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Protein

Platelet glycoprotein Ib alpha chain

Gene

GP1BA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • protein kinase inhibitor activity Source: GO_Central
  • thrombin-activated receptor activity Source: UniProtKB

GO - Biological processi

  • blood coagulation Source: MGI
  • blood coagulation, intrinsic pathway Source: Reactome
  • cell adhesion Source: MGI
  • cell morphogenesis Source: Ensembl
  • cell surface receptor signaling pathway Source: ProtInc
  • cytokine-mediated signaling pathway Source: GO_Central
  • fibrinolysis Source: UniProtKB
  • negative regulation of JAK-STAT cascade Source: GO_Central
  • negative regulation of protein kinase activity Source: GO_Central
  • platelet activation Source: UniProtKB
  • platelet aggregation Source: Ensembl
  • regulation of blood coagulation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Cell adhesion, Hemostasis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000174409-MONOMER.
ReactomeiR-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-HSA-430116. GP1b-IX-V activation signalling.
R-HSA-75892. Platelet Adhesion to exposed collagen.
R-HSA-76009. Platelet Aggregation (Plug Formation).
SignaLinkiP07359.

Names & Taxonomyi

Protein namesi
Recommended 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:
Gene namesi
Name:GP1BA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:4439. GP1BA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini17 – 531ExtracellularSequence analysisAdd BLAST515
Transmembranei532 – 552HelicalSequence analysisAdd BLAST21
Topological domaini553 – 652CytoplasmicSequence analysisAdd BLAST100

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: Ensembl
  • cell surface Source: UniProtKB
  • cytoplasm Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Non-arteritic anterior ischemic optic neuropathy (NAION)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:258660
Bernard-Soulier syndrome (BSS)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, thrombocytopenia, and impaired prothrombin consumption.
See also OMIM:231200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01420673L → F in BSS. 1 PublicationCorresponds to variant rs121908063dbSNPEnsembl.1
Natural variantiVAR_00525681C → R in BSS. 1 PublicationCorresponds to variant rs781541857dbSNPEnsembl.1
Natural variantiVAR_014207145L → P in BSS. 1 PublicationCorresponds to variant rs771048666dbSNPEnsembl.1
Natural variantiVAR_005258172A → V in BSS and BSSA2. 2 PublicationsCorresponds to variant rs121908065dbSNPEnsembl.1
Natural variantiVAR_005259195Missing in BSS. 1 Publication1
Natural variantiVAR_005260225C → S in BSS. 1 Publication1
Bernard-Soulier syndrome A2, autosomal dominant (BSSA2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:153670
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005258172A → V in BSS and BSSA2. 2 PublicationsCorresponds to variant rs121908065dbSNPEnsembl.1
Pseudo-von Willebrand disease (VWDP)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:177820
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019657249G → S in VWDP. 1 Publication1
Natural variantiVAR_005261249G → V in VWDP. 2 PublicationsCorresponds to variant rs121908062dbSNPEnsembl.1
Natural variantiVAR_005262255M → V in VWDP; increased binding to vWF. 2 PublicationsCorresponds to variant rs121908064dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi249G → A: No change. 1 Publication1
Mutagenesisi249G → K or D: Decreased binding to vWF. 1 Publication1
Mutagenesisi249G → S or V: Increased binding to vWF. 1 Publication1

Keywords - Diseasei

Bernard Soulier syndrome, Disease mutation, von Willebrand disease

Organism-specific databases

DisGeNETi2811.
MalaCardsiGP1BA.
MIMi153670. phenotype.
177820. phenotype.
231200. phenotype.
258660. phenotype.
OpenTargetsiENSG00000185245.
Orphaneti274. Bernard-Soulier syndrome.
853. Fetal and neonatal alloimmune thrombocytopenia.
52530. Pseudo-von Willebrand disease.

