CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007997
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
157WVTIKFMKVDGAKELacetylation[1]
162FMKVDGAKELPDVLEubiquitination[2, 3]
172PDVLERVKFSCMAWTubiquitination[2]
196SYPQQDGKSDGTETSubiquitination[2]
325FRDPEESKWKVLVPEubiquitination[2]
428VFREVTVKGIDASDYubiquitination[4]
516EYGETWHKGGILANKubiquitination[2, 5, 6]
523KGGILANKQNCFDDFubiquitination[2]
546KEGYTSPKRLTINGGubiquitination[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] 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]
 [5] 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]
 [6] 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
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.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Polymorphism; Protease; Reference proteome; Serine protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 710 AA 
Protein Sequence
MLSLQYPDVY RDETAVQDYH GHKICDPYAW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR 60
GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNILS 120
DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFSCMAWTH 180
DGKGMFYNSY PQQDGKSDGT ETSTNLHQKL YYHVLGTDQS EDILCAEFPD EPKWMGGAEL 240
SDDGRYVLLS IREGCDPVNR LWYCDLQQES SGIAGILKWV KLIDNFEGEY DYVTNEGTVF 300
TFKTNRQSPN YRVINIDFRD PEESKWKVLV PEHEKDVLEW IACVRSNFLV LCYLHDVKNI 360
LQLHDLTTGA LLKTFPLDVG SIVGYSGQKK DTEIFYQFTS FLSPGIIYHC DLTKEELEPR 420
VFREVTVKGI DASDYQTVQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI 480
TPNYSVSRLI FVRHMGGILA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE 540
GYTSPKRLTI NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKYT IGHAWTTDYG 600
CSDSKQHFEW LVKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV 660
GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNVDWIP 710 
Gene Ontology
 GO:0005737; C:cytoplasm; TAS:ProtInc.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
 GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; TAS:ProtInc. 
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.