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P07359 (GP1BA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet glycoprotein Ib alpha chain

Short name=GP-Ib alpha
Short name=GPIb-alpha
Short name=GPIbA
Short name=Glycoprotein Ibalpha
Alternative name(s):
Antigen CD42b-alpha
CD_antigen=CD42b

Cleaved into the following chain:

  1. Glycocalicin
Gene names
Name:GP1BA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length652 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium.

Subunit structure

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. Interacts with FLNB. Ref.11 Ref.12 Ref.14

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Glycocalicin, which is approximately coextensive with the extracellular part of the molecule, is cleaved off by calpain during platelet lysis.

Polymorphism

Position 161 is associated with platelet-specific alloantigen Siba. Siba- has Thr-161 and Siba+ has Met-161. Siba is involved in neonatal alloimmune thrombocytopenia (NATP).

Polymorphisms arise from a variable number of tandem 13-amino acid repeats of S-E-P-A-P-S-P-T-T-P-E-P-T in the mucin-like macroglycopeptide (Pro/Thr-rich) domain. Allele D contains one repeat starting at position 415, allele C contains two repeats, allele B (shown here) contains three repeats and allele A contains four repeats. Allele B is associated with susceptibility to nonarteritic anterior ischemic optic neuropathy.

Involvement in disease

Non-arteritic anterior ischemic optic neuropathy (NAION) [MIM:258660]: An ocular disease due to ischemic injury to the optic nerve. It usually affects the optic disk and leads to visual loss and optic disk swelling of a pallid nature. Visual loss is usually sudden, or over a few days at most and is usually permanent, with some recovery possibly occurring within the first weeks or months. Patients with small disks having smaller or non-existent cups have an anatomical predisposition for non-arteritic anterior ischemic optic neuropathy. As an ischemic episode evolves, the swelling compromises circulation, with a spiral of ischemia resulting in further neuronal damage.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.34

Bernard-Soulier syndrome (BSS) [MIM:231200]: A coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, thrombocytopenia, and impaired prothrombin consumption.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.22 Ref.23 Ref.28 Ref.29 Ref.32 Ref.33

Bernard-Soulier syndrome A2, autosomal dominant (BSSA2) [MIM:153670]: A coagulation disorder characterized by mild to moderate bleeding tendency, thrombocytopenia, and an increased mean platelet volume. Some individuals have no symptoms. Mild bleeding tendencies manifest as epistaxis, gingival bleeding, menorrhagia, easy bruising, or prolonged bleeding after dental surgery.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33

Pseudo-von Willebrand disease (VWDP) [MIM:177820]: A bleeding disorder characterized by abnormally enhanced binding of von Willebrand factor by the platelet glycoprotein Ib (GP Ib) receptor complex. Hemostatic function is impaired due to the removal of VWF multimers from the circulation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.24 Ref.25 Ref.26

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.

Binding sites for vWF and thrombin (the latter site with unknown function) are in the N-terminal part of the molecule.

Sequence similarities

Contains 7 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Ontologies

Keywords
   Biological processBlood coagulation
Cell adhesion
Hemostasis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseBernard Soulier syndrome
Disease mutation
von Willebrand disease
   DomainLeucine-rich repeat
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Sulfation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from mutant phenotype PubMed 21037087. Source: MGI

blood coagulation, intrinsic pathway

Traceable author statement. Source: Reactome

cell adhesion

Inferred from direct assay PubMed 9410473. Source: MGI

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Traceable author statement PubMed 3353370. Source: ProtInc

fibrinolysis

Inferred from direct assay PubMed 12855810. Source: UniProtKB

platelet activation

Traceable author statement PubMed 12855810. Source: UniProtKB

regulation of blood coagulation

Traceable author statement PubMed 12855810. Source: UniProtKB

thrombin receptor signaling pathway

Traceable author statement PubMed 12855810PubMed 3759960. Source: GOC

   Cellular_componentanchored component of external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement PubMed 3353370. Source: ProtInc

membrane

Inferred from direct assay PubMed 15297306. Source: MGI

plasma membrane

Inferred from direct assay PubMed 15297306. Source: MGI

   Molecular_functionthrombin receptor activity

Traceable author statement PubMed 12855810. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VWFP042752EBI-297082,EBI-981819

