GP1BA

Protein-coding gene in the species Homo sapiens
GP1BA
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1GWB, 1M0Z, 1M10, 1OOK, 1P8V, 1P9A, 1QYY, 1SQ0, 1U0N, 2BP3, 3P72, 3PMH, 4C2A, 4C2B, 4CH2, 4CH8, 4MGX, 4YR6

Identifiers
AliasesGP1BA, BDPLT1, BDPLT3, BSS, CD42B, CD42b-alpha, DBPLT3, GP1B, GPIbA, VWDP, GPIbalpha, glycoprotein Ib platelet alpha subunit, glycoprotein Ib platelet subunit alpha
External IDsOMIM: 606672 MGI: 1333744 HomoloGene: 143 GeneCards: GP1BA
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for GP1BA
Genomic location for GP1BA
Band17p13.2Start4,932,277 bp[1]
End4,935,023 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for GP1BA
Genomic location for GP1BA
Band11 B3|11 43.2 cMStart70,529,948 bp[2]
End70,532,862 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • lymph node

  • secondary oocyte

  • trabecular bone

  • blood

  • bone marrow cells

  • tibialis anterior muscle

  • appendix

  • thymus

  • optic nerve
Top expressed in
  • blood

  • yolk sac

  • spleen

  • morula

  • right ventricle

  • submandibular gland

  • abdominal wall

  • body of femur

  • lip

  • skeletal muscle tissue
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein kinase inhibitor activity
  • thrombin-activated receptor activity
  • protein binding
Cellular component
  • cytoplasm
  • integral component of membrane
  • membrane
  • plasma membrane
  • integral component of plasma membrane
  • cell surface
  • anchored component of external side of plasma membrane
  • extracellular exosome
  • extracellular space
  • extracellular matrix
Biological process
  • blood coagulation, intrinsic pathway
  • hemostasis
  • fibrinolysis
  • negative regulation of protein kinase activity
  • cytokine-mediated signaling pathway
  • blood coagulation
  • platelet activation
  • cell surface receptor signaling pathway
  • cell adhesion
  • cell morphogenesis
  • regulation of blood coagulation
  • negative regulation of receptor signaling pathway via JAK-STAT
  • thrombin-activated receptor signaling pathway
  • platelet aggregation
  • regulation of megakaryocyte differentiation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
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: 4.93 – 4.94 MbChr 11: 70.53 – 70.53 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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

Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein receptor composed of a heterodimer, an alpha chain and a beta chain, that are linked by disulfide bonds.[5] 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 to form the glycoprotein Ib-IX-V complex. Binding of the GP Ib-IX-V complex to VWF facilitates initial platelet adhesion to vascular subendothelium after vascular injury,[6] and also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis.[7] 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.[8]

Interactions

GP1BA has been shown to interact with YWHAZ[9][10][11] and FLNB.[12]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185245 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000050675 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lopez JA, Chung DW, Fujikawa K, Hagen FS, Papayannopoulou T, Roth GJ (August 1987). "Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein". Proceedings of the National Academy of Sciences of the United States of America. 84 (16): 5615–5619. Bibcode:1987PNAS...84.5615L. doi:10.1073/pnas.84.16.5615. PMC 298913. PMID 3303030.
  6. ^ Arya M, Anvari B, Romo GM, Cruz MA, Dong JF, McIntire LV, et al. (June 2002). "Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex: studies using optical tweezers". Blood. 99 (11): 3971–3977. doi:10.1182/blood-2001-11-0060. PMID 12010796. S2CID 24850350. Retrieved 2023-09-08.
  7. ^ Jackson SP, Nesbitt WS, Kulkarni S (July 2003). "Signaling events underlying thrombus formation". Journal of Thrombosis and Haemostasis. 1 (7): 1602–1612. doi:10.1046/j.1538-7836.2003.00267.x. PMID 12871297. S2CID 22088432.
  8. ^ "Entrez Gene: GP1BA glycoprotein Ib (platelet), alpha polypeptide".
  9. ^ 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): 1295–1303. doi:10.1182/blood.V91.4.1295. PMID 9454760.
  10. ^ 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". The Journal of Biological Chemistry. 271 (13): 7362–7367. doi:10.1074/jbc.271.13.7362. PMID 8631758.
  11. ^ 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): 551–557. doi:10.1182/blood.V95.2.551. PMID 10627461. S2CID 77799615.
  12. ^ 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". The Journal of Biological Chemistry. 273 (28): 17531–17538. doi:10.1074/jbc.273.28.17531. PMID 9651345.

