A0A7I2V6E3 · A0A7I2V6E3_HUMAN

  • Protein
    dipeptidyl-peptidase I
  • Gene
    CTSC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    2/5

Function

Catalytic activity

  • Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.
    EC:3.4.14.1 (UniProtKB | ENZYME | Rhea)

Cofactor

chloride (UniProtKB | Rhea| CHEBI:17996 )

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 Componentcentrosome
Cellular Componentintracellular membrane-bounded organelle
Molecular Functioncysteine-type peptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    dipeptidyl-peptidase I
  • EC number

Gene names

    • Name
      CTSC

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    A0A7I2V6E3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

Disease & Variants

Variants

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

The viewer provides 498 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Signal1-24UniProt
ChainPRO_502979495025-419UniProtdipeptidyl-peptidase I
Modified residue (large scale data)285PRIDEPhosphoserine

Keywords

Proteomic databases

Expression

Gene expression databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain231-414Peptidase C1A papain C-terminal

Sequence similarities

Belongs to the peptidase C1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    419
  • Mass (Da)
    47,128
  • Last updated
    2021-04-07 v1
  • Checksum
    77E476C2FFCA5422
MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL

Computationally mapped potential isoform sequences

There are 17 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
P53634CATC_HUMANCTSC463
H0YDA2H0YDA2_HUMANCTSC21
H0YCY8H0YCY8_HUMANCTSC325
A0A7I2YQ96A0A7I2YQ96_HUMANCTSC60
A0A7I2YQT5A0A7I2YQT5_HUMANCTSC342
A0A7I2V2F3A0A7I2V2F3_HUMANCTSC117
A0A7I2V2Q8A0A7I2V2Q8_HUMANCTSC452
A0A7I2V2V5A0A7I2V2V5_HUMANCTSC143
A0A7I2V3A2A0A7I2V3A2_HUMANCTSC135
A0A7I2V3A6A0A7I2V3A6_HUMANCTSC48
A0A7I2V3M6A0A7I2V3M6_HUMANCTSC165
A0A7I2V466A0A7I2V466_HUMANCTSC450
A0A7I2V4Z3A0A7I2V4Z3_HUMANCTSC134
A0A7I2V592A0A7I2V592_HUMANCTSC75
A0A7I2V5C5A0A7I2V5C5_HUMANCTSC302
A0A7I2V5J2A0A7I2V5J2_HUMANCTSC150
A0A7I2V5L5A0A7I2V5L5_HUMANCTSC108

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC011088
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AP000795
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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