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P07359

- GP1BA_HUMAN

UniProt

P07359 - GP1BA_HUMAN

Protein

Platelet glycoprotein Ib alpha chain

Gene

GP1BA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 2 (16 Apr 2014)
      Previous versions | rss
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    Functioni

    GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. thrombin receptor activity Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: MGI
    2. blood coagulation, intrinsic pathway Source: Reactome
    3. cell adhesion Source: MGI
    4. cell morphogenesis Source: Ensembl
    5. cell surface receptor signaling pathway Source: ProtInc
    6. fibrinolysis Source: UniProtKB
    7. platelet activation Source: UniProtKB
    8. regulation of blood coagulation Source: UniProtKB
    9. thrombin receptor signaling pathway Source: GOC

    Keywords - Biological processi

    Blood coagulation, Cell adhesion, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_1230. Platelet Adhesion to exposed collagen.
    REACT_23847. GP1b-IX-V activation signalling.
    REACT_278. Platelet Aggregation (Plug Formation).
    REACT_326. Intrinsic Pathway.
    SignaLinkiP07359.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet glycoprotein Ib alpha chain
    Short name:
    GP-Ib alpha
    Short name:
    GPIb-alpha
    Short name:
    GPIbA
    Short name:
    Glycoprotein Ibalpha
    Alternative name(s):
    Antigen CD42b-alpha
    CD_antigen: CD42b
    Cleaved into the following chain:
    Gene namesi
    Name:GP1BA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:4439. GP1BA.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: Ensembl
    2. integral component of plasma membrane Source: ProtInc
    3. membrane Source: MGI
    4. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Non-arteritic anterior ischemic optic neuropathy (NAION) [MIM:258660]: An ocular disease due to ischemic injury to the optic nerve. It usually affects the optic disk and leads to visual loss and optic disk swelling of a pallid nature. Visual loss is usually sudden, or over a few days at most and is usually permanent, with some recovery possibly occurring within the first weeks or months. Patients with small disks having smaller or non-existent cups have an anatomical predisposition for non-arteritic anterior ischemic optic neuropathy. As an ischemic episode evolves, the swelling compromises circulation, with a spiral of ischemia resulting in further neuronal damage.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Bernard-Soulier syndrome (BSS) [MIM:231200]: A coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, thrombocytopenia, and impaired prothrombin consumption.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti73 – 731L → F in BSS. 1 Publication
    VAR_014206
    Natural varianti81 – 811C → R in BSS. 1 Publication
    VAR_005256
    Natural varianti145 – 1451L → P in BSS. 1 Publication
    VAR_014207
    Natural varianti172 – 1721A → V in BSS and BSSA2. 2 Publications
    VAR_005258
    Natural varianti195 – 1951Missing in BSS. 1 Publication
    VAR_005259
    Natural varianti225 – 2251C → S in BSS. 1 Publication
    VAR_005260
    Bernard-Soulier syndrome A2, autosomal dominant (BSSA2) [MIM:153670]: A coagulation disorder characterized by mild to moderate bleeding tendency, thrombocytopenia, and an increased mean platelet volume. Some individuals have no symptoms. Mild bleeding tendencies manifest as epistaxis, gingival bleeding, menorrhagia, easy bruising, or prolonged bleeding after dental surgery.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti172 – 1721A → V in BSS and BSSA2. 2 Publications
    VAR_005258
    Pseudo-von Willebrand disease (VWDP) [MIM:177820]: A bleeding disorder characterized by abnormally enhanced binding of von Willebrand factor by the platelet glycoprotein Ib (GP Ib) receptor complex. Hemostatic function is impaired due to the removal of VWF multimers from the circulation.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti249 – 2491G → S in VWDP. 1 Publication
    VAR_019657
    Natural varianti249 – 2491G → V in VWDP. 2 Publications
    VAR_005261
    Natural varianti255 – 2551M → V in VWDP; increased binding to vWF. 1 Publication
    VAR_005262

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi249 – 2491G → A: No change. 1 Publication
    Mutagenesisi249 – 2491G → K or D: Decreased binding to vWF. 1 Publication
    Mutagenesisi249 – 2491G → S or V: Increased binding to vWF. 1 Publication

    Keywords - Diseasei

    Bernard Soulier syndrome, Disease mutation, von Willebrand disease

    Organism-specific databases

    MIMi153670. phenotype.
    177820. phenotype.
    231200. phenotype.
    258660. phenotype.
    Orphaneti274. Bernard-Soulier syndrome.
    853. Fetal and neonatal alloimmune thrombocytopenia.
    52530. Von Willebrand disease, platelet type.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16161 PublicationAdd
    BLAST
    Chaini17 – 652636Platelet glycoprotein Ib alpha chainPRO_0000021343Add
    BLAST
    Chaini17 – ?GlycocalicinPRO_0000021344

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi20 ↔ 331 Publication
    Glycosylationi37 – 371N-linked (GlcNAc...)1 Publication
    Glycosylationi175 – 1751N-linked (GlcNAc...)
    Disulfide bondi225 ↔ 2641 Publication
    Disulfide bondi227 ↔ 2801 Publication
    Modified residuei292 – 2921Sulfotyrosine1 Publication
    Modified residuei294 – 2941Sulfotyrosine1 Publication
    Modified residuei295 – 2951Sulfotyrosine1 Publication
    Glycosylationi308 – 3081O-linked (GalNAc...)
    Disulfide bondi526 – 526Interchain (with C-147 in GP1BB)1 Publication
    Disulfide bondi527 – 527Interchain (with C-147 in GP1BB)1 Publication
    Modified residuei629 – 6291Phosphoserine1 Publication
    Modified residuei632 – 6321Phosphoserine1 Publication

    Post-translational modificationi

    Glycocalicin, which is approximately coextensive with the extracellular part of the molecule, is cleaved off by calpain during platelet lysis.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

    Proteomic databases

    PaxDbiP07359.
    PRIDEiP07359.

    PTM databases

    PhosphoSiteiP07359.
    UniCarbKBiP07359.

    Miscellaneous databases

    PMAP-CutDBP07359.

    Expressioni

    Gene expression databases

    ArrayExpressiP07359.
    BgeeiP07359.
    CleanExiHS_GP1BA.
    GenevestigatoriP07359.

    Organism-specific databases

    HPAiCAB002496.
    HPA013316.

    Interactioni

    Subunit structurei

    Two GP-Ib beta are disulfide-linked to one GP-Ib alpha. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage. Interacts with FLNB.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VWFP042752EBI-297082,EBI-981819

    Protein-protein interaction databases

    IntActiP07359. 12 interactions.
    MINTiMINT-147226.
    STRINGi9606.ENSP00000329380.

    Structurei

    Secondary structure

    1
    652
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 235
    Beta strandi30 – 323
    Beta strandi51 – 533
    Beta strandi60 – 634
    Helixi64 – 674
    Beta strandi75 – 773
    Beta strandi85 – 873
    Beta strandi97 – 993
    Turni112 – 1143
    Beta strandi120 – 1223
    Turni135 – 1384
    Beta strandi144 – 1463
    Turni157 – 1626
    Beta strandi168 – 1703
    Turni181 – 1866
    Beta strandi192 – 1943
    Turni205 – 2106
    Beta strandi214 – 2174
    Helixi227 – 2293
    Helixi230 – 2389
    Helixi240 – 2423
    Beta strandi243 – 2497
    Helixi252 – 2543
    Helixi259 – 2613
    Beta strandi262 – 2643
    Turni265 – 2684
    Helixi272 – 2743
    Beta strandi283 – 2875
    Beta strandi605 – 6139