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.8
Chain17 – 652636Platelet glycoprotein Ib alpha chain
PRO_0000021343
Chain17 – ?GlycocalicinPRO_0000021344

Regions

Topological domain17 – 531515Extracellular Potential
Transmembrane532 – 55221Helical; Potential
Topological domain553 – 652100Cytoplasmic Potential
Domain17 – 4731LRRNT
Repeat48 – 6821LRR 1
Repeat72 – 9322LRR 2
Repeat94 – 11522LRR 3
Repeat117 – 13721LRR 4
Repeat141 – 16222LRR 5
Repeat165 – 18622LRR 6
Repeat189 – 21022LRR 7
Domain221 – 28262LRRCT
Compositional bias345 – 482138Pro/Thr-rich

Amino acid modifications

Modified residue2921Sulfotyrosine Ref.16
Modified residue2941Sulfotyrosine Ref.16
Modified residue2951Sulfotyrosine Ref.16
Modified residue6291Phosphoserine Ref.15
Modified residue6321Phosphoserine Ref.15
Glycosylation371N-linked (GlcNAc...) Ref.13
Glycosylation1751N-linked (GlcNAc...)
Glycosylation3081O-linked (GalNAc...)
Disulfide bond20 ↔ 33 Ref.11 Ref.14
Disulfide bond225 ↔ 264 Ref.11 Ref.14
Disulfide bond227 ↔ 280 Ref.11 Ref.14
Disulfide bond526Interchain (with C-147 in GP1BB) Ref.11 Ref.14
Disulfide bond527Interchain (with C-147 in GP1BB) Ref.11 Ref.14

Natural variations

Natural variant721R → H. Ref.30
Corresponds to variant rs6068 [ dbSNP | Ensembl ].
VAR_011909
Natural variant731L → F in BSS. Ref.20
VAR_014206
Natural variant811C → R in BSS. Ref.29
VAR_005256
Natural variant861L → F. Ref.3
Corresponds to variant rs13306411 [ dbSNP | Ensembl ].
VAR_013511
Natural variant1451L → P in BSS. Ref.32
VAR_014207
Natural variant1611T → M in Siba(+). Ref.5 Ref.19 Ref.27 Ref.30
Corresponds to variant rs6065 [ dbSNP | Ensembl ].
VAR_005257
Natural variant1721A → V in BSS and BSSA2. Ref.22 Ref.33
VAR_005258
Natural variant1951Missing in BSS. Ref.28
VAR_005259
Natural variant2251C → S in BSS. Ref.23
VAR_005260
Natural variant2491G → S in VWDP. Ref.4
VAR_019657
Natural variant2491G → V in VWDP. Ref.24 Ref.25
VAR_005261
Natural variant2541A → S.
Corresponds to variant rs382524 [ dbSNP | Ensembl ].
VAR_011910
Natural variant2551M → V in VWDP; increased binding to vWF. Ref.4 Ref.26
VAR_005262

Experimental info

Mutagenesis2491G → A: No change. Ref.4
Mutagenesis2491G → K or D: Decreased binding to vWF. Ref.4
Mutagenesis2491G → S or V: Increased binding to vWF. Ref.4
Sequence conflict6191V → L in AAH27955. Ref.7

Secondary structure

...................................................... 652
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07359 [UniParc].

Last modified April 16, 2014. Version 2.
Checksum: 053346683AEB927E

FASTA65271,540
        10         20         30         40         50         60 
MPLLLLLLLL PSPLHPHPIC EVSKVASHLE VNCDKRNLTA LPPDLPKDTT ILHLSENLLY 

        70         80         90        100        110        120 
TFSLATLMPY TRLTQLNLDR CELTKLQVDG TLPVLGTLDL SHNQLQSLPL LGQTLPALTV 

       130        140        150        160        170        180 
LDVSFNRLTS LPLGALRGLG ELQELYLKGN ELKTLPPGLL TPTPKLEKLS LANNNLTELP 

