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Q12158

- SCC1_YEAST

UniProt

Q12158 - SCC1_YEAST

Protein

Sister chromatid cohesion protein 1

Gene

MCD1

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 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei180 – 1812Cleavage; by ESP1
    Sitei268 – 2692Cleavage; by ESP1

    GO - Molecular functioni

    1. chromatin binding Source: SGD
    2. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: SGD
    2. cellular response to DNA damage stimulus Source: SGD
    3. DNA unwinding involved in DNA replication Source: SGD
    4. double-strand break repair Source: SGD
    5. establishment of mitotic sister chromatid cohesion Source: SGD
    6. mitotic chromosome condensation Source: SGD
    7. protein acetylation Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Mitosis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29434-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sister chromatid cohesion protein 1
    Gene namesi
    Name:MCD1
    Synonyms:PDS3, RHC21, SCC1
    Ordered Locus Names:YDL003W
    ORF Names:YD8119.04
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL003w.
    SGDiS000002161. MCD1.

    Subcellular locationi

    Nucleus. Chromosome. Chromosomecentromere
    Note: Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin except at centromeres, where cohesin complexes remain. At anaphase, it is cleaved by ESP1, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB-SubCell
    2. condensed nuclear chromosome Source: SGD
    3. mitochondrion Source: SGD
    4. nuclear mitotic cohesin complex Source: SGD
    5. nucleus Source: SGD

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi175 – 1751S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-263. 1 Publication
    Mutagenesisi180 – 1801R → D: Abolishes cleavage by ESP1; when associated with D-268. 1 Publication
    Mutagenesisi210 – 2101K → R: Loss of acetylation by ECO1. 1 Publication
    Mutagenesisi252 – 2521K → R: No effect on acetylation by ECO1. 1 Publication
    Mutagenesisi263 – 2631S → A: Reduces phosphorylation. Abolishes phosphorylation; when associated with A-175. 1 Publication
    Mutagenesisi268 – 2681R → D: Abolishes first cleavage by ESP1. Abolishes all cleavage by ESP1; when associated with D-180. 1 Publication
    Mutagenesisi290 – 2901K → R: No effect on acetylation by ECO1. 1 Publication
    Mutagenesisi310 – 3101K → R: No effect on acetylation by ECO1. 1 Publication
    Mutagenesisi319 – 3191K → R: No effect on acetylation by ECO1. 1 Publication
    Mutagenesisi324 – 3241K → R: No effect on acetylation by ECO1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 566566Sister chromatid cohesion protein 1PRO_0000097881Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei161 – 1611Phosphoserine1 Publication
    Modified residuei175 – 1751Phosphoserine; by CDC51 Publication
    Modified residuei210 – 2101N6-acetyllysine; by ECO11 Publication
    Modified residuei263 – 2631Phosphoserine; by CDC51 Publication
    Modified residuei307 – 3071Phosphoserine1 Publication
    Modified residuei354 – 3541Phosphothreonine1 Publication

    Post-translational modificationi

    Cleaved by ESP1 at the onset of anaphase.
    Phosphorylated by CDC5/Polo-like kinase at the onset of anaphase. Phosphorylation takes places at proximity to cleavage sites and is required for an efficient cleavage by ESP1.3 Publications
    Acetylated by ECO1.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ12158.
    PaxDbiQ12158.
    PeptideAtlasiQ12158.

    Miscellaneous databases

    PMAP-CutDBQ12158.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12158.

    Interactioni

    Subunit structurei

    Interacts directly with IRR1/SCC3 in cohesin complex. Cohesin complexes are composed of the SMC1 and SMC3 heterodimer attached via their hinge domain, MCD1/SCC1 which link them, and IRR1, which interacts with MCD1. The cohesin complex also interacts with SCC2, which is required for its association with chromosomes.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IRR1P405415EBI-16655,EBI-16667
    SMC1P329088EBI-16655,EBI-17402
    SMC3P4703713EBI-16655,EBI-17423

    Protein-protein interaction databases

    BioGridi32051. 120 interactions.
    DIPiDIP-5812N.
    IntActiQ12158. 36 interactions.
    MINTiMINT-627334.