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GWBX-ray2.80A/B16-296[»]
    1K13model-A52-216[»]
    1M0ZX-ray1.85A/B17-306[»]
    1M10X-ray3.10B17-306[»]
    1OOKX-ray2.30G17-306[»]
    1P8VX-ray2.60A17-294[»]
    1P9AX-ray1.70G17-306[»]
    1QYYX-ray2.80A/G17-306[»]
    1SQ0X-ray2.60B17-304[»]
    1U0NX-ray2.95D17-281[»]
    2BP3X-ray2.32S/T598-619[»]
    3P72X-ray1.90A17-281[»]
    3PMHX-ray3.20G17-306[»]
    4C2AX-ray2.08B17-306[»]
    4C2BX-ray2.80B/D/F/H17-306[»]
    4CH2X-ray1.60P/Q287-300[»]
    4CH8X-ray1.75P/Q/R/S287-300[»]
    4MGXX-ray3.16B603-611[»]
    ProteinModelPortaliP07359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07359.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 531515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini553 – 652100CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei532 – 55221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 4731LRRNTAdd
    BLAST
    Repeati48 – 6821LRR 1Add
    BLAST
    Repeati72 – 9322LRR 2Add
    BLAST
    Repeati94 – 11522LRR 3Add
    BLAST
    Repeati117 – 13721LRR 4Add
    BLAST
    Repeati141 – 16222LRR 5Add
    BLAST
    Repeati165 – 18622LRR 6Add
    BLAST
    Repeati189 – 21022LRR 7Add
    BLAST
    Domaini221 – 28262LRRCTAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi345 – 482138Pro/Thr-richAdd
    BLAST

    Sequence similaritiesi

    Contains 7 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG294000.
    HOVERGENiHBG051790.
    InParanoidiP07359.
    KOiK06261.
    OMAiTVPRAWL.
    OrthoDBiEOG7GBFXK.
    PhylomeDBiP07359.
    TreeFamiTF351114.

    Family and domain databases

    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PfamiPF00560. LRR_1. 1 hit.
    PF13504. LRR_7. 1 hit.
    PF13855. LRR_8. 1 hit.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 2 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07359-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLLLLLLLL PSPLHPHPIC EVSKVASHLE VNCDKRNLTA LPPDLPKDTT    50
    ILHLSENLLY TFSLATLMPY TRLTQLNLDR CELTKLQVDG TLPVLGTLDL 100
    SHNQLQSLPL LGQTLPALTV LDVSFNRLTS LPLGALRGLG ELQELYLKGN 150
    ELKTLPPGLL TPTPKLEKLS LANNNLTELP AGLLNGLENL DTLLLQENSL 200
    YTIPKGFFGS HLLPFAFLHG NPWLCNCEIL YFRRWLQDNA ENVYVWKQGV 250
    DVKAMTSNVA SVQCDNSDKF PVYKYPGKGC PTLGDEGDTD LYDYYPEEDT 300
    EGDKVRATRT VVKFPTKAHT TPWGLFYSWS TASLDSQMPS SLHPTQESTK 350
    EQTTFPPRWT PNFTLHMESI TFSKTPKSTT EPTPSPTTSE PVPEPAPNMT 400
    TLEPTPSPTT PEPTSEPAPS PTTPEPTSEP APSPTTPEPT SEPAPSPTTP 450
    EPTPIPTIAT SPTILVSATS LITPKSTFLT TTKPVSLLES TKKTIPELDQ 500
    PPKLRGVLQG HLESSRNDPF LHPDFCCLLP LGFYVLGLFW LLFASVVLIL 550
    LLSWVGHVKP QALDSGQGAA LTTATQTTHL ELQRGRQVTV PRAWLLFLRG 600
    SLPTFRSSLF LWVRPNGRVG PLVAGRRPSA LSQGRGQDLL STVSIRYSGH 650
    SL 652
    Length:652
    Mass (Da):71,540
    Last modified:April 16, 2014 - v2
    Checksum:i053346683AEB927E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti619 – 6191V → L in AAH27955. (PubMed:15489334)Curated

