Q9JJM7 · GP1BB_RAT

  • Protein
    Platelet glycoprotein Ib beta chain
  • Gene
    Gp1bb
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

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.

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentglycoprotein Ib-IX-V complex
Molecular Functionidentical protein binding
Biological Processblood coagulation
Biological Processblood coagulation, intrinsic pathway
Biological Processcell adhesion
Biological Processmegakaryocyte development
Biological Processpositive regulation of platelet activation
Biological Processrelease of sequestered calcium ion into cytosol

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Platelet glycoprotein Ib beta chain
  • Short names
    GP-Ib beta; GPIb-beta; GPIbB
  • CD Antigen Name
    • CD42c

Gene names

    • Name
      Gp1bb

Organism names

  • Taxonomic identifier
  • Strain
    • Wistar
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    Q9JJM7

Proteomes

Organism-specific databases

Subcellular Location

Membrane
; Single-pass type I membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain27-150Extracellular
Transmembrane151-171Helical
Topological domain172-206Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, disulfide bond, chain, modified residue.

TypeIDPosition(s)Description
Signal1-26
Disulfide bond26↔32
ChainPRO_000032652827-206Platelet glycoprotein Ib beta chain
Disulfide bond30↔39
Disulfide bond93↔118
Disulfide bond95↔141
Disulfide bond147Interchain (with C-608 or C-609 in GP1BA)
Modified residue186Phosphoserine
Modified residue191Phosphoserine; by PKA
Modified residue193Phosphothreonine
Modified residue200Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

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 TRAF4 (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, repeat.

TypeIDPosition(s)Description
Domain27-55LRRNT
Repeat60-83LRR
Domain89-143LRRCT

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    206
  • Mass (Da)
    22,175
  • Last updated
    2000-10-01 v1
  • Checksum
    38ECE6E99DEF22B8
MGSRPRGALSLLLLLLAPPSRPASGCPAPCRCSETRVDCGRRGLTWASLPAAFPPDTTELVLTDNNLTALPPGLLDTLPALRRVHLGANPWRCDCRLLPLRAWLAGRPEREFYRDLRCVAPLALRGRLLPYVAEDELRAACAPGLLCWGALVAQLALLVLGLLHALLLALLLSRLRRLRAQARARSTREFSLTAPLVAESAGGGAS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB027146
EMBL· GenBank· DDBJ
BAA98053.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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