Polymorphism and mutation databases

DMDMi121531.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 161 PublicationAdd BLAST16
ChainiPRO_000002134317 – 652Platelet glycoprotein Ib alpha chainAdd BLAST636
ChainiPRO_000002134417 – ?Glycocalicin

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi20 ↔ 331 Publication
Glycosylationi37N-linked (GlcNAc...)2 Publications1
Glycosylationi175N-linked (GlcNAc...)1 Publication1
Disulfide bondi225 ↔ 2641 Publication
Disulfide bondi227 ↔ 2801 Publication
Modified residuei292Sulfotyrosine1 Publication1
Modified residuei294Sulfotyrosine1 Publication1
Modified residuei295Sulfotyrosine1 Publication1
Glycosylationi308O-linked (GalNAc...)1 Publication1
Disulfide bondi526Interchain (with C-147 in GP1BB)1 Publication
Disulfide bondi527Interchain (with C-147 in GP1BB)1 Publication
Modified residuei629PhosphoserineCombined sources1
Modified residuei632PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

EPDiP07359.
PaxDbiP07359.
PeptideAtlasiP07359.
PRIDEiP07359.

PTM databases

iPTMnetiP07359.
PhosphoSitePlusiP07359.
UniCarbKBiP07359.

Miscellaneous databases

PMAP-CutDBP07359.

Expressioni

Gene expression databases

BgeeiENSG00000185245.
CleanExiHS_GP1BA.
ExpressionAtlasiP07359. baseline and differential.
GenevisibleiP07359. HS.

Organism-specific databases

HPAiCAB002496.
HPA013316.

Interactioni

Subunit structurei

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 (PubMed:17008541, PubMed:2070794). Interacts with FLNB (PubMed:9651345). Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) (PubMed:19828450).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GP1BBP132246EBI-297082,EBI-2833037
VWFP042752EBI-297082,EBI-981819

Protein-protein interaction databases

BioGridi109073. 8 interactors.
IntActiP07359. 12 interactors.
MINTiMINT-147226.
STRINGi9606.ENSP00000329380.

Structurei

Secondary structure

1652
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 23Combined sources5
Beta strandi30 – 32Combined sources3
Beta strandi51 – 53Combined sources3
Beta strandi60 – 63Combined sources4
Helixi64 – 67Combined sources4
Beta strandi75 – 77Combined sources3
Beta strandi85 – 87Combined sources3
Beta strandi97 – 99Combined sources3
Turni112 – 114Combined sources3
Beta strandi120 – 122Combined sources3
Turni135 – 138Combined sources4
Beta strandi144 – 146Combined sources3
Turni157 – 162Combined sources6
Beta strandi168 – 170Combined sources3
Turni181 – 186Combined sources6
Beta strandi192 – 194Combined sources3
Turni205 – 210Combined sources6
Beta strandi214 – 217Combined sources4
Helixi227 – 229Combined sources3
Helixi230 – 238Combined sources9
Helixi240 – 242Combined sources3
Beta strandi243 – 249Combined sources7
Helixi252 – 254Combined sources3
Helixi259 – 261Combined sources3
Beta strandi262 – 264Combined sources3
Turni265 – 268Combined sources4
Helixi272 – 274Combined sources3
Beta strandi283 – 287Combined sources5
Beta strandi291 – 293Combined sources3
Helixi507 – 509Combined sources3
Beta strandi605 – 613Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray3.16B603-611[»]
4YR6X-ray2.38C/F503-512[»]
ProteinModelPortaliP07359.
SMRiP07359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07359.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 47LRRNTAdd BLAST31
Repeati48 – 68LRR 1Add BLAST21
Repeati72 – 93LRR 2Add BLAST22
Repeati94 – 115LRR 3Add BLAST22
Repeati117 – 137LRR 4Add BLAST21
Repeati141 – 162LRR 5Add BLAST22
Repeati165 – 186LRR 6Add BLAST22
Repeati189 – 210LRR 7Add BLAST22
Domaini221 – 282LRRCTAdd BLAST62

