ID SPC34_YEAST Reviewed; 295 AA. AC P36131; D6VXA0; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 182. DE RecName: Full=DASH complex subunit SPC34; DE AltName: Full=34 kDa spindle pole component protein; DE AltName: Full=Outer kinetochore protein SPC34; GN Name=SPC34; OrderedLocusNames=YKR037C; 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 PROTEIN SEQUENCE OF 93-98, FUNCTION, AND IDENTIFICATION IN THE DASH RP 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 [4] RP FUNCTION, AND PHOSPHORYLATION AT THR-199. 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 [5] 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 [6] 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 [7] 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 [8] 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 [9] RP FUNCTION. RX PubMed=15846338; DOI=10.1038/nature03483; RA Tanaka K., Mukae N., Dewar H., van Breugel M., James E.K., Prescott A.R., RA Antony C., Tanaka T.U.; RT "Molecular mechanisms of kinetochore capture by spindle microtubules."; RL Nature 434:987-994(2005). RN [10] 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 [11] 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 [12] 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 [13] 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 [14] RP FUNCTION. RX PubMed=17620411; DOI=10.1083/jcb.200702141; RA Tanaka K., Kitamura E., Kitamura Y., Tanaka T.U.; RT "Molecular mechanisms of microtubule-dependent kinetochore transport toward RT spindle poles."; RL J. Cell Biol. 178:269-281(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-199, AND IDENTIFICATION BY RP 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 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 [17] 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 [18] 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 [19] 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 [20] 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:15846338, PubMed:17620411). When the end of a CC disassembling microtubule reaches the laterally attached kinetochore, CC the DASH complex together with the NDC80 complex and STU2 convert CC lateral attachment to end-on capture to produce a structure that can CC track with microtubule shortening and sustain attachment when tension CC is applied across sister kinetochores upon their biorientation CC (PubMed:11782438, PubMed:15640796, PubMed:15664196, PubMed:15846338, CC PubMed:17620411, 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:15846338, CC ECO:0000269|PubMed:16415853, ECO:0000269|PubMed:16777964, CC ECO:0000269|PubMed:17460120, ECO:0000269|PubMed:17620411, 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:O14285, 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 P36131; P53267: DAM1; NbExp=5; IntAct=EBI-26401, EBI-23268; CC P36131; P53168: DUO1; NbExp=3; IntAct=EBI-26401, EBI-23800; CC P36131; Q03954: SPC19; NbExp=5; IntAct=EBI-26401, EBI-38809; 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 -!- SIMILARITY: Belongs to the DASH complex SPC34 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; Z28262; CAA82111.1; -; Genomic_DNA. DR EMBL; BK006944; DAA09190.1; -; Genomic_DNA. DR PIR; S38109; S38109. DR RefSeq; NP_012963.3; NM_001179827.3. DR PDB; 8Q84; EM; 3.15 A; O/a=1-295. DR PDB; 8Q85; EM; 3.97 A; a=1-295. DR AlphaFoldDB; P36131; -. DR EMDB; EMD-18246; -. DR EMDB; EMD-18247; -. DR SMR; P36131; -. DR BioGRID; 34168; 61. DR ComplexPortal; CPX-1041; DASH complex. DR DIP; DIP-1649N; -. DR FunCoup; P36131; 57. DR IntAct; P36131; 12. DR MINT; P36131; -. DR STRING; 4932.YKR037C; -. DR iPTMnet; P36131; -. DR PaxDb; 4932-YKR037C; -. DR PeptideAtlas; P36131; -. DR EnsemblFungi; YKR037C_mRNA; YKR037C; YKR037C. DR GeneID; 853909; -. DR KEGG; sce:YKR037C; -. DR AGR; SGD:S000001745; -. DR SGD; S000001745; SPC34. DR VEuPathDB; FungiDB:YKR037C; -. DR eggNOG; ENOG502QSS0; Eukaryota. DR HOGENOM; CLU_970457_0_0_1; -. DR InParanoid; P36131; -. DR OMA; LIRDCNP; -. DR OrthoDB; 10016597at2759; -. DR BioCyc; YEAST:G3O-32009-MONOMER; -. DR BioGRID-ORCS; 853909; 4 hits in 10 CRISPR screens. DR CD-CODE; 876000F7; Centrosome. DR PRO; PR:P36131; -. DR Proteomes; UP000002311; Chromosome XI. DR RNAct; P36131; 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:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0005876; C:spindle microtubule; IEA:InterPro. 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; IPR013966; Spc34. DR Pfam; PF08657; DASH_Spc34; 1. DR PDBsum; 8Q84; -. DR PDBsum; 8Q85; -. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; KW Chromosome partition; Coiled coil; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Kinetochore; Microtubule; Mitosis; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..295 FT /note="DASH complex subunit SPC34" FT /id="PRO_0000211554" FT COILED 223..295 FT /evidence="ECO:0000255" FT MOD_RES 199 FT /note="Phosphothreonine; by IPL1" FT /evidence="ECO:0000269|PubMed:12408861, FT ECO:0007744|PubMed:17330950" FT HELIX 3..21 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 29..37 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 41..51 FT /evidence="ECO:0007829|PDB:8Q84" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 57..63 FT /evidence="ECO:0007829|PDB:8Q84" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:8Q84" FT TURN 68..71 FT /evidence="ECO:0007829|PDB:8Q84" FT STRAND 72..75 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 82..98 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 101..104 FT /evidence="ECO:0007829|PDB:8Q84" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 112..124 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 159..167 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 172..183 FT /evidence="ECO:0007829|PDB:8Q84" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:8Q84" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:8Q84" FT STRAND 197..202 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 207..220 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 224..264 FT /evidence="ECO:0007829|PDB:8Q84" SQ SEQUENCE 295 AA; 34078 MW; C1061B49F6D4D308 CRC64; MGESLDRCID DINRAVDSMS TLYFKPPGIF HNAILQGASN KASIRKDITR LIKDCNHDEA YLLFKVNPEK QSVSRRDGKE GVFDYVIKRD TDMKRNRRLG RPGEKPIIHV PKEVYLNKDR LDLNNKRRRT ATTSGGGLNG FIFDTDLIGS SVISNSSSGT FKALSAVFKD DPQIQRLLYA LENGSVLMEE ESNNQRRKTI FVEDFPTDLI LKVMAEVTDL WPLTEFKQDY DQLYHNYEQL SSKLRFIKKE VLLQDDRLKT MSQYHPSSSH DVAKIIRKEK DEIRRLEMEI ANLQE //