       190        200        210        220        230        240 
AGLLNGLENL DTLLLQENSL YTIPKGFFGS HLLPFAFLHG NPWLCNCEIL YFRRWLQDNA 

       250        260        270        280        290        300 
ENVYVWKQGV DVKAMTSNVA SVQCDNSDKF PVYKYPGKGC PTLGDEGDTD LYDYYPEEDT 

       310        320        330        340        350        360 
EGDKVRATRT VVKFPTKAHT TPWGLFYSWS TASLDSQMPS SLHPTQESTK EQTTFPPRWT 

       370        380        390        400        410        420 
PNFTLHMESI TFSKTPKSTT EPTPSPTTSE PVPEPAPNMT TLEPTPSPTT PEPTSEPAPS 

       430        440        450        460        470        480 
PTTPEPTSEP APSPTTPEPT SEPAPSPTTP EPTPIPTIAT SPTILVSATS LITPKSTFLT 

       490        500        510        520        530        540 
TTKPVSLLES TKKTIPELDQ PPKLRGVLQG HLESSRNDPF LHPDFCCLLP LGFYVLGLFW 

       550        560        570        580        590        600 
LLFASVVLIL LLSWVGHVKP QALDSGQGAA LTTATQTTHL ELQRGRQVTV PRAWLLFLRG 

