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DASH complex subunit SPC19 (19 kDa spindle pole component protein) (Outer kinetochore protein SPC19)

 SPC19_YEAST             Reviewed;         165 AA.
Q03954; D6VSI3;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 136.
RecName: Full=DASH complex subunit SPC19;
AltName: Full=19 kDa spindle pole component protein;
AltName: Full=Outer kinetochore protein SPC19;
Name=SPC19; OrderedLocusNames=YDR201W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
PHOSPHORYLATION AT SER-107 AND SER-116.
PubMed=12408861; DOI=10.1016/S0092-8674(02)00973-X;
Cheeseman I.M., Anderson S., Jwa M., Green E.M., Kang J.-S.,
Yates J.R. III, Chan C.S.M., Drubin D.G., Barnes G.;
"Phospho-regulation of kinetochore-microtubule attachments by the
Aurora kinase Ipl1p.";
Cell 111:163-172(2002).
[5]
COMPONENT OF DASH COMPLEX.
PubMed=11799062; DOI=10.1101/gad.959402;
Li Y., Bachant J.B., Alcasabas A.A., Wang Y., Qin J., Elledge S.J.;
"The mitotic spindle is required for loading of the DASH complex onto
the kinetochore.";
Genes Dev. 16:183-197(2002).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
FUNCTION.
PubMed=15664196; DOI=10.1016/j.molcel.2004.12.019;
Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J.,
Drubin D.G., Nogales E., Barnes G.;
"Formation of a dynamic kinetochore-microtubule interface through
assembly of the Dam1 ring complex.";
Mol. Cell 17:277-290(2005).
[9]
FUNCTION.
PubMed=16415853; DOI=10.1038/nature04409;
Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E.,
Barnes G.;
"The Dam1 kinetochore ring complex moves processively on
depolymerizing microtubule ends.";
Nature 440:565-569(2006).
[10]
SUBUNIT.
PubMed=16715078; DOI=10.1038/ncb1414;
Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.;
"Molecular architecture of a kinetochore-microtubule attachment
site.";
Nat. Cell Biol. 8:581-585(2006).
[11]
FUNCTION.
PubMed=16777964; DOI=10.1073/pnas.0602249103;
Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N.;
"The Dam1 kinetochore complex harnesses microtubule dynamics to
produce force and movement.";
Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-116, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[14]
ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES.
PubMed=15640796; DOI=10.1038/nsmb896;
Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C.;
"The yeast DASH complex forms closed rings on microtubules.";
Nat. Struct. Mol. Biol. 12:138-143(2005).
-!- FUNCTION: Component of the DASH complex, a microtubule-binding
subcomplex of the outer kinetochore that is essential for proper
chromosome segregation. The DASH complex mediates the formation
and maintenance of bipolar kinetochore-microtubule attachments by
forming closed rings around spindle microtubules and establishing
interactions with proteins from the central kinetochore. The DASH
ring complex may both stabilize microtubules during chromosome
attachment in anaphase A, and allow the chromosome to remain
attached to the depolymerizing microtubule in anaphase B.
Microtubule depolymerization proceeds by protofilament splaying
and induces the kinetochore-attached ring to slide longitudinally,
thereby helping to transduce depolymerization energy into pulling
forces to disjoin chromatids. {ECO:0000269|PubMed:15664196,
ECO:0000269|PubMed:16415853, ECO:0000269|PubMed:16777964}.
-!- SUBUNIT: The DASH complex is an approximately 210 kDa
heterodecamer, which consists of ASK1, DAD1, DAD2, DAD3, DAD4,
DAM1, DUO1, HSK3, SPC19 and SPC34, with an apparent stoichiometry
of one copy of each subunit. DASH oligomerizes into a 50 nm ring
composed of about 16 molecules that encircles the microtubule.
Integrity of the complex and interactions with central kinetochore
proteins are regulated by the spindle assembly checkpoint kinase
IPL1. {ECO:0000269|PubMed:16715078}.
-!- INTERACTION:
P35734:ASK1; NbExp=8; IntAct=EBI-38809, EBI-26682;
Q12248:DAD1; NbExp=4; IntAct=EBI-38809, EBI-35662;
P36162:DAD2; NbExp=3; IntAct=EBI-38809, EBI-26515;
P53267:DAM1; NbExp=3; IntAct=EBI-38809, EBI-23268;
P53168:DUO1; NbExp=5; IntAct=EBI-38809, EBI-23800;
P36131:SPC34; NbExp=7; IntAct=EBI-38809, EBI-26401;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:14562095}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:14562095}.
Note=Associates with the mitotic spindle and the kinetochore.
-!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DASH complex SPC19 family.
{ECO:0000305}.
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EMBL; Z48784; CAA88713.1; -; Genomic_DNA.
EMBL; AY557667; AAS55993.1; -; Genomic_DNA.
EMBL; BK006938; DAA12043.1; -; Genomic_DNA.
PIR; S52707; S52707.
RefSeq; NP_010487.3; NM_001180509.3.
ProteinModelPortal; Q03954; -.
BioGrid; 32252; 223.
DIP; DIP-1579N; -.
IntAct; Q03954; 23.
MINT; Q03954; -.
STRING; 4932.YDR201W; -.
iPTMnet; Q03954; -.
MaxQB; Q03954; -.
PaxDb; Q03954; -.
PRIDE; Q03954; -.
EnsemblFungi; YDR201W; YDR201W; YDR201W.
GeneID; 851782; -.
KEGG; sce:YDR201W; -.
EuPathDB; FungiDB:YDR201W; -.
SGD; S000002609; SPC19.
HOGENOM; HOG000154374; -.
InParanoid; Q03954; -.
KO; K11572; -.
OMA; MEDIEPL; -.
OrthoDB; EOG092C5S5F; -.
BioCyc; YEAST:G3O-29786-MONOMER; -.
PRO; PR:Q03954; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0042729; C:DASH complex; IDA:SGD.
GO; GO:0005876; C:spindle microtubule; IEA:InterPro.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:1990758; P:mitotic sister chromatid biorientation; IBA:GO_Central.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IDA:SGD.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD.
InterPro; IPR013251; DASH_Spc19.
PANTHER; PTHR28262; PTHR28262; 1.
Pfam; PF08287; DASH_Spc19; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Centromere; Chromosome;
Chromosome partition; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 165 DASH complex subunit SPC19.
/FTId=PRO_0000142593.
COILED 74 104 {ECO:0000255}.
COILED 132 165 {ECO:0000255}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:12408861}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:12408861}.
SEQUENCE 165 AA; 18910 MW; 74615FE2186DAFE6 CRC64;
MTDALEQSVL ALEGTVSVLK DSVESLKCAN EPSTNLASTM LQTKRVFRLV PEYDVERSKL
DLIEEVEPLV RTLGDKLRKS MGRMQRELDT LQQTYELNDL RLKKNISMDD DDALNSPDMG
QEYEGRDADD VVMMASSTNE ELEELKKLKE KKKQLENKLE ILKQK


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