Further reading

  • Kunishima S, Kamiya T, Saito H (November 2002). "Genetic abnormalities of Bernard-Soulier syndrome". International Journal of Hematology. 76 (4): 319–327. doi:10.1007/BF02982690. PMID 12463594. S2CID 23635810.
  • Du X (May 2007). "Signaling and regulation of the platelet glycoprotein Ib-IX-V complex". Current Opinion in Hematology. 14 (3): 262–269. doi:10.1097/MOH.0b013e3280dce51a. PMID 17414217. S2CID 39904506.
  • Clemetson KJ (July 2007). "A short history of platelet glycoprotein Ib complex". Thrombosis and Haemostasis. 98 (1): 63–68. doi:10.1160/th07-05-0327. PMID 17597992. S2CID 958810.
  • López JA, Ludwig EH, McCarthy BJ (May 1992). "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". The Journal of Biological Chemistry. 267 (14): 10055–10061. doi:10.1016/S0021-9258(19)50199-5. PMID 1577776.
  • Murata M, Furihata K, Ishida F, Russell SR, Ware J, Ruggeri ZM (June 1992). "Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness". Blood. 79 (11): 3086–3090. doi:10.1182/blood.V79.11.3086.3086. PMID 1586750.
  • Girma JP, Takahashi Y, Yoshioka A, Diaz J, Meyer D (October 1990). "Ristocetin and botrocetin involve two distinct domains of von Willebrand factor for binding to platelet membrane glycoprotein Ib". Thrombosis and Haemostasis. 64 (2): 326–332. doi:10.1055/s-0038-1647310. PMID 1702906. S2CID 27425464.
  • Miller JL, Lyle VA, Cunningham D (January 1992). "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". Blood. 79 (2): 439–446. doi:10.1182/blood.V79.2.439.439. PMID 1730088.
  • Modderman PW, Admiraal LG, Sonnenberg A, von dem Borne AE (January 1992). "Glycoproteins V and Ib-IX form a noncovalent complex in the platelet membrane". The Journal of Biological Chemistry. 267 (1): 364–369. doi:10.1016/S0021-9258(18)48503-1. PMID 1730602.
  • Miller JL, Cunningham D, Lyle VA, Finch CN (June 1991). "Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease". Proceedings of the National Academy of Sciences of the United States of America. 88 (11): 4761–4765. Bibcode:1991PNAS...88.4761M. doi:10.1073/pnas.88.11.4761. PMC 51746. PMID 2052556.
  • Hess D, Schaller J, Rickli EE, Clemetson KJ (July 1991). "Identification of the disulphide bonds in human platelet glycocalicin". European Journal of Biochemistry. 199 (2): 389–393. doi:10.1111/j.1432-1033.1991.tb16135.x. PMID 2070794.
  • Du X, Beutler L, Ruan C, Castaldi PA, Berndt MC (May 1987). "Glycoprotein Ib and glycoprotein IX are fully complexed in the intact platelet membrane". Blood. 69 (5): 1524–1527. doi:10.1182/blood.V69.5.1524.1524. PMID 2436691.
  • Andrews RK, Booth WJ, Gorman JJ, Castaldi PA, Berndt MC (October 1989). "Purification of botrocetin from Bothrops jararaca venom. Analysis of the botrocetin-mediated interaction between von Willebrand factor and the human platelet membrane glycoprotein Ib-IX complex". Biochemistry. 28 (21): 8317–8326. doi:10.1021/bi00447a009. PMID 2557900.
  • Wenger RH, Wicki AN, Kieffer N, Adolph S, Hameister H, Clemetson KJ (December 1989). "The 5' flanking region and chromosomal localization of the gene encoding human platelet membrane glycoprotein Ib alpha". Gene. 85 (2): 517–524. doi:10.1016/0378-1119(89)90446-0. PMID 2628181.
  • Wenger RH, Kieffer N, Wicki AN, Clemetson KJ (October 1988). "Structure of the human blood platelet membrane glycoprotein Ib alpha gene". Biochemical and Biophysical Research Communications. 156 (1): 389–395. doi:10.1016/S0006-291X(88)80853-2. PMID 2845978.
  • Wicki AN, Clemetson KJ (November 1985). "Structure and function of platelet membrane glycoproteins Ib and V. Effects of leukocyte elastase and other proteases on platelets response to von Willebrand factor and thrombin". European Journal of Biochemistry. 153 (1): 1–11. doi:10.1111/j.1432-1033.1985.tb09259.x. PMID 2933256.
  • Adelman B, Michelson AD, Greenberg J, Handin RI (December 1986). "Proteolysis of platelet glycoprotein Ib by plasmin is facilitated by plasmin lysine-binding regions". Blood. 68 (6): 1280–1284. doi:10.1182/blood.V68.6.1280.1280. PMID 2946332.
  • Lopez JA, Chung DW, Fujikawa K, Hagen FS, Papayannopoulou T, Roth GJ (August 1987). "Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein". Proceedings of the National Academy of Sciences of the United States of America. 84 (16): 5615–5619. Bibcode:1987PNAS...84.5615L. doi:10.1073/pnas.84.16.5615. PMC 298913. PMID 3303030.
  • Lopez JA, Chung DW, Fujikawa K, Hagen FS, Davie EW, Roth GJ (April 1988). "The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence". Proceedings of the National Academy of Sciences of the United States of America. 85 (7): 2135–2139. Bibcode:1988PNAS...85.2135L. doi:10.1073/pnas.85.7.2135. PMC 279943. PMID 3353370.
  • Titani K, Takio K, Handa M, Ruggeri ZM (August 1987). "Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib". Proceedings of the National Academy of Sciences of the United States of America. 84 (16): 5610–5614. Bibcode:1987PNAS...84.5610T. doi:10.1073/pnas.84.16.5610. PMC 298912. PMID 3497398.
  • Harmon JT, Jamieson GA (October 1986). "The glycocalicin portion of platelet glycoprotein Ib expresses both high and moderate affinity receptor sites for thrombin. A soluble radioreceptor assay for the interaction of thrombin with platelets". The Journal of Biological Chemistry. 261 (28): 13224–13229. doi:10.1016/S0021-9258(18)69294-4. PMID 3759960.