       610        620        630        640        650 
SLPTFRSSLF LWVRPNGRVG PLVAGRRPSA LSQGRGQDLL STVSIRYSGH SL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein."
Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Papayannopoulou T., Roth G.J.
Proc. Natl. Acad. Sci. U.S.A. 84:5615-5619(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Structure of the human blood platelet membrane glycoprotein Ib alpha gene."
Wenger R.H., Kieffer N., Wicki A.N., Clemetson K.J.
Biochem. Biophys. Res. Commun. 156:389-395(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"A novel polymorphism, 70Leu/Phe, disrupts a consensus Leu residue within the leucine-rich repeat sequence of platelet glycoprotein Ibalpha."
Matsubara Y., Murata M., Moriki T., Yokoyama K., Watanabe N., Nakajima H., Handa M., Kawano K., Aoki N., Yoshino H., Ikeda Y.
Thromb. Haemost. 87:867-872(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-86.
[4]"Identification of a novel point mutation in platelet glycoprotein Ibalpha, Gly to Ser at residue 233, in a Japanese family with platelet-type von Willebrand disease."
Matsubara Y., Murata M., Sugita K., Ikeda Y.
J. Thromb. Haemost. 1:2198-2205(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VWDP SER-249, CHARACTERIZATION OF VARIANT VWDP VAL-255, MUTAGENESIS OF GLY-249.
[5]SeattleSNPs variation discovery resource
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-161.
[6]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[8]"Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib."
Titani K., Takio K., Handa M., Ruggeri Z.M.
Proc. Natl. Acad. Sci. U.S.A. 84:5610-5614(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-315, STRUCTURE OF CARBOHYDRATE.
[9]"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 128-137.
Tissue: Platelet.
[10]"StyI polymorphism at nucleotide 1610 in the human platelet glycoprotein Ib alpha gene."
Suzuki K., Hayashi T., Akiba J., Yahagi A., Tajima K., Satoh S., Sasaki H.
Jpn. J. Hum. Genet. 41:419-421(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-397.
[11]"Identification of the disulphide bonds in human platelet glycocalicin."
Hess D., Schaller J., Rickli E.E., Clemetson K.J.
Eur. J. Biochem. 199:389-393(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[12]"Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha."
Takafuta T., Wu G., Murphy G.F., Shapiro S.S.
J. Biol. Chem. 273:17531-17538(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLNB.
Tissue: Endothelial cell and Placenta.
[13]"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
Lewandrowski U., Moebius J., Walter U., Sickmann A.
Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37.
Tissue: Platelet.
[14]"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 BONDS.
[15]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629 AND SER-632, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[16]"Crystal structure of the platelet glycoprotein Ibalpha N-terminal domain reveals an unmasking mechanism for receptor activation."
Uff S., Clemetson J.M., Harrison T., Clemetson K.J., Emsley J.
J. Biol. Chem. 277:35657-35663(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-304, SULFATION AT TYR-292; TYR-294 AND TYR-295.
[17]"Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain."
Huizinga E.G., Tsuji S., Romijn R.A., Schiphorst M.E., de Groot P.G., Sixma J.J., Gros P.
Science 297:1176-1179(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[18]"Molecular modeling of the seven tandem leucine-rich repeats within the ligand-binding region of platelet glycoprotein Ib alpha."
Whisstock J.C., Shen Y., Lopez J.A., Andrews R.K., Berndt M.C.
Thromb. Haemost. 87:329-333(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 52-216.
[19]"Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness."
Murata M., Furihata K., Ishida F., Russell S.R., Ware J., Ruggeri Z.M.
Blood 79:3086-3090(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SIBA MET-161.
[20]"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."
Miller J.L., Lyle V.A., Cunningham D.
Blood 79:439-446(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSS PHE-73.
[21]"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."
Lopez J.A., Ludwig E.H., McCarthy B.J.
J. Biol. Chem. 267:10055-10061(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM OF PRO/THR-RICH DOMAIN.
[22]"Point mutation in a leucine-rich repeat of platelet glycoprotein Ib alpha resulting in the Bernard-Soulier syndrome."
Ware J., Russell S.R., Marchese P., Murata M., Mazzucato M., de Marco L., Ruggeri Z.M.
J. Clin. Invest. 92:1213-1220(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSS VAL-172.
[23]"Cys209 Ser mutation in the platelet membrane glycoprotein Ib alpha gene is associated with Bernard-Soulier syndrome."
Simsek S., Noris P., Lozano M., Pico M., von Dem Borne A.E.G.K., Ribera A., Gallardo D.
Br. J. Haematol. 88:839-844(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSS SER-225.
[24]"Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease."
Miller J.L., Cunningham D., Lyle V.A., Finch C.N.
Proc. Natl. Acad. Sci. U.S.A. 88:4761-4765(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VWDP VAL-249.
[25]"Expression of the phenotypic abnormality of platelet-type von Willebrand disease in a recombinant glycoprotein Ib alpha fragment."
Murata M., Russell S.R., Ruggeri Z.M., Ware J.
J. Clin. Invest. 91:2133-2137(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VWDP VAL-249.
[26]"Pseudo-von Willebrand disease: a mutation in the platelet glycoprotein Ib alpha gene associated with a hyperactive surface receptor."
Russell S.D., Roth G.J.
Blood 81:1787-1791(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VWDP VAL-255.
[27]"The largest variant of platelet glycoprotein Ib alpha has four tandem repeats of 13 amino acids in the macroglycopeptide region and a genetic linkage with methionine145."
Ishida F., Furihata K., Ishida K., Yan J., Kitano K., Kiyosawa K., Furuta S.
Blood 86:1357-1360(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SIBA MET-161, POLYMORPHISM OF PRO/THR-RICH DOMAIN.
[28]"A three-base deletion removing a leucine residue in a leucine-rich repeat of platelet glycoprotein Ib alpha associated with a variant of Bernard-Soulier syndrome (Nancy I)."
de la Salle C., Baas M.-J., Lanza F., Schwartz A., Hanau D., Chevalier J., Gachet C., Briquel M.-E., Cazenave J.-P.
Br. J. Haematol. 89:386-396(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSS LEU-195 DEL.
[29]"Naturally occurring mutations in glycoprotein Ibalpha that result in defective ligand binding and synthesis of a truncated protein."
Kenny D., Jonsson O.G., Morateck P.A., Montgomery R.R.
Blood 92:175-183(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSS ARG-81.
[30]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-72 AND MET-161.
[31]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[32]"Molecular characterization of two mutations in platelet glycoprotein (GP) Ib alpha in two Finnish Bernard-Soulier syndrome families."
Koskela S., Partanen J., Salmi T.T., Kekomaki R.
Eur. J. Haematol. 62:160-168(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSS PRO-145.
[33]"Autosomal dominant macrothrombocytopenia in Italy is most frequently a type of heterozygous Bernard-Soulier syndrome."
Savoia A., Balduini C.L., Savino M., Noris P., Del Vecchio M., Perrotta S., Belletti S., Poggi V., Iolascon A.
Blood 97:1330-1335(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSSA2 VAL-172.
[34]"Nonarteritic anterior ischemic optic neuropathy is associated with a specific platelet polymorphism located on the glycoprotein Ibalpha gene."
Salomon O., Rosenberg N., Steinberg D.M., Huna-Baron R., Moisseiev J., Dardik R., Goldan O., Kurtz S., Ifrah A., Seligsohn U.
Ophthalmology 111:184-188(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO NAION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02940 mRNA. Translation: AAA52595.1.
M22403 Genomic DNA. Translation: AAA52596.1.
AB038516 Genomic DNA. Translation: BAB12038.1.
AB086948 Genomic DNA. Translation: BAC10305.1.
AF395009 Genomic DNA. Translation: AAK71325.1.
AC233723 Genomic DNA. No translation available.
BC027955 mRNA. Translation: AAH27955.1.
D85894 Genomic DNA. Translation: BAA12911.1.
S34436 Genomic DNA. Translation: AAB22152.1.
S34439 Genomic DNA. Translation: AAB22153.1.
L39103 Genomic DNA. Translation: AAA69491.1.
PIRNBHUIA. A94174.
I70082.
UniGeneHs.1472.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWBX-ray2.80A/B16-296[»]
1K13model-A52-216[»]
1M0ZX-ray1.85A/B17-306[»]
1M10X-ray3.10B17-306[»]
1OOKX-ray2.30G17-306[»]
1P8VX-ray2.60A17-294[»]
1P9AX-ray1.70G17-306[»]
1QYYX-ray2.80A/G17-306[»]
1SQ0X-ray2.60B17-304[»]
1U0NX-ray2.95D17-281[»]
2BP3X-ray2.32S/T598-619[»]
3P72X-ray1.90A17-281[»]
3PMHX-ray3.20G17-306[»]
4C2AX-ray2.08B17-306[»]
4C2BX-ray2.80B/D/F/H17-306[»]
4CH2X-ray1.60P/Q287-300[»]
4CH8X-ray1.75P/Q/R/S287-300[»]
4MGXX-ray3.16B577-585[»]
ProteinModelPortalP07359.
SMRP07359. Positions 17-300.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP07359. 10 interactions.
MINTMINT-147226.
STRING9606.ENSP00000329380.

