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 27-MAR-2024, entry version 126.
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 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 [4]
RP IDENTIFICATION IN THE 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 [5]
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 [6]
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 [7]
RP IDENTIFICATION IN THE DASH COMPLEX.
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP FUNCTION, IDENTIFICATION IN THE DASH COMPLEX, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
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 [13]
RP FUNCTION.
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 [14]
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 [15]
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 depolymerisation 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:15664196, PubMed:16415853, PubMed:16777964,
CC PubMed:17460120). Kinetochores also serve as an input point for the
CC spindle assembly checkpoint, which delays anaphase until all
CC chromosomes have bioriented on the mitotic spindle (PubMed:12408861).
CC During spindle-kinetochore attachment, kinetochores first attach to the
CC lateral surface of spindle microtubules, which supports the congression
CC of chromosomes toward the middle of the dividing cell; they then slide
CC along towards the spindle pole, a process independent of the DASH
CC complex but requiring the NDC80 complex (PubMed:25236177). When the end
CC of a disassembling microtubule reaches the laterally attached
CC kinetochore, the DASH complex together with the NDC80 complex and STU2
CC convert lateral attachment to end-on capture to produce a structure
CC that can track with microtubule shortening and sustain attachment when
CC tension is applied across sister kinetochores upon their biorientation
CC (PubMed:15640796, PubMed:15664196, PubMed:25236177). Microtubule
CC depolymerization proceeds by protofilament splaying and induces the
CC kinetochore-attached DASH complex to slide longitudinally, thereby
CC helping to transduce depolymerization energy into pulling forces to
CC disjoin chromatids (PubMed:16415853, PubMed:16777964). Incorrect
CC microtubule attachments are corrected by releasing microubules from the
CC kinetochore through phosphorylation by IPL1 of kinetochore components
CC (PubMed:12408861). Links the microtubule cytoskeleton to chromosomes
CC during interphase (PubMed:36701236). Also contributes to the poleward
CC transport of kinetochores on microtubules following centromeric DNA
CC replication in S-phase (PubMed:18079178). {ECO:0000269|PubMed:12408861,
CC ECO:0000269|PubMed:15640796, ECO:0000269|PubMed:15664196,
CC ECO:0000269|PubMed:16415853, ECO:0000269|PubMed:16777964,
CC ECO:0000269|PubMed:17460120, ECO:0000269|PubMed:17643123,
CC ECO:0000269|PubMed:18079178, ECO:0000269|PubMed:25236177,
CC 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:15632076, PubMed:16715078,
CC PubMed:17460120, PubMed:25236177, PubMed:15640796, PubMed:17643123).
CC Multiple DASH complexes oligomerize to form a ring that encircles
CC spindle microtubules and organizes the rod-like NDC80 complexes of the
CC outer kinetochore (PubMed:16715078, PubMed:17460120, PubMed:25236177,
CC PubMed:17643123). DASH complex oligomerization strengthens microtubule
CC attachments (PubMed:25236177). On cytoplasmic microtubules, DASH
CC complexes appear to form patches instead of rings (By similarity).
CC {ECO:0000250|UniProtKB:O94483, ECO:0000269|PubMed:15632076,
CC ECO:0000269|PubMed:15640796, ECO:0000269|PubMed:16715078,
CC ECO:0000269|PubMed:17460120, ECO:0000269|PubMed:17643123,
CC ECO:0000269|PubMed:25236177}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:25236177}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000305|PubMed:25236177}. Chromosome,
CC centromere, kinetochore {ECO:0000305|PubMed:25236177}. Note=Associates
CC with the mitotic spindle and the kinetochore.
CC -!- DISRUPTION PHENOTYPE: Degron-mediated knockdown disrupts
CC oligomerization of the DASH complex and leads to defective sister
CC kinetochore biorientation and mitotic arrest with large buds.
CC {ECO:0000269|PubMed:25236177}.
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 PDB; 8Q84; EM; 3.15 A; Q/c=1-69.
DR PDB; 8Q85; EM; 3.97 A; c=1-69.
DR PDBsum; 8Q84; -.
DR PDBsum; 8Q85; -.
DR AlphaFoldDB; P69852; -.
DR SMR; P69852; -.
DR BioGRID; 33998; 63.
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 PeptideAtlas; P69852; -.
DR EnsemblFungi; YKL138C-A_mRNA; YKL138C-A; YKL138C-A.
DR GeneID; 853719; -.
DR KEGG; sce:YKL138C-A; -.
DR AGR; SGD:S000028421; -.
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 OrthoDB; 2026924at2759; -.
DR BioCyc; YEAST:G3O-32096-MONOMER; -.
DR BioGRID-ORCS; 853719; 3 hits in 10 CRISPR screens.
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; NAS: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 GO; GO:1990976; P:protein transport along microtubule to mitotic spindle pole body; IMP:UniProtKB.
DR InterPro; IPR042332; Hsk3.
DR InterPro; IPR013183; Hsk3-like.
DR PANTHER; PTHR28289; DASH COMPLEX SUBUNIT HSK3; 1.
DR PANTHER; PTHR28289:SF1; DASH COMPLEX SUBUNIT HSK3; 1.
DR Pfam; PF08227; DASH_Hsk3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; Kinetochore;
KW Microtubule; Mitosis; 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
//
