TOS4_YEAST
ID TOS4_YEAST Reviewed; 489 AA.
AC Q06266; D6VYI7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein TOS4;
DE AltName: Full=Target of SBF protein 4;
GN Name=TOS4; OrderedLocusNames=YLR183C; ORFNames=L94705.22;
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 INDUCTION.
RX PubMed=11206552; DOI=10.1038/35054095;
RA Iyer V.R., Horak C.E., Scafe C.S., Botstein D., Snyder M., Brown P.O.;
RT "Genomic binding sites of the yeast cell-cycle transcription factors SBF
RT and MBF.";
RL Nature 409:533-538(2001).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=12464632; DOI=10.1101/gad.1039602;
RA Horak C.E., Luscombe N.M., Qian J., Bertone P., Piccirrillo S.,
RA Gerstein M., Snyder M.;
RT "Complex transcriptional circuitry at the G1/S transition in Saccharomyces
RT cerevisiae.";
RL Genes Dev. 16:3017-3033(2002).
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 BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [7]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15282802; DOI=10.1002/yea.1133;
RA Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.;
RT "Localization of proteins that are coordinately expressed with Cln2 during
RT the cell cycle.";
RL Yeast 21:793-800(2004).
RN [8]
RP INDUCTION.
RX PubMed=15965243; DOI=10.1534/genetics.105.044560;
RA Bean J.M., Siggia E.D., Cross F.R.;
RT "High functional overlap between MluI cell-cycle box binding factor and
RT Swi4/6 cell-cycle box binding factor in the G1/S transcriptional program in
RT Saccharomyces cerevisiae.";
RL Genetics 171:49-61(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, 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).
CC -!- FUNCTION: Binds to the promoters of genes with functions important for
CC the G1/S (start) transition; primarily genes involved in pheromone
CC response, polarized growth and transcription.
CC {ECO:0000269|PubMed:12464632}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15282802}.
CC -!- INDUCTION: Regulated in a cell cycle-dependent manner, peaking in G1
CC phase. Appears exclusively during the G1 and S phases (at protein
CC level). Negatively regulated by transcription factor SBF (SWI4-SWI6
CC cell-cycle box binding factor). {ECO:0000269|PubMed:11206552,
CC ECO:0000269|PubMed:12464632, ECO:0000269|PubMed:15282802,
CC ECO:0000269|PubMed:15965243}.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- MISCELLANEOUS: Present with 284 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PLM2/TOS4 family. {ECO:0000305}.
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DR EMBL; U17246; AAB67474.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09503.1; -; Genomic_DNA.
DR PIR; S51428; S51428.
DR RefSeq; NP_013284.1; NM_001182070.1.
DR AlphaFoldDB; Q06266; -.
DR BioGRID; 31454; 64.
DR DIP; DIP-4800N; -.
DR IntAct; Q06266; 4.
DR STRING; 4932.YLR183C; -.
DR iPTMnet; Q06266; -.
DR MaxQB; Q06266; -.
DR PaxDb; Q06266; -.
DR PRIDE; Q06266; -.
DR EnsemblFungi; YLR183C_mRNA; YLR183C; YLR183C.
DR GeneID; 850880; -.
DR KEGG; sce:YLR183C; -.
DR SGD; S000004173; TOS4.
DR VEuPathDB; FungiDB:YLR183C; -.
DR eggNOG; ENOG502RZJP; Eukaryota.
DR GeneTree; ENSGT00940000176669; -.
DR HOGENOM; CLU_027153_0_0_1; -.
DR InParanoid; Q06266; -.
DR OMA; ANDEYPT; -.
DR BioCyc; YEAST:G3O-32307-MON; -.
DR PRO; PR:Q06266; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06266; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:SGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:SGD.
DR CDD; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..489
FT /note="Protein TOS4"
FT /id="PRO_0000262748"
FT DOMAIN 118..170
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 489 AA; 55468 MW; 1C8FE885E8269297 CRC64;
MSSQFPSSPY RTVDPYSPPN YKQQPNCPSS NYEKAGKTAS ESIGNFGKGD YPTPFPSSSI
GRVSSPVRSN KVDAIPSSPA FPGQLAETSP KFSSKLSSPS RHTRVINAEL DPSKISTITV
GRNSSQCDVA LCKNKFISRV HASITYLPQT NEVKIHCFSM NGLIVTYRKQ FDCYQLKDTM
NNNNRAYRLV PRFSNEKCVK EIQDEGGFIN FTLEEGDTVY MTYYKGIMLD FRQVLLRISL
KEKNSSSEPL RFEKKAEFES ESETKHMGSI RKHPLIFTDT SMDRPKKILK DSNKISIGSD
SGVAERMLNH FLNSKSSPLS SVSSVDHEEQ TLRQDSLSSD KNPMTMKKPK LNKRVLPSKP
KKSVKENLDE LSRRNIDVMH LQHILTNHLA FANVQQTPLF QLQQVNSQIS ELSRDELRSI
LSDAKCVGVI YRHGKDAAGK PLDEEYFYDL ENDDDYERRN LVSSLKGGRT GLRSCRRTHK
QYFWKKPAK
