CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021145
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dipeptidyl peptidase 2 
Protein Synonyms/Alias
 Dipeptidyl aminopeptidase II; Dipeptidyl peptidase 7; Dipeptidyl peptidase II; DPP II; Quiescent cell proline dipeptidase 
Gene Name
 Dpp7 
Gene Synonyms/Alias
 Dpp2; Qpp 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
72QRFLVSDKFWKMGEGubiquitination[1]
122AEHRYYGKSLPFGVQacetylation[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 Plays an important role in the degradation of some oligopeptides. 
Sequence Annotation
 ACT_SITE 172 172 Charge relay system (Potential).
 ACT_SITE 428 428 Charge relay system (Potential).
 ACT_SITE 453 453 Charge relay system (Potential).
 CARBOHYD 60 60 N-linked (GlcNAc...) (Potential).
 CARBOHYD 96 96 N-linked (GlcNAc...) (Potential).
 CARBOHYD 325 325 N-linked (GlcNAc...) (Potential).
 CARBOHYD 366 366 N-linked (GlcNAc...) (Potential).
 CARBOHYD 373 373 N-linked (GlcNAc...) (Potential).
 CARBOHYD 438 438 N-linked (GlcNAc...) (Potential).  
Keyword
 Aminopeptidase; Complete proteome; Cytoplasmic vesicle; Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 506 AA 
Protein Sequence
MNFHPCYPVD HGVPSWILVL LLSLGLCNLQ ARADRVLDPD FHENYFEQYM DHFNFESFGN 60
KTFGQRFLVS DKFWKMGEGP IFFYTGNEGD IWSFANNSGF MVELAAQQEA LLVFAEHRYY 120
GKSLPFGVQS TQRGYTQLLT VEQALADFAV LLQALRQDLG VHDAPTIAFG GSYGGMLSAY 180
MRMKYPHLVA GALAASAPVV AVAGLGDSYQ FFRDVTADFY GQSPKCAQAV RDAFQQIKDL 240
FLQGAYDTIS QNFGTCQSLS SPKDLTQLFG FARNAFTVLA MMDYPYPTDF LGPLPANPVK 300
VGCQRLLNEG QRIMGLRALA GLVYNSSGTE PCYDIYRLYQ SCADPTGCGT GSDARAWDYQ 360
ACTEINLTFD SNNVTDMFPE IPFSEELRQQ YCLDTWGVWP RQDWLQTSFW GGDLKAASNI 420
IFSNGDLDPW AGGGIQSNLS TSVIAVTIQG GAHHLDLRAS NSEDPPSVVE VRKLESTLIR 480
EWVAAARLKQ PAMPRWPGPK KQHPSR 506 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
 GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
 GO:0008239; F:dipeptidyl-peptidase activity; IEA:Compara.
 GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR008758; Peptidase_S28. 
Pfam
 PF05577; Peptidase_S28 
SMART
  
PROSITE
  
PRINTS