ID DAD1_YEAST Reviewed; 94 AA. AC Q12248; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-OCT-2010, entry version 70. 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 (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomyceta; OC Saccharomycotina; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=97313263; PubMed=9169867; 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., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA 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 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., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [3] RP COMPONENT OF 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 RT the kinetochore."; RL Genes Dev. 16:183-197(2002). RN [4] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; 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 [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] 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 RT assembly of the Dam1 ring complex."; RL Mol. Cell 17:277-290(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-87; SER-89 AND SER-91, RP AND MASS SPECTROMETRY. 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [8] 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 RT depolymerizing microtubule ends."; RL Nature 440:565-569(2006). RN [9] 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 RT site."; RL Nat. Cell Biol. 8:581-585(2006). RN [10] 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 RT produce force and movement."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006). RN [11] 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 CC and maintenance of bipolar kinetochore-microtubule attachments by CC forming closed rings around spindle microtubules and establishing CC interactions with proteins from the central kinetochore. The DASH CC ring complex may both stabilize microtubules during chromosome CC attachment in anaphase A, and allow the chromosome to remain CC attached to the depolymerizing microtubule in anaphase B. CC Microtubule depolymerization proceeds by protofilament splaying CC and induces the kinetochore-attached ring to slide longitudinally, CC thereby helping to transduce depolymerization energy into pulling CC forces to disjoin chromatids. CC -!- SUBUNIT: The DASH complex is an approximately 210 kDa CC heterodecamer, which consists of ASK1, DAD1, DAD2, DAD3, DAD4, CC DAM1, DUO1, HSK3, SPC19 and SPC34, with an apparent stoichiometry CC of one copy of each subunit. DASH oligomerizes into a 50 nm ring CC composed of about 16 molecules that encircles the microtubule. CC Integrity of the complex and interactions with central kinetochore CC proteins are regulated by the spindle assembly checkpoint kinase CC IPL1. CC -!- INTERACTION: CC P53267:DAM1; NbExp=1; IntAct=EBI-35662, EBI-23268; CC P53168:DUO1; NbExp=2; IntAct=EBI-35662, EBI-23800; CC P36131:SPC34; NbExp=1; IntAct=EBI-35662, EBI-26401; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. CC Chromosome, centromere, kinetochore. Note=Associates with the CC mitotic spindle and the kinetochore. CC -!- MISCELLANEOUS: Present with 799 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the DASH complex DAD1 family. 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 PIR; S54639; S54639. DR ProteinModelPortal; Q12248; -. DR DIP; DIP-1296N; -. DR IntAct; Q12248; 28. DR MINT; MINT-409635; -. DR STRING; Q12248; -. DR EnsemblFungi; YDR016C; YDR016C; YDR016C. DR GenomeReviews; Z71256_GR; YDR016C. DR KEGG; sce:YDR016C; -. DR NMPDR; fig|4932.3.peg.1042; -. DR CYGD; YDR016c; -. DR SGD; S000002423; DAD1. DR eggNOG; fuNOG12986; -. DR HOGENOM; HBG398797; -. DR OMA; IGKEFDD; -. DR OrthoDB; EOG9GJ15F; -. DR PhylomeDB; Q12248; -. DR NextBio; 969040; -. DR ArrayExpress; Q12248; -. DR Genevestigator; Q12248; -. DR GermOnline; YDR016C; Saccharomyces cerevisiae. 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:0005819; C:spindle; IPI:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0005200; F:structural constituent of cytoskeleton; IPI:SGD. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW. DR GO; GO:0030472; P:mitotic spindle organization in nucleus; IPI:SGD. DR GO; GO:0031110; P:regulation of microtubule polymerization or...; IDA:SGD. DR InterPro; IPR013958; DASH_Dad1. DR Pfam; PF08649; DASH_Dad1; 1. PE 1: Evidence at protein level; KW Cell cycle; Cell division; Centromere; Chromosome; KW Chromosome partition; Complete proteome; Cytoplasm; Cytoskeleton; KW Kinetochore; Microtubule; Mitosis; Nucleus; Phosphoprotein. FT CHAIN 1 94 DASH complex subunit DAD1. FT /FTId=PRO_0000127613. FT MOD_RES 87 87 Phosphothreonine. FT MOD_RES 89 89 Phosphoserine. FT MOD_RES 91 91 Phosphoserine. SQ SEQUENCE 94 AA; 10516 MW; 6D27737AC5A39D51 CRC64; MMASTSNDEE KLISTTDKYF IEQRNIVLQE INETMNSILN GLNGLNISLE SSIAVGREFQ SVSDLWKTLY DGLESLSDEA PIDEQPTLSQ SKTK //