    Polymorphismi

    Position 161 is associated with platelet-specific alloantigen Siba. Siba- has Thr-161 and Siba+ has Met-161. Siba is involved in neonatal alloimmune thrombocytopenia (NATP).
    Polymorphisms arise from a variable number of tandem 13-amino acid repeats of S-E-P-A-P-S-P-T-T-P-E-P-T in the mucin-like macroglycopeptide (Pro/Thr-rich) domain. Allele D contains one repeat starting at position 415, allele C contains two repeats, allele B (shown here) contains three repeats and allele A contains four repeats. Allele B is associated with susceptibility to nonarteritic anterior ischemic optic neuropathy.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti72 – 721R → H.1 Publication
    Corresponds to variant rs6068 [ dbSNP | Ensembl ].
    VAR_011909
    Natural varianti73 – 731L → F in BSS. 1 Publication
    VAR_014206
    Natural varianti81 – 811C → R in BSS. 1 Publication
    VAR_005256
    Natural varianti86 – 861L → F.1 Publication
    Corresponds to variant rs13306411 [ dbSNP | Ensembl ].
    VAR_013511
    Natural varianti145 – 1451L → P in BSS. 1 Publication
    VAR_014207
    Natural varianti161 – 1611T → M in Siba(+). 4 Publications
    Corresponds to variant rs6065 [ dbSNP | Ensembl ].
    VAR_005257
    Natural varianti172 – 1721A → V in BSS and BSSA2. 2 Publications
    VAR_005258
    Natural varianti195 – 1951Missing in BSS. 1 Publication
    VAR_005259
    Natural varianti225 – 2251C → S in BSS. 1 Publication
    VAR_005260
    Natural varianti249 – 2491G → S in VWDP. 1 Publication
    VAR_019657
    Natural varianti249 – 2491G → V in VWDP. 2 Publications
    VAR_005261
    Natural varianti254 – 2541A → S.
    Corresponds to variant rs382524 [ dbSNP | Ensembl ].
    VAR_011910
    Natural varianti255 – 2551M → V in VWDP; increased binding to vWF. 1 Publication
    VAR_005262

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02940 mRNA. Translation: AAA52595.1.
    M22403 Genomic DNA. Translation: AAA52596.1.
    AB038516 Genomic DNA. Translation: BAB12038.1.
    AB086948 Genomic DNA. Translation: BAC10305.1.
    AF395009 Genomic DNA. Translation: AAK71325.1.
    AC233723 Genomic DNA. No translation available.
    BC027955 mRNA. Translation: AAH27955.1.
    D85894 Genomic DNA. Translation: BAA12911.1.
    S34436 Genomic DNA. Translation: AAB22152.1.
    S34439 Genomic DNA. Translation: AAB22153.1.
    L39103 Genomic DNA. Translation: AAA69491.1.
    CCDSiCCDS54068.1.
    PIRiA94174. NBHUIA.
    I70082.
    RefSeqiNP_000164.5. NM_000173.5.
    UniGeneiHs.1472.

    Genome annotation databases

    EnsembliENST00000329125; ENSP00000329380; ENSG00000185245.
    GeneIDi2811.
    KEGGihsa:2811.

