GP1BA

From Wikipedia, the free encyclopedia
Jump to: navigation, search
GP1BA
Protein GP1BA PDB 1gwb.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases GP1BA, BDPLT1, BDPLT3, BSS, CD42B, CD42b-alpha, DBPLT3, GP1B, GPIbA, VWDP, GPIbalpha, glycoprotein Ib platelet alpha subunit
External IDs MGI: 1333744 HomoloGene: 143 GeneCards: 2811
RNA expression pattern
PBB GE GP1BA 207389 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000173

NM_010326

RefSeq (protein)

NP_000164.5

NP_034456.2

Location (UCSC) Chr 17: 4.93 – 4.94 Mb Chr 11: 70.64 – 70.64 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Platelet glycoprotein Ib alpha chain also known as glycoprotein Ib (platelet), alpha polypeptide or CD42b (Cluster of Differentiation 42b), is a protein that in humans is encoded by the GP1BA gene.

Function[edit]

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 DC, Kavanagh TJ, Roth GJ (February 1998). "Human signaling protein 14-3-3zeta interacts with platelet glycoprotein Ib subunits Ibalpha and Ibbeta". Blood 91 (4): 1295–303. PMID 9454760. 
  3. ^ Du X, Fox JE, 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. 271 (13): 7362–7. doi:10.1074/jbc.271.13.7362. PMID 8631758. 
  4. ^ Feng S, Christodoulides N, Reséndiz JC, Berndt MC, Kroll MH (January 2000). "Cytoplasmic domains of GpIbalpha and GpIbbeta regulate 14-3-3zeta binding to GpIb/IX/V". Blood 95 (2): 551–7. PMID 10627461. 
  5. ^ Takafuta T, Wu G, Murphy GF, Shapiro SS (July 1998). "Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha". J. Biol. Chem. 273 (28): 17531–8. doi:10.1074/jbc.273.28.17531. 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.