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Q03018

- ESP1_YEAST

UniProt

Q03018 - ESP1_YEAST

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Protein

Separin

Gene
ESP1, YGR098C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 SLK19.4 Publications

Catalytic activityi

All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.

Enzyme regulationi

It is inactivated via its interaction with PDS1, which probably covers its active site. PDS1 degradation at anaphase, liberates it and triggers MCD1 cleavage.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1531 – 15311 By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: SGD
  2. protein binding Source: IntAct

GO - Biological processi

  1. apoptotic process Source: SGD
  2. mitotic sister chromatid segregation Source: SGD
  3. negative regulation of protein phosphatase type 2A activity Source: SGD
  4. regulation of exit from mitosis Source: SGD
  5. regulation of mitotic spindle elongation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Chromosome partition

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciYEAST:G3O-30808-MONOMER.
ReactomeiREACT_188906. Separation of Sister Chromatids.

Protein family/group databases

MEROPSiC50.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Separin (EC:3.4.22.49)
Alternative name(s):
Separase
Gene namesi
Name:ESP1
Ordered Locus Names:YGR098C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR098c.
SGDiS000003330. ESP1.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centerspindle pole body. Cytoplasm
Note: Accumulates in the nucleus in G2 and is mobilized onto the spindle pole bodies and spindle midzone at anaphase onset, where it persists into midanaphase. The association with MCD1 may be important for its nuclear targeting.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
  3. spindle Source: SGD
  4. spindle pole body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1568 – 15703DKD → AKA: Reduces function. Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16301630SeparinPRO_0000205904Add
BLAST

Proteomic databases

MaxQBiQ03018.
PaxDbiQ03018.

Expressioni

Gene expression databases

GenevestigatoriQ03018.

Interactioni

Subunit structurei

May bind calcium. Interacts with PDS1. Interacts with MCD1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC55Q003622EBI-6657,EBI-1942

Protein-protein interaction databases

BioGridi33341. 35 interactions.
DIPiDIP-2933N.
IntActiQ03018. 7 interactions.
MINTiMINT-614508.
STRINGi4932.YGR098C.

Structurei

3D structure databases

ProteinModelPortaliQ03018.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1443 – 1542100Peptidase C50Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5155.
GeneTreeiENSGT00390000004990.
HOGENOMiHOG000065988.
KOiK02365.
OMAiFDILLFH.
OrthoDBiEOG7V76G0.

Family and domain databases

InterProiIPR005314. Peptidase_C50.
[Graphical view]
PANTHERiPTHR12792. PTHR12792. 1 hit.
PfamiPF03568. Peptidase_C50. 1 hit.
[Graphical view]
PROSITEiPS51700. SEPARIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03018-1 [UniParc]FASTAAdd to Basket

« Hide

MMVKQEEPLN EISPNTPMTS KSYLLNDTLS KVHHSGQTRP LTSVLSGDAS     50
SNSIGILAMH NNIIRDFTKI ASNNIDLAIE DITTVDHSLN SIYSLLKSHH 100
MWGHINSTVK QHLMIIVKLI NNNALGLASS EIIFLFNETN LFQAHSLKNI 150
LLADFSTWND YYLSNLKILA LQIILKRKLV DEYLPHILEL FSHDKRYLLK 200
DPNLKAHALT KIVLSFFSVT TSCKVLFGLK FLQYIKQFKL PFKKFISNIT 250
VECFSKNLLH KNYLEMGPNK IYLNSFYLSY SMLYDGLDKI MLLDILSYEE 300
TTEVQRAIKS KKEFNEYCNM SENRLLWSCI SVDDLNVILE NATNFLQNKG 350
KHISATLKCL VCLWSTIRLE GLPKNKDILR QFDCTVIYIN SNIKSINDES 400
AAALLSELLG VLSEICIDYK EPKRLSNIIS VLFNASVLFK SHSFLLKTAN 450
LEISNVLISN DSKTSHRTIL KFEKFISSAQ SAQKKIEIFS CLFNVYCMLR 500
NDTLSFVFDF CQNAFIHCFT RLKITKFIEF SNSSEIMLSV LYGNSSIENI 550
PSENWSQLSR MIFCSLRGIF DLDPLELNNT FDKLHLLNKY ELLIRIVYLL 600
NLDMSKHLTT NLSKITKLYI NKWLQKSDEK AERISSFEMD FVKMLLCYLN 650
FNNFDKLSIE LSLCIKSKEK YYSSIVPYAD NYLLEAYLSL YMIDDALMMK 700
NQLQKTMNLS TAKIEQALLH ASSLINVHLW DSDLTAFQIY FGKTLPAMKP 750
ELFDINNDHN LPMSLYIKVI LLNIKIFNES AKLNIKAGNV ISAVIDCRKA 800
QNLALSLLKK KNKLSQGSRL ALLKSLSFSF FQLIKIHIRI GSARDCEFYS 850
KELSRIISDL EEPIIVYRCL HFLHRYYMIT EQTCLQNITL GKANKAFDYL 900
DAEADITSLT MFLYDNKEFV KLEQSLVLYF GDQLEKTFLP NLWKLHLGKD 950
IDDSICLSEY MPKNVINRVH NMWQKVMSQL EEDPFFKGMF ESTLGIPSSL 1000
PVIPSTMPNN ILKTPSKHST GLKLCDSPRS SSMTPRGKNI RQKFDRIAAI 1050
SKLKQMKELL ESLKLDTLDN HELSKISSLS SLTLTILSNI TSIHNAESSL 1100
ITNFSLTDLP RHMPLLFDKV LNNIDNKNYR EFRVSSLIAP NNISTITESI 1150
RVSAAQKDLM ESNLNINVIT IDFCPITGNL LLSKLEPRRK RRTHLRLPLI 1200
RSNSRDLDEV HLSFPEATKK LLSIINESNQ TTSVEVTNKI KTREERKSWW 1250
TTRYDLDKRM QQLLNNIENS WFNGVQGFFS PEVVDNSLFE KFKDKFYEIL 1300
HQNLPSRKLY GNPAMFIKVE DWVIELFLKL NPQEIDFLSK MEDLIYFVLD 1350
ILLFHGEENA YDEIDFSMLH VQLEEQIKKY RATMTTNSIF HTFLVVSSSC 1400
HLFPWECLSF LKDLSITRVP SYVCLNKLLS RFHYQLPLQV TIEDNISMIL 1450
NPNGDLSRTE SKFKGMFQKI IDAKPSSQLV MNEKPEEETL LKMLQNSNLF 1500
VYIGHGGGEQ YVRSKEIKKC TKIAPSFLLG CSSAAMKYYG KLEPTGTIYT 1550
YLLGGCPMVL GNLWDVTDKD IDKFSEELFE KMGFRCNTDD LNGNSLSVSY 1600
AVSKSRGVCH LRYLNGAAPV IYGLPIKFVS 1630
Length:1,630
Mass (Da):187,447
Last modified:October 1, 1996 - v2
Checksum:iFBAFD33FF706C6BA
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361F → S in AAB03897. 1 Publication
Sequence conflicti250 – 2534TVEC → IRRV in AAB03897. 1 Publication
Sequence conflicti540 – 5401V → L in AAB03897. 1 Publication
Sequence conflicti636 – 6361S → Y in AAB03897. 1 Publication
Sequence conflicti782 – 7821K → E in AAB03897. 1 Publication
Sequence conflicti800 – 8001A → E in AAB03897. 1 Publication
Sequence conflicti1146 – 11461I → T in AAB03897. 1 Publication
Sequence conflicti1295 – 12951K → R in AAB03897. 1 Publication
Sequence conflicti1333 – 13364QEID → ARKSI in AAB03897. 1 Publication
Sequence conflicti1443 – 14431E → Q in AAB03897. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07289 Genomic DNA. Translation: AAB03897.1.
Z72883 Genomic DNA. Translation: CAA97101.1.
BK006941 Genomic DNA. Translation: DAA08191.1.
PIRiS64403.
RefSeqiNP_011612.3. NM_001181227.3.