    Polymorphism databases

    DMDMi121531.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J02940 mRNA. Translation: AAA52595.1 .
    M22403 Genomic DNA. Translation: AAA52596.1 .
    AB038516 Genomic DNA. Translation: BAB12038.1 .
    AB086948 Genomic DNA. Translation: BAC10305.1 .
    AF395009 Genomic DNA. Translation: AAK71325.1 .
    AC233723 Genomic DNA. No translation available.
    BC027955 mRNA. Translation: AAH27955.1 .
    D85894 Genomic DNA. Translation: BAA12911.1 .
    S34436 Genomic DNA. Translation: AAB22152.1 .
    S34439 Genomic DNA. Translation: AAB22153.1 .
    L39103 Genomic DNA. Translation: AAA69491.1 .
    CCDSi CCDS54068.1.
    PIRi A94174. NBHUIA.
    I70082.
    RefSeqi NP_000164.5. NM_000173.5.
    UniGenei Hs.1472.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GWB X-ray 2.80 A/B 16-296 [» ]
    1K13 model - A 52-216 [» ]
    1M0Z X-ray 1.85 A/B 17-306 [» ]
    1M10 X-ray 3.10 B 17-306 [» ]
    1OOK X-ray 2.30 G 17-306 [» ]
    1P8V X-ray 2.60 A 17-294 [» ]
    1P9A X-ray 1.70 G 17-306 [» ]
    1QYY X-ray 2.80 A/G 17-306 [» ]
    1SQ0 X-ray 2.60 B 17-304 [» ]
    1U0N X-ray 2.95 D 17-281 [» ]
    2BP3 X-ray 2.32 S/T 598-619 [» ]
    3P72 X-ray 1.90 A 17-281 [» ]
    3PMH X-ray 3.20 G 17-306 [» ]
    4C2A X-ray 2.08 B 17-306 [» ]
    4C2B X-ray 2.80 B/D/F/H 17-306 [» ]
    4CH2 X-ray 1.60 P/Q 287-300 [» ]
    4CH8 X-ray 1.75 P/Q/R/S 287-300 [» ]
    4MGX X-ray 3.16 B 603-611 [» ]
    ProteinModelPortali P07359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P07359. 12 interactions.
    MINTi MINT-147226.
    STRINGi 9606.ENSP00000329380.

    PTM databases

    PhosphoSitei P07359.
    UniCarbKBi P07359.

    Polymorphism databases

    DMDMi 121531.

    Proteomic databases

    PaxDbi P07359.
    PRIDEi P07359.

    Protocols and materials databases

    DNASUi 2811.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000329125 ; ENSP00000329380 ; ENSG00000185245 .
    GeneIDi 2811.
    KEGGi hsa:2811.

    Organism-specific databases

    CTDi 2811.
    GeneCardsi GC17P004835.
    H-InvDB HIX0212275.
    HGNCi HGNC:4439. GP1BA.
    HPAi CAB002496.
    HPA013316.
    MIMi 153670. phenotype.
    177820. phenotype.
    231200. phenotype.
    258660. phenotype.
    606672. gene.
    neXtProti NX_P07359.
    Orphaneti 274. Bernard-Soulier syndrome.
    853. Fetal and neonatal alloimmune thrombocytopenia.
    52530. Von Willebrand disease, platelet type.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG294000.
    HOVERGENi HBG051790.
    InParanoidi P07359.
    KOi K06261.
    OMAi TVPRAWL.
    OrthoDBi EOG7GBFXK.
    PhylomeDBi P07359.
    TreeFami TF351114.

    Enzyme and pathway databases

    Reactomei REACT_1230. Platelet Adhesion to exposed collagen.
    REACT_23847. GP1b-IX-V activation signalling.
    REACT_278. Platelet Aggregation (Plug Formation).
    REACT_326. Intrinsic Pathway.
    SignaLinki P07359.

    Miscellaneous databases

    EvolutionaryTracei P07359.
    NextBioi 11075.
    PMAP-CutDB P07359.
    PROi P07359.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07359.
    Bgeei P07359.
    CleanExi HS_GP1BA.
    Genevestigatori P07359.

