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Q03018

- ESP1_YEAST

UniProt

Q03018 - ESP1_YEAST

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Protein

Separin

Gene

ESP1

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 – 15311By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: SGD

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 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centerspindle pole body 1 Publication. Cytoplasm 1 Publication
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.

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
  3. spindle Source: SGD
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 peptidase C50 domain.Curated

Phylogenomic databases

eggNOGiCOG5155.
GeneTreeiENSGT00390000004990.
HOGENOMiHOG000065988.
InParanoidiQ03018.
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

        10         20         30         40         50
MMVKQEEPLN EISPNTPMTS KSYLLNDTLS KVHHSGQTRP LTSVLSGDAS
60 70 80 90 100
SNSIGILAMH NNIIRDFTKI ASNNIDLAIE DITTVDHSLN SIYSLLKSHH
110 120 130 140 150
MWGHINSTVK QHLMIIVKLI NNNALGLASS EIIFLFNETN LFQAHSLKNI
160 170 180 190 200
LLADFSTWND YYLSNLKILA LQIILKRKLV DEYLPHILEL FSHDKRYLLK
210 220 230 240 250
DPNLKAHALT KIVLSFFSVT TSCKVLFGLK FLQYIKQFKL PFKKFISNIT
260 270 280 290 300
VECFSKNLLH KNYLEMGPNK IYLNSFYLSY SMLYDGLDKI MLLDILSYEE
310 320 330 340 350
TTEVQRAIKS KKEFNEYCNM SENRLLWSCI SVDDLNVILE NATNFLQNKG
360 370 380 390 400
KHISATLKCL VCLWSTIRLE GLPKNKDILR QFDCTVIYIN SNIKSINDES
410 420 430 440 450
AAALLSELLG VLSEICIDYK EPKRLSNIIS VLFNASVLFK SHSFLLKTAN
460 470 480 490 500
LEISNVLISN DSKTSHRTIL KFEKFISSAQ SAQKKIEIFS CLFNVYCMLR
510 520 530 540 550
NDTLSFVFDF CQNAFIHCFT RLKITKFIEF SNSSEIMLSV LYGNSSIENI
560 570 580 590 600
PSENWSQLSR MIFCSLRGIF DLDPLELNNT FDKLHLLNKY ELLIRIVYLL
610 620 630 640 650
NLDMSKHLTT NLSKITKLYI NKWLQKSDEK AERISSFEMD FVKMLLCYLN
660 670 680 690 700
FNNFDKLSIE LSLCIKSKEK YYSSIVPYAD NYLLEAYLSL YMIDDALMMK
710 720 730 740 750
NQLQKTMNLS TAKIEQALLH ASSLINVHLW DSDLTAFQIY FGKTLPAMKP
760 770 780 790 800
ELFDINNDHN LPMSLYIKVI LLNIKIFNES AKLNIKAGNV ISAVIDCRKA
810 820 830 840 850
QNLALSLLKK KNKLSQGSRL ALLKSLSFSF FQLIKIHIRI GSARDCEFYS
860 870 880 890 900
KELSRIISDL EEPIIVYRCL HFLHRYYMIT EQTCLQNITL GKANKAFDYL
910 920 930 940 950
DAEADITSLT MFLYDNKEFV KLEQSLVLYF GDQLEKTFLP NLWKLHLGKD
960 970 980 990 1000
IDDSICLSEY MPKNVINRVH NMWQKVMSQL EEDPFFKGMF ESTLGIPSSL
1010 1020 1030 1040 1050
PVIPSTMPNN ILKTPSKHST GLKLCDSPRS SSMTPRGKNI RQKFDRIAAI
1060 1070 1080 1090 1100
SKLKQMKELL ESLKLDTLDN HELSKISSLS SLTLTILSNI TSIHNAESSL
1110 1120 1130 1140 1150
ITNFSLTDLP RHMPLLFDKV LNNIDNKNYR EFRVSSLIAP NNISTITESI
1160 1170 1180 1190 1200
RVSAAQKDLM ESNLNINVIT IDFCPITGNL LLSKLEPRRK RRTHLRLPLI
1210 1220 1230 1240 1250
RSNSRDLDEV HLSFPEATKK LLSIINESNQ TTSVEVTNKI KTREERKSWW
1260 1270 1280 1290 1300
TTRYDLDKRM QQLLNNIENS WFNGVQGFFS PEVVDNSLFE KFKDKFYEIL
1310 1320 1330 1340 1350
HQNLPSRKLY GNPAMFIKVE DWVIELFLKL NPQEIDFLSK MEDLIYFVLD
1360 1370 1380 1390 1400
ILLFHGEENA YDEIDFSMLH VQLEEQIKKY RATMTTNSIF HTFLVVSSSC
1410 1420 1430 1440 1450
HLFPWECLSF LKDLSITRVP SYVCLNKLLS RFHYQLPLQV TIEDNISMIL
1460 1470 1480 1490 1500
NPNGDLSRTE SKFKGMFQKI IDAKPSSQLV MNEKPEEETL LKMLQNSNLF
1510 1520 1530 1540 1550
VYIGHGGGEQ YVRSKEIKKC TKIAPSFLLG CSSAAMKYYG KLEPTGTIYT
1560 1570 1580 1590 1600
YLLGGCPMVL GNLWDVTDKD IDKFSEELFE KMGFRCNTDD LNGNSLSVSY
1610 1620 1630
AVSKSRGVCH LRYLNGAAPV IYGLPIKFVS
Length:1,630
Mass (Da):187,447
Last modified:October 1, 1996 - v2
Checksum:iFBAFD33FF706C6BA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361F → S in AAB03897. (PubMed:1493337)Curated
Sequence conflicti250 – 2534TVEC → IRRV in AAB03897. (PubMed:1493337)Curated
Sequence conflicti540 – 5401V → L in AAB03897. (PubMed:1493337)Curated
Sequence conflicti636 – 6361S → Y in AAB03897. (PubMed:1493337)Curated
Sequence conflicti782 – 7821K → E in AAB03897. (PubMed:1493337)Curated
Sequence conflicti800 – 8001A → E in AAB03897. (PubMed:1493337)Curated
Sequence conflicti1146 – 11461I → T in AAB03897. (PubMed:1493337)Curated
Sequence conflicti1295 – 12951K → R in AAB03897. (PubMed:1493337)Curated
Sequence conflicti1333 – 13364QEID → ARKSI in AAB03897. (PubMed:1493337)Curated
Sequence conflicti1443 – 14431E → Q in AAB03897. (PubMed:1493337)Curated

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.
InParanoidi Q03018.
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: October 29, 2014
This is version 125 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