    Structurei

    Secondary structure

    1
    566
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi484 – 49512
    Helixi504 – 5096
    Helixi522 – 53716
    Beta strandi539 – 5446
    Beta strandi551 – 5555
    Helixi557 – 5593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W1WX-ray2.90E/F/G/H451-564[»]
    ProteinModelPortaliQ12158.
    SMRiQ12158. Positions 483-560.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12158.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi258 – 2614Poly-Asp

    Domaini

    The C-terminal part associates with the head of SMC1, while the N-terminal part binds to the head of SMC3.

    Sequence similaritiesi

    Belongs to the rad21 family.Curated

    Phylogenomic databases

    eggNOGiNOG249424.
    HOGENOMiHOG000141751.
    KOiK06670.
    OMAiIWLASNM.
    OrthoDBiEOG7KSXM4.

    Family and domain databases

    Gene3Di1.10.10.580. 1 hit.
    InterProiIPR023093. Rad21/Rec8_C.
    IPR006909. Rad21/Rec8_C_eu.
    IPR006910. Rad21_Rec8_N.
    [Graphical view]
    PfamiPF04824. Rad21_Rec8. 1 hit.
    PF04825. Rad21_Rec8_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12158-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVTENPQRLT VLRLATNKGP LAQIWLASNM SNIPRGSVIQ THIAESAKEI    50
    AKASGCDDES GDNEYITLRT SGELLQGIVR VYSKQATFLL TDIKDTLTKI 100
    SMLFKTSQKM TSTVNRLNTV TRVHQLMLED AVTEREVLVT PGLEFLDDTT 150
    IPVGLMAQEN SMERKVQGAA PWDTSLEVGR RFSPDEDFEH NNLSSMNLDF 200
    DIEEGPITSK SWEEGTRQSS RNFDTHENYI QDDDFPLDDA GTIGWDLGIT 250
    EKNDQNNDDD DNSVEQGRRL GESIMSEEPT DFGFDLDIEK EAPAGNIDTI 300
    TDAMTESQPK QTGTRRNSKL LNTKSIQIDE ETENSESIAS SNTYKEERSN 350
    NLLTPQPTNF TTKRLWSEIT ESMSYLPDPI LKNFLSYESL KKRKIHNGRE 400
    GSIEEPELNV SLNLTDDVIS NAGTNDNSFN ELTDNMSDFV PIDAGLNEAP 450
    FPEENIIDAK TRNEQTTIQT EKVRPTPGEV ASKAIVQMAK ILRKELSEEK 500
    EVIFTDVLKS QANTEPENIT KREASRGFFD ILSLATEGCI GLSQTEAFGN 550
    IKIDAKPALF ERFINA 566
    Length:566
    Mass (Da):63,290
    Last modified:November 1, 1996 - v1
    Checksum:iEB6C7CA33BAC208F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y14280 Genomic DNA. Translation: CAA74657.1.
    U23759 Genomic DNA. Translation: AAB38803.1.
    Z48008 Genomic DNA. Translation: CAA88058.1.
    Z48432 Genomic DNA. Translation: CAA88356.1.
    Z74051 Genomic DNA. Translation: CAA98559.1.
    BK006938 Genomic DNA. Translation: DAA11845.1.
    PIRiS50979.
    RefSeqiNP_010281.1. NM_001180062.1.

