CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012361
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Separin 
Protein Synonyms/Alias
 Caspase-like protein ESPL1; Extra spindle poles-like 1 protein; Separase 
Gene Name
 ESPL1 
Gene Synonyms/Alias
 ESP1; KIAA0165 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27EELLPALKEFLSNPPubiquitination[1]
64CNQQLTAKLACPRHLubiquitination[2, 3, 4]
277KAISAVEKAHSYLRNubiquitination[4]
299QLCQLGVKLLQVGEEubiquitination[4]
313EGPQAVAKLLIKASAubiquitination[4]
324KASAVLSKSMEAPSPubiquitination[4]
515RLQVESLKKLGKQAQubiquitination[4]
562DAARAGDKELQLKTLubiquitination[4]
567GDKELQLKTLRDSLSubiquitination[4]
593REELQAYKAVRADTGubiquitination[1, 4, 5, 6]
722NDLNYEDKLQEDRFLubiquitination[1, 5]
755DQALALWKELLTKGQubiquitination[4]
760LWKELLTKGQAPAVRubiquitination[1, 4, 5, 6]
1008LGSVSEAKAFCLEALubiquitination[4, 5, 6]
1016AFCLEALKLTTKLQIubiquitination[4]
1020EALKLTTKLQIPRQCubiquitination[4]
1083KVHLQKGKQQAQVPCubiquitination[4]
1189DLLQVVLKGCPEAAEubiquitination[4]
1252KVLQSGLKFVAARIPubiquitination[4]
1322RSGRGRQKLASAPLRubiquitination[4]
1336RLNNTSQKGLEGRGLubiquitination[4]
1692GHFPQPEKESFQERLubiquitination[4, 6]
1732LLLTRLEKDSPPVSVubiquitination[1, 4]
1747QIPTGQNKLHLRSVLubiquitination[4]
1762NEFDAIQKAQKENSSubiquitination[4]
1796VLIASLEKSVLGCWKubiquitination[4]
1803KSVLGCWKGLLLPSSubiquitination[4, 5, 6]
1832LLQDCGWKYPDRTLLubiquitination[4, 5, 6]
1901VLDKDLQKLPWESMPubiquitination[1]
1994QVQEALTKHDLYIYAubiquitination[4, 6]
2103ARQAPRLKYLIGAAPubiquitination[4]
Reference
 [1] 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]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] 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]
 [5] 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]
 [6] 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
 Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the SCC1/RAD21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by different mechanisms. 
Sequence Annotation
 ACT_SITE 2029 2029
 MOD_RES 1126 1126 Phosphoserine.
 MOD_RES 1396 1396 Phosphoserine.
 MOD_RES 1399 1399 Phosphoserine.
 MOD_RES 1508 1508 Phosphoserine.  
Keyword
 Alternative splicing; Autocatalytic cleavage; Chromosome partition; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protease; Reference proteome; Thiol protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2120 AA 
Protein Sequence
MRSFKRVNFG TLLSSQKEAE ELLPALKEFL SNPPAGFPSS RSDAERRQAC DAILRACNQQ 60
LTAKLACPRH LGSLLELAEL ACDGYLVSTP QRPPLYLERI LFVLLRNAAA QGSPEATLRL 120
AQPLHACLVQ CSREAAPQDY EAVARGSFSL LWKGAEALLE RRAAFAARLK ALSFLVLLED 180
ESTPCEVPHF ASPTACRAVA AHQLFDASGH GLNEADADFL DDLLSRHVIR ALVGERGSSS 240
GLLSPQRALC LLELTLEHCR RFCWSRHHDK AISAVEKAHS YLRNTNLAPS LQLCQLGVKL 300
LQVGEEGPQA VAKLLIKASA VLSKSMEAPS PPLRALYESC QFFLSGLERG TKRRYRLDAI 360
