Basic Information

NameSeparin (EC 3.4.22.49) (Separase)
Uniprot IDQ03018
Systematic gene nameYGR098C
Standard gene nameESP1
Gene namesESP1 YGR098C
Description from SGDYGR098C ESP1 SGDID:S000003330, Chr VII from 687458-682566, Genome Release 64-3-1, reverse complement, Verified ORF, "Separase/separin, a caspase-like cysteine protease; cleaves Mcd1p/Scc1p, a mitotic cohesin complex subunit, resulting in the dissociation of cohesin from chromatin and sister chromatid separation; cleaves meiotic-cohesin subunit Rec8p along chromosome arms in meiosis I and at centromeric sites during meiosis II; inhibits PP2A-Cdc55p to promote mitotic exit; inhibited by Pds1p (securin); relative distribution to the nucleus increases upon DNA replication stress"
Protein length1630
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MMVKQEEPLN EISPNTPMTS KSYLLNDTLS KVHHSGQTRP LTSVLSGDAS
SNSIGILAMH NNIIRDFTKI ASNNIDLAIE DITTVDHSLN SIYSLLKSHH
MWGHINSTVK QHLMIIVKLI NNNALGLASS EIIFLFNETN LFQAHSLKNI
LLADFSTWND YYLSNLKILA LQIILKRKLV DEYLPHILEL FSHDKRYLLK
DPNLKAHALT KIVLSFFSVT TSCKVLFGLK FLQYIKQFKL PFKKFISNIT
VECFSKNLLH KNYLEMGPNK IYLNSFYLSY SMLYDGLDKI MLLDILSYEE
TTEVQRAIKS KKEFNEYCNM SENRLLWSCI SVDDLNVILE NATNFLQNKG
KHISATLKCL VCLWSTIRLE GLPKNKDILR QFDCTVIYIN SNIKSINDES
AAALLSELLG VLSEICIDYK EPKRLSNIIS VLFNASVLFK SHSFLLKTAN
LEISNVLISN DSKTSHRTIL KFEKFISSAQ SAQKKIEIFS CLFNVYCMLR
NDTLSFVFDF CQNAFIHCFT RLKITKFIEF SNSSEIMLSV LYGNSSIENI
PSENWSQLSR MIFCSLRGIF DLDPLELNNT FDKLHLLNKY ELLIRIVYLL
NLDMSKHLTT NLSKITKLYI NKWLQKSDEK AERISSFEMD FVKMLLCYLN
FNNFDKLSIE LSLCIKSKEK YYSSIVPYAD NYLLEAYLSL YMIDDALMMK
NQLQKTMNLS TAKIEQALLH ASSLINVHLW DSDLTAFQIY FGKTLPAMKP
ELFDINNDHN LPMSLYIKVI LLNIKIFNES AKLNIKAGNV ISAVIDCRKA
QNLALSLLKK KNKLSQGSRL ALLKSLSFSF FQLIKIHIRI GSARDCEFYS
KELSRIISDL EEPIIVYRCL HFLHRYYMIT EQTCLQNITL GKANKAFDYL
DAEADITSLT MFLYDNKEFV KLEQSLVLYF GDQLEKTFLP NLWKLHLGKD
IDDSICLSEY MPKNVINRVH NMWQKVMSQL EEDPFFKGMF ESTLGIPSSL
PVIPSTMPNN ILKTPSKHST GLKLCDSPRS SSMTPRGKNI RQKFDRIAAI
SKLKQMKELL ESLKLDTLDN HELSKISSLS SLTLTILSNI TSIHNAESSL
ITNFSLTDLP RHMPLLFDKV LNNIDNKNYR EFRVSSLIAP NNISTITESI
RVSAAQKDLM ESNLNINVIT IDFCPITGNL LLSKLEPRRK RRTHLRLPLI
RSNSRDLDEV HLSFPEATKK LLSIINESNQ TTSVEVTNKI KTREERKSWW
TTRYDLDKRM QQLLNNIENS WFNGVQGFFS PEVVDNSLFE KFKDKFYEIL
HQNLPSRKLY GNPAMFIKVE DWVIELFLKL NPQEIDFLSK MEDLIYFVLD
ILLFHGEENA YDEIDFSMLH VQLEEQIKKY RATMTTNSIF HTFLVVSSSC
HLFPWECLSF LKDLSITRVP SYVCLNKLLS RFHYQLPLQV TIEDNISMIL
NPNGDLSRTE SKFKGMFQKI IDAKPSSQLV MNEKPEEETL LKMLQNSNLF
VYIGHGGGEQ YVRSKEIKKC TKIAPSFLLG CSSAAMKYYG KLEPTGTIYT
YLLGGCPMVL GNLWDVTDKD IDKFSEELFE KMGFRCNTDD LNGNSLSVSY
AVSKSRGVCH LRYLNGAAPV IYGLPIKFVS

Legend

  • X Phoshorylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


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References

[13, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[16, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[490, Phos]Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications)
[490, Phos]Holt, L.J.,  Tuch, B.B.,  Villén, J.,  Johnson, A.D.,  Gygi, S.P.,  Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications)
[490, Phos]Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications)
[1027, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[1027, Phos]MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications)
[1032, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[1034, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[1091, Phos]Jones, M.H., Keck, J.M., Wong, C.C., Xu, T., Yates, J.R., Winey, M. (2011). Cell cycle phosphorylation of mitotic exit network (MEN) proteins. Cell Cycle 10: 3435-3440. (Publication) (All modifications)
[1092, Phos]Jones, M.H., Keck, J.M., Wong, C.C., Xu, T., Yates, J.R., Winey, M. (2011). Cell cycle phosphorylation of mitotic exit network (MEN) proteins. Cell Cycle 10: 3435-3440. (Publication) (All modifications)
[1204, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)