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P13224

- GP1BB_HUMAN

UniProt

P13224 - GP1BB_HUMAN

Protein

Platelet glycoprotein Ib beta chain

Gene

GP1BB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      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 von Willebrand factor, which is already bound to the subendothelium.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. blood coagulation, intrinsic pathway Source: Reactome
    3. cell adhesion Source: UniProtKB-KW
    4. cell surface receptor signaling pathway Source: ProtInc
    5. platelet activation Source: UniProtKB

    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.
    SignaLinkiP13224.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet glycoprotein Ib beta chain
    Short name:
    GP-Ib beta
    Short name:
    GPIb-beta
    Short name:
    GPIbB
    Alternative name(s):
    Antigen CD42b-beta
    CD_antigen: CD42c
    Gene namesi
    Name:GP1BB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4440. GP1BB.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Bernard-Soulier syndrome (BSS) [MIM:231200]: A coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, thrombocytopenia, and impaired prothrombin consumption.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti113 – 1131Y → C in BSS. 1 Publication
    VAR_025000
    Natural varianti133 – 1331A → P in BSS. 1 Publication
    VAR_025001

    Keywords - Diseasei

    Bernard Soulier syndrome, Disease mutation

    Organism-specific databases

    MIMi231200. phenotype.
    Orphaneti567. 22q11.2 deletion syndrome.
    274. Bernard-Soulier syndrome.
    853. Fetal and neonatal alloimmune thrombocytopenia.
    PharmGKBiPA179.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 206180Platelet glycoprotein Ib beta chainPRO_0000021345Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 321 Publication
    Disulfide bondi30 ↔ 391 Publication
    Glycosylationi66 – 661N-linked (GlcNAc...)2 Publications
    Disulfide bondi93 ↔ 1181 Publication
    Disulfide bondi95 ↔ 1411 Publication
    Disulfide bondi147 – 147Interchain (with C-500 or C-501 in GP1BA)1 Publication
    Modified residuei191 – 1911Phosphoserine; by PKA3 Publications
    Modified residuei193 – 1931Phosphothreonine1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP13224.
    PaxDbiP13224.
    PRIDEiP13224.

    2D gel databases

    OGPiP13224.

    PTM databases

    PhosphoSiteiP13224.

    Expressioni

    Tissue specificityi

    Expressed in heart and brain.1 Publication

    Gene expression databases

    GenevestigatoriP13224.

    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.2 Publications

    Protein-protein interaction databases

    BioGridi109074. 6 interactions.
    IntActiP13224. 3 interactions.
    MINTiMINT-1530456.
    STRINGi9606.ENSP00000383382.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 333
    Beta strandi36 – 383
    Turni46 – 483
    Beta strandi58 – 614
    Turni72 – 743
    Helixi75 – 773
    Beta strandi83 – 853
    Helixi95 – 973
    Helixi98 – 1058
    Helixi111 – 1133
    Beta strandi117 – 1215
    Turni122 – 1265
    Helixi129 – 1313
    Helixi134 – 1396

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3REZX-ray2.35A/B/C/D26-146[»]
    3RFEX-ray1.24A/B26-146[»]
    ProteinModelPortaliP13224.
    SMRiP13224. Positions 26-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 147121ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini173 – 20634CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei148 – 17225HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 5529LRRNTAdd
    BLAST
    Repeati60 – 8324LRRAdd
    BLAST
    Domaini89 – 14355LRRCTAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Leucine-rich repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG266400.
    HOGENOMiHOG000060136.
    HOVERGENiHBG051791.
    InParanoidiP13224.
    KOiK06262.
    OMAiFPPDTTE.
    OrthoDBiEOG75MVZ1.
    PhylomeDBiP13224.

