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SPC34_YEAST
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   03-AUG-2022, entry version 167.
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   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   [4]
RP   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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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       P36131; P53267: DAM1; NbExp=4; IntAct=EBI-26401, EBI-23268;
CC       P36131; P53168: DUO1; NbExp=2; IntAct=EBI-26401, EBI-23800;
CC       P36131; Q03954: SPC19; NbExp=4; IntAct=EBI-26401, EBI-38809;
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   -!- SIMILARITY: Belongs to the DASH complex SPC34 family. {ECO:0000305}.
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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   AlphaFoldDB; P36131; -.
DR   SMR; P36131; -.
DR   BioGRID; 34168; 58.
DR   ComplexPortal; CPX-1041; DASH complex.
DR   DIP; DIP-1649N; -.
DR   IntAct; P36131; 9.
DR   MINT; P36131; -.
DR   STRING; 4932.YKR037C; -.
DR   iPTMnet; P36131; -.
DR   MaxQB; P36131; -.
DR   PaxDb; P36131; -.
DR   PRIDE; P36131; -.
DR   EnsemblFungi; YKR037C_mRNA; YKR037C; YKR037C.
DR   GeneID; 853909; -.
DR   KEGG; sce:YKR037C; -.
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   BioCyc; YEAST:G3O-32009-MON; -.
DR   PRO; PR:P36131; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P36131; protein.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0042729; C:DASH complex; IDA:SGD.
DR   GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
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: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; IPR013966; Spc34.
DR   Pfam; PF08657; DASH_Spc34; 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; 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"
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
 
 
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