ID DAD1_YEAST Reviewed; 94 AA. AC Q12248; D6VS02; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JUL-2024, entry version 163. DE RecName: Full=DASH complex subunit DAD1; DE AltName: Full=DUO1 and DAM1-interacting protein 1; DE AltName: Full=Outer kinetochore protein DAD1; GN Name=DAD1; OrderedLocusNames=YDR016C; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; DOI=10.1038/387s075; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [2] 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 [3] 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 [4] RP FUNCTION. RX PubMed=12408861; DOI=10.1016/s0092-8674(02)00973-x; RA Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S., RA Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.; RT "Phospho-regulation of kinetochore-microtubule attachments by the Aurora RT kinase Ipl1p."; RL Cell 111:163-172(2002). RN [5] RP FUNCTION, IDENTIFICATION IN THE DASH COMPLEX, IDENTIFICATION BY MASS RP SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=11782438; DOI=10.1093/emboj/21.1.181; RA Janke C., Ortiz J., Tanaka T.U., Lechner J., Schiebel E.; RT "Four new subunits of the Dam1-Duo1 complex reveal novel functions in RT sister kinetochore biorientation."; RL EMBO J. 21:181-193(2002). RN [6] RP IDENTIFICATION IN THE DASH COMPLEX. RX PubMed=11799062; DOI=10.1101/gad.959402; RA Li Y., Bachant J.B., Alcasabas A.A., Wang Y., Qin J., Elledge S.J.; RT "The mitotic spindle is required for loading of the DASH complex onto the RT kinetochore."; RL Genes Dev. 16:183-197(2002). RN [7] 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 [8] 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 [9] 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 [10] 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 [11] RP IDENTIFICATION IN THE DASH COMPLEX. 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 [12] 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 [13] RP FUNCTION. RX PubMed=18079178; DOI=10.1101/gad.449407; RA Kitamura E., Tanaka K., Kitamura Y., Tanaka T.U.; RT "Kinetochore microtubule interaction during S phase in Saccharomyces RT cerevisiae."; RL Genes Dev. 21:3319-3330(2007). RN [14] RP FUNCTION, AND IDENTIFICATION IN THE DASH COMPLEX. RX PubMed=17460120; DOI=10.1091/mbc.e07-02-0135; RA Miranda J.J., King D.S., Harrison S.C.; RT "Protein arms in the kinetochore-microtubule interface of the yeast DASH RT complex."; RL Mol. Biol. Cell 18:2503-2510(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [17] RP IDENTIFICATION IN THE DASH COMPLEX. RX PubMed=24930965; DOI=10.1016/j.cub.2014.05.014; RA Aravamudhan P., Felzer-Kim I., Gurunathan K., Joglekar A.P.; RT "Assembling the protein architecture of the budding yeast kinetochore- RT microtubule attachment using FRET."; RL Curr. Biol. 24:1437-1446(2014). RN [18] RP FUNCTION, IDENTIFICATION IN THE DASH COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=25236177; DOI=10.1038/ncomms5951; RA Umbreit N.T., Miller M.P., Tien J.F., Ortola J.C., Gui L., Lee K.K., RA Biggins S., Asbury C.L., Davis T.N.; RT "Kinetochores require oligomerization of Dam1 complex to maintain RT microtubule attachments against tension and promote biorientation."; RL Nat. Commun. 5:4951-4951(2014). RN [19] RP FUNCTION. RX PubMed=36701236; DOI=10.1016/j.celrep.2023.112045; RA Weibeta M., Chanou A., Schauer T., Tvardovskiy A., Meiser S., Koenig A.C., RA Schmidt T., Kruse E., Ummethum H., Trauner M., Werner M., Lalonde M., RA Hauck S.M., Scialdone A., Hamperl S.; RT "Single-copy locus proteomics of early- and late-firing DNA replication RT origins identifies a role of Ask1/DASH complex in replication timing RT control."; RL Cell Rep. 42:112045-112045(2023). RN [20] RP MUTAGENESIS OF GLU-50. RX PubMed=36651597; DOI=10.15252/embj.2022112600; RA Haase M.A.B., Olafsson G., Flores R.L., Boakye-Ansah E., Zelter A., RA Dickinson M.S., Lazar-Stefanita L., Truong D.M., Asbury C.L., Davis T.N., RA Boeke J.D.; RT "DASH/Dam1 complex mutants stabilize ploidy in histone-humanized yeast by RT weakening kinetochore-microtubule attachments."; RL EMBO J. 42:e112600-e112600(2023). RN [21] RP ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES, RP FUNCTION, AND IDENTIFICATION IN THE DASH COMPLEX. 