    Family and domain databases

    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR000372. LRR-contain_N.
    [Graphical view]
    PfamiPF01463. LRRCT. 1 hit.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    SMARTiSM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P13224-1) [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

    MGSGPRGALS LLLLLLAPPS RPAAGCPAPC SCAGTLVDCG RRGLTWASLP    50
    TAFPVDTTEL VLTGNNLTAL PPGLLDALPA LRTAHLGANP WRCDCRLVPL 100
    RAWLAGRPER APYRDLRCVA PPALRGRLLP YLAEDELRAA CAPGPLCWGA 150
    LAAQLALLGL GLLHALLLVL LLCRLRRLRA RARARAAARL SLTDPLVAER 200
    AGTDES 206
    Length:206
    Mass (Da):21,718
    Last modified:January 1, 1990 - v1
    Checksum:iB5E81EB6F57DE0D9
    GO
    Isoform 2 (identifier: P13224-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-3: MGS → MIPSRHTMLR...RSAYCGASLA

    Show »
    Length:411
    Mass (Da):43,158
    Checksum:i7D84D76AA079DFCF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti113 – 1131Y → C in BSS. 1 Publication
    VAR_025000
    Natural varianti133 – 1331A → P in BSS. 1 Publication
    VAR_025001

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 33MGS → MIPSRHTMLRFLPVVNAASC PGDRRTMLVNVAAGVRVLRV PLRAGGSGSLSGLRPPAIVC YLPLQRASAASGLFLARPQH CGRCGRGRGGAALSLGSPAY ASRCRVSRAAVFSPWAPVSL ESGRAPGCSLGRPGLRGALV VWLQLGETWVRLRGDFQPAC GVVRVERLAGYRDAGHQGLD GAGPAVWVLRDVAQVPADRS AYCGASLA in isoform 2. 1 PublicationVSP_032671

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03259 mRNA. Translation: AAA52594.1.
    AF006988 Genomic DNA. Translation: AAC39781.1.
    L20860 mRNA. Translation: AAA20398.1.
    U59632 mRNA. Translation: AAB93437.1.
    AB086231 Genomic DNA. Translation: BAC00777.1.
    CCDSiCCDS42980.1. [P13224-1]
    PIRiA54137. NBHUIB.
    I55604.
    RefSeqiNP_000398.1. NM_000407.4. [P13224-1]
    UniGeneiHs.283743.
    Hs.728762.

    Genome annotation databases

    EnsembliENST00000366425; ENSP00000383382; ENSG00000203618. [P13224-1]
    GeneIDi2812.
    KEGGihsa:2812.
    UCSCiuc002zpz.2. human. [P13224-1]

    Polymorphism databases

    DMDMi121532.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03259 mRNA. Translation: AAA52594.1 .
    AF006988 Genomic DNA. Translation: AAC39781.1 .
    L20860 mRNA. Translation: AAA20398.1 .
    U59632 mRNA. Translation: AAB93437.1 .
    AB086231 Genomic DNA. Translation: BAC00777.1 .
    CCDSi CCDS42980.1. [P13224-1 ]
    PIRi A54137. NBHUIB.
    I55604.
    RefSeqi NP_000398.1. NM_000407.4. [P13224-1 ]
    UniGenei Hs.283743.
    Hs.728762.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3REZ X-ray 2.35 A/B/C/D 26-146 [» ]
    3RFE X-ray 1.24 A/B 26-146 [» ]
    ProteinModelPortali P13224.
    SMRi P13224. Positions 26-143.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109074. 6 interactions.
    IntActi P13224. 3 interactions.
    MINTi MINT-1530456.
    STRINGi 9606.ENSP00000383382.

    PTM databases

    PhosphoSitei P13224.

    Polymorphism databases

    DMDMi 121532.

    2D gel databases

    OGPi P13224.

    Proteomic databases

    MaxQBi P13224.
    PaxDbi P13224.
    PRIDEi P13224.