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi345 – 482Pro/Thr-richAdd BLAST138

Sequence similaritiesi

Contains 7 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00860000133896.
HOVERGENiHBG051790.
InParanoidiP07359.
KOiK06261.
OMAiHLLPFAF.
OrthoDBiEOG091G08IS.
PhylomeDBiP07359.
TreeFamiTF351114.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF13855. LRR_8. 1 hit.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 5 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07359-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLLLLLLLL PSPLHPHPIC EVSKVASHLE VNCDKRNLTA LPPDLPKDTT
60 70 80 90 100
ILHLSENLLY TFSLATLMPY TRLTQLNLDR CELTKLQVDG TLPVLGTLDL
110 120 130 140 150
SHNQLQSLPL LGQTLPALTV LDVSFNRLTS LPLGALRGLG ELQELYLKGN
160 170 180 190 200
ELKTLPPGLL TPTPKLEKLS LANNNLTELP AGLLNGLENL DTLLLQENSL
210 220 230 240 250
YTIPKGFFGS HLLPFAFLHG NPWLCNCEIL YFRRWLQDNA ENVYVWKQGV
260 270 280 290 300
DVKAMTSNVA SVQCDNSDKF PVYKYPGKGC PTLGDEGDTD LYDYYPEEDT
310 320 330 340 350
EGDKVRATRT VVKFPTKAHT TPWGLFYSWS TASLDSQMPS SLHPTQESTK
360 370 380 390 400
EQTTFPPRWT PNFTLHMESI TFSKTPKSTT EPTPSPTTSE PVPEPAPNMT
410 420 430 440 450
TLEPTPSPTT PEPTSEPAPS PTTPEPTSEP APSPTTPEPT SEPAPSPTTP
460 470 480 490 500
EPTPIPTIAT SPTILVSATS LITPKSTFLT TTKPVSLLES TKKTIPELDQ
510 520 530 540 550
PPKLRGVLQG HLESSRNDPF LHPDFCCLLP LGFYVLGLFW LLFASVVLIL
560 570 580 590 600
LLSWVGHVKP QALDSGQGAA LTTATQTTHL ELQRGRQVTV PRAWLLFLRG
610 620 630 640 650
SLPTFRSSLF LWVRPNGRVG PLVAGRRPSA LSQGRGQDLL STVSIRYSGH

SL
Length:652
Mass (Da):71,540
Last modified:April 16, 2014 - v2
Checksum:i053346683AEB927E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti619V → L in AAH27955 (PubMed:15489334).Curated1

Polymorphismi

Position 161 is associated with platelet-specific alloantigen Siba (PubMed:1586750). Siba- has Thr-161 and Siba+ has Met-161 (PubMed:1586750). Siba is involved in neonatal alloimmune thrombocytopenia (NATP) (PubMed:1586750, PubMed:7632942).2 Publications
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 (PubMed:1577776, PubMed:7632942). 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 (PubMed:1577776). Allele B is associated with susceptibility to nonarteritic anterior ischemic optic neuropathy (PubMed:1577776).2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01190972R → H.1 PublicationCorresponds to variant rs6068dbSNPEnsembl.1
Natural variantiVAR_01420673L → F in BSS. 1 PublicationCorresponds to variant rs121908063dbSNPEnsembl.1
Natural variantiVAR_00525681C → R in BSS. 1 PublicationCorresponds to variant rs781541857dbSNPEnsembl.1
Natural variantiVAR_01351186L → F.1 PublicationCorresponds to variant rs13306411dbSNPEnsembl.1
Natural variantiVAR_014207145L → P in BSS. 1 PublicationCorresponds to variant rs771048666dbSNPEnsembl.1
Natural variantiVAR_005257161T → M in Siba(+). 4 PublicationsCorresponds to variant rs6065dbSNPEnsembl.1
Natural variantiVAR_005258172A → V in BSS and BSSA2. 2 PublicationsCorresponds to variant rs121908065dbSNPEnsembl.1
Natural variantiVAR_005259195Missing in BSS. 1 Publication1
Natural variantiVAR_005260225C → S in BSS. 1 Publication1
Natural variantiVAR_019657249G → S in VWDP. 1 Publication1
Natural variantiVAR_005261249G → V in VWDP. 2 PublicationsCorresponds to variant rs121908062dbSNPEnsembl.1
Natural variantiVAR_011910254A → S.Corresponds to variant rs382524dbSNPEnsembl.1
Natural variantiVAR_005262255M → V in VWDP; increased binding to vWF. 2 PublicationsCorresponds to variant rs121908064dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS54068.1.
PIRiA94174. NBHUIA.
I70082.
RefSeqiNP_000164.5. NM_000173.6.
UniGeneiHs.1472.

