ASK1_YEAST
ID ASK1_YEAST Reviewed; 292 AA.
AC P35734; D6VXN5; Q68EC3; Q6B290;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DASH complex subunit ASK1;
DE AltName: Full=Associated with spindles and kinetochores protein 1;
DE AltName: Full=Outer kinetochore protein ASK1;
GN Name=ASK1; OrderedLocusNames=YKL052C; ORFNames=YKL306;
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=8091862; DOI=10.1002/yea.320100008;
RA Rasmussen S.W.;
RT "Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1 and
RT TOA2 genes, an open reading frame (ORF) similar to a translationally
RT controlled tumour protein, one ORF containing motifs also found in plant
RT storage proteins and 13 ORFs with weak or no homology to known proteins.";
RL Yeast 10:S63-S68(1994).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 14.
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 IDENTIFICATION, AND COMPONENT OF 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 [6]
RP PHOSPHORYLATION AT SER-26; SER-118; SER-134; THR-140; SER-200 AND SER-250.
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 [7]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=12695666;
RA Li Y., Elledge S.J.;
RT "The DASH complex component Ask1 is a cell cycle-regulated Cdk substrate in
RT Saccharomyces cerevisiae.";
RL Cell Cycle 2:143-148(2003).
RN [8]
RP INTERACTION WITH DAM1.
RX PubMed=12925767; DOI=10.1091/mbc.e02-11-0765;
RA Shang C., Hazbun T.R., Cheeseman I.M., Aranda J., Fields S., Drubin D.G.,
RA Barnes G.;
RT "Kinetochore protein interactions and their regulation by the Aurora kinase
RT Ipl1p.";
RL Mol. Biol. Cell 14:3342-3355(2003).
RN [9]
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 [10]
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 [11]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-155; SER-156 AND
RP SER-200, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-155; SER-156 AND
RP SER-200, AND IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-155; SER-156;
RP SER-200 AND SER-216, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
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}.
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 P35734; Q00684: CDC14; NbExp=2; IntAct=EBI-26682, EBI-4192;
CC P35734; P24869: CLB2; NbExp=2; IntAct=EBI-26682, EBI-4515;
CC P35734; P36162: DAD2; NbExp=7; IntAct=EBI-26682, EBI-26515;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:14562095}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:14562095}. Note=Associates
CC with the mitotic spindle and the kinetochore.
CC -!- MISCELLANEOUS: Present with 2836 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DASH complex ASK1 family. {ECO:0000305}.
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DR EMBL; X75781; CAA53419.1; -; Genomic_DNA.
DR EMBL; Z28052; CAA81888.1; -; Genomic_DNA.
DR EMBL; AY692840; AAT92859.1; -; Genomic_DNA.
DR EMBL; BK000645; DAA01815.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09105.1; -; Genomic_DNA.
DR PIR; S37874; S37874.
DR RefSeq; NP_012872.2; NM_001179618.1.
DR AlphaFoldDB; P35734; -.
DR SMR; P35734; -.
DR BioGRID; 34081; 300.
DR ComplexPortal; CPX-1041; DASH complex.
DR DIP; DIP-1928N; -.
DR IntAct; P35734; 14.
DR MINT; P35734; -.
DR STRING; 4932.YKL052C; -.
DR iPTMnet; P35734; -.
DR MaxQB; P35734; -.
DR PaxDb; P35734; -.
DR PRIDE; P35734; -.
DR EnsemblFungi; YKL052C_mRNA; YKL052C; YKL052C.
DR GeneID; 853814; -.
DR KEGG; sce:YKL052C; -.
DR SGD; S000001535; ASK1.
DR VEuPathDB; FungiDB:YKL052C; -.
DR eggNOG; ENOG502S2V2; Eukaryota.
DR HOGENOM; CLU_090087_0_0_1; -.
DR InParanoid; P35734; -.
DR OMA; TIIHFST; -.
DR BioCyc; YEAST:G3O-31853-MON; -.
DR PRO; PR:P35734; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P35734; 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:0044732; C:mitotic spindle pole body; IBA:GO_Central.
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; IPR013964; DASH_Ask1.
DR PANTHER; PTHR28200; PTHR28200; 2.
DR Pfam; PF08655; DASH_Ask1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..292
FT /note="DASH complex subunit ASK1"
FT /id="PRO_0000211317"
FT REGION 99..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12408861,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12408861"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12408861,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 140
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12408861"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 200
FT /note="Phosphoserine; by IPL1"
FT /evidence="ECO:0000269|PubMed:12408861,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 250
FT /note="Phosphoserine; by CDC28"
FT /evidence="ECO:0000269|PubMed:12408861"
FT CONFLICT 14
FT /note="D -> V (in Ref. 1; CAA53419 and 2; CAA81888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 32072 MW; C72BA50C3A9578E2 CRC64;
MDSASKEETL EKLDQEITVN LQKIDSNLSF CFHKITQDII PHVATYSEIC ERIMDSTEWL
GTMFQETGLV NLQANAAAPV GNAPVKSLVS NNVGIFPTSA EEASRQSQTD NGPNEADSAV
HVNRDVHSMF NNDSIDDFHT ANITSTGQIL KLPDSSDEDT GSEAVPSREQ TDLTGEGHGG
ADDEQDESTI QRQSRKRKIS LLLQQQYGSS SSMVPSPIVP NKMRKQLAHE EHINNDGDND
DENSNNIESS PLKQGHHHPK GQADDNNEGP DEEESTKEVP KPGTIIHFST NR
