CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019903
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dipeptidyl peptidase 3 
Protein Synonyms/Alias
 Dipeptidyl aminopeptidase III; Dipeptidyl arylamidase III; Dipeptidyl peptidase III; DPP III 
Gene Name
 Dpp3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
113YKSFGDTKFVPNLPKubiquitination[1]
131GRVILGSKAAQQRPEubiquitination[1]
165LRHLGLGKEGVTTYFubiquitination[1]
202AYNTRLFKVVGQEGKacetylation[2]
202AYNTRLFKVVGQEGKubiquitination[1]
209KVVGQEGKSHYEVRLubiquitination[1]
233LDSELTSKLKRYEFQacetylation[3]
233LDSELTSKLKRYEFQubiquitination[1]
342VNKAMSAKFERLVASacetylation[2]
365PWPLAFEKDKFLTPDubiquitination[1]
405LRQTEGFKNVSLGNVubiquitination[1]
423AYAAKREKLTFLEEEubiquitination[1]
466KLFVQDEKGAFNFDKubiquitination[1]
473KGAFNFDKETVINPEubiquitination[1]
629LRRLQVLKSTGDVVAacetylation[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]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Cleaves Arg-Arg-beta-naphthylamide (By similarity). 
Sequence Annotation
 ACT_SITE 451 451 By similarity.
 METAL 450 450 Zinc; catalytic (By similarity).
 METAL 455 455 Zinc; catalytic (By similarity).  
Keyword
 Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 738 AA 
Protein Sequence
MADTQYILPN DIGVSSLDCR EAFRLLSPTE RLYAHHLSRA AWYGGLAVLL QTSPEAPYIY 60
ALLSRLFRAQ DPDQLRQHAL AEGLTEEEYQ AFLVYAAGVY SNMGNYKSFG DTKFVPNLPK 120
DKLGRVILGS KAAQQRPEEV RDLWQTCGDL MFSLEPRLRH LGLGKEGVTT YFSGDCTMED 180
AKLAQDFLDS QNLSAYNTRL FKVVGQEGKS HYEVRLASVL NTDPALDSEL TSKLKRYEFQ 240
GNHFQVTRGD YAPILQKVVE HLEKAKAYAA NSHQEQMLAQ YVESFTQGSI EAHKRGSRFW 300
IQDKGPIVES YIGFIESYRD PFGSRGEFEG FVAMVNKAMS AKFERLVASA EQLLKELPWP 360
LAFEKDKFLT PDFTSLDVLT FAGSGIPAGI NIPNYDDLRQ TEGFKNVSLG NVLAVAYAAK 420
REKLTFLEEE DKDLYIRWKG PSFDVQVGLH ELLGHGSGKL FVQDEKGAFN FDKETVINPE 480
TGEQIQSWYR SGETWDSKFS TIASSYEECR AESVGLYLCL NPQVLEIFGF EGADAEDVIY 540
VNWLNMVRAG LLALEFYTPE AANWRQAHMQ ARFVILRVLL EAGEGLVTVT PTTGSDGRPD 600
ARVRLDRSKI RSVGRPALER FLRRLQVLKS TGDVVAGRAL YEGYAAVTDA PPECFLTLRD 660
TVLLRKESRK LIVQPNTRLE GSEVQLVEYE ASAAGLIRSF CERFPEDGPE LEEVLIQLAA 720
ADARFWRNQA QEAPPGQA 738 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
 GO:0008239; F:dipeptidyl-peptidase activity; IEA:InterPro.
 GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR005317; Dipeptidyl-peptase3. 
Pfam
  
SMART
  
PROSITE
  
PRINTS