Q9CYD3 · CRTAP_MOUSE

  • Protein
    Cartilage-associated protein
  • Gene
    Crtap
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues.

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 Componentendoplasmic reticulum
Cellular Componentextracellular space
Cellular Componentprotein-containing complex
Biological Processchaperone-mediated protein folding
Biological Processcollagen fibril organization
Biological Processnegative regulation of post-translational protein modification
Biological Processprotein stabilization
Biological Processspermatogenesis

Names & Taxonomy

Protein names

  • Recommended name
    Cartilage-associated protein

Gene names

    • Name
      Crtap
    • Synonyms
      Casp

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9CYD3
  • Secondary accessions
    • O88698
    • Q8C8C5

Proteomes

Organism-specific databases

Phenotypes & Variants

Involvement in disease

  • Defects in Crtap are a cause of osteochondrodysplasia characterized by severe osteoporosis and decreased osteoid production

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 21 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_000000632026-400Cartilage-associated protein
Glycosylation86N-linked (GlcNAc...) asparagine
Glycosylation362N-linked (GlcNAc...) asparagine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Found in articular chondrocytes. Expressed in a variety of tissues.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Belongs to the leprecan family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    400
  • Mass (Da)
    46,169
  • Last updated
    2011-07-27 v3
  • Checksum
    F6080CEC275CC5A4
MGPRSPTAALLVLLCVGCAPTPGRGQYERYSFRSFPRDELMPLESAYRHALDQYSGEHWAESVGYLEVSLRLHRLLRDSEAFCHRNCSAATPAPAPAGPASHAELRLFGSVLRRAQCLKRCKQGLPAFRQSQPSRSVLADFQQREPYKFLQFAYFKANDLPKAIAAAHTYLLKHPDDEMMKRNMEYYKSLPGAEDHIKDLETKSYESLFVRAVRAYNGENWRTSISDMELALPDFLKAFYECLAACEGSREIKDFKDFYLSIADHYVEVLECKIRCEETLTPVIGGYPVEKFVATMYHYLQFAYYKLNDLKNAAPCAVSYLLFDQSDRVMQQNLVYYQYHRDKWGLSDEHFQPRPEAVQFFNVTTLQKELYDFAQEHLMDDDEGEVVEYVDDLLETEESA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict7in Ref. 1; CAA07053
Sequence conflict34in Ref. 1; CAA07053
Sequence conflict79-80in Ref. 2; BAB30938
Sequence conflict249-250in Ref. 2; BAB30938
Sequence conflict254in Ref. 2; BAB30938

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ006469
EMBL· GenBank· DDBJ
CAA07053.1
EMBL· GenBank· DDBJ
mRNA
AK017797
EMBL· GenBank· DDBJ
BAB30938.1
EMBL· GenBank· DDBJ
mRNA
AK047506
EMBL· GenBank· DDBJ
BAC33076.1
EMBL· GenBank· DDBJ
mRNA
BC049890
EMBL· GenBank· DDBJ
AAH49890.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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