Genome annotation databases

EnsembliENST00000329125; ENSP00000329380; ENSG00000185245.
GeneIDi2811.
KEGGihsa:2811.
UCSCiuc021tnz.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS54068.1.
PIRiA94174. NBHUIA.
I70082.
RefSeqiNP_000164.5. NM_000173.6.
UniGeneiHs.1472.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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-ray3.16B603-611[»]
4YR6X-ray2.38C/F503-512[»]
ProteinModelPortaliP07359.
SMRiP07359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109073. 8 interactors.
IntActiP07359. 12 interactors.
MINTiMINT-147226.
STRINGi9606.ENSP00000329380.

PTM databases

iPTMnetiP07359.
PhosphoSitePlusiP07359.
UniCarbKBiP07359.

Polymorphism and mutation databases

DMDMi121531.

Proteomic databases

EPDiP07359.
PaxDbiP07359.
PeptideAtlasiP07359.
PRIDEiP07359.

Protocols and materials databases

DNASUi2811.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329125; ENSP00000329380; ENSG00000185245.
GeneIDi2811.
KEGGihsa:2811.
UCSCiuc021tnz.1. human.

Organism-specific databases

CTDi2811.
DisGeNETi2811.
GeneCardsiGP1BA.
H-InvDBHIX0212275.
HGNCiHGNC:4439. GP1BA.
HPAiCAB002496.
HPA013316.
MalaCardsiGP1BA.
MIMi153670. phenotype.
177820. phenotype.
231200. phenotype.
258660. phenotype.
606672. gene.
neXtProtiNX_P07359.
OpenTargetsiENSG00000185245.
Orphaneti274. Bernard-Soulier syndrome.
853. Fetal and neonatal alloimmune thrombocytopenia.
52530. Pseudo-von Willebrand disease.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00860000133896.
HOVERGENiHBG051790.
InParanoidiP07359.
KOiK06261.
OMAiHLLPFAF.
OrthoDBiEOG091G08IS.
PhylomeDBiP07359.
TreeFamiTF351114.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000174409-MONOMER.
ReactomeiR-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-HSA-430116. GP1b-IX-V activation signalling.
R-HSA-75892. Platelet Adhesion to exposed collagen.
R-HSA-76009. Platelet Aggregation (Plug Formation).
SignaLinkiP07359.

Miscellaneous databases

EvolutionaryTraceiP07359.
GenomeRNAii2811.
PMAP-CutDBP07359.
PROiP07359.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000185245.
CleanExiHS_GP1BA.
ExpressionAtlasiP07359. baseline and differential.
GenevisibleiP07359. HS.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR000483. Cys-rich_flank_reg_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRRNT.
[Graphical view]
PfamiPF13855. LRR_8. 1 hit.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 5 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGP1BA_HUMAN
AccessioniPrimary (citable) accession number: P07359
Secondary accession number(s): E7ES66
, Q14441, Q16469, Q8N1F3, Q8NG39, Q9HDC7, Q9UEK1, Q9UQS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 16, 2014
Last modified: November 30, 2016
This is version 213 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.