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). RN [22] RP ELECTRON MICROSCOPY OF DASH COMPLEX, FUNCTION, IDENTIFICATION IN THE DASH RP COMPLEX, AND SUBUNIT. RX PubMed=17643123; DOI=10.1038/nsmb1274; RA Wang H.W., Ramey V.H., Westermann S., Leschziner A.E., Welburn J.P., RA Nakajima Y., Drubin D.G., Barnes G., Nogales E.; RT "Architecture of the Dam1 kinetochore ring complex and implications for RT microtubule-driven assembly and force-coupling mechanisms."; RL Nat. Struct. Mol. Biol. 14:721-726(2007). CC -!- FUNCTION: Component of the DASH complex that connects microtubules with CC kinetochores and couples microtubule depolymerisation to chromosome CC movement; it is involved in retrieving kinetochores to the spindle CC poles before their re-orientation on the spindle in early mitosis and CC allows microtubule depolymerization to pull chromosomes apart and CC resist detachment during anaphase (PubMed:15664196, PubMed:16415853, CC PubMed:16777964, PubMed:17460120, PubMed:17643123). Kinetochores, CC consisting of a centromere-associated inner segment and a microtubule- CC contacting outer segment, play a crucial role in chromosome segregation CC by mediating the physical connection between centromeric DNA and CC microtubules (PubMed:11782438). Kinetochores also serve as an input CC point for the spindle assembly checkpoint, which delays anaphase until CC all chromosomes have bioriented on the mitotic spindle CC (PubMed:11782438). During spindle-kinetochore attachment, kinetochores CC first attach to the lateral surface of spindle microtubules, which CC supports the congression of chromosomes toward the middle of the CC dividing cell; they then slide along towards the spindle pole, a CC process independent of the DASH complex but requiring the NDC80 complex CC (PubMed:25236177). When the end of a disassembling microtubule reaches CC the laterally attached kinetochore, the DASH complex together with the CC NDC80 complex and STU2 convert lateral attachment to end-on capture to CC produce a structure that can track with microtubule shortening and CC sustain attachment when tension is applied across sister kinetochores CC upon their biorientation (PubMed:15640796, PubMed:15664196, CC PubMed:25236177). Microtubule depolymerization proceeds by CC protofilament splaying and induces the kinetochore-attached DASH CC complex to slide longitudinally, thereby helping to transduce CC depolymerization energy into pulling forces to disjoin chromatids CC (PubMed:16415853, PubMed:16777964). Incorrect microtubule attachments CC are corrected by releasing microubules from the kinetochore through CC phosphorylation by IPL1 of kinetochore components (PubMed:12408861). CC Links the microtubule cytoskeleton to chromosomes during interphase CC (PubMed:36701236). Also contributes to the poleward transport of CC kinetochores on microtubules following centromeric DNA replication in CC S-phase (PubMed:18079178). {ECO:0000269|PubMed:11782438, CC ECO:0000269|PubMed:12408861, ECO:0000269|PubMed:15640796, CC ECO:0000269|PubMed:15664196, ECO:0000269|PubMed:16415853, CC ECO:0000269|PubMed:16777964, ECO:0000269|PubMed:17460120, CC ECO:0000269|PubMed:17643123, ECO:0000269|PubMed:18079178, CC ECO:0000269|PubMed:25236177, ECO:0000269|PubMed:36701236}. CC -!- SUBUNIT: Component of the DASH complex consisting of ASK1, DAD1, DAD2, CC DAD3, DAD4, DAM1, DUO1, HSK3, SPC19 and SPC34, with a stoichiometry of CC one copy of each subunit per complex (PubMed:11782438, PubMed:11799062, CC PubMed:15640796, PubMed:16715078, PubMed:17460120, PubMed:17643123, CC PubMed:24930965, PubMed:25236177). Multiple DASH complexes oligomerize CC to form a ring that encircles spindle microtubules and organizes the CC rod-like NDC80 complexes of the outer kinetochore (PubMed:16715078, CC PubMed:17460120, PubMed:17643123, PubMed:25236177). DASH complex CC oligomerization strengthens microtubule attachments (PubMed:25236177). CC On cytoplasmic microtubules, DASH complexes appear to form patches CC instead of rings (By similarity). {ECO:0000250|UniProtKB:P87297, CC ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:11799062, CC ECO:0000269|PubMed:15640796, ECO:0000269|PubMed:16715078, CC ECO:0000269|PubMed:17460120, ECO:0000269|PubMed:17643123, CC ECO:0000269|PubMed:24930965, ECO:0000269|PubMed:25236177}. CC -!- INTERACTION: CC Q12248; P53267: DAM1; NbExp=4; IntAct=EBI-35662, EBI-23268; CC Q12248; P53168: DUO1; NbExp=3; IntAct=EBI-35662, EBI-23800; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:25236177}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:25236177}. Chromosome, centromere, kinetochore CC {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:25236177}. Note=Associates with the mitotic spindle CC and the kinetochore. {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:25236177}. CC -!- MISCELLANEOUS: Present with 799 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the DASH complex DAD1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z74312; CAA98836.1; -; Genomic_DNA. DR EMBL; Z49770; CAA89841.1; -; Genomic_DNA. DR EMBL; AY557635; AAS55961.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11862.1; -; Genomic_DNA. DR PIR; S54639; S54639. DR RefSeq; NP_010299.3; NM_001180324.3. DR PDB; 8Q84; EM; 3.15 A; L/X=1-94. DR PDB; 8Q85; EM; 3.97 A; X=1-94. DR PDBsum; 8Q84; -. DR PDBsum; 8Q85; -. DR AlphaFoldDB; Q12248; -. DR EMDB; EMD-18246; -. DR EMDB; EMD-18247; -. DR SMR; Q12248; -. DR BioGRID; 32066; 362. DR ComplexPortal; CPX-1041; DASH complex. DR DIP; DIP-1296N; -. DR IntAct; Q12248; 9. DR MINT; Q12248; -. DR STRING; 4932.YDR016C; -. DR iPTMnet; Q12248; -. DR PaxDb; Q12248; -. DR PeptideAtlas; Q12248; -. DR EnsemblFungi; YDR016C_mRNA; YDR016C; YDR016C. DR GeneID; 851579; -. DR KEGG; sce:YDR016C; -. DR AGR; SGD:S000002423; -. DR SGD; S000002423; DAD1. DR VEuPathDB; FungiDB:YDR016C; -. DR eggNOG; ENOG502SBWQ; Eukaryota. DR HOGENOM; CLU_142427_2_2_1; -. DR InParanoid; Q12248; -. DR OMA; ENVSELW; -. DR OrthoDB; 2348292at2759; -. DR BioCyc; YEAST:G3O-29634-MONOMER; -. DR BioGRID-ORCS; 851579; 6 hits in 10 CRISPR screens. DR PRO; PR:Q12248; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; Q12248; Protein. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0042729; C:DASH complex; IDA:SGD. DR GO; GO:0072686; C:mitotic spindle; NAS:ComplexPortal. DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central. DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central. 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:ComplexPortal. DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD. DR GO; GO:1990976; P:protein transport along microtubule to mitotic spindle pole body; IMP:UniProtKB. DR InterPro; IPR013958; DASH_Dad1. DR PANTHER; PTHR28025; DASH COMPLEX SUBUNIT DAD1; 1. DR PANTHER; PTHR28025:SF1; DASH COMPLEX SUBUNIT DAD1; 1. DR Pfam; PF08649; DASH_Dad1; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; KW Chromosome partition; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; KW Mitosis; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..94 FT /note="DASH complex subunit DAD1" FT /id="PRO_0000127613" FT MOD_RES 91 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MUTAGEN 50 FT /note="E->D: Perturbs DASH complex formation and weakens FT microtubule attachments. Decreases sporulation efficiency FT and spore viability." FT /evidence="ECO:0000269|PubMed:36651597" SQ SEQUENCE 94 AA; 10516 MW; 6D27737AC5A39D51 CRC64; MMASTSNDEE KLISTTDKYF IEQRNIVLQE INETMNSILN GLNGLNISLE SSIAVGREFQ SVSDLWKTLY DGLESLSDEA PIDEQPTLSQ SKTK //