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P13224

- GP1BB_HUMAN

UniProt

P13224 - GP1BB_HUMAN

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Protein

Platelet glycoprotein Ib beta chain

Gene

GP1BB

Organism
Homo sapiens (Human)
Status
Reviewed - 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 von Willebrand factor, which is already bound to the subendothelium.

GO - Molecular functioni

  1. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. blood coagulation, intrinsic pathway Source: Reactome
  3. cell adhesion Source: UniProtKB-KW
  4. cell surface receptor signaling pathway Source: ProtInc
  5. platelet activation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Cell adhesion, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_1230. Platelet Adhesion to exposed collagen.
REACT_23847. GP1b-IX-V activation signalling.
REACT_278. Platelet Aggregation (Plug Formation).
REACT_326. Intrinsic Pathway.
SignaLinkiP13224.

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet glycoprotein Ib beta chain
Short name:
GP-Ib beta
Short name:
GPIb-beta
Short name:
GPIbB
Alternative name(s):
Antigen CD42b-beta
CD_antigen: CD42c
Gene namesi
Name:GP1BB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:4440. GP1BB.

Subcellular locationi

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Bernard-Soulier syndrome (BSS) [MIM:231200]: A coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, thrombocytopenia, and impaired prothrombin consumption.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti113 – 1131Y → C in BSS. 1 Publication
VAR_025000
Natural varianti133 – 1331A → P in BSS. 1 Publication
VAR_025001

Keywords - Diseasei

Bernard Soulier syndrome, Disease mutation

Organism-specific databases

MIMi231200. phenotype.
Orphaneti567. 22q11.2 deletion syndrome.
274. Bernard-Soulier syndrome.
853. Fetal and neonatal alloimmune thrombocytopenia.
PharmGKBiPA179.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 206180Platelet glycoprotein Ib beta chainPRO_0000021345Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi26 ↔ 321 Publication
Disulfide bondi30 ↔ 391 Publication
Glycosylationi66 – 661N-linked (GlcNAc...)2 Publications
Disulfide bondi93 ↔ 1181 Publication
Disulfide bondi95 ↔ 1411 Publication
Disulfide bondi147 – 147Interchain (with C-500 or C-501 in GP1BA)1 Publication
Modified residuei191 – 1911Phosphoserine; by PKA2 Publications
Modified residuei193 – 1931Phosphothreonine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP13224.
PaxDbiP13224.
PRIDEiP13224.

2D gel databases

OGPiP13224.

PTM databases

PhosphoSiteiP13224.

Expressioni

Tissue specificityi

Expressed in heart and brain.1 Publication

Gene expression databases

GenevestigatoriP13224.

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.2 Publications

Protein-protein interaction databases

BioGridi109074. 17 interactions.
IntActiP13224. 3 interactions.
MINTiMINT-1530456.
STRINGi9606.ENSP00000383382.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333
Beta strandi36 – 383
Turni46 – 483
Beta strandi58 – 614
Turni72 – 743
Helixi75 – 773
Beta strandi83 – 853
Helixi95 – 973
Helixi98 – 1058
Helixi111 – 1133
Beta strandi117 – 1215
Turni122 – 1265
Helixi129 – 1313
Helixi134 – 1396

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3REZX-ray2.35A/B/C/D26-146[»]
3RFEX-ray1.24A/B26-146[»]
ProteinModelPortaliP13224.
SMRiP13224. Positions 26-143.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 147121ExtracellularSequence AnalysisAdd
BLAST
Topological domaini173 – 20634CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei148 – 17225HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 5529LRRNTAdd
BLAST
Repeati60 – 8324LRRAdd
BLAST
Domaini89 – 14355LRRCTAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Leucine-rich repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG266400.
GeneTreeiENSGT00530000064244.
HOGENOMiHOG000060136.
HOVERGENiHBG051791.
InParanoidiP13224.
KOiK06262.
OMAiFPPDTTE.
OrthoDBiEOG75MVZ1.
PhylomeDBiP13224.