    Family and domain databases

    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    Pfami PF00560. LRR_1. 1 hit.
    PF13504. LRR_7. 1 hit.
    PF13855. LRR_8. 1 hit.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 2 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein."
      Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Papayannopoulou T., Roth G.J.
      Proc. Natl. Acad. Sci. U.S.A. 84:5615-5619(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Structure of the human blood platelet membrane glycoprotein Ib alpha gene."
      Wenger R.H., Kieffer N., Wicki A.N., Clemetson K.J.
      Biochem. Biophys. Res. Commun. 156:389-395(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "A novel polymorphism, 70Leu/Phe, disrupts a consensus Leu residue within the leucine-rich repeat sequence of platelet glycoprotein Ibalpha."
      Matsubara Y., Murata M., Moriki T., Yokoyama K., Watanabe N., Nakajima H., Handa M., Kawano K., Aoki N., Yoshino H., Ikeda Y.
      Thromb. Haemost. 87:867-872(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-86.
    4. "Identification of a novel point mutation in platelet glycoprotein Ibalpha, Gly to Ser at residue 233, in a Japanese family with platelet-type von Willebrand disease."
      Matsubara Y., Murata M., Sugita K., Ikeda Y.
      J. Thromb. Haemost. 1:2198-2205(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VWDP SER-249, CHARACTERIZATION OF VARIANT VWDP VAL-255, MUTAGENESIS OF GLY-249.
    5. SeattleSNPs variation discovery resource
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-161.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Lung.
    8. "Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib."
      Titani K., Takio K., Handa M., Ruggeri Z.M.
      Proc. Natl. Acad. Sci. U.S.A. 84:5610-5614(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-315, STRUCTURE OF CARBOHYDRATE.
    9. "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 128-137.
      Tissue: Platelet.
    10. "StyI polymorphism at nucleotide 1610 in the human platelet glycoprotein Ib alpha gene."
      Suzuki K., Hayashi T., Akiba J., Yahagi A., Tajima K., Satoh S., Sasaki H.
      Jpn. J. Hum. Genet. 41:419-421(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-397.
    11. "Identification of the disulphide bonds in human platelet glycocalicin."
      Hess D., Schaller J., Rickli E.E., Clemetson K.J.
      Eur. J. Biochem. 199:389-393(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BONDS.
    12. "Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha."
      Takafuta T., Wu G., Murphy G.F., Shapiro S.S.
      J. Biol. Chem. 273:17531-17538(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLNB.
      Tissue: Endothelial cell and Placenta.
    13. "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-37.
      Tissue: Platelet.
    14. "Glycoprotein Ibalpha forms disulfide bonds with 2 glycoprotein Ibbeta subunits in the resting platelet."
      Luo S.Z., Mo X., Afshar-Kharghan V., Srinivasan S., Lopez J.A., Li R.
      Blood 109:603-609(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERCHAIN DISULFIDE BONDS.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629 AND SER-632, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    16. "Crystal structure of the platelet glycoprotein Ibalpha N-terminal domain reveals an unmasking mechanism for receptor activation."
      Uff S., Clemetson J.M., Harrison T., Clemetson K.J., Emsley J.
      J. Biol. Chem. 277:35657-35663(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-304, SULFATION AT TYR-292; TYR-294 AND TYR-295.
    17. "Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain."
      Huizinga E.G., Tsuji S., Romijn R.A., Schiphorst M.E., de Groot P.G., Sixma J.J., Gros P.
      Science 297:1176-1179(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
    18. "Molecular modeling of the seven tandem leucine-rich repeats within the ligand-binding region of platelet glycoprotein Ib alpha."
      Whisstock J.C., Shen Y., Lopez J.A., Andrews R.K., Berndt M.C.
      Thromb. Haemost. 87:329-333(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 52-216.
    19. "Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness."
      Murata M., Furihata K., Ishida F., Russell S.R., Ware J., Ruggeri Z.M.
      Blood 79:3086-3090(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SIBA MET-161.
    20. "Mutation of leucine-57 to phenylalanine in a platelet glycoprotein Ib alpha leucine tandem repeat occurring in patients with an autosomal dominant variant of Bernard-Soulier disease."
      Miller J.L., Lyle V.A., Cunningham D.
      Blood 79:439-446(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSS PHE-73.
