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P53168

- DUO1_YEAST

UniProt

P53168 - DUO1_YEAST

Protein

DASH complex subunit DUO1

Gene

DUO1

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 114 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The DASH complex mediates the formation and maintenance of bipolar kinetochore-microtubule attachments by forming closed rings around spindle microtubules and establishing interactions with proteins from the central kinetochore. The DASH ring complex may both stabilize microtubules during chromosome attachment in anaphase A, and allow the chromosome to remain attached to the depolymerizing microtubule in anaphase B. Microtubule depolymerization proceeds by protofilament splaying and induces the kinetochore-attached ring to slide longitudinally, thereby helping to transduce depolymerization energy into pulling forces to disjoin chromatids.4 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. attachment of spindle microtubules to kinetochore Source: SGD
    2. mitotic nuclear division Source: UniProtKB-KW
    3. positive regulation of attachment of spindle microtubules to kinetochore Source: SGD
    4. positive regulation of microtubule polymerization Source: SGD

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Mitosis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30569-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DASH complex subunit DUO1
    Alternative name(s):
    Death upon overproduction protein 1
    Outer kinetochore protein DUO1
    Gene namesi
    Name:DUO1
    Ordered Locus Names:YGL061C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGL061c.
    SGDiS000003029. DUO1.

    Subcellular locationi

    Nucleus. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore
    Note: Associates with the mitotic spindle and the kinetochore.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. DASH complex Source: SGD
    3. microtubule Source: UniProtKB-KW
    4. mitotic spindle Source: InterPro

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Microtubule, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671E → K in DUO1-1; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with V-157. 1 Publication
    Mutagenesisi117 – 1171A → T in DUO1-2; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with I-124. 1 Publication
    Mutagenesisi124 – 1241M → I in DUO1-2; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with T-117. 1 Publication
    Mutagenesisi157 – 1571A → V in DUO1-1; produces abnormal spindles resulting in growth arrest at 37 degrees Celsius; when associated with K-67. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 247246DASH complex subunit DUO1PRO_0000215595Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP53168.
    PaxDbiP53168.
    PeptideAtlasiP53168.

    Expressioni

    Gene expression databases

    GenevestigatoriP53168.

    Interactioni

    Subunit structurei

    The DASH complex is an approximately 210 kDa heterodecamer, which consists of ASK1, DAD1, DAD2, DAD3, DAD4, DAM1, DUO1, HSK3, SPC19 and SPC34, with an apparent stoichiometry of one copy of each subunit. DASH oligomerizes into a 50 nm ring composed of about 16 molecules that encircles the microtubule. Integrity of the complex and interactions with central kinetochore proteins are regulated by the spindle assembly checkpoint kinase IPL1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAD1Q122484EBI-23800,EBI-35662
    DAM1P532676EBI-23800,EBI-23268
    SPC34P361313EBI-23800,EBI-26401

    Protein-protein interaction databases

    BioGridi33186. 162 interactions.
    DIPiDIP-1287N.
    IntActiP53168. 7 interactions.
    MINTiMINT-405719.
    STRINGi4932.YGL061C.

    Structurei

    3D structure databases

    ProteinModelPortaliP53168.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili152 – 18029Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DASH complex DUO1 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG42829.
    HOGENOMiHOG000112294.
    KOiK11570.
    OMAiHEVCKST.
    OrthoDBiEOG74FFDB.

    Family and domain databases

    InterProiIPR013960. DASH_Duo1.
    [Graphical view]
    PfamiPF08651. DASH_Duo1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P53168-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEQSQLDDS TIDKLIPQIF NEMRSNLNNT TNKFPKSTGG GASDNISANS    50
    NSIRSFNSIT TQSLLKESES LDKITAMIKN VTAALKNNLP VYVNQVHEVC 100
    KSTNSILDSW INIHSQAGYI HKLMSDQTYL KLINDRLHNE NVNTNDEDGS 150
    TLHNVIALKK KEILDLRQKL ENRKGEKDAA PAKPPNQGLN PRYGVQSGRR 200
    PVPSAGISNN GRVRKTHVPA SKRPSGIPRV TNRWTKPTAS SSRKMFR 247
    Length:247
    Mass (Da):27,473
    Last modified:October 1, 1996 - v1
    Checksum:i787F8AF869E3C978
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z72583 Genomic DNA. Translation: CAA96764.1.
    AY558484 Genomic DNA. Translation: AAS56810.1.
    BK006941 Genomic DNA. Translation: DAA08041.1.
    PIRiS64065.
    RefSeqiNP_011454.1. NM_001180926.1.

    Genome annotation databases

    EnsemblFungiiYGL061C; YGL061C; YGL061C.
    GeneIDi852819.
    KEGGisce:YGL061C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z72583 Genomic DNA. Translation: CAA96764.1 .
    AY558484 Genomic DNA. Translation: AAS56810.1 .
    BK006941 Genomic DNA. Translation: DAA08041.1 .
    PIRi S64065.
    RefSeqi NP_011454.1. NM_001180926.1.

    3D structure databases

    ProteinModelPortali P53168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33186. 162 interactions.
    DIPi DIP-1287N.
    IntActi P53168. 7 interactions.
    MINTi MINT-405719.
    STRINGi 4932.YGL061C.

    Proteomic databases

    MaxQBi P53168.
    PaxDbi P53168.
    PeptideAtlasi P53168.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGL061C ; YGL061C ; YGL061C .
    GeneIDi 852819.
    KEGGi sce:YGL061C.

    Organism-specific databases

    CYGDi YGL061c.
    SGDi S000003029. DUO1.

    Phylogenomic databases

    eggNOGi NOG42829.
    HOGENOMi HOG000112294.
    KOi K11570.
    OMAi HEVCKST.
    OrthoDBi EOG74FFDB.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30569-MONOMER.

    Miscellaneous databases

    NextBioi 972363.

    Gene expression databases

    Genevestigatori P53168.

    Family and domain databases

    InterProi IPR013960. DASH_Duo1.
    [Graphical view ]
    Pfami PF08651. DASH_Duo1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The characterization of two new clusters of duplicated genes suggests a 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes."
      Feuermann M., de Montigny J., Potier S., Souciet J.-L.
      Yeast 13:861-869(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "Saccharomyces cerevisiae Duo1p and Dam1p, novel proteins involved in mitotic spindle function."
      Hofmann C., Cheeseman I.M., Goode B.L., McDonald K.L., Barnes G., Drubin D.G.
      J. Cell Biol. 143:1029-1040(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-67; ALA-117; MET-124 AND ALA-157.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Formation of a dynamic kinetochore-microtubule interface through assembly of the Dam1 ring complex."
      Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J., Drubin D.G., Nogales E., Barnes G.
      Mol. Cell 17:277-290(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The Dam1 kinetochore ring complex moves processively on depolymerizing microtubule ends."
      Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E., Barnes G.
      Nature 440:565-569(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Molecular architecture of a kinetochore-microtubule attachment site."
      Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.
      Nat. Cell Biol. 8:581-585(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    11. "The Dam1 kinetochore complex harnesses microtubule dynamics to produce force and movement."
      Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N.
      Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. "The yeast DASH complex forms closed rings on microtubules."
      Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C.
      Nat. Struct. Mol. Biol. 12:138-143(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES.

    Entry informationi

    Entry nameiDUO1_YEAST
    AccessioniPrimary (citable) accession number: P53168
    Secondary accession number(s): D6VU80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 114 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 996 molecules/cell in log phase SD medium.1 Publication

    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 VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3