Family and domain databases

InterProiIPR000483. Cys-rich_flank_reg_C.
IPR000372. LRR-contain_N.
[Graphical view]
PfamiPF01463. LRRCT. 1 hit.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P13224-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGSGPRGALS LLLLLLAPPS RPAAGCPAPC SCAGTLVDCG RRGLTWASLP
60 70 80 90 100
TAFPVDTTEL VLTGNNLTAL PPGLLDALPA LRTAHLGANP WRCDCRLVPL
110 120 130 140 150
RAWLAGRPER APYRDLRCVA PPALRGRLLP YLAEDELRAA CAPGPLCWGA
160 170 180 190 200
LAAQLALLGL GLLHALLLVL LLCRLRRLRA RARARAAARL SLTDPLVAER

AGTDES
Length:206
Mass (Da):21,718
Last modified:January 1, 1990 - v1
Checksum:iB5E81EB6F57DE0D9
GO
Isoform 2 (identifier: P13224-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MGS → MIPSRHTMLR...RSAYCGASLA

Show »
Length:411
Mass (Da):43,158
Checksum:i7D84D76AA079DFCF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti113 – 1131Y → C in BSS. 1 Publication
VAR_025000
Natural varianti133 – 1331A → P in BSS. 1 Publication
VAR_025001

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 33MGS → MIPSRHTMLRFLPVVNAASC PGDRRTMLVNVAAGVRVLRV PLRAGGSGSLSGLRPPAIVC YLPLQRASAASGLFLARPQH CGRCGRGRGGAALSLGSPAY ASRCRVSRAAVFSPWAPVSL ESGRAPGCSLGRPGLRGALV VWLQLGETWVRLRGDFQPAC GVVRVERLAGYRDAGHQGLD GAGPAVWVLRDVAQVPADRS AYCGASLA in isoform 2. 1 PublicationVSP_032671

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03259 mRNA. Translation: AAA52594.1.
AF006988 Genomic DNA. Translation: AAC39781.1.
L20860 mRNA. Translation: AAA20398.1.
U59632 mRNA. Translation: AAB93437.1.
AB086231 Genomic DNA. Translation: BAC00777.1.
CCDSiCCDS42980.1. [P13224-1]
PIRiA54137. NBHUIB.
I55604.
RefSeqiNP_000398.1. NM_000407.4. [P13224-1]
UniGeneiHs.283743.
Hs.728762.

Genome annotation databases

EnsembliENST00000366425; ENSP00000383382; ENSG00000203618. [P13224-1]
GeneIDi2812.
KEGGihsa:2812.
UCSCiuc002zpz.2. human. [P13224-1]

Polymorphism databases

DMDMi121532.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03259 mRNA. Translation: AAA52594.1 .
AF006988 Genomic DNA. Translation: AAC39781.1 .
L20860 mRNA. Translation: AAA20398.1 .
U59632 mRNA. Translation: AAB93437.1 .
AB086231 Genomic DNA. Translation: BAC00777.1 .
CCDSi CCDS42980.1. [P13224-1 ]
PIRi A54137. NBHUIB.
I55604.
RefSeqi NP_000398.1. NM_000407.4. [P13224-1 ]
UniGenei Hs.283743.
Hs.728762.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3REZ X-ray 2.35 A/B/C/D 26-146 [» ]
3RFE X-ray 1.24 A/B 26-146 [» ]
ProteinModelPortali P13224.
SMRi P13224. Positions 26-143.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109074. 17 interactions.
IntActi P13224. 3 interactions.
MINTi MINT-1530456.
STRINGi 9606.ENSP00000383382.

PTM databases

PhosphoSitei P13224.

Polymorphism databases

DMDMi 121532.

2D gel databases

OGPi P13224.

Proteomic databases

MaxQBi P13224.
PaxDbi P13224.
PRIDEi P13224.

