GP1BA

GP1BA
Available structures PDB Ortholog 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
Aliases	GP1BA, BDPLT1, BDPLT3, BSS, CD42B, CD42b-alpha, DBPLT3, GP1B, GPIbA, VWDP, GPIbalpha, glycoprotein Ib platelet alpha subunit, glycoprotein Ib platelet subunit alpha
External IDs	OMIM: 606672 MGI: 1333744 HomoloGene: 143 GeneCards: GP1BA
Gene location (Human) Chr. Chromosome 17 (human) Band 17p13.2 Start 4,932,277 bp End 4,935,023 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 B3|11 43.2 cM Start 70,529,948 bp End 70,532,862 bp
RNA expression pattern Bgee Human Mouse (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 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: 4.93 – 4.94 Mb Chr 11: 70.53 – 70.53 Mb PubMed search
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

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. 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, 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.

Interactions

GP1BA has been shown to interact with YWHAZ and FLNB.

See also

• Cluster of differentiation

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

• GP1BA+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

v t e PDB gallery

1gwb: STRUCTURE OF GLYCOPROTEIN 1B 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 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 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 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

v t e Coagulation cascade
Coagulation factors	Primary hemostasis (platelet activation) von Willebrand factor (vWF) Platelet membrane glycoproteins: Glycoprotein Ib (GPIb) (GP1BA GP1BB Glycoprotein IX (GP9)) Glycoprotein IIb/IIIa (GPIIb GPIIIa) Glycoprotein VI (GPVI) Intrinsic pathway (contact activation) High-molecular-weight kininogen (HMWK) Bradykinin Prekallikrein Kallikrein Factor XII (Hageman factor) Factor XI Factor IX Factor VIII Extrinsic pathway (tissue factor) Factor III (tissue factor) Factor VII Common pathway Factor X Factor V Prothrombin (factor II) Thrombin (factor IIa) Fibrinogen (factor I) (FGA, FGG) Fibrin (factor Ia) Factor XIII
Anticoagulant factors	Antithrombin (inhibits FII, FIX, FX, FXI, FXII) Protein C (inhibits FV, FVIII) Protein S (cofactor for protein C) Protein Z (inhibits FX) Protein Z-related protease inhibitor (ZPI) (inhibits FX, FXI) Tissue factor pathway inhibitor (TFPI) (inhibits FIII)
Fibrinolytic factors	Plasminogen Plasmin Tissue plasminogen activator (tPA) Urokinase Plasminogen activator inhibitor-1 (PAI-1) Plasminogen activator inhibitor-2 (PAI-2) α2-Antiplasmin α2-Macroglobulin Thrombin-activatable fibrinolysis inhibitor (TAFI)
Coagulation markers	Platelet activation Platelet factor 4 (PF4) β-Thromboglobulin (β-TG) Thrombin generation Prothrombin fragment 1+2 (F1+2) Thrombin–antithrombin complex (TAT) Activated protein C–protein C inhibitor (APC–PCI) Fibrin generation Fibrinopeptide A (FpA) Fibrinopeptide B (FpB) Fibrin monomers (FM) Fibrinolysis Plasmin-α2-antiplasmin complex (PAP) D-Dimer (DD)

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

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