CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022597
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prolyl endopeptidase 
Protein Synonyms/Alias
 PE; Post-proline cleaving enzyme 
Gene Name
 Prep 
Gene Synonyms/Alias
 Pep 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
75TELYDYPKYSCHFKKacetylation[1]
162FMKVDGAKELPDVLEubiquitination[2]
172PDVLERVKFTCMAWTacetylation[1]
196SYPQQDGKSDGTETSubiquitination[2]
325FTDPDESKWKVLVPEacetylation[1]
335VLVPEHEKDVLEWVAacetylation[1]
457IPMFIVHKKGIKLDGacetylation[1]
588MDMLKFHKFTIGHAWacetylation[1]
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] 
Functional Description
 Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. 
Sequence Annotation
 ACT_SITE 554 554 Charge relay system (By similarity).
 ACT_SITE 641 641 Charge relay system (By similarity).
 ACT_SITE 680 680 Charge relay system (By similarity).
 MOD_RES 157 157 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 710 AA 
Protein Sequence
MLSFQYPDVY RDETSVQEYH GHKICDPYSW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR 60
GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNTLS 120
DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFTCMAWTH 180
DGKGMFYNSY PQQDGKSDGT ETSTNLHQKL CYHVLGTDQS EDILCAEFPD EPKWMGGAEL 240
SDDGRYVLLS IWEGCDPVNR LWYCDLQQEP NGITGILKWV KLIDNFEGEY DYVTNEGTVF 300
TFKTNRNSPN YRLINIDFTD PDESKWKVLV PEHEKDVLEW VACVRSNFLV LCYLHDVKNI 360
LQLHDLTTGA LLKTFPLDVG SVVGYSGRKK DSEIFYQFTS FLSPGVIYHC DLTKEELEPM 420
VFREVTVKGI DAADYQTIQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI 480
TPNYSVSRLI FVRHMGGVLA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE 540
GYTSPKRLTI NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKFT IGHAWTTDYG 600
CSDTKQHFEW LLKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV 660
GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNIEWIQ 710 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
 GO:0019538; P:protein metabolic process; ISS:MGI.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR002471; Pept_S9_AS.
 IPR023302; Pept_S9A_oligopept_N.
 IPR001375; Peptidase_S9.
 IPR002470; Peptidase_S9A.
 IPR004106; Peptidase_S9A_B_C_N. 
Pfam
 PF00326; Peptidase_S9
 PF02897; Peptidase_S9_N 
SMART
  
PROSITE
 PS00708; PRO_ENDOPEP_SER 
PRINTS
 PR00862; PROLIGOPTASE.