HSK3_YEAST
ID HSK3_YEAST Reviewed; 69 AA.
AC P69852; D6VX58;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DASH complex subunit HSK3;
DE AltName: Full=Helper of ASK1 protein 3;
DE AltName: Full=Outer kinetochore protein HSK3;
GN Name=HSK3; OrderedLocusNames=YKL138C-A;
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=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 [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 COMPONENT OF DASH COMPLEX.
RX PubMed=15632076; DOI=10.1128/mcb.25.2.767-778.2005;
RA Li J.-M., Li Y., Elledge S.J.;
RT "Genetic analysis of the kinetochore DASH complex reveals an antagonistic
RT relationship with the ras/protein kinase A pathway and a novel subunit
RT required for Ask1 association.";
RL Mol. Cell. Biol. 25:767-778(2005).
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS 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 [9]
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 -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC Chromosome, centromere, kinetochore. Note=Associates with the mitotic
CC spindle and the kinetochore.
CC -!- SIMILARITY: Belongs to the DASH complex HSK3 family. {ECO:0000305}.
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DR EMBL; Z28139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006944; DAA09024.1; -; Genomic_DNA.
DR RefSeq; NP_690844.1; NM_001184513.1.
DR AlphaFoldDB; P69852; -.
DR SMR; P69852; -.
DR BioGRID; 33998; 61.
DR ComplexPortal; CPX-1041; DASH complex.
DR IntAct; P69852; 1.
DR MINT; P69852; -.
DR STRING; 4932.YKL138C-A; -.
DR MaxQB; P69852; -.
DR PaxDb; P69852; -.
DR PRIDE; P69852; -.
DR EnsemblFungi; YKL138C-A_mRNA; YKL138C-A; YKL138C-A.
DR GeneID; 853719; -.
DR KEGG; sce:YKL138C-A; -.
DR SGD; S000028421; HSK3.
DR VEuPathDB; FungiDB:YKL138C-A; -.
DR eggNOG; KOG4853; Eukaryota.
DR HOGENOM; CLU_193155_0_0_1; -.
DR InParanoid; P69852; -.
DR OMA; QCNKNIV; -.
DR BioCyc; YEAST:G3O-32096-MON; -.
DR PRO; PR:P69852; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P69852; 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: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:SGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD.
DR InterPro; IPR042332; Hsk3.
DR InterPro; IPR013183; Hsk3-like.
DR PANTHER; PTHR28289; PTHR28289; 1.
DR Pfam; PF08227; DASH_Hsk3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore; Microtubule; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..69
FT /note="DASH complex subunit HSK3"
FT /id="PRO_0000084079"
FT COILED 1..39
FT /evidence="ECO:0000255"
SQ SEQUENCE 69 AA; 8088 MW; C74C1BB9C17C31D0 CRC64;
MNANKQRQYN QLAHELRELQ TNLQETTKQL DIMSKQCNEN LVGQLGKVHG SWLIGSYIYY
MEQMLGKTQ