    21. "Polymorphism of human glycoprotein Ib alpha results from a variable number of tandem repeats of a 13-amino acid sequence in the mucin-like macroglycopeptide region. Structure/function implications."
      Lopez J.A., Ludwig E.H., McCarthy B.J.
      J. Biol. Chem. 267:10055-10061(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM OF PRO/THR-RICH DOMAIN.
    22. "Point mutation in a leucine-rich repeat of platelet glycoprotein Ib alpha resulting in the Bernard-Soulier syndrome."
      Ware J., Russell S.R., Marchese P., Murata M., Mazzucato M., de Marco L., Ruggeri Z.M.
      J. Clin. Invest. 92:1213-1220(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSS VAL-172.
    23. "Cys209 Ser mutation in the platelet membrane glycoprotein Ib alpha gene is associated with Bernard-Soulier syndrome."
      Simsek S., Noris P., Lozano M., Pico M., von Dem Borne A.E.G.K., Ribera A., Gallardo D.
      Br. J. Haematol. 88:839-844(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSS SER-225.
    24. "Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease."
      Miller J.L., Cunningham D., Lyle V.A., Finch C.N.
      Proc. Natl. Acad. Sci. U.S.A. 88:4761-4765(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWDP VAL-249.
    25. "Expression of the phenotypic abnormality of platelet-type von Willebrand disease in a recombinant glycoprotein Ib alpha fragment."
      Murata M., Russell S.R., Ruggeri Z.M., Ware J.
      J. Clin. Invest. 91:2133-2137(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWDP VAL-249.
    26. "Pseudo-von Willebrand disease: a mutation in the platelet glycoprotein Ib alpha gene associated with a hyperactive surface receptor."
      Russell S.D., Roth G.J.
      Blood 81:1787-1791(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWDP VAL-255.
    27. "The largest variant of platelet glycoprotein Ib alpha has four tandem repeats of 13 amino acids in the macroglycopeptide region and a genetic linkage with methionine145."
      Ishida F., Furihata K., Ishida K., Yan J., Kitano K., Kiyosawa K., Furuta S.
      Blood 86:1357-1360(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SIBA MET-161, POLYMORPHISM OF PRO/THR-RICH DOMAIN.
    28. "A three-base deletion removing a leucine residue in a leucine-rich repeat of platelet glycoprotein Ib alpha associated with a variant of Bernard-Soulier syndrome (Nancy I)."
      de la Salle C., Baas M.-J., Lanza F., Schwartz A., Hanau D., Chevalier J., Gachet C., Briquel M.-E., Cazenave J.-P.
      Br. J. Haematol. 89:386-396(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSS LEU-195 DEL.
    29. "Naturally occurring mutations in glycoprotein Ibalpha that result in defective ligand binding and synthesis of a truncated protein."
      Kenny D., Jonsson O.G., Morateck P.A., Montgomery R.R.
      Blood 92:175-183(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSS ARG-81.
    30. Cited for: VARIANTS HIS-72 AND MET-161.
    31. "Molecular characterization of two mutations in platelet glycoprotein (GP) Ib alpha in two Finnish Bernard-Soulier syndrome families."
      Koskela S., Partanen J., Salmi T.T., Kekomaki R.
      Eur. J. Haematol. 62:160-168(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSS PRO-145.
    32. "Autosomal dominant macrothrombocytopenia in Italy is most frequently a type of heterozygous Bernard-Soulier syndrome."
      Savoia A., Balduini C.L., Savino M., Noris P., Del Vecchio M., Perrotta S., Belletti S., Poggi V., Iolascon A.
      Blood 97:1330-1335(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT BSSA2 VAL-172.
    33. "Nonarteritic anterior ischemic optic neuropathy is associated with a specific platelet polymorphism located on the glycoprotein Ibalpha gene."
      Salomon O., Rosenberg N., Steinberg D.M., Huna-Baron R., Moisseiev J., Dardik R., Goldan O., Kurtz S., Ifrah A., Seligsohn U.
      Ophthalmology 111:184-188(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO NAION.

    Entry informationi

    Entry nameiGP1BA_HUMAN
    AccessioniPrimary (citable) accession number: P07359
    Secondary accession number(s): E7ES66
    , Q14441, Q16469, Q8N1F3, Q8NG39, Q9HDC7, Q9UEK1, Q9UQS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 16, 2014
    Last modified: October 1, 2014
    This is version 190 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

    Miscellaneous

    Platelet activation apparently involves disruption of the macromolecular complex of GP-Ib with the platelet glycoprotein IX (GP-IX) and dissociation of GP-Ib from the actin-binding protein.
    Binding sites for vWF and thrombin (the latter site with unknown function) are in the N-terminal part of the molecule.

    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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3