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SPC29_YEAST
ID   SPC29_YEAST             Reviewed;         253 AA.
AC   P33419; D6W3P3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Spindle pole component 29;
GN   Name=SPC29; Synonyms=LPH3, NIP29; OrderedLocusNames=YPL124W;
GN   ORFNames=LPH3W;
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 [GENOMIC DNA].
RA   Schlenstedt G., Silver P.A.;
RL   Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
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   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE SPC110 COMPLEX.
RX   PubMed=10339566; DOI=10.1073/pnas.96.11.6205;
RA   Elliott S., Knop M., Schlenstedt G., Schiebel E.;
RT   "Spc29p is a component of the Spc110p subcomplex and is essential for
RT   spindle pole body duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:6205-6210(1999).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH BBP1.
RX   PubMed=10654940; DOI=10.1093/emboj/19.3.421;
RA   Schramm C., Elliott S., Shevchenko A., Schiebel E.;
RT   "The Bbp1p-Mps2p complex connects the SPB to the nuclear envelope and is
RT   essential for SPB duplication.";
RL   EMBO J. 19:421-433(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-65, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [7]
RP   IDENTIFICATION BY 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   [8]
RP   PHOSPHORYLATION AT THR-240, MUTAGENESIS OF THR-240, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND FUNCTION.
RX   PubMed=19269975; DOI=10.1074/jbc.m900088200;
RA   Holinger E.P., Old W.M., Giddings T.H. Jr., Wong C., Yates J.R. III,
RA   Winey M.;
RT   "Budding yeast centrosome duplication requires stabilization of Spc29 via
RT   Mps1-mediated phosphorylation.";
RL   J. Biol. Chem. 284:12949-12955(2009).
RN   [9]
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).
CC   -!- FUNCTION: Component of the spindle pole body (SPB) required for the
CC       proper execution of spindle pole body (SPB) duplication. Links the
CC       central plaque component SPC42 to the inner plaque component SPC110.
CC       {ECO:0000269|PubMed:10339566, ECO:0000269|PubMed:10654940,
CC       ECO:0000269|PubMed:19269975}.
CC   -!- SUBUNIT: Component of the SPC110 complex containing at least CMD1,
CC       SPC29, SPC42 and SCP110. Interacts with BBP1.
CC       {ECO:0000269|PubMed:10339566, ECO:0000269|PubMed:10654940}.
CC   -!- INTERACTION:
CC       P33419; Q12365: BBP1; NbExp=3; IntAct=EBI-12041, EBI-3448;
CC       P33419; P28743: KIP2; NbExp=4; IntAct=EBI-12041, EBI-9749;
CC       P33419; P40457: MLP2; NbExp=2; IntAct=EBI-12041, EBI-25261;
CC       P33419; P33419: SPC29; NbExp=7; IntAct=EBI-12041, EBI-12041;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10339566}. Cytoplasm,
CC       cytoskeleton, microtubule organizing center, spindle pole body
CC       {ECO:0000269|PubMed:10339566}.
CC   -!- PTM: MPS1-mediated phosphorylation at Thr-240 is required for spindle
CC       pole body duplication. {ECO:0000269|PubMed:19269975}.
CC   -!- SIMILARITY: Belongs to the SPC29 family. {ECO:0000305}.
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DR   EMBL; X72226; CAA51029.1; -; Genomic_DNA.
DR   EMBL; U43503; AAB68238.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11309.1; -; Genomic_DNA.
DR   PIR; S34342; S34342.
DR   RefSeq; NP_015201.1; NM_001183938.1.
DR   AlphaFoldDB; P33419; -.
DR   SMR; P33419; -.
DR   BioGRID; 36057; 200.
DR   ComplexPortal; CPX-1419; Spindle pole body central plaque complex.
DR   DIP; DIP-2445N; -.
DR   IntAct; P33419; 29.
DR   MINT; P33419; -.
DR   STRING; 4932.YPL124W; -.
DR   iPTMnet; P33419; -.
DR   MaxQB; P33419; -.
DR   PaxDb; P33419; -.
DR   PRIDE; P33419; -.
DR   EnsemblFungi; YPL124W_mRNA; YPL124W; YPL124W.
DR   GeneID; 855979; -.
DR   KEGG; sce:YPL124W; -.
DR   SGD; S000006045; SPC29.
DR   VEuPathDB; FungiDB:YPL124W; -.
DR   HOGENOM; CLU_1099229_0_0_1; -.
DR   BioCyc; YEAST:G3O-34023-MON; -.
DR   PRO; PR:P33419; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P33419; protein.
DR   GO; GO:0005823; C:central plaque of spindle pole body; IC:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005816; C:spindle pole body; HDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0010968; P:regulation of microtubule nucleation; IC:ComplexPortal.
DR   GO; GO:0030474; P:spindle pole body duplication; IEA:InterPro.
DR   InterPro; IPR031392; Spc29.
DR   Pfam; PF17082; Spc29; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..253
FT                   /note="Spindle pole component 29"
FT                   /id="PRO_0000096846"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          31..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         240
FT                   /note="Phosphothreonine; by MPS1"
FT                   /evidence="ECO:0000269|PubMed:19269975"
FT   MUTAGEN         240
FT                   /note="T->A: Lead to defects in spindle pole body
FT                   assembly."
FT                   /evidence="ECO:0000269|PubMed:19269975"
SQ   SEQUENCE   253 AA;  29280 MW;  0730B17A86136621 CRC64;
     MDYSNFGNSA SKKFQDDTLN RVRKEHEEAL KKLREENFSS NTSELGNKKH YRAQERMSSP
     LHRLSPTGKS DDRKVKSPLD DKLRRQLREG NTRLPPPPFS SYGMPPTNRS NLDRIRRRTS
     SPVRTDKFAS QNVIDDQRLE IKYLERIVYD QGTVIDNLTS RITRLESFIL NSISDRGDKN
     FASLEHSRSF SGFPTNKTYG LQMGGLYEND MPYRRSSDNI NKEGAREDRS SQIHIENEST
     EDILKILSSS FHN
 
 
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