位置:首页 > 蛋白库 > SPC19_YEAST
SPC19_YEAST
ID   SPC19_YEAST             Reviewed;         165 AA.
AC   Q03954; D6VSI3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 162.
DE   RecName: Full=DASH complex subunit SPC19;
DE   AltName: Full=19 kDa spindle pole component protein;
DE   AltName: Full=Outer kinetochore protein SPC19;
GN   Name=SPC19; OrderedLocusNames=YDR201W;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   PHOSPHORYLATION AT SER-107 AND SER-116.
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   COMPONENT OF 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   [6]
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   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(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=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   [10]
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   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-116, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [14]
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       Q03954; P36131: SPC34; NbExp=4; IntAct=EBI-38809, EBI-26401;
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   -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the DASH complex SPC19 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; Z48784; CAA88713.1; -; Genomic_DNA.
DR   EMBL; AY557667; AAS55993.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA12043.1; -; Genomic_DNA.
DR   PIR; S52707; S52707.
DR   RefSeq; NP_010487.3; NM_001180509.3.
DR   AlphaFoldDB; Q03954; -.
DR   SMR; Q03954; -.
DR   BioGRID; 32252; 227.
DR   ComplexPortal; CPX-1041; DASH complex.
DR   DIP; DIP-1579N; -.
DR   IntAct; Q03954; 15.
DR   MINT; Q03954; -.
DR   STRING; 4932.YDR201W; -.
DR   iPTMnet; Q03954; -.
DR   MaxQB; Q03954; -.
DR   PaxDb; Q03954; -.
DR   PRIDE; Q03954; -.
DR   EnsemblFungi; YDR201W_mRNA; YDR201W; YDR201W.
DR   GeneID; 851782; -.
DR   KEGG; sce:YDR201W; -.
DR   SGD; S000002609; SPC19.
DR   VEuPathDB; FungiDB:YDR201W; -.
DR   eggNOG; ENOG502SDEQ; Eukaryota.
DR   HOGENOM; CLU_1678217_0_0_1; -.
DR   InParanoid; Q03954; -.
DR   OMA; YDVQRAK; -.
DR   BioCyc; YEAST:G3O-29786-MON; -.
DR   PRO; PR:Q03954; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03954; 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; IPR013251; DASH_Spc19.
DR   PANTHER; PTHR28262; PTHR28262; 1.
DR   Pfam; PF08287; DASH_Spc19; 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..165
FT                   /note="DASH complex subunit SPC19"
FT                   /id="PRO_0000142593"
FT   COILED          74..104
FT                   /evidence="ECO:0000255"
FT   COILED          132..165
FT                   /evidence="ECO:0000255"
FT   MOD_RES         107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:12408861,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:12408861,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   165 AA;  18910 MW;  74615FE2186DAFE6 CRC64;
     MTDALEQSVL ALEGTVSVLK DSVESLKCAN EPSTNLASTM LQTKRVFRLV PEYDVERSKL
     DLIEEVEPLV RTLGDKLRKS MGRMQRELDT LQQTYELNDL RLKKNISMDD DDALNSPDMG
     QEYEGRDADD VVMMASSTNE ELEELKKLKE KKKQLENKLE ILKQK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024