ID DAD2_YEAST Reviewed; 133 AA. AC P36162; D6VXE3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 177. DE RecName: Full=DASH complex subunit DAD2; DE AltName: Full=DUO1 and DAM1-interacting protein 2; DE AltName: Full=Helper of ASK1 protein 1; DE AltName: Full=Outer kinetochore protein DAD2; GN Name=DAD2; Synonyms=HSK1; OrderedLocusNames=YKR083C; ORFNames=YKR403; 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]. RX PubMed=8203164; DOI=10.1002/yea.320100210; RA Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G., RA Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.; RT "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae RT chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open RT reading frames."; RL Yeast 10:231-245(1994). 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8196765; DOI=10.1038/369371a0; RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., RA Becker I., Mewes H.-W.; RT "Complete DNA sequence of yeast chromosome XI."; RL Nature 369:371-378(1994). 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. 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 [6] 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 [7] 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 [8] 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 [9] 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 [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [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, AND IDENTIFICATION IN THE DASH COMPLEX. 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, AND SUBCELLULAR LOCATION. 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 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 [21] 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 depolymerization 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, PubMed:12408861). During spindle-kinetochore CC attachment, kinetochores first attach to the lateral surface of spindle CC microtubules, which supports the congression of chromosomes toward the CC middle of the dividing cell; they then slide along towards the spindle CC pole, a process independent of the DASH complex but requiring the NDC80 CC complex (PubMed:25236177). When the end of a disassembling microtubule CC reaches the laterally attached kinetochore, the DASH complex together CC with the NDC80 complex and STU2 convert lateral attachment to end-on CC capture to produce a structure that can track with microtubule CC shortening and sustain attachment when tension is applied across sister CC kinetochores upon their biorientation (PubMed:15640796, CC PubMed:15664196, PubMed:25236177). Microtubule depolymerization CC proceeds by protofilament splaying and induces the kinetochore-attached CC DASH 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:Q9UTG8, 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 P36162; P35734: ASK1; NbExp=8; IntAct=EBI-26515, EBI-26682; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000269|PubMed:11782438, CC ECO:0000269|PubMed:14562095}. Chromosome, centromere, kinetochore CC {ECO:0000269|PubMed:11782438, ECO:0000269|PubMed:14562095}. Chromosome CC {ECO:0000269|PubMed:36701236}. Note=Associates with the mitotic spindle CC and the kinetochore (PubMed:14562095). Associates with origin of CC replication (ORI) sites during interphase (PubMed:36701236). CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:36701236}. CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the DASH complex DAD2 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; Z27116; CAA81634.1; -; Genomic_DNA. DR EMBL; Z28308; CAA82162.1; -; Genomic_DNA. DR EMBL; AY558397; AAS56723.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09233.1; -; Genomic_DNA. DR PIR; S38161; S38161. DR RefSeq; NP_013009.1; NM_001179873.1. DR PDB; 8Q84; EM; 3.15 A; K/W=1-133. DR PDB; 8Q85; EM; 3.97 A; W=1-133. DR AlphaFoldDB; P36162; -. DR EMDB; EMD-18246; -. DR EMDB; EMD-18247; -. DR SMR; P36162; -. DR BioGRID; 34214; 222. DR ComplexPortal; CPX-1041; DASH complex. DR DIP; DIP-1927N; -. DR FunCoup; P36162; 57. DR IntAct; P36162; 10. DR MINT; P36162; -. DR STRING; 4932.YKR083C; -. DR iPTMnet; P36162; -. DR PaxDb; 4932-YKR083C; -. DR PeptideAtlas; P36162; -. DR EnsemblFungi; YKR083C_mRNA; YKR083C; YKR083C. DR GeneID; 853958; -. DR KEGG; sce:YKR083C; -. DR AGR; SGD:S000001791; -. DR SGD; S000001791; DAD2. DR VEuPathDB; FungiDB:YKR083C; -. DR eggNOG; ENOG502S93M; Eukaryota. DR HOGENOM; CLU_138063_1_0_1; -. DR InParanoid; P36162; -. DR OMA; DYEVGVW; -. DR OrthoDB; 3230169at2759; -. DR BioCyc; YEAST:G3O-32046-MONOMER; -. DR BioGRID-ORCS; 853958; 1 hit in 10 CRISPR screens. DR PRO; PR:P36162; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P36162; protein. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0042729; C:DASH complex; IDA:SGD. DR GO; GO:0072686; C:mitotic spindle; NAS:ComplexPortal. DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central. DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD. 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; IPR013963; DASH_Dad2. DR PANTHER; PTHR28036; DASH COMPLEX SUBUNIT DAD2; 1. DR PANTHER; PTHR28036:SF1; DASH COMPLEX SUBUNIT DAD2; 1. DR Pfam; PF08654; DASH_Dad2; 1. DR PDBsum; 8Q84; -. DR PDBsum; 8Q85; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell cycle; Cell division; Centromere; KW Chromosome; Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; KW Kinetochore; Microtubule; Mitosis; Nucleus; Reference proteome. FT CHAIN 1..133 FT /note="DASH complex subunit DAD2" FT /id="PRO_0000211598" FT REGION 81..133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1..51 FT /evidence="ECO:0000255" FT COMPBIAS 82..92 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 106..117 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT HELIX 4..53 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 55..66 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 69..72 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:8Q84" FT STRAND 124..128 FT /evidence="ECO:0007829|PDB:8Q84" SQ SEQUENCE 133 AA; 15072 MW; 82730D4AA5B66951 CRC64; MDSIDEQIAI KRKELQSLQK ITSLTDGLKI QLTELNEQIK EMGMNADSVA QLMNNWDSII NNISQASLGL LQYAEGDYEI GPWKDSKKKE SEQSNETGLE AQENDKNDED NDEDEDLVPL PETMVRIRVD GNE //