Q9CYD3 · CRTAP_MOUSE
- ProteinCartilage-associated protein
- GeneCrtap
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids400 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular space | |
Cellular Component | protein-containing complex | |
Biological Process | chaperone-mediated protein folding | |
Biological Process | collagen fibril organization | |
Biological Process | negative regulation of post-translational protein modification | |
Biological Process | protein stabilization | |
Biological Process | spermatogenesis |
Names & Taxonomy
Protein names
- Recommended nameCartilage-associated protein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9CYD3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
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.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MGPRSPTAALLVLLCVGCAPTPGRG | ||||||
Chain | PRO_0000006320 | 26-400 | Cartilage-associated protein | |||
Sequence: QYERYSFRSFPRDELMPLESAYRHALDQYSGEHWAESVGYLEVSLRLHRLLRDSEAFCHRNCSAATPAPAPAGPASHAELRLFGSVLRRAQCLKRCKQGLPAFRQSQPSRSVLADFQQREPYKFLQFAYFKANDLPKAIAAAHTYLLKHPDDEMMKRNMEYYKSLPGAEDHIKDLETKSYESLFVRAVRAYNGENWRTSISDMELALPDFLKAFYECLAACEGSREIKDFKDFYLSIADHYVEVLECKIRCEETLTPVIGGYPVEKFVATMYHYLQFAYYKLNDLKNAAPCAVSYLLFDQSDRVMQQNLVYYQYHRDKWGLSDEHFQPRPEAVQFFNVTTLQKELYDFAQEHLMDDDEGEVVEYVDDLLETEESA | ||||||
Glycosylation | 86 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 362 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in articular chondrocytes. Expressed in a variety of tissues.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length400
- Mass (Da)46,169
- Last updated2011-07-27 v3
- ChecksumF6080CEC275CC5A4
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 7 | in Ref. 1; CAA07053 | ||||
Sequence: T → A | ||||||
Sequence conflict | 34 | in Ref. 1; CAA07053 | ||||
Sequence: S → N | ||||||
Sequence conflict | 79-80 | in Ref. 2; BAB30938 | ||||
Sequence: SE → RQ | ||||||
Sequence conflict | 249-250 | in Ref. 2; BAB30938 | ||||
Sequence: SR → VA | ||||||
Sequence conflict | 254 | in Ref. 2; BAB30938 | ||||
Sequence: D → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |