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P13224 (GP1BB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GP1BB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length206 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 von Willebrand factor, 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. Ref.9 Ref.13

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed in heart and brain. Ref.3

Involvement in disease

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.5

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.

Sequence similarities

Contains 1 LRR (leucine-rich) repeat.

Contains 1 LRRCT domain.

Contains 1 LRRNT domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P13224-1)

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.
Isoform 2 (identifier: P13224-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.6
Chain27 – 206180Platelet glycoprotein Ib beta chain
PRO_0000021345

Regions

Topological domain27 – 147121Extracellular Potential
Transmembrane148 – 17225Helical; Potential
Topological domain173 – 20634Cytoplasmic Potential
Domain27 – 5529LRRNT
Repeat60 – 8324LRR
Domain89 – 14355LRRCT

Amino acid modifications

Modified residue1911Phosphoserine; by PKA Ref.8 Ref.11 Ref.12
Modified residue1931Phosphothreonine Ref.11
Glycosylation661N-linked (GlcNAc...) Ref.1 Ref.13
Disulfide bond26 ↔ 32 Ref.9 Ref.13
Disulfide bond30 ↔ 39 Ref.9 Ref.13
Disulfide bond93 ↔ 118 Ref.9 Ref.13
Disulfide bond95 ↔ 141 Ref.9 Ref.13
Disulfide bond147Interchain (with C-500 or C-501 in GP1BA) Ref.9 Ref.13

Natural variations

Alternative sequence1 – 33MGS → MIPSRHTMLRFLPVVNAASC PGDRRTMLVNVAAGVRVLRV PLRAGGSGSLSGLRPPAIVC YLPLQRASAASGLFLARPQH CGRCGRGRGGAALSLGSPAY ASRCRVSRAAVFSPWAPVSL ESGRAPGCSLGRPGLRGALV VWLQLGETWVRLRGDFQPAC GVVRVERLAGYRDAGHQGLD GAGPAVWVLRDVAQVPADRS AYCGASLA in isoform 2.
VSP_032671
Natural variant1131Y → C in BSS. Ref.5
VAR_025000
Natural variant1331A → P in BSS. Ref.5
VAR_025001

Secondary structure

.......................... 206
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: B5E81EB6F57DE0D9

FASTA20621,718
        10         20         30         40         50         60 
MGSGPRGALS LLLLLLAPPS RPAAGCPAPC SCAGTLVDCG RRGLTWASLP TAFPVDTTEL 

        70         80         90        100        110        120 
VLTGNNLTAL PPGLLDALPA LRTAHLGANP WRCDCRLVPL RAWLAGRPER APYRDLRCVA 

       130        140        150        160        170        180 
PPALRGRLLP YLAEDELRAA CAPGPLCWGA LAAQLALLGL GLLHALLLVL LLCRLRRLRA 

       190        200 
RARARAAARL SLTDPLVAER AGTDES 

« Hide

Isoform 2 [UniParc].

Checksum: 7D84D76AA079DFCF
Show »

FASTA41143,158

References

« Hide 'large scale' references
[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]"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-191 AND THR-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]Carrascal M., Abian J.
Submitted (JAN-2008) to UniProtKB
Cited for: PHOSPHORYLATION AT SER-191, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRNBHUIB. A54137.
I55604.
RefSeqNP_000398.1. NM_000407.4.
UniGeneHs.283743.
Hs.728762.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3REZX-ray2.35A/B/C/D26-146[»]
3RFEX-ray1.24A/B26-146[»]
ProteinModelPortalP13224.
SMRP13224. Positions 26-143.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109074. 6 interactions.
IntActP13224. 3 interactions.
MINTMINT-1530456.
STRING9606.ENSP00000383382.

PTM databases

PhosphoSiteP13224.

Polymorphism databases

DMDM121532.

2D gel databases

OGPP13224.

Proteomic databases

PaxDbP13224.
PRIDEP13224.

Protocols and materials databases

DNASU2812.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366425; ENSP00000383382; ENSG00000203618. [P13224-1]
GeneID2812.
KEGGhsa:2812.
UCSCuc002zpz.2. human. [P13224-1]

Organism-specific databases

CTD2812.
GeneCardsGC22P019710.
HGNCHGNC:4440. GP1BB.
MIM138720. gene.
231200. phenotype.
neXtProtNX_P13224.
Orphanet567. 22q11.2 deletion syndrome.
274. Bernard-Soulier syndrome.
853. Fetal and neonatal alloimmune thrombocytopenia.
PharmGKBPA179.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266400.
HOGENOMHOG000060136.
HOVERGENHBG051791.
InParanoidP13224.
KOK06262.
OMAFPPDTTE.
OrthoDBEOG75MVZ1.
PhylomeDBP13224.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
SignaLinkP13224.

Gene expression databases

GenevestigatorP13224.

Family and domain databases

InterProIPR000483. Cys-rich_flank_reg_C.
IPR000372. LRR-contain_N.
[Graphical view]
PfamPF01463. LRRCT. 1 hit.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiGP1BB.
GenomeRNAi2812.
NextBio11079.
PROP13224.
SOURCESearch...

Entry information

Entry nameGP1BB_HUMAN
AccessionPrimary (citable) accession number: P13224
Secondary accession number(s): Q14422, Q8NG40
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 135 of the entry and version 1 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 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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