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P40316

- SECU_YEAST

UniProt

P40316 - SECU_YEAST

Protein

Securin

Gene

PDS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Regulatory protein, which plays a central role in chromosome stability. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESP1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESP1.1 Publication

    GO - Molecular functioni

    1. enzyme binding Source: SGD

    GO - Biological processi

    1. meiosis I Source: SGD
    2. mitotic sister chromatid segregation Source: SGD
    3. protein localization Source: SGD
    4. recombinational repair Source: SGD

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Mitosis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29713-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Securin
    Gene namesi
    Name:PDS1
    Ordered Locus Names:YDR113C
    ORF Names:YD9727.08C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR113c.
    SGDiS000002520. PDS1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 884RLPL → ALPA: Abolishes ubiquitination and subsequent degradation. 1 Publication
    Mutagenesisi277 – 2771S → A: Affects phosphorylation and the interaction with ESP1. 2 Publications
    Mutagenesisi292 – 2921S → A: Affects phosphorylation and the interaction with ESP1. 2 Publications
    Mutagenesisi304 – 3041T → A: No effect. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 373373SecurinPRO_0000206366Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei185 – 1851Phosphoserine2 Publications
    Modified residuei186 – 1861Phosphoserine2 Publications
    Modified residuei212 – 2121Phosphoserine2 Publications
    Modified residuei213 – 2131Phosphoserine2 Publications
    Modified residuei277 – 2771Phosphoserine2 Publications
    Modified residuei292 – 2921Phosphoserine; by CDC281 Publication

    Post-translational modificationi

    Phosphorylated by CDC28. The phosphorylation may be important for ESP1 localization to the nucleus.3 Publications
    Ubiquitinated by the anaphase promoting complex (APC) at the onset of anaphase, conducting to its degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP40316.
    PaxDbiP40316.

    Expressioni

    Gene expression databases

    GenevestigatoriP40316.

    Interactioni

    Subunit structurei

    Interacts with the caspase-like ESP1, and prevents its protease activity probably by covering its active site. Interacts with CDC20.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NUP84P528911EBI-16908,EBI-12337
    SRP1Q028211EBI-16908,EBI-1797

    Protein-protein interaction databases

    BioGridi32170. 119 interactions.
    DIPiDIP-2798N.
    IntActiP40316. 7 interactions.
    MINTiMINT-551568.
    STRINGi4932.YDR113C.

    Structurei

    3D structure databases

    DisProtiDP00256.
    ProteinModelPortaliP40316.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi85 – 884D-box

    Domaini

    The N-terminal destruction box (D-box) acts as a recognition signal for degradation via the ubiquitin-proteasome pathway.By similarity

    Sequence similaritiesi

    Belongs to the securin family.Curated

    Phylogenomic databases

    eggNOGiNOG39016.
    HOGENOMiHOG000154282.
    KOiK02627.
    OMAiDCESANE.
    OrthoDBiEOG7ZGXG5.

    Family and domain databases

    InterProiIPR006940. Securin_separation_inhibitor.
    [Graphical view]
    PfamiPF04856. Securin. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P40316-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMPANEDKEN NIVYTGNESS GINFPQTPAH LLKRSHSNIL KPPVRLDQLK    50
    RDANSNNGNT LKYIQGGKEV SPTKRLHTHA QQQGRLPLAA KDNNRSKSFI 100
    FPETSNQSKD ADLPQLQNTL SIRKNDQLRK LSQISRSRSR ANHNDLLSNS 150
    RKLQKYGSVL GYNALPKMKS LVLKDLADSG KNEESSDDDE GNEDSESKLG 200
    KKLQSALLKQ DSSDGENELN GGLGLFNEQG GLQQLIKNST KNEQKTKNDK 250
    SDKTDDYDIE IAPQRQEPLP YVPEGYSPFQ QDDIEKLKTF NSPYKLDLED 300
    EDDTPDKVDL LPLEQIDEEG EKDETECITR NQEEGAALPL LSKNFKEVAA 350
    VPTMELVYSE EGLDPEELED LVT 373
    Length:373
    Mass (Da):41,838
    Last modified:February 1, 1995 - v1
    Checksum:i7B31777C539433F4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12185 Genomic DNA. Translation: AAB00106.1.
    Z48758 Genomic DNA. Translation: CAA88666.1.
    AY558573 Genomic DNA. Translation: AAS56899.1.
    BK006938 Genomic DNA. Translation: DAA11958.1.
    PIRiS47911.
    RefSeqiNP_010398.3. NM_001180421.3.

    Genome annotation databases

    EnsemblFungiiYDR113C; YDR113C; YDR113C.
    GeneIDi851691.
    KEGGisce:YDR113C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12185 Genomic DNA. Translation: AAB00106.1 .
    Z48758 Genomic DNA. Translation: CAA88666.1 .
    AY558573 Genomic DNA. Translation: AAS56899.1 .
    BK006938 Genomic DNA. Translation: DAA11958.1 .
    PIRi S47911.
    RefSeqi NP_010398.3. NM_001180421.3.

    3D structure databases

    DisProti DP00256.
    ProteinModelPortali P40316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32170. 119 interactions.
    DIPi DIP-2798N.
    IntActi P40316. 7 interactions.
    MINTi MINT-551568.
    STRINGi 4932.YDR113C.

    Proteomic databases

    MaxQBi P40316.
    PaxDbi P40316.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR113C ; YDR113C ; YDR113C .
    GeneIDi 851691.
    KEGGi sce:YDR113C.

    Organism-specific databases

    CYGDi YDR113c.
    SGDi S000002520. PDS1.

    Phylogenomic databases

    eggNOGi NOG39016.
    HOGENOMi HOG000154282.
    KOi K02627.
    OMAi DCESANE.
    OrthoDBi EOG7ZGXG5.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29713-MONOMER.

    Miscellaneous databases

    NextBioi 969344.

    Gene expression databases

    Genevestigatori P40316.

    Family and domain databases

    InterProi IPR006940. Securin_separation_inhibitor.
    [Graphical view ]
    Pfami PF04856. Securin. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Pds1p, an inhibitor of anaphase in budding yeast, plays a critical role in the APC and checkpoint pathway(s)."
      Yamamoto A., Guacci V., Koshland D.
      J. Cell Biol. 133:99-110(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204626 / S288c / A364A.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p."
      Cohen-Fix O., Peters J.M., Kirschner M.W., Koshland D.
      Genes Dev. 10:3081-3093(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, MUTAGENESIS OF 85-ARG--LEU-88.
    6. "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 ESP1.
    7. "The anaphase inhibitor Pds1 binds to the APC/C-associated protein Cdc20 in a destruction box-dependent manner."
      Hilioti Z., Chung Y.-S., Mochizuki Y., Hardy C.F.J., Cohen-Fix O.
      Curr. Biol. 11:1347-1352(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDC20.
    8. "Phosphorylation of the mitotic regulator Pds1/securin by Cdc28 is required for efficient nuclear localization of Esp1/separase."
      Agarwal R., Cohen-Fix O.
      Genes Dev. 16:1371-1382(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CDC28, MUTAGENESIS OF SER-277; SER-292 AND THR-304.
    9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185; SER-186; SER-212 AND SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSECU_YEAST
    AccessioniPrimary (citable) accession number: P40316
    Secondary accession number(s): D6VS98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3