    Genome annotation databases

    EnsemblFungiiYDL003W; YDL003W; YDL003W.
    GeneIDi851561.
    KEGGisce:YDL003W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y14280 Genomic DNA. Translation: CAA74657.1 .
    U23759 Genomic DNA. Translation: AAB38803.1 .
    Z48008 Genomic DNA. Translation: CAA88058.1 .
    Z48432 Genomic DNA. Translation: CAA88356.1 .
    Z74051 Genomic DNA. Translation: CAA98559.1 .
    BK006938 Genomic DNA. Translation: DAA11845.1 .
    PIRi S50979.
    RefSeqi NP_010281.1. NM_001180062.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W1W X-ray 2.90 E/F/G/H 451-564 [» ]
    ProteinModelPortali Q12158.
    SMRi Q12158. Positions 483-560.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32051. 120 interactions.
    DIPi DIP-5812N.
    IntActi Q12158. 36 interactions.
    MINTi MINT-627334.

    Proteomic databases

    MaxQBi Q12158.
    PaxDbi Q12158.
    PeptideAtlasi Q12158.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL003W ; YDL003W ; YDL003W .
    GeneIDi 851561.
    KEGGi sce:YDL003W.

    Organism-specific databases

    CYGDi YDL003w.
    SGDi S000002161. MCD1.

    Phylogenomic databases

    eggNOGi NOG249424.
    HOGENOMi HOG000141751.
    KOi K06670.
    OMAi IWLASNM.
    OrthoDBi EOG7KSXM4.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29434-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q12158.
    NextBioi 968995.
    PMAP-CutDB Q12158.

    Gene expression databases

    Genevestigatori Q12158.

    Family and domain databases

    Gene3Di 1.10.10.580. 1 hit.
    InterProi IPR023093. Rad21/Rec8_C.
    IPR006909. Rad21/Rec8_C_eu.
    IPR006910. Rad21_Rec8_N.
    [Graphical view ]
    Pfami PF04824. Rad21_Rec8. 1 hit.
    PF04825. Rad21_Rec8_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cohesins: chromosomal proteins that prevent premature separation of sister chromatids."
      Michaelis C., Ciosk R., Nasmyth K.
      Cell 91:35-45(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
      Strain: ATCC 200060 / W303.
    2. "A direct link between sister chromatid cohesion and chromosome condensation revealed through the analysis of MCD1 in S. cerevisiae."
      Guacci V., Koshland D., Strunnikov A.V.
      Cell 91:47-57(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
      Strain: ATCC 204508 / S288c.
    3. "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.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The RHC21 gene of budding yeast, a homologue of the fission yeast rad21+ gene, is essential for chromosome segregation."
      Heo S.-J., Tatebayashi K., Kato J., Ikeda H.
      Mol. Gen. Genet. 257:149-156(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to establish cohesion between sister chromatids during DNA replication."
      Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.
      Genes Dev. 13:320-333(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH IRR1, IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND IRR1, INTERACTION OF THE COHESIN COMPLEX WITH SCC2.
    7. "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 BY ESP1, FUNCTION, MUTAGENESIS OF ARG-180 AND ARG-268.
    8. "Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast."
      Alexandru G., Uhlmann F., Mechtler K., Poupart M.-A., Nasmyth K.
      Cell 105:459-472(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-175 AND SER-263 BY CDC5, MUTAGENESIS OF SER-175 AND SER-263.
    9. "Molecular architecture of SMC proteins and the yeast cohesin complex."
      Haering C.H., Loewe J., Hochwagen A., Nasmyth K.
      Mol. Cell 9:773-788(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; SMC3 AND IRR1, STRUCTURE.
    10. "Eco1 is a novel acetyltransferase that can acetylate proteins involved in cohesion."
      Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H., Nasmyth K.
      Curr. Biol. 12:323-328(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-210, MUTAGENESIS OF LYS-210; LYS-252; LYS-290; LYS-310; LYS-319 AND LYS-324.
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "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-161; SER-307 AND THR-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSCC1_YEAST
    AccessioniPrimary (citable) accession number: Q12158
    Secondary accession number(s): D6VRY5, Q05325
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 9, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 124 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 1040 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3