CTSC
entrez
1075
canonical
uniprot
P53634
canonical
ensembl
ENSG00000109861
resolver
ensp
ENSP00000227266
resolver
ensp
ENSP00000432541
resolver
ensp
ENSP00000433539
resolver
genesymbol
CTSC
resolver
genesymbol_syn
CPPI
resolver
hgnc
HGNC:2528
resolver
uniprot
A8K7V2
resolver
uniprot
B5MDD5
resolver
uniprot
Q2HIY8
resolver
uniprot
Q53G93
resolver
uniprot
Q71E75
resolver
uniprot
Q71E76
resolver
uniprot
Q7M4N9
resolver
uniprot
Q7Z3G7
resolver
uniprot
Q7Z5U7
resolver
uniprot
Q8WY99
resolver
uniprot
Q8WYA7
resolver
uniprot
Q8WYA8
resolver
uniprot_entry
CATC_HUMAN
resolver
uniprot_sec
A8K7V2
resolver
uniprot_sec
B5MDD5
resolver
uniprot_sec
Q2HIY8
resolver
uniprot_sec
Q53G93
resolver
uniprot_sec
Q71E75
resolver
uniprot_sec
Q71E76
resolver
uniprot_sec
Q7M4N9
resolver
uniprot_sec
Q7Z3G7
resolver
uniprot_sec
Q7Z5U7
resolver
uniprot_sec
Q8WY99
resolver
uniprot_sec
Q8WYA7
resolver
uniprot_sec
Q8WYA8
resolver
activity_regulation
ACTIVITY REGULATION: Strongly inhibited by the cysteine peptidase inhibitors mersalyl acid, iodoacetic acid and cystatin. Inhibited by N-ethylmaleimide, Gly-Phe-diazomethane, TLCK, TPCK and, at low pH, by dithiodipyridine. Not inhibited by the serine peptidase inhibitor PMSF, the aminopeptidase inhibitor bestatin, or metal ion chelators. {ECO:0000269|PubMed:1586157}.
uniprot
proteins
amino_acid_sequence
MGAGPSLLLAALLLLLSGDGAVRCDTPANCTYLDLLGTWVFQVGSSGSQRDVNCSVMGPQEKKVVVYLQKLDTAYDDLGNSGHFTIIYNQGFEIVLNDYKWFAFFKYKEEGSKVTTYCNETMTGWVHDVLGRNWACFTGKKVGTASENVYVNIAHLKNSQEKYSNRLYKYDHNFVKAINAIQKSWTATTYMEYETLTLGDMIRRSGGHSRKIPRPKPAPLTAEIQQKILHLPTSWDWRNVHGINFVSPVRNQASCGSCYSFASMGMLEARIRILTNNSQTPILSPQEVVSCSQYAQGCEGGFPYLIAGKYAQDFGLVEEACFPYTGTDSPCKMKEDCFRYYSSEYHYVGGFYGGCNEALMKLELVHHGPMAVAFEVYDDFLHYKKGIYHHTGLRDPFNPFELTNHAVLLVGYGTDSASGMDYWIVKNSWGTGWGENGYFRIRRGTDECAIESIAVAATPIPKL
uniprot
proteins
disease_involvement
DISEASE: Papillon-Lefevre syndrome (PLS) [MIM:245000]: An autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees. {ECO:0000269|PubMed:10581027, ECO:0000269|PubMed:10662808, ECO:0000269|PubMed:11106356, ECO:0000269|PubMed:11158173, ECO:0000269|PubMed:11180012, ECO:0000269|PubMed:11180601, ECO:0000269|PubMed:11886537, ECO:0000269|PubMed:12112662, ECO:0000269|PubMed:12809647, ECO:0000269|PubMed:14974080, ECO:0000269|PubMed:15108292, ECO:0000269|PubMed:15991336, ECO:0000269|PubMed:25799584}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Haim-Munk syndrome (HMS) [MIM:245010]: An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis. {ECO:0000269|PubMed:10662807}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Periodontititis, aggressive, 1 (PDON1) [MIM:170650]: An autosomal recessive disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting. {ECO:0000269|PubMed:10662808, ECO:0000269|PubMed:14974080}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.14.1
uniprot
proteins
function
FUNCTION: Thiol protease (PubMed:1586157). Has dipeptidylpeptidase activity (PubMed:1586157). Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids (PubMed:1586157). Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate (PubMed:1586157). Can act as both an exopeptidase and endopeptidase (PubMed:1586157). Activates serine proteases such as elastase, cathepsin G and granzymes A and B (PubMed:8428921). {ECO:0000269|PubMed:1586157, ECO:0000269|PubMed:8428921}.
uniprot
proteins
mass_dalton
51854
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes. {ECO:0000269|PubMed:11726493, ECO:0000269|PubMed:1586157, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19167329, ECO:0000269|PubMed:9507095}.; PTM: In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.
uniprot
proteins
protein_family
Peptidase C1 family
uniprot
proteins
pubmed
10581027
uniprot
proteins
pubmed
10662807
uniprot
proteins
pubmed
10662808
uniprot
proteins
pubmed
11015218
uniprot
proteins
pubmed
11106356
uniprot
proteins
pubmed
11158173
uniprot
proteins
pubmed
11180012
uniprot
proteins
pubmed
11180601
uniprot
proteins
pubmed
11726493
uniprot
proteins
pubmed
11886537
uniprot
proteins
pubmed
12112662
uniprot
proteins
pubmed
12809647
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14974080
uniprot
proteins
pubmed
15108292
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1586157
uniprot
proteins
pubmed
15991336
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19167329
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25799584
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
7649281
uniprot
proteins
pubmed
7665576
uniprot
proteins
pubmed
8428921
uniprot
proteins
pubmed
9092576
uniprot
proteins
pubmed
9507095
uniprot
proteins
sequence_length
463
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000305|PubMed:7665576}.
uniprot
proteins