DUO1_YEAST
ID DUO1_YEAST Reviewed; 247 AA.
AC P53168; D6VU80;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=DASH complex subunit DUO1;
DE AltName: Full=Death upon overproduction protein 1;
DE AltName: Full=Outer kinetochore protein DUO1;
GN Name=DUO1; OrderedLocusNames=YGL061C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9234674;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT "The characterization of two new clusters of duplicated genes suggests a
RT 'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL Yeast 13:861-869(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-67; ALA-117; MET-124
RP AND ALA-157.
RX PubMed=9817759; DOI=10.1083/jcb.143.4.1029;
RA Hofmann C., Cheeseman I.M., Goode B.L., McDonald K.L., Barnes G.,
RA Drubin D.G.;
RT "Saccharomyces cerevisiae Duo1p and Dam1p, novel proteins involved in
RT mitotic spindle function.";
RL J. Cell Biol. 143:1029-1040(1998).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=15664196; DOI=10.1016/j.molcel.2004.12.019;
RA Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J.,
RA Drubin D.G., Nogales E., Barnes G.;
RT "Formation of a dynamic kinetochore-microtubule interface through assembly
RT of the Dam1 ring complex.";
RL Mol. Cell 17:277-290(2005).
RN [9]
RP FUNCTION.
RX PubMed=16415853; DOI=10.1038/nature04409;
RA Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E.,
RA Barnes G.;
RT "The Dam1 kinetochore ring complex moves processively on depolymerizing
RT microtubule ends.";
RL Nature 440:565-569(2006).
RN [10]
RP SUBUNIT.
RX PubMed=16715078; DOI=10.1038/ncb1414;
RA Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.;
RT "Molecular architecture of a kinetochore-microtubule attachment site.";
RL Nat. Cell Biol. 8:581-585(2006).
RN [11]
RP FUNCTION.
RX PubMed=16777964; DOI=10.1073/pnas.0602249103;
RA Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N.;
RT "The Dam1 kinetochore complex harnesses microtubule dynamics to produce
RT force and movement.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES.
RX PubMed=15640796; DOI=10.1038/nsmb896;
RA Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C.;
RT "The yeast DASH complex forms closed rings on microtubules.";
RL Nat. Struct. Mol. Biol. 12:138-143(2005).
CC -!- FUNCTION: Component of the DASH complex, a microtubule-binding
CC subcomplex of the outer kinetochore that is essential for proper
CC chromosome segregation. The DASH complex mediates the formation and
CC maintenance of bipolar kinetochore-microtubule attachments by forming
CC closed rings around spindle microtubules and establishing interactions
CC with proteins from the central kinetochore. The DASH ring complex may
CC both stabilize microtubules during chromosome attachment in anaphase A,
CC and allow the chromosome to remain attached to the depolymerizing
CC microtubule in anaphase B. Microtubule depolymerization proceeds by
CC protofilament splaying and induces the kinetochore-attached ring to
CC slide longitudinally, thereby helping to transduce depolymerization
CC energy into pulling forces to disjoin chromatids.
CC {ECO:0000269|PubMed:15664196, ECO:0000269|PubMed:16415853,
CC ECO:0000269|PubMed:16777964, ECO:0000269|PubMed:9817759}.
CC -!- SUBUNIT: The DASH complex is an approximately 210 kDa heterodecamer,
CC which consists of ASK1, DAD1, DAD2, DAD3, DAD4, DAM1, DUO1, HSK3, SPC19
CC and SPC34, with an apparent stoichiometry of one copy of each subunit.
CC DASH oligomerizes into a 50 nm ring composed of about 16 molecules that
CC encircles the microtubule. Integrity of the complex and interactions
CC with central kinetochore proteins are regulated by the spindle assembly
CC checkpoint kinase IPL1. {ECO:0000269|PubMed:16715078}.