External links

  • v
  • t
  • e
  • 1gwb: STRUCTURE OF GLYCOPROTEIN 1B
    1gwb: STRUCTURE OF GLYCOPROTEIN 1B
  • 1m0z: Crystal Structure of the von Willebrand Factor Binding Domain of Glycoprotein Ib alpha
    1m0z: Crystal Structure of the von Willebrand Factor Binding Domain of Glycoprotein Ib alpha
  • 1m10: Crystal structure of the complex of Glycoprotein Ib alpha and the von Willebrand Factor A1 Domain
    1m10: Crystal structure of the complex of Glycoprotein Ib alpha and the von Willebrand Factor A1 Domain
  • 1ook: Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin
    1ook: Crystal Structure of the Complex of Platelet Receptor GPIb-alpha and Human alpha-Thrombin
  • 1p8v: CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND ALPHA-THROMBIN AT 2.6A
    1p8v: CRYSTAL STRUCTURE OF THE COMPLEX OF PLATELET RECEPTOR GPIB-ALPHA AND ALPHA-THROMBIN AT 2.6A
  • 1p9a: Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution
    1p9a: Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 1.7 Angstrom Resolution
  • 1qyy: Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 2.8 Angstrom Resolution
    1qyy: Crystal Structure of N-Terminal Domain of Human Platelet Receptor Glycoprotein Ib-alpha at 2.8 Angstrom Resolution
  • 1sq0: Crystal Structure of the Complex of the Wild-type Von Willebrand Factor A1 domain and Glycoprotein Ib alpha at 2.6 Angstrom Resolution
    1sq0: Crystal Structure of the Complex of the Wild-type Von Willebrand Factor A1 domain and Glycoprotein Ib alpha at 2.6 Angstrom Resolution
  • 1u0n: The ternary von Willebrand Factor A1-glycoprotein Ibalpha-botrocetin complex
    1u0n: The ternary von Willebrand Factor A1-glycoprotein Ibalpha-botrocetin complex
  • v
  • t
  • e
Coagulation factors
Primary hemostasis
(platelet activation)
Intrinsic pathway
(contact activation)
Extrinsic pathway
(tissue factor)
Common pathway
Anticoagulant factors
Fibrinolytic factors
Coagulation markers
Platelet activation
Thrombin generation
Fibrin generation
Fibrinolysis
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1–50
51–100
101–150
151–200
201–250
251–300
301–350

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

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