.
    PF00362. Integrin_beta. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002512. Integrin_B. 1 hit.
    PRINTSi PR01186. INTEGRINB.
    SMARTi SM00187. INB. 1 hit.
    SM00423. PSI. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103575. SSF103575. 1 hit.
    SSF53300. SSF53300. 1 hit.
    SSF69687. SSF69687. 1 hit.
    PROSITEi PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 1 hit.
    PS00243. INTEGRIN_BETA. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Protein sequence of endothelial glycoprotein IIIa derived from a cDNA clone. Identity with platelet glycoprotein IIIa and similarity to 'integrin'."
      Fitzgerald L.A., Steiner B., Rall S.C. Jr., Lo S., Phillips D.R.
      J. Biol. Chem. 262:3936-3939(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A).
    2. "Structure of platelet glycoprotein IIIa. A common subunit for two different membrane receptors."
      Zimrin A.B., Eisman R., Vilaire G., Schwartz E., Bennett J.S., Poncz M.
      J. Clin. Invest. 81:1470-1475(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A).
    3. "GPIIb and GPIIIa amino acid sequences deduced from human megakaryocyte cDNAs."
      Frachet P., Uzan G., Thevenon D., Denarier E., Prandini M.H., Marguerie G.
      Mol. Biol. Rep. 14:27-33(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3A).
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-3C).
      Tissue: Osteoclastoma.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-3A).
    7. "Isolation and characterization of a TATA-less promoter for the human beta 3 integrin gene."
      Villa-Garcia M., Li L., Riely G., Bray P.F.
      Blood 83:668-676(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
      Tissue: Blood.
    8. "Cloning of glycoprotein IIIa cDNA from human erythroleukemia cells and localization of the gene to chromosome 17."
      Rosa J.P., Bray P.F., Gayet O., Johnston G.I., Cook R.G., Jackson K.W., Shuman M.A., McEver R.P.
      Blood 72:593-600(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-788.
      Tissue: Erythroleukemia.
    9. "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."
      Catimel B., Parmentier S., Leung L.L., McGregor J.L.
      Biochem. J. 279:419-425(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-37.
      Tissue: Platelet.
    10. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-34.
      Tissue: Platelet.
    11. "The genomic organization of platelet glycoprotein IIIa."
      Zimrin A.B., Gidwitz S., Lord S., Schwartz E., Bennett J.S., White G.C. II, Poncz M.
      J. Biol. Chem. 265:8590-8595(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-788.
    12. "Characterization of the human platelet glycoprotein IIIa gene. Comparison with the fibronectin receptor beta-subunit gene."
      Lanza F., Kieffer N., Phillips D.R., Fitzgerald L.A.
      J. Biol. Chem. 265:18098-18103(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-788.
    13. "A new exon II polymorphism in the platelet glycoprotein IIIa."
      Pascual C., Balas A., Garcia-Sanchez F., Rodriguez de la Rua A., Vicario J.L.
      Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-120, VARIANTS PRO-59 AND ARG-66.
      Tissue: Blood.
    14. "The gene organization of the human beta 7 subunit, the common beta subunit of the leukocyte integrins HML-1 and LPAM-1."
      Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D., Krissansen G.W.
      Int. Immunol. 4:1031-1040(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 122-204.
    15. "Purification and partial amino acid sequence of human platelet membrane glycoproteins IIb and IIIa."
      Hiraiwa A., Matsukage A., Shiku H., Takahashi T., Naito K., Yamada K.
      Blood 69:560-564(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 218-234 AND 439-443.
    16. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 707-788 (ISOFORM BETA-3B).
      Tissue: Placenta.
    17. "Assignment of disulphide bonds in human platelet GPIIIa. A disulphide pattern for the beta-subunits of the integrin family."
      Calvete J.J., Henschen A., Gonzalez-Rodriguez J.
      Biochem. J. 274:63-71(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
    18. "Outside-in integrin signal transduction. Alpha IIb beta 3-(GP IIb IIIa) tyrosine phosphorylation induced by platelet aggregation."
      Law D.A., Nannizzi-Alaimo L., Phillips D.R.
      J. Biol. Chem. 271:10811-10815(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-773 AND TYR-785 (ISOFORM BETA-3A).
    19. "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."
      Barillari G., Sgadari C., Fiorelli V., Samaniego F., Colombini S., Manzari V., Modesti A., Nair B.C., Cafaro A., Stuerzl M., Ensoli B.
      Blood 94:663-672(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    20. "Threonine phosphorylation of the beta 3 integrin cytoplasmic tail, at a site recognized by PDK1 and Akt/PKB in vitro, regulates Shc binding."
      Kirk R.I., Sanderson M.R., Lerea K.M.
      J. Biol. Chem. 275:30901-30906(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-779.
    21. "Coordinate interactions of Csk, Src, and Syk kinases with [alpha]IIb[beta]3 initiate integrin signaling to the cytoskeleton."
      Obergfell A., Eto K., Mocsai A., Buensuceso C., Moores S.L., Brugge J.S., Lowell C.A., Shattil S.J.
      J. Cell Biol. 157:265-275(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYK.
    22. "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."
      van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.
      J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLNB.
      Tissue: Keratinocyte and Skeletal muscle.
    23. "Myosin-X provides a motor-based link between integrins and the cytoskeleton."
      Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A., Cheney R.E., Stromblad S.
      Nat. Cell Biol. 6:523-531(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYO10.
    24. "A role for the thiol isomerase protein ERP5 in platelet function."
      Jordan P.A., Stevens J.M., Hubbard G.P., Barrett N.E., Sage T., Authi K.S., Gibbins J.M.
      Blood 105:1500-1507(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDIA6.
    25. "Cartilage oligomeric matrix protein/thrombospondin 5 supports chondrocyte attachment through interaction with integrins."
      Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.
      J. Biol. Chem. 280:32655-32661(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COMP.
    26. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
      Tissue: Plasma.
    27. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
      Lewandrowski U., Moebius J., Walter U., Sickmann A.
      Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125.
      Tissue: Platelet.
    28. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-773, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    29. "Integrin alphaVbeta3 Binds to the RGD motif of glycoprotein B of Kaposi's sarcoma-associated herpesvirus and functions as an RGD-dependent entry receptor."
      Garrigues H.J., Rubinchikova Y.E., Dipersio C.M., Rose T.M.
      J. Virol. 82:1570-1580(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-8 GLYCOPROTEIN B.
    30. "Naturally processed peptides spanning the HPA-1a polymorphism are efficiently generated and displayed from platelet glycoprotein by HLA-DRB3*0101-positive antigen-presenting cells."
      Anani Sarab G., Moss M., Barker R.N., Urbaniak S.J.
      Blood 114:1954-1957(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF ALLOANTIGEN HPA-1A BY MASS SPECTROMETRY, ASSOCIATION TO ALLELE HLA-DRB3*01:01.
    31. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-680.
      Tissue: Liver.
    32. "Tyrosine phosphorylation of integrin beta3 regulates kindlin-2 binding and integrin activation."
      Bledzka K., Bialkowska K., Nie H., Qin J., Byzova T., Wu C., Plow E.F., Ma Y.Q.
      J. Biol. Chem. 285:30370-30374(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FERMT2, SUBCELLULAR LOCATION.
    33. "Crystal structure of the extracellular segment of integrin alpha Vbeta3."
      Xiong J.P., Stehle T., Diefenbach B., Zhang R., Dunker R., Scott D.L., Joachimiak A., Goodman S.L., Arnaout M.A.
      Science 294:339-345(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-718.
    34. "Crystallographic structure of the human leukocyte antigen DRA, DRB3*0101: models of a directional alloimmune response and autoimmunity."
      Parry C.S., Gorski J., Stern L.J.