PTM databases

PhosphoSiteP07359.
UniCarbKBP07359.

Polymorphism databases

DMDM121531.

Proteomic databases

PaxDbP07359.
PRIDEP07359.

Protocols and materials databases

DNASU2811.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329125; ENSP00000329380; ENSG00000185245.

Organism-specific databases

GeneCardsGC17P004835.
H-InvDBHIX0212275.
HGNCHGNC:4439. GP1BA.
HPACAB002496.
HPA013316.
MIM153670. phenotype.
177820. phenotype.
231200. phenotype.
258660. phenotype.
606672. gene.
neXtProtNX_P07359.
Orphanet274. Bernard-Soulier syndrome.
853. Fetal and neonatal alloimmune thrombocytopenia.
52530. Von Willebrand disease, platelet type.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG294000.
HOVERGENHBG051790.
InParanoidP07359.
OMATVPRAWL.
OrthoDBEOG7GBFXK.
PhylomeDBP07359.
TreeFamTF351114.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
SignaLinkP07359.

Gene expression databases

ArrayExpressP07359.
BgeeP07359.
CleanExHS_GP1BA.
GenevestigatorP07359.

Family and domain databases

InterProIPR000483. Cys-rich_flank_reg_C.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF00560. LRR_1. 1 hit.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07359.
NextBio13604195.
PMAP-CutDBP07359.
PROP07359.
SOURCESearch...

Entry information

Entry nameGP1BA_HUMAN
AccessionPrimary (citable) accession number: P07359
Secondary accession number(s): E7ES66 expand/collapse secondary AC list , Q14441, Q16469, Q8N1F3, Q8NG39, Q9HDC7, Q9UEK1, Q9UQS4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 16, 2014
Last modified: April 16, 2014
This is version 185 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries