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DASH complex subunit ASK1 (Associated with spindles and kinetochores protein 1) (Outer kinetochore protein ASK1)

 ASK1_YEAST              Reviewed;         292 AA.
P35734; D6VXN5; Q68EC3; Q6B290;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 2.
10-OCT-2018, entry version 140.
RecName: Full=DASH complex subunit ASK1;
AltName: Full=Associated with spindles and kinetochores protein 1;
AltName: Full=Outer kinetochore protein ASK1;
Name=ASK1; OrderedLocusNames=YKL052C; ORFNames=YKL306;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8091862; DOI=10.1002/yea.320100008;
Rasmussen S.W.;
"Sequence of a 28.6 kb region of yeast chromosome XI includes the FBA1
and TOA2 genes, an open reading frame (ORF) similar to a
translationally controlled tumour protein, one ORF containing motifs
also found in plant storage proteins and 13 ORFs with weak or no
homology to known proteins.";
Yeast 10:S63-S68(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[3]
GENOME REANNOTATION, AND SEQUENCE REVISION TO 14.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
IDENTIFICATION, AND COMPONENT OF THE DASH COMPLEX.
PubMed=11799062; DOI=10.1101/gad.959402;
Li Y., Bachant J.B., Alcasabas A.A., Wang Y., Qin J., Elledge S.J.;
"The mitotic spindle is required for loading of the DASH complex onto
the kinetochore.";
Genes Dev. 16:183-197(2002).
[6]
PHOSPHORYLATION AT SER-26; SER-118; SER-134; THR-140; SER-200 AND
SER-250.
PubMed=12408861; DOI=10.1016/S0092-8674(02)00973-X;
Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,
Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.;
"Phospho-regulation of kinetochore-microtubule attachments by the
Aurora kinase Ipl1p.";
Cell 111:163-172(2002).
[7]
PHOSPHORYLATION BY CDC28.
PubMed=12695666;
Li Y., Elledge S.J.;
"The DASH complex component Ask1 is a cell cycle-regulated Cdk
substrate in Saccharomyces cerevisiae.";
Cell Cycle 2:143-148(2003).
[8]
INTERACTION WITH DAM1.
PubMed=12925767; DOI=10.1091/mbc.E02-11-0765;
Shang C., Hazbun T.R., Cheeseman I.M., Aranda J., Fields S.,
Drubin D.G., Barnes G.;
"Kinetochore protein interactions and their regulation by the Aurora
kinase Ipl1p.";
Mol. Biol. Cell 14:3342-3355(2003).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
FUNCTION.
PubMed=15664196; DOI=10.1016/j.molcel.2004.12.019;
Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J.,
Drubin D.G., Nogales E., Barnes G.;
"Formation of a dynamic kinetochore-microtubule interface through
assembly of the Dam1 ring complex.";
Mol. Cell 17:277-290(2005).
[12]
FUNCTION.
PubMed=16415853; DOI=10.1038/nature04409;
Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E.,
Barnes G.;
"The Dam1 kinetochore ring complex moves processively on
depolymerizing microtubule ends.";
Nature 440:565-569(2006).
[13]
SUBUNIT.
PubMed=16715078; DOI=10.1038/ncb1414;
Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.;
"Molecular architecture of a kinetochore-microtubule attachment
site.";
Nat. Cell Biol. 8:581-585(2006).
[14]
FUNCTION.
PubMed=16777964; DOI=10.1073/pnas.0602249103;
Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N.;
"The Dam1 kinetochore complex harnesses microtubule dynamics to
produce force and movement.";
Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-155; SER-156
AND SER-200, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-155; SER-156 AND
SER-200, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-155; SER-156;
SER-200 AND SER-216, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[18]
ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES.
PubMed=15640796; DOI=10.1038/nsmb896;
Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C.;
"The yeast DASH complex forms closed rings on microtubules.";
Nat. Struct. Mol. Biol. 12:138-143(2005).
-!- FUNCTION: Component of the DASH complex, a microtubule-binding
subcomplex of the outer kinetochore that is essential for proper
chromosome segregation. The DASH complex mediates the formation
and maintenance of bipolar kinetochore-microtubule attachments by
forming closed rings around spindle microtubules and establishing
interactions with proteins from the central kinetochore. The DASH
ring complex may both stabilize microtubules during chromosome
attachment in anaphase A, and allow the chromosome to remain
attached to the depolymerizing microtubule in anaphase B.
Microtubule depolymerization proceeds by protofilament splaying
and induces the kinetochore-attached ring to slide longitudinally,
thereby helping to transduce depolymerization energy into pulling
forces to disjoin chromatids. {ECO:0000269|PubMed:15664196,
ECO:0000269|PubMed:16415853, ECO:0000269|PubMed:16777964}.
-!- SUBUNIT: The DASH complex is an approximately 210 kDa
heterodecamer, which consists of ASK1, DAD1, DAD2, DAD3, DAD4,
DAM1, DUO1, HSK3, SPC19 and SPC34, with an apparent stoichiometry
of one copy of each subunit. DASH oligomerizes into a 50 nm ring
composed of about 16 molecules that encircles the microtubule.
Integrity of the complex and interactions with central kinetochore
proteins are regulated by the spindle assembly checkpoint kinase
IPL1. {ECO:0000269|PubMed:16715078}.
-!- INTERACTION:
Q00684:CDC14; NbExp=2; IntAct=EBI-26682, EBI-4192;
P24869:CLB2; NbExp=2; IntAct=EBI-26682, EBI-4515;
P36162:DAD2; NbExp=7; IntAct=EBI-26682, EBI-26515;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:14562095}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14562095}.
Note=Associates with the mitotic spindle and the kinetochore.
-!- MISCELLANEOUS: Present with 2836 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DASH complex ASK1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X75781; CAA53419.1; -; Genomic_DNA.
EMBL; Z28052; CAA81888.1; -; Genomic_DNA.
EMBL; AY692840; AAT92859.1; -; Genomic_DNA.
EMBL; BK000645; DAA01815.1; -; Genomic_DNA.
EMBL; BK006944; DAA09105.1; -; Genomic_DNA.
PIR; S37874; S37874.
RefSeq; NP_012872.2; NM_001179618.1.
ProteinModelPortal; P35734; -.
SMR; P35734; -.
BioGrid; 34081; 295.
ComplexPortal; CPX-1041; DASH complex.
DIP; DIP-1928N; -.
IntAct; P35734; 14.
MINT; P35734; -.
STRING; 4932.YKL052C; -.
iPTMnet; P35734; -.
MaxQB; P35734; -.
PaxDb; P35734; -.
PRIDE; P35734; -.
EnsemblFungi; YKL052C; YKL052C; YKL052C.
GeneID; 853814; -.
KEGG; sce:YKL052C; -.
EuPathDB; FungiDB:YKL052C; -.
SGD; S000001535; ASK1.
HOGENOM; HOG000034102; -.
InParanoid; P35734; -.
KO; K11566; -.
OrthoDB; EOG092C5NUZ; -.
BioCyc; YEAST:G3O-31853-MONOMER; -.
PRO; PR:P35734; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0042729; C:DASH complex; IDA:SGD.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0072686; C:mitotic spindle; IEA:InterPro.
GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IC:SGD.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:1990758; P:mitotic sister chromatid biorientation; IBA:GO_Central.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IDA:SGD.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD.
InterPro; IPR013964; DASH_Ask1.
Pfam; PF08655; DASH_Ask1; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Centromere; Chromosome;
Chromosome partition; Complete proteome; Cytoplasm; Cytoskeleton;
Kinetochore; Microtubule; Mitosis; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 292 DASH complex subunit ASK1.
/FTId=PRO_0000211317.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000269|PubMed:12408861}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000269|PubMed:12408861}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:12408861}.
MOD_RES 140 140 Phosphothreonine.
{ECO:0000269|PubMed:12408861}.
MOD_RES 155 155 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 200 200 Phosphoserine; by IPL1.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:12408861}.
MOD_RES 216 216 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 250 250 Phosphoserine; by CDC28.
{ECO:0000269|PubMed:12408861}.
CONFLICT 14 14 D -> V (in Ref. 1; CAA53419 and 2;
CAA81888). {ECO:0000305}.
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


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