Genome annotation databases

EnsemblFungiiYGR098C; YGR098C; YGR098C.
GeneIDi852990.
KEGGisce:YGR098C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07289 Genomic DNA. Translation: AAB03897.1 .
Z72883 Genomic DNA. Translation: CAA97101.1 .
BK006941 Genomic DNA. Translation: DAA08191.1 .
PIRi S64403.
RefSeqi NP_011612.3. NM_001181227.3.

3D structure databases

ProteinModelPortali Q03018.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33341. 35 interactions.
DIPi DIP-2933N.
IntActi Q03018. 7 interactions.
MINTi MINT-614508.
STRINGi 4932.YGR098C.

Protein family/group databases

MEROPSi C50.001.

Proteomic databases

MaxQBi Q03018.
PaxDbi Q03018.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR098C ; YGR098C ; YGR098C .
GeneIDi 852990.
KEGGi sce:YGR098C.

Organism-specific databases

CYGDi YGR098c.
SGDi S000003330. ESP1.

Phylogenomic databases

eggNOGi COG5155.
GeneTreei ENSGT00390000004990.
HOGENOMi HOG000065988.
KOi K02365.
OMAi FDILLFH.
OrthoDBi EOG7V76G0.

Enzyme and pathway databases

BioCyci YEAST:G3O-30808-MONOMER.
Reactomei REACT_188906. Separation of Sister Chromatids.

Miscellaneous databases

NextBioi 972815.
PROi Q03018.

Gene expression databases

Genevestigatori Q03018.

Family and domain databases

InterProi IPR005314. Peptidase_C50.
[Graphical view ]
PANTHERi PTHR12792. PTHR12792. 1 hit.
Pfami PF03568. Peptidase_C50. 1 hit.
[Graphical view ]
PROSITEi PS51700. SEPARIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Requirement for ESP1 in the nuclear division of Saccharomyces cerevisiae."
    McGrew J.T., Goetsch L., Byers B.E., Baum P.
    Mol. Biol. Cell 3:1443-1454(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 59-1630.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast."
    Ciosk R., Zachariae W., Michaelis C., Shevchenko A., Mann M., Nasmyth K.
    Cell 93:1067-1076(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PDS1.
  5. "Sister-chromatid separation at anaphase onset is promoted by cleavage of the cohesin subunit Scc1."
    Uhlmann F., Lottspeich F., Nasmyth K.
    Nature 400:37-42(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF MCD1, FUNCTION.
  6. "A novel role of the budding yeast separin Esp1 in anaphase spindle elongation: evidence that proper spindle association of Esp1 is regulated by Pds1."
    Jensen S., Segal M., Clarke D.J., Reed S.I.
    J. Cell Biol. 152:27-40(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 1568-ASP--ASP-1570.
  7. "Separase, polo kinase, the kinetochore protein Slk19, and Spo12 function in a network that controls Cdc14 localization during early anaphase."
    Stegmeier F., Visintin R., Amon A.
    Cell 108:207-220(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A COMPONENT OF THE FEAR NETWORK.

Entry informationi

Entry nameiESP1_YEAST
AccessioniPrimary (citable) accession number: Q03018
Secondary accession number(s): D6VUN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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