CC -!- INTERACTION:
CC P53168; Q12248: DAD1; NbExp=3; IntAct=EBI-23800, EBI-35662;
CC P53168; P53267: DAM1; NbExp=6; IntAct=EBI-23800, EBI-23268;
CC P53168; P36131: SPC34; NbExp=2; IntAct=EBI-23800, EBI-26401;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9817759}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9817759}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:9817759}. Note=Associates
CC with the mitotic spindle and the kinetochore.
CC {ECO:0000269|PubMed:9817759}.
CC -!- MISCELLANEOUS: Present with 996 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DASH complex DUO1 family. {ECO:0000305}.
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DR EMBL; Z72583; CAA96764.1; -; Genomic_DNA.
DR EMBL; AY558484; AAS56810.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08041.1; -; Genomic_DNA.
DR PIR; S64065; S64065.
DR RefSeq; NP_011454.1; NM_001180926.1.
DR AlphaFoldDB; P53168; -.
DR SMR; P53168; -.
DR BioGRID; 33186; 432.
DR ComplexPortal; CPX-1041; DASH complex.
DR DIP; DIP-1287N; -.
DR IntAct; P53168; 7.
DR MINT; P53168; -.
DR STRING; 4932.YGL061C; -.
DR CarbonylDB; P53168; -.
DR iPTMnet; P53168; -.
DR MaxQB; P53168; -.
DR PaxDb; P53168; -.
DR PRIDE; P53168; -.
DR EnsemblFungi; YGL061C_mRNA; YGL061C; YGL061C.
DR GeneID; 852819; -.
DR KEGG; sce:YGL061C; -.
DR SGD; S000003029; DUO1.
DR VEuPathDB; FungiDB:YGL061C; -.
DR eggNOG; ENOG502S4KM; Eukaryota.
DR HOGENOM; CLU_114619_0_0_1; -.
DR InParanoid; P53168; -.
DR OMA; WIKIQSQ; -.
DR BioCyc; YEAST:G3O-30569-MON; -.
DR PRO; PR:P53168; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53168; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0042729; C:DASH complex; IDA:SGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IDA:ComplexPortal.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IDA:SGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD.
DR InterPro; IPR013960; DASH_Duo1.
DR PANTHER; PTHR28216; PTHR28216; 1.
DR Pfam; PF08651; DASH_Duo1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Mitosis; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..247
FT /note="DASH complex subunit DUO1"
FT /id="PRO_0000215595"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 152..180
FT /evidence="ECO:0000255"
FT COMPBIAS 231..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 67
FT /note="E->K: In DUO1-1; produces abnormal spindles
FT resulting in growth arrest at 37 degrees Celsius; when
FT associated with V-157."
FT /evidence="ECO:0000269|PubMed:9817759"
FT MUTAGEN 117
FT /note="A->T: In DUO1-2; produces abnormal spindles
FT resulting in growth arrest at 37 degrees Celsius; when
FT associated with I-124."
FT /evidence="ECO:0000269|PubMed:9817759"
FT MUTAGEN 124
FT /note="M->I: In DUO1-2; produces abnormal spindles
FT resulting in growth arrest at 37 degrees Celsius; when
FT associated with T-117."
FT /evidence="ECO:0000269|PubMed:9817759"
FT MUTAGEN 157
FT /note="A->V: In DUO1-1; produces abnormal spindles
FT resulting in growth arrest at 37 degrees Celsius; when
FT associated with K-67."
FT /evidence="ECO:0000269|PubMed:9817759"
SQ SEQUENCE 247 AA; 27473 MW; 787F8AF869E3C978 CRC64;
MSEQSQLDDS TIDKLIPQIF NEMRSNLNNT TNKFPKSTGG GASDNISANS NSIRSFNSIT
TQSLLKESES LDKITAMIKN VTAALKNNLP VYVNQVHEVC KSTNSILDSW INIHSQAGYI
HKLMSDQTYL KLINDRLHNE NVNTNDEDGS TLHNVIALKK KEILDLRQKL ENRKGEKDAA
PAKPPNQGLN PRYGVQSGRR PVPSAGISNN GRVRKTHVPA SKRPSGIPRV TNRWTKPTAS
SSRKMFR
