CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013291
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Prolyl endopeptidase-like 
Protein Synonyms/Alias
 Prolylendopeptidase-like 
Gene Name
 PREPL 
Gene Synonyms/Alias
 KIAA0436 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
95ENMDAFEKVRTKLETubiquitination[1, 2]
152LFNLEELKLDQPFIDubiquitination[3]
173DEKYVAAKIRTEDSEubiquitination[2]
426TYKFAEGKLFEETGHubiquitination[4, 5, 6]
439GHEDPITKTSRVLRLubiquitination[4, 5, 6, 7]
661VSYTEKLKEAIAEHAubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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]
 [4] 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]
 [5] 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]
 [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]
 [7] 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
Functional Description
 Probable serine peptidase whose precise substrate specificity remains unclear. Does not cleave peptides after a arginine or lysine residue. 
Sequence Annotation
 ACT_SITE 559 559 Charge relay system (By similarity).
 ACT_SITE 645 645 Charge relay system (By similarity).
 ACT_SITE 690 690 Charge relay system.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Hydrolase; Protease; Reference proteome; Serine protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 727 AA 
Protein Sequence
MQQKTKLFLQ ALKYSIPHLG KCMQKQHLNH YNFADHCYNR IKLKKYHLTK CLQNKPKISE 60
LARNIPSRSF SCKDLQPVKQ ENEKPLPENM DAFEKVRTKL ETQPQEEYEI INVEVKHGGF 120
VYYQEGCCLV RSKDEEADND NYEVLFNLEE LKLDQPFIDC IRVAPDEKYV AAKIRTEDSE 180
ASTCVIIKLS DQPVMEASFP NVSSFEWVKD EEDEDVLFYT FQRNLRCHDV YRATFGDNKR 240
NERFYTEKDP SYFVFLYLTK DSRFLTINIM NKTTSEVWLI DGLSPWDPPV LIQKRIHGVL 300
YYVEHRDDEL YILTNVGEPT EFKLMRTAAD TPAIMNWDLF FTMKRNTKVI DLDMFKDHCV 360
LFLKHSNLLY VNVIGLADDS VRSLKLPPWA CGFIMDTNSD PKNCPFQLCS PIRPPKYYTY 420
KFAEGKLFEE TGHEDPITKT SRVLRLEAKS KDGKLVPMTV FHKTDSEDLQ KKPLLVHVYG 480
AYGMDLKMNF RPERRVLVDD GWILAYCHVR GGGELGLQWH ADGRLTKKLN GLADLEACIK 540
TLHGQGFSQP SLTTLTAFSA GGVLAGALCN SNPELVRAVT LEAPFLDVLN TMMDTTLPLT 600
LEELEEWGNP SSDEKHKNYI KRYCPYQNIK PQHYPSIHIT AYENDERVPL KGIVSYTEKL 660
KEAIAEHAKD TGEGYQTPNI ILDIQPGGNH VIEDSHKKIT AQIKFLYEEL GLDSTSVFED 720
LKKYLKF 727 
Gene Ontology
 GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
 GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 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.