Protocols and materials databases

DNASUi 2812.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366425 ; ENSP00000383382 ; ENSG00000203618 . [P13224-1 ]
GeneIDi 2812.
KEGGi hsa:2812.
UCSCi uc002zpz.2. human. [P13224-1 ]

Organism-specific databases

CTDi 2812.
GeneCardsi GC22P019710.
HGNCi HGNC:4440. GP1BB.
MIMi 138720. gene.
231200. phenotype.
neXtProti NX_P13224.
Orphaneti 567. 22q11.2 deletion syndrome.
274. Bernard-Soulier syndrome.
853. Fetal and neonatal alloimmune thrombocytopenia.
PharmGKBi PA179.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG266400.
GeneTreei ENSGT00530000064244.
HOGENOMi HOG000060136.
HOVERGENi HBG051791.
InParanoidi P13224.
KOi K06262.
OMAi FPPDTTE.
OrthoDBi EOG75MVZ1.
PhylomeDBi P13224.

Enzyme and pathway databases

Reactomei REACT_1230. Platelet Adhesion to exposed collagen.
REACT_23847. GP1b-IX-V activation signalling.
REACT_278. Platelet Aggregation (Plug Formation).
REACT_326. Intrinsic Pathway.
SignaLinki P13224.

Miscellaneous databases

GeneWikii GP1BB.
GenomeRNAii 2812.
NextBioi 11079.
PROi P13224.
SOURCEi Search...

Gene expression databases

Genevestigatori P13224.

Family and domain databases

InterProi IPR000483. Cys-rich_flank_reg_C.
IPR000372. LRR-contain_N.
[Graphical view ]
Pfami PF01463. LRRCT. 1 hit.
PF01462. LRRNT. 1 hit.
[Graphical view ]
SMARTi SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence."
    Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Davie E.W., Roth G.J.
    Proc. Natl. Acad. Sci. U.S.A. 85:2135-2139(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION AT ASN-66.
  2. "Structural characterization and chromosomal location of the gene encoding human platelet glycoprotein Ib beta."
    Yagi M., Edelhoff S., Disteche C.M., Roth G.J.
    J. Biol. Chem. 269:17424-17427(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  3. "Complementary DNA cloning of the alternatively expressed endothelial cell glycoprotein Ib beta (GPIb beta) and localization of the GPIb beta gene to chromosome 22."
    Kelly M.D., Essex D.W., Shapiro S.S., Meloni F.J., Druck T., Huebner K., Konkle B.A.
    J. Clin. Invest. 93:2417-2424(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Umbilical vein.
  4. "Alternative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence."
    Zieger B., Hashimoto Y., Ware J.
    J. Clin. Invest. 99:520-525(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Missense mutations of the glycoprotein (GP) Ib beta gene impairing the GPIb alpha/beta disulfide linkage in a family with giant platelet disorder."
    Kunishima S., Lopez J.A., Kobayashi S., Imai N., Kamiya T., Saito H., Naoe T.
    Blood 89:2404-2412(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-206, VARIANTS BSS CYS-113 AND PRO-133.
  6. "Isolation and characterization of the alpha and beta chains of human platelet glycoprotein Ib."
    Canfield V.A., Ozols J., Nugent D., Roth G.J.
    Biochem. Biophys. Res. Commun. 147:526-534(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-40.
  7. "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 83-92 AND 190-200.
    Tissue: Platelet.
  8. "Platelet glycoprotein Ib beta is phosphorylated on serine 166 by cyclic AMP-dependent protein kinase."
    Wardell M.R., Reynolds C.C., Berndt M.C., Wallace R.W., Fox J.E.B.
    J. Biol. Chem. 264:15656-15661(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-191, PROTEIN SEQUENCE OF 186-200.
  9. "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 BOND.
  10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND THR-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. "Quaternary organization of GPIb-IX complex and insights into Bernard-Soulier syndrome revealed by the structures of GPIbbeta and a GPIbbeta/GPIX chimera."
    McEwan P.A., Yang W., Carr K.H., Mo X., Zheng X., Li R., Emsley J.
    Blood 118:5292-5301(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 26-146, GLYCOSYLATION AT ASN-66, DISULFIDE BONDS.

Entry informationi

Entry nameiGP1BB_HUMAN
AccessioniPrimary (citable) accession number: P13224
Secondary accession number(s): Q14422, Q8NG40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: October 29, 2014
This is version 141 of the entry and version 1 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.

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 22
    Human chromosome 22: 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

External Data

Dasty 3