CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008726
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dipeptidyl peptidase 1 
Protein Synonyms/Alias
 Cathepsin C; Cathepsin J; Dipeptidyl peptidase I; DPP-I; DPPI; Dipeptidyl transferase; Dipeptidyl peptidase 1 exclusion domain chain; Dipeptidyl peptidase I exclusion domain chain; Dipeptidyl peptidase 1 heavy chain; Dipeptidyl peptidase I heavy chain; Dipeptidyl peptidase 1 light chain; Dipeptidyl peptidase I light chain 
Gene Name
 CTSC 
Gene Synonyms/Alias
 CPPI 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
133DLPHLRNKLVIK***ubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII. 
Sequence Annotation
 ACT_SITE 258 258
 ACT_SITE 405 405
 ACT_SITE 427 427
 BINDING 302 302 Chloride.
 BINDING 304 304 Chloride; via amide nitrogen.
 BINDING 347 347 Chloride.
 CARBOHYD 29 29 N-linked (GlcNAc...).
 CARBOHYD 53 53 N-linked (GlcNAc...).
 CARBOHYD 119 119 N-linked (GlcNAc...).
 CARBOHYD 276 276 N-linked (GlcNAc...).
 DISULFID 30 118
 DISULFID 54 136
 DISULFID 255 298
 DISULFID 291 331
 DISULFID 321 337  
Keyword
 3D-structure; Alternative splicing; Chloride; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Palmoplantar keratoderma; Polymorphism; Protease; Reference proteome; Signal; Thiol protease; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 463 AA 
Protein Sequence
MGAGPSLLLA ALLLLLSGDG AVRCDTPANC TYLDLLGTWV FQVGSSGSQR DVNCSVMGPQ 60
EKKVVVYLQK LDTAYDDLGN SGHFTIIYNQ GFEIVLNDYK WFAFFKDVTD FISHLFMQLG 120
TVGIYDLPHL RNKLVIK 137 
Gene Ontology
 GO:0005783; C:endoplasmic reticulum; IEA:Compara.
 GO:0005794; C:Golgi apparatus; IEA:Compara.
 GO:0005764; C:lysosome; TAS:UniProtKB.
 GO:0031404; F:chloride ion binding; IEA:Compara.
 GO:0008234; F:cysteine-type peptidase activity; IDA:UniProtKB.
 GO:0004252; F:serine-type endopeptidase activity; IEA:Compara.
 GO:0007568; P:aging; IEA:Compara.
 GO:0006955; P:immune response; TAS:ProtInc.
 GO:0006508; P:proteolysis; IDA:UniProtKB.
 GO:0010033; P:response to organic substance; IEA:Compara.
 GO:0001913; P:T cell mediated cytotoxicity; IEA:Compara. 
Interpro
 IPR014882; CathepsinC_exc.
 IPR025661; Pept_asp_AS.
 IPR000169; Pept_cys_AS.
 IPR025660; Pept_his_AS.
 IPR013128; Peptidase_C1A.
 IPR000668; Peptidase_C1A_C. 
Pfam
 PF08773; CathepsinC_exc
 PF00112; Peptidase_C1 
SMART
 SM00645; Pept_C1 
PROSITE
 PS00640; THIOL_PROTEASE_ASN
 PS00139; THIOL_PROTEASE_CYS
 PS00639; THIOL_PROTEASE_HIS 
PRINTS
 PR00705; PAPAIN.