CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022949
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
112AEHRYYGKSLPFGAQubiquitination[1, 2, 3, 4]
215DFEGQSPKCTQGVREubiquitination[2, 3, 5, 6]
228REAFRQIKDLFLQGAubiquitination[1, 2, 3, 4]
463ASVVEARKLEATIIGubiquitination[3]
474TIIGEWVKAARREQQubiquitination[3]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
Functional Description
 Plays an important role in the degradation of some oligopeptides. 
Sequence Annotation
 ACT_SITE 162 162 Charge relay system (Potential).
 ACT_SITE 418 418 Charge relay system (Potential).
 ACT_SITE 443 443 Charge relay system (Potential).
 CARBOHYD 50 50 N-linked (GlcNAc...).
 CARBOHYD 86 86 N-linked (GlcNAc...) (Potential).
 CARBOHYD 315 315 N-linked (GlcNAc...).
 CARBOHYD 356 356 N-linked (GlcNAc...) (Potential).
 CARBOHYD 363 363 N-linked (GlcNAc...) (Potential).
 CARBOHYD 428 428 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Aminopeptidase; Cleavage on pair of basic residues; Complete proteome; Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Polymorphism; Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 492 AA 
Protein Sequence
MGSAPWAPVL LLALGLRGLQ AGARRAPDPG FQERFFQQRL DHFNFERFGN KTFPQRFLVS 60
DRFWVRGEGP IFFYTGNEGD VWAFANNSAF VAELAAERGA LLVFAEHRYY GKSLPFGAQS 120
TQRGHTELLT VEQALADFAE LLRALRRDLG AQDAPAIAFG GSYGGMLSAY LRMKYPHLVA 180
GALAASAPVL AVAGLGDSNQ FFRDVTADFE GQSPKCTQGV REAFRQIKDL FLQGAYDTVR 240
WEFGTCQPLS DEKDLTQLFM FARNAFTVLA MMDYPYPTDF LGPLPANPVK VGCDRLLSEA 300
QRITGLRALA GLVYNASGSE HCYDIYRLYH SCADPTGCGT GPDARAWDYQ ACTEINLTFA 360
SNNVTDMFPD LPFTDELRQR YCLDTWGVWP RPDWLLTSFW GGDLRAASNI IFSNGNLDPW 420
AGGGIRRNLS ASVIAVTIQG GAHHLDLRAS HPEDPASVVE ARKLEATIIG EWVKAARREQ 480
QPALRGGPRL SL 492 
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; TAS:ProtInc.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR008758; Peptidase_S28. 
Pfam
 PF05577; Peptidase_S28 
SMART
  
PROSITE
  
PRINTS