LSLFAFLGGY CSLLQQLRDD GVYGGSSKQQ QSFLQMYFQG LHLYTVVVYD FAQGCQIVDL 420
ADLTQLVDSC KSTVVWMLEA LEGLSGQELT DHMGMTASYT SNLAYSFYSH KLYAEACAIS 480
EPLCQHLGLV KPGTYPEVPP EKLHRCFRLQ VESLKKLGKQ AQGCKMVILW LAALQPCSPE 540
HMAEPVTFWV RVKMDAARAG DKELQLKTLR DSLSGWDPET LALLLREELQ AYKAVRADTG 600
QERFNIICDL LELSPEETPA GAWARATHLV ELAQVLCYHD FTQQTNCSAL DAIREALQLL 660
DSVRPEAQAR DQLLDDKAQA LLWLYICTLE AKMQEGIERD RRAQAPGNLE EFEVNDLNYE 720
DKLQEDRFLY SNIAFNLAAD AAQSKCLDQA LALWKELLTK GQAPAVRCLQ QTAASLQILA 780
ALYQLVAKPM QALEVLLLLR IVSERLKDHS KAAGSSCHIT QLLLTLGCPS YAQLHLEEAA 840
SSLKHLDQTT DTYLLLSLTC DLLRSQLYWT HQKVTKGVSL LLSVLRDPAL QKSSKAWYLL 900
RVQVLQLVAA YLSLPSNNLS HSLWEQLCAQ GWQTPEIALI DSHKLLRSII LLLMGSDILS 960
TQKAAVETSF LDYGENLVQK WQVLSEVLSC SEKLVCHLGR LGSVSEAKAF CLEALKLTTK 1020
LQIPRQCALF LVLKGELELA RNDIDLCQSD LQQVLFLLES CTEFGGVTQH LDSVKKVHLQ 1080
KGKQQAQVPC PPQLPEEELF LRGPALELVA TVAKEPGPIA PSTNSSPVLK TKPQPIPNFL 1140
SHSPTCDCSL CASPVLTAVC LRWVLVTAGV RLAMGHQAQG LDLLQVVLKG CPEAAERLTQ 1200
ALQASLNHKT PPSLVPSLLD EILAQAYTLL ALEGLNQPSN ESLQKVLQSG LKFVAARIPH 1260
LEPWRASLLL IWALTKLGGL SCCTTQLFAS SWGWQPPLIK SVPGSEPSKT QGQKRSGRGR 1320
QKLASAPLRL NNTSQKGLEG RGLPCTPKPP DRIRQAGPHV PFTVFEEVCP TESKPEVPQA 1380
PRVQQRVQTR LKVNFSDDSD LEDPVSAEAW LAEEPKRRGT ASRGRGRARK GLSLKTDAVV 1440
APGSAPGNPG LNGRSRRAKK VASRHCEERR PQRASDQARP GPEIMRTIPE EELTDNWRKM 1500
SFEILRGSDG EDSASGGKTP APGPEAASGE WELLRLDSSK KKLPSPCPDK ESDKDLGPRL 1560
RLPSAPVATG LSTLDSICDS LSVAFRGISH CPPSGLYAHL CRFLALCLGH RDPYATAFLV 1620
TESVSITCRH QLLTHLHRQL SKAQKHRGSL EIADQLQGLS LQEMPGDVPL ARIQRLFSFR 1680
ALESGHFPQP EKESFQERLA LIPSGVTVCV LALATLQPGT VGNTLLLTRL EKDSPPVSVQ 1740
IPTGQNKLHL RSVLNEFDAI QKAQKENSSC TDKREWWTGR LALDHRMEVL IASLEKSVLG 1800
CWKGLLLPSS EEPGPAQEAS RLQELLQDCG WKYPDRTLLK IMLSGAGALT PQDIQALAYG 1860
LCPTQPERAQ ELLNEAVGRL QGLTVPSNSH LVLVLDKDLQ KLPWESMPSL QALPVTRLPS 1920
FRFLLSYSII KEYGASPVLS QGVDPRSTFY VLNPHNNLSS TEEQFRANFS SEAGWRGVVG 1980
EVPRPEQVQE ALTKHDLYIY AGHGAGARFL DGQAVLRLSC RAVALLFGCS SAALAVRGNL 2040
EGAGIVLKYI MAGCPLFLGN LWDVTDRDID RYTEALLQGW LGAGPGAPLL YYVNQARQAP 2100
RLKYLIGAAP IAYGLPVSLR 2120 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008234; F:cysteine-type peptidase activity; NAS:UniProtKB.
 GO:0006915; P:apoptotic process; TAS:UniProtKB.
 GO:0000910; P:cytokinesis; NAS:UniProtKB.
 GO:0040001; P:establishment of mitotic spindle localization; NAS:UniProtKB.
 GO:0045143; P:homologous chromosome segregation; IEA:Compara.
 GO:0000212; P:meiotic spindle organization; IEA:Compara.
 GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
 GO:0045875; P:negative regulation of sister chromatid cohesion; NAS:UniProtKB.
 GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; NAS:UniProtKB.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 
Interpro
 IPR005314; Peptidase_C50. 
Pfam
 PF03568; Peptidase_C50 
SMART
  
PROSITE
  
PRINTS