CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011023
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Separin 
Protein Synonyms/Alias
 Separase 
Gene Name
 ESP1 
Gene Synonyms/Alias
 YGR098C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
617TNLSKITKLYINKWLacetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the MCD1/SCC1 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/PDS1 protein. It also promotes anaphase spindle elongation. A component of the FEAR (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Cleaves SLK19. 
Sequence Annotation
 ACT_SITE 1531 1531 By similarity.  
Keyword
 Calcium; Chromosome partition; Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1630 AA 
Protein Sequence
MMVKQEEPLN EISPNTPMTS KSYLLNDTLS KVHHSGQTRP LTSVLSGDAS SNSIGILAMH 60
NNIIRDFTKI ASNNIDLAIE DITTVDHSLN SIYSLLKSHH MWGHINSTVK QHLMIIVKLI 120
NNNALGLASS EIIFLFNETN LFQAHSLKNI LLADFSTWND YYLSNLKILA LQIILKRKLV 180
DEYLPHILEL FSHDKRYLLK DPNLKAHALT KIVLSFFSVT TSCKVLFGLK FLQYIKQFKL 240
PFKKFISNIT VECFSKNLLH KNYLEMGPNK IYLNSFYLSY SMLYDGLDKI MLLDILSYEE 300
TTEVQRAIKS KKEFNEYCNM SENRLLWSCI SVDDLNVILE NATNFLQNKG KHISATLKCL 360
VCLWSTIRLE GLPKNKDILR QFDCTVIYIN SNIKSINDES AAALLSELLG VLSEICIDYK 420
EPKRLSNIIS VLFNASVLFK SHSFLLKTAN LEISNVLISN DSKTSHRTIL KFEKFISSAQ 480
SAQKKIEIFS CLFNVYCMLR NDTLSFVFDF CQNAFIHCFT RLKITKFIEF SNSSEIMLSV 540
LYGNSSIENI PSENWSQLSR MIFCSLRGIF DLDPLELNNT FDKLHLLNKY ELLIRIVYLL 600
NLDMSKHLTT NLSKITKLYI NKWLQKSDEK AERISSFEMD FVKMLLCYLN FNNFDKLSIE 660
LSLCIKSKEK YYSSIVPYAD NYLLEAYLSL YMIDDALMMK NQLQKTMNLS TAKIEQALLH 720
ASSLINVHLW DSDLTAFQIY FGKTLPAMKP ELFDINNDHN LPMSLYIKVI LLNIKIFNES 780
AKLNIKAGNV ISAVIDCRKA QNLALSLLKK KNKLSQGSRL ALLKSLSFSF FQLIKIHIRI 840
GSARDCEFYS KELSRIISDL EEPIIVYRCL HFLHRYYMIT EQTCLQNITL GKANKAFDYL 900
DAEADITSLT MFLYDNKEFV KLEQSLVLYF GDQLEKTFLP NLWKLHLGKD IDDSICLSEY 960
MPKNVINRVH NMWQKVMSQL EEDPFFKGMF ESTLGIPSSL PVIPSTMPNN ILKTPSKHST 1020
GLKLCDSPRS SSMTPRGKNI RQKFDRIAAI SKLKQMKELL ESLKLDTLDN HELSKISSLS 1080
SLTLTILSNI TSIHNAESSL ITNFSLTDLP RHMPLLFDKV LNNIDNKNYR EFRVSSLIAP 1140
NNISTITESI RVSAAQKDLM ESNLNINVIT IDFCPITGNL LLSKLEPRRK RRTHLRLPLI 1200
RSNSRDLDEV HLSFPEATKK LLSIINESNQ TTSVEVTNKI KTREERKSWW TTRYDLDKRM 1260
QQLLNNIENS WFNGVQGFFS PEVVDNSLFE KFKDKFYEIL HQNLPSRKLY GNPAMFIKVE 1320
DWVIELFLKL NPQEIDFLSK MEDLIYFVLD ILLFHGEENA YDEIDFSMLH VQLEEQIKKY 1380
RATMTTNSIF HTFLVVSSSC HLFPWECLSF LKDLSITRVP SYVCLNKLLS RFHYQLPLQV 1440
TIEDNISMIL NPNGDLSRTE SKFKGMFQKI IDAKPSSQLV MNEKPEEETL LKMLQNSNLF 1500
VYIGHGGGEQ YVRSKEIKKC TKIAPSFLLG CSSAAMKYYG KLEPTGTIYT YLLGGCPMVL 1560
GNLWDVTDKD IDKFSEELFE KMGFRCNTDD LNGNSLSVSY AVSKSRGVCH LRYLNGAAPV 1620
IYGLPIKFVS 1630 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005819; C:spindle; IDA:SGD.
 GO:0005816; C:spindle pole body; IEA:UniProtKB-SubCell.
 GO:0004197; F:cysteine-type endopeptidase activity; IDA:SGD.
 GO:0006915; P:apoptotic process; IMP:SGD.
 GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
 GO:0034048; P:negative regulation of protein phosphatase type 2A activity; IMP:SGD.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0007096; P:regulation of exit from mitosis; IGI:SGD.
 GO:0032888; P:regulation of mitotic spindle elongation; IMP:SGD. 
Interpro
 IPR005314; Peptidase_C50. 
Pfam
 PF03568; Peptidase_C50 
SMART
  
PROSITE
  
PRINTS