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CMS1_YEAST
ID   CMS1_YEAST              Reviewed;         291 AA.
AC   Q07897; D6VY05;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Protein CMS1;
DE   AltName: Full=Complementation of MCM10 suppressor protein 1;
GN   Name=CMS1; OrderedLocusNames=YLR003C;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   FUNCTION.
RX   PubMed=11787774; DOI=10.1038/sj.cr.7290098;
RA   Wang J.W., Wu J.R.;
RT   "Overexpression of a novel gene, Cms1, can rescue the growth arrest of a
RT   Saccharomyces cerevisiae mcm10 suppressor.";
RL   Cell Res. 11:285-291(2001).
RN   [4]
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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP   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).
CC   -!- FUNCTION: May play a role in the regulation of DNA replication and cell
CC       cycle control. {ECO:0000269|PubMed:11787774}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1200 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the CMS1 family. {ECO:0000305}.
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DR   EMBL; Z73175; CAA97525.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09321.1; -; Genomic_DNA.
DR   PIR; S64825; S64825.
DR   RefSeq; NP_013103.1; NM_001181890.1.
DR   AlphaFoldDB; Q07897; -.
DR   SMR; Q07897; -.
DR   BioGRID; 31276; 86.
DR   DIP; DIP-2550N; -.
DR   IntAct; Q07897; 6.
DR   MINT; Q07897; -.
DR   STRING; 4932.YLR003C; -.
DR   iPTMnet; Q07897; -.
DR   MaxQB; Q07897; -.
DR   PaxDb; Q07897; -.
DR   PRIDE; Q07897; -.
DR   EnsemblFungi; YLR003C_mRNA; YLR003C; YLR003C.
DR   GeneID; 850689; -.
DR   KEGG; sce:YLR003C; -.
DR   SGD; S000003993; CMS1.
DR   VEuPathDB; FungiDB:YLR003C; -.
DR   eggNOG; KOG3089; Eukaryota.
DR   GeneTree; ENSGT00390000006574; -.
DR   HOGENOM; CLU_082468_0_0_1; -.
DR   InParanoid; Q07897; -.
DR   OMA; RILCCTP; -.
DR   BioCyc; YEAST:G3O-32164-MON; -.
DR   PRO; PR:Q07897; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q07897; protein.
DR   GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   InterPro; IPR032704; Cms1.
DR   PANTHER; PTHR24030; PTHR24030; 1.
DR   Pfam; PF14617; CMS1; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..291
FT                   /note="Protein CMS1"
FT                   /id="PRO_0000247153"
FT   REGION          22..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
SQ   SEQUENCE   291 AA;  33394 MW;  85BF73700FE0D986 CRC64;
     MSNPDDLDDG LAYDFDAEHE VIFDAKDGSP PTKKVQKRSI EQDDDDVDDI DGKKEERNSE
     DDSNRPISKR QKKLQKKSKL IEKKKEESQY IVSQRKALPA SSPEKIIEYL TTLIREKNPD
     LSVLELEELY FKRNDFLSTE KFDAERRLSN FPAFIQKFSV APKKIVFSMS NIRVADVYRS
     LNGGKNCVKL FSKSKLKDDI ATVERLLTDS SKKSNKNKDS LYFIATPTRM QKIIEATDLL
     FQGKEKLDII LDASYLDPKD NTILSFENAA VLCQVLKTFL NKKSSVKILL Y
 
 
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