CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014640
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tripeptidyl-peptidase 2 
Protein Synonyms/Alias
 TPP-2; Tripeptidyl aminopeptidase; Tripeptidyl-peptidase II; TPP-II 
Gene Name
 Tpp2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
19FHGLLPKKETGASSFacetylation[1]
19FHGLLPKKETGASSFubiquitination[2]
61MQVTTDGKPKIIDIIubiquitination[2]
98GLSGRVLKIPANWTNubiquitination[2]
109NWTNPLGKYHIGIKNubiquitination[2]
115GKYHIGIKNGYDFYPubiquitination[2]
136IQKERKEKIWDPIHRubiquitination[2]
152ALAEACRKQEEFDIAubiquitination[2]
186ELLNSFEKKYSDPGPubiquitination[2]
187LLNSFEKKYSDPGPVacetylation[1]
401AEYSLREKLPANQYTacetylation[1, 3]
401AEYSLREKLPANQYTubiquitination[2]
655AFTDVHFKPGQIRRHubiquitination[2]
697LHAVQLVKQRAYRSHacetylation[1]
708YRSHEFYKFCSLPEKubiquitination[2]
715KFCSLPEKGTLIEAFubiquitination[2]
791LAPCITLKSWVQTLRubiquitination[2]
880YPHQYSLKLEKGDYTacetylation[1]
880YPHQYSLKLEKGDYTubiquitination[2]
883QYSLKLEKGDYTIRLacetylation[1, 3, 4, 5]
883QYSLKLEKGDYTIRLubiquitination[2]
904ISDLDRLKDLPFIVSacetylation[1]
958VTSLPDDKIPKGAGPacetylation[5]
1031SEKEKDLKEEFTEALubiquitination[2]
1080LHQLDAEKERMKRLNubiquitination[2]
1206YKHALVNKMYGRGLKacetylation[1]
1206YKHALVNKMYGRGLKubiquitination[2]
1217RGLKFATKLVEEKPTubiquitination[2]
1225LVEEKPTKENWKNCIubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [5] 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
 Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited (By similarity). 
Sequence Annotation
 ACT_SITE 44 44 Charge relay system (By similarity).
 ACT_SITE 264 264 Charge relay system (By similarity).
 ACT_SITE 449 449 Charge relay system (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 CROSSLNK 1018 1018 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1026 1026 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Alternative splicing; Aminopeptidase; Complete proteome; Cytoplasm; Hydrolase; Isopeptide bond; Nucleus; Protease; Reference proteome; Serine protease; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1262 AA 
Protein Sequence
MATAATEEPF PFHGLLPKKE TGASSFLCRY PEYDGRGVLI AVLDTGVDPG APGMQVTTDG 60
KPKIIDIIDT TGSGDVNTAT EVEPKDGEII GLSGRVLKIP ANWTNPLGKY HIGIKNGYDF 120
YPKALKERIQ KERKEKIWDP IHRVALAEAC RKQEEFDIAN NGSSQANKLI KEELQSQVEL 180
LNSFEKKYSD PGPVYDCLVW HDGETWRACV DSNENGDLSK CAVLRNYKEA QEYSSFGTAE 240
MLNYSVNIYD DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR 300
LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW KHNTIYVSSA 360
GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE KLPANQYTWS SRGPSADGAL 420
GVSISAPGGA IASVPNWTLR GTQLMNGTSM SSPNACGGIA LVLSGLKANN VDYTVHSVRR 480
ALENTAIKAD NIEVFAQGHG IIQVDKAYDY LIQNTSFANR LGFTVTVGNN RGIYLRDPVQ 540
VAAPSDHGVG IEPVFPENTE NSEKISFQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD 600
PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT DVHFKPGQIR 660
RHFVEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA YRSHEFYKFC SLPEKGTLIE 720
AFPVLGGKAI EFCIARWWAS LSDVNIDYTI SFHGIVCTAP QLNIHASEGI NRFDVQSSLK 780
YEDLAPCITL KSWVQTLRPV NAKTRPLGSR DVLPNNRQLY EMVLTYSFHQ PKSGEVTPSC 840
PLLCELLYES EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL 900
DRLKDLPFIV SHRLSNTLSL DIHENHSLAL LGKKKSSSLT LPPKYNQPFF VTSLPDDKIP 960
KGAGPGCYLA GSLTLSKTEL GKKAGQSAAK RQGKFKKDVI PVHYYLIPPP TKIKNGSKDK 1020
EKDSEKEKDL KEEFTEALRD LKIQWMTKLD STDIYNELKE TYPAYLPLYV ARLHQLDAEK 1080
ERMKRLNEIV DAANAVISHI DQTALAVYIA MKTDPRPDAA TIKNDMDKQK STLIDALCRK 1140
GCALADHLLH TQPHDGAAAG DAEAKEEEGE STMESLSETY WETTKWTDLF DTKVLIFAYK 1200
HALVNKMYGR GLKFATKLVE EKPTKENWKN CIQLMKLLGW THCASFTENW LPIMYPPDYC 1260
VF 1262 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
 GO:0004252; F:serine-type endopeptidase activity; IBA:RefGenome.
 GO:0006508; P:proteolysis; IBA:RefGenome. 
Interpro
 IPR000209; Peptidase_S8/S53_dom.
 IPR022398; Peptidase_S8_His-AS.
 IPR023828; Peptidase_S8_Ser-AS.
 IPR015500; Peptidase_S8_subtilisin-rel.
 IPR022229; Peptidase_S8A_TPPII. 
Pfam
 PF00082; Peptidase_S8
 PF12580; TPPII 
SMART
  
PROSITE
 PS00136; SUBTILASE_ASP
 PS00137; SUBTILASE_HIS
 PS00138; SUBTILASE_SER 
PRINTS
 PR00723; SUBTILISIN.