      J. Mol. Biol. 371:435-446(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 50-61 (ALLOANTIGEN HPA-1A) IN COMPLEX WITH HLA-DRA/HLA-DRB3 HETERODIMER.
    35. "Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization."
      Bray P.F.
      Thromb. Haemost. 72:492-502(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON GT VARIANTS.
    36. "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."
      Newman P.J., Derbes R.S., Aster R.H.
      J. Clin. Invest. 83:1778-1781(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HPA-1B PRO-59, DESCRIPTION OF ALLOANTIGEN SYSTEM PL(A).
    37. "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."
      Wang R., Furihata K., McFarland J.G., Friedman K., Aster R.H., Newman P.J.
      J. Clin. Invest. 90:2038-2043(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HPA-4B GLN-169, DESCRIPTION OF ALLOANTIGEN SYSTEM PEN.
    38. "Single point mutation in human glycoprotein IIIa is associated with a new platelet-specific alloantigen (Mo) involved in neonatal alloimmune thrombocytopenia."
      Kuijpers R.W.A.M., Simsek S., Faber N.M., Goldschmeding R., van Wermerkerken R.K.V., von Dem Borne A.E.G.K.
      Blood 81:70-76(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MO(+) ALA-433.
    39. "Amino acid 489 is encoded by a mutational 'hot spot' on the beta 3 integrin chain: the CA/TU human platelet alloantigen system."
      Wang R., McFarland J.G., Kekomaki R., Newman P.J.
      Blood 82:3386-3391(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CA(+)/TU(+) GLN-515, DESCRIPTION OF ALLOANTIGEN SYSTEM CA/TU.
    40. "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."
      Santoso S., Kalb R., Kroll H., Walka M., Kiefel V., Mueller-Eckhardt C., Newman P.J.
      J. Biol. Chem. 269:8439-8444(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SR(A) CYS-662, DESCRIPTION OF ALLOANTIGEN SYSTEM SR(A).
    41. "A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation."
      Loftus J.C., O'Toole T.E., Plow E.F., Glass A., Frelinger A.L. III, Ginsberg M.H.
      Science 249:915-918(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT TYR-145.
    42. "A spontaneous mutation of integrin alpha IIb beta 3 (platelet glycoprotein IIb-IIIa) helps define a ligand binding site."
      Bajt M.L., Ginsberg M.H., Frelinger A.L. III, Berndt M.C., Loftus J.C.
      J. Biol. Chem. 267:3789-3794(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT GLN-240.
    43. "A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets with functionally defective glycoprotein IIb-IIIa complexes and a glycoprotein IIIa 214Arg-->214Trp mutation."
      Lanza F., Stierle A., Fournier D., Morales M., Andre G., Nurden A.T., Cazenave J.-P.
      J. Clin. Invest. 89:1995-2004(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT TRP-240.
    44. "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."
      Chen Y.-P., Djaffar I., Pidard D., Steiner B., Cieutat A.-M., Caen J.P., Rosa J.-P.
      Proc. Natl. Acad. Sci. U.S.A. 89:10169-10173(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT PRO-778.
    45. "A Cys374Tyr homozygous mutation of platelet glycoprotein IIIa (beta 3) in a Chinese patient with Glanzmann's thrombasthenia."
      Grimaldi C.M., Chen F., Scudder L.E., Coller B.S., French D.L.
      Blood 88:1666-1675(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT TYR-400.
    46. "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."
      Basani R.B., Brown D.L., Vilaire G., Bennett J.S., Poncz M.
      Blood 90:3082-3088(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT TRP-143.
    47. "Hematologically important mutations: Glanzmann thrombasthenia."
      French D.L., Coller B.S.
      Blood Cells Mol. Dis. 23:39-51(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT ASN-145; GLN-242 AND PRO-288.
    48. "Three novel integrin beta3 subunit missense mutations (H280P, C560F, and G579S) in thrombasthenia, including one (H280P) prevalent in Japanese patients."