    Protocols and materials databases

    DNASUi 2812.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366425 ; ENSP00000383382 ; ENSG00000203618 . [P13224-1 ]
    GeneIDi 2812.
    KEGGi hsa:2812.
    UCSCi uc002zpz.2. human. [P13224-1 ]

    Organism-specific databases

    CTDi 2812.
    GeneCardsi GC22P019710.
    HGNCi HGNC:4440. GP1BB.
    MIMi 138720. gene.
    231200. phenotype.
    neXtProti NX_P13224.
    Orphaneti 567. 22q11.2 deletion syndrome.
    274. Bernard-Soulier syndrome.
    853. Fetal and neonatal alloimmune thrombocytopenia.
    PharmGKBi PA179.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG266400.
    HOGENOMi HOG000060136.
    HOVERGENi HBG051791.
    InParanoidi P13224.
    KOi K06262.
    OMAi FPPDTTE.
    OrthoDBi EOG75MVZ1.
    PhylomeDBi P13224.

    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 P13224.

    Miscellaneous databases

    GeneWikii GP1BB.
    GenomeRNAii 2812.
    NextBioi 11079.
    PROi P13224.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P13224.

    Family and domain databases

    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR000372. LRR-contain_N.
    [Graphical view ]
    Pfami PF01463. LRRCT. 1 hit.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    SMARTi SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence."
      Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Davie E.W., Roth G.J.
      Proc. Natl. Acad. Sci. U.S.A. 85:2135-2139(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION AT ASN-66.
    2. "Structural characterization and chromosomal location of the gene encoding human platelet glycoprotein Ib beta."
      Yagi M., Edelhoff S., Disteche C.M., Roth G.J.
      J. Biol. Chem. 269:17424-17427(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Brain.
    3. "Complementary DNA cloning of the alternatively expressed endothelial cell glycoprotein Ib beta (GPIb beta) and localization of the GPIb beta gene to chromosome 22."
      Kelly M.D., Essex D.W., Shapiro S.S., Meloni F.J., Druck T., Huebner K., Konkle B.A.
      J. Clin. Invest. 93:2417-2424(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Umbilical vein.
    4. "Alternative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence."
      Zieger B., Hashimoto Y., Ware J.
      J. Clin. Invest. 99:520-525(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Missense mutations of the glycoprotein (GP) Ib beta gene impairing the GPIb alpha/beta disulfide linkage in a family with giant platelet disorder."
      Kunishima S., Lopez J.A., Kobayashi S., Imai N., Kamiya T., Saito H., Naoe T.
      Blood 89:2404-2412(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-206, VARIANTS BSS CYS-113 AND PRO-133.
    6. "Isolation and characterization of the alpha and beta chains of human platelet glycoprotein Ib."
      Canfield V.A., Ozols J., Nugent D., Roth G.J.
      Biochem. Biophys. Res. Commun. 147:526-534(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 27-40.
    7. "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 83-92 AND 190-200.
      Tissue: Platelet.
    8. "Platelet glycoprotein Ib beta is phosphorylated on serine 166 by cyclic AMP-dependent protein kinase."
      Wardell M.R., Reynolds C.C., Berndt M.C., Wallace R.W., Fox J.E.B.
      J. Biol. Chem. 264:15656-15661(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-191, PROTEIN SEQUENCE OF 186-200.
    9. "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 BOND.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND THR-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. Carrascal M., Abian J.
      Submitted (JAN-2008) to UniProtKB
      Cited for: PHOSPHORYLATION AT SER-191, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "Quaternary organization of GPIb-IX complex and insights into Bernard-Soulier syndrome revealed by the structures of GPIbbeta and a GPIbbeta/GPIX chimera."
      McEwan P.A., Yang W., Carr K.H., Mo X., Zheng X., Li R., Emsley J.
      Blood 118:5292-5301(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 26-146, GLYCOSYLATION AT ASN-66, DISULFIDE BONDS.

    Entry informationi

    Entry nameiGP1BB_HUMAN
    AccessioniPrimary (citable) accession number: P13224
    Secondary accession number(s): Q14422, Q8NG40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 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.

    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 22
      Human chromosome 22: 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