GP1BA

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Glycoprotein Ib (platelet), alpha polypeptide
Protein GP1BA PDB 1gwb.png
PDB rendering based on 1gwb.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols GP1BA ; BDPLT1; BDPLT3; BSS; CD42B; CD42b-alpha; DBPLT3; GP1B; GPIbA; VWDP
External IDs OMIM606672 MGI1333744 HomoloGene143 GeneCards: GP1BA Gene
RNA expression pattern
PBB GE GP1BA 207389 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 2811 14723
Ensembl ENSG00000185245 ENSMUSG00000050675
UniProt P07359 O35930
RefSeq (mRNA) NM_000173 NM_010326
RefSeq (protein) NP_000164 NP_034456
Location (UCSC) Chr 17:
4.84 – 4.84 Mb
Chr 11:
70.64 – 70.64 Mb
PubMed search [1] [2]

Glycoprotein Ib (platelet), alpha polypeptide (GP1BA) also known as CD42b (Cluster of Differentiation 42b), is a human gene.

Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds. The Gp Ib functions as a receptor for von Willebrand factor (VWF). The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX and platelet glycoprotein V. The binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury, and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis. This gene encodes the alpha subunit. Several polymorphisms and mutations have been described in this gene, some of which are the cause of Bernard-Soulier syndromes and platelet-type von Willebrand disease.[1]

Interactions[edit]

GP1BA has been shown to interact with YWHAZ[2][3][4] and FLNB.[5]

See also[edit]

References[edit]

  1. ^ "Entrez Gene: GP1BA glycoprotein Ib (platelet), alpha polypeptide". 
  2. ^ Calverley, D C; Kavanagh T J; Roth G J (February 1998). "Human signaling protein 14-3-3zeta interacts with platelet glycoprotein Ib subunits Ibalpha and Ibbeta". Blood (UNITED STATES) 91 (4): 1295–303. ISSN 0006-4971. PMID 9454760. 
  3. ^ Du, X; Fox J E; Pei S (March 1996). "Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ib alpha". J. Biol. Chem. (UNITED STATES) 271 (13): 7362–7. doi:10.1074/jbc.271.13.7362. ISSN 0021-9258. PMID 8631758. 
  4. ^ Feng, S; Christodoulides N; Reséndiz J C; Berndt M C; Kroll M H (January 2000). "Cytoplasmic domains of GpIbalpha and GpIbbeta regulate 14-3-3zeta binding to GpIb/IX/V". Blood (UNITED STATES) 95 (2): 551–7. ISSN 0006-4971. PMID 10627461. 
  5. ^ Takafuta, T; Wu G; Murphy G F; Shapiro S S (July 1998). "Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha". J. Biol. Chem. (UNITED STATES) 273 (28): 17531–8. doi:10.1074/jbc.273.28.17531. ISSN 0021-9258. PMID 9651345. 

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.