      Ambo H., Kamata T., Handa M., Taki M., Kuwajima M., Kawai Y., Oda A., Murata M., Takada Y., Watanabe K., Ikeda Y.
      Biochem. Biophys. Res. Commun. 251:763-768(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT PRO-306; PHE-586; SER-598 AND SER-605.
    49. "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."
      Jackson D.E., White M.M., Jennings L.K., Newman P.J.
      Thromb. Haemost. 80:42-48(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT LEU-188.
    50. "Homozygous Cys542-->Arg substitution in GPIIIa in a Swiss patient with type I Glanzmann's thrombasthenia."
      Ruan J., Schmugge M., Clemetson K.J., Cazes E., Combrie R., Bourre F., Nurden A.T.
      Br. J. Haematol. 105:523-531(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT ARG-568.
    51. Cited for: VARIANTS PRO-59; GLN-169 AND ILE-453.
    52. "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."
      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.
      Blood 98:2432-2441(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT ARG-586, CHARACTERIZATION OF VARIANT GT ARG-586.
    53. "A new platelet polymorphism Duv(a+), localized within the RGD binding domain of glycoprotein IIIa, is associated with neonatal thrombocytopenia."
      Jallu V., Meunier M., Brement M., Kaplan C.
      Blood 99:4449-4456(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ILE-166, CHARACTERIZATION OF VARIANT ILE-166.
    54. "A novel 196Leu to Pro substitution in the beta3 subunit of the alphaIIbbeta3 integrin in a patient with a variant form of Glanzmann thrombasthenia."
      Nurden A.T., Ruan J., Pasquet J.-M., Gauthier B., Combrie R., Kunicki T., Nurden P.
      Platelets 13:101-111(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT PRO-222.
    55. "Glanzmann's thrombasthenia: identification of 19 new mutations in 30 patients."
      D'Andrea G., Colaizzo D., Vecchione G., Grandone E., Di Minno G., Margaglione M.
      Thromb. Haemost. 87:1034-1042(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT TRP-119; VAL-243 AND ARG-601.
    56. "Two new beta3 integrin mutations in Indian patients with Glanzmann thrombasthenia: localization of mutations affecting cysteine residues in integrin beta3."
      Nair S., Li J., Mitchell W.B., Mohanty D., Coller B.S., French D.L.
      Thromb. Haemost. 88:503-509(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT TYR-532.
    57. "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."
      Gonzalez-Manchon C., Butta N., Larrucea S., Arias-Salgado E.G., Alonso S., Lopez A., Parrilla R.
      Thromb. Haemost. 92:1377-1386(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GT VAL-150, CHARACTERIZATION OF VARIANT GT VAL-150.
    58. "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."
      Tanaka S., Hayashi T., Yoshimura K., Nakayama M., Fujita T., Amano T., Tani Y.
      J. Thromb. Haemost. 3:68-73(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT PRO-306 AND ASN-330, CHARACTERIZATION OF VARIANT GT ASN-330.
    59. "Mutations in GPIIIa molecule as a cause for Glanzmann thrombasthenia in Indian patients."
      Nair S., Ghosh K., Shetty S., Mohanty D.
      J. Thromb. Haemost. 3:482-488(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GT CYS-141 AND LEU-321.
    60. "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."
      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.
      Blood 111:3407-3414(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BDPLT16 HIS-749, CHARACTERIZATION OF VARIANT BDPLT16 HIS-749.
    61. "AlphaIIbbeta3 integrin: new allelic variants in Glanzmann thrombasthenia, effects on ITGA2B and ITGB3 mRNA splicing, expression, and structure-function."
      Jallu V., Dusseaux M., Panzer S., Torchet M.F., Hezard N., Goudemand J., de Brevern A.G., Kaplan C.
      Hum. Mutat. 31:237-246(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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.

    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: October 1, 2014
    This is version 206 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

    External Data

    Dasty 3