WHI5_YEAST
ID WHI5_YEAST Reviewed; 295 AA.
AC Q12416; D6W2E5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=G1-specific transcriptional repressor WHI5;
GN Name=WHI5; OrderedLocusNames=YOR083W; ORFNames=YOR3116W;
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].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 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 [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, PHOSPHORYLATION AT THR-47; SER-59; SER-62; SER-161 AND SER-262,
RP INTERACTION WITH SBF, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15210110; DOI=10.1016/j.cell.2004.05.025;
RA de Bruin R.A.M., McDonald W.H., Kalashnikova T.I., Yates J. III,
RA Wittenberg C.;
RT "Cln3 activates G1-specific transcription via phosphorylation of the SBF
RT bound repressor Whi5.";
RL Cell 117:887-898(2004).
RN [9]
RP FUNCTION, PHOSPHORYLATION BY CDC28, INTERACTION WITH MBF AND SBF, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15210111; DOI=10.1016/j.cell.2004.05.024;
RA Costanzo M., Nishikawa J.L., Tang X., Millman J.S., Schub O.,
RA Breitkreuz K., Dewar D., Rupes I., Andrews B., Tyers M.;
RT "CDK activity antagonizes Whi5, an inhibitor of G1/S transcription in
RT yeast.";
RL Cell 117:899-913(2004).
RN [10]
RP INDUCTION.
RX PubMed=16912276; DOI=10.1101/gad.1450606;
RA Pramila T., Wu W., Miles S., Noble W.S., Breeden L.L.;
RT "The Forkhead transcription factor Hcm1 regulates chromosome segregation
RT genes and fills the S-phase gap in the transcriptional circuitry of the
RT cell cycle.";
RL Genes Dev. 20:2266-2278(2006).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-115; SER-154 AND
RP SER-156, AND 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; SER-59; SER-62; SER-88;
RP SER-113; SER-115; SER-154; SER-156; SER-288 AND THR-290, AND IDENTIFICATION
RP 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: Transcriptional repressor that negatively regulates G1-
CC specific, SBF- and MBF-dependent transcription. Binds via SBF to
CC promoters of G1-specific genes to repress transcription in early G1.
CC During G1, phosphorylated by cyclin-CDK CLN3-CDC28 and progressively
CC hyperphosphorylated by CDK associated with other G1-cyclins, which
CC leads to dissociation of WHI5 from SBF, activating SBF-dependent
CC transcription in late G1. Elimination of CDK activity at the end of
CC mitosis by the mitotic exit network (MEN) allows WHI5 to reassociate
CC with SBF to again repress G1/S transcription.
CC {ECO:0000269|PubMed:15210110, ECO:0000269|PubMed:15210111}.
CC -!- SUBUNIT: Interacts with the heterodimeric transcription factors SBF
CC (SWI4-SWI6 cell-cycle box binding factor) and MBF (MluI cell-cycle box
CC binding factor), each composed of the transcriptional coactivator SWI6
CC and a sequence-specific DNA-binding protein SWI4 or MBP1, respectively.
CC {ECO:0000269|PubMed:15210110, ECO:0000269|PubMed:15210111}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:15210111}. Note=Shuttles in a cell cycle-regulated
CC manner. Localizes to the nucleus, where it is associated with SBF-
CC dependent promoters. In late G1 phase, phosphorylation by G1-specific
CC cyclin-CDK causes its export to the cytoplasm. Elimination of CDK
CC activity at the end of mitosis allows WHI5 to reenter the nucleus.
CC {ECO:0000269|PubMed:15210111}.
CC -!- INDUCTION: By transcription factor HCM1 during S phase.
CC {ECO:0000269|PubMed:16912276}.
CC -!- PTM: Phosphorylation by the cyclin-dependent kinase (CDK) CDC28
CC controls both subcellular location and association of WHI5 with SBF.
CC {ECO:0000269|PubMed:14574415, ECO:0000269|PubMed:15210110,
CC ECO:0000269|PubMed:15210111}.
CC -!- MISCELLANEOUS: Present with 1440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WHI5/NRM1 family. {ECO:0000305}.
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DR EMBL; X94335; CAA64005.1; -; Genomic_DNA.
DR EMBL; Z74990; CAA99277.1; -; Genomic_DNA.
DR EMBL; AY558033; AAS56359.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10861.1; -; Genomic_DNA.
DR PIR; S61644; S61644.
DR RefSeq; NP_014726.1; NM_001183502.1.
DR AlphaFoldDB; Q12416; -.
DR BioGRID; 34481; 385.
DR DIP; DIP-8958N; -.
DR IntAct; Q12416; 7.
DR MINT; Q12416; -.
DR STRING; 4932.YOR083W; -.
DR CarbonylDB; Q12416; -.
DR iPTMnet; Q12416; -.
DR MaxQB; Q12416; -.
DR PaxDb; Q12416; -.
DR PRIDE; Q12416; -.
DR EnsemblFungi; YOR083W_mRNA; YOR083W; YOR083W.
DR GeneID; 854249; -.
DR KEGG; sce:YOR083W; -.
DR SGD; S000005609; WHI5.
DR VEuPathDB; FungiDB:YOR083W; -.
DR eggNOG; ENOG502RW1U; Eukaryota.
DR HOGENOM; CLU_082190_0_0_1; -.
DR InParanoid; Q12416; -.
DR OMA; DENEENX; -.
DR BioCyc; YEAST:G3O-33619-MON; -.
DR PRO; PR:Q12416; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12416; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0033309; C:SBF transcription complex; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD.
DR GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0008361; P:regulation of cell size; HMP:SGD.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR InterPro; IPR039198; Srl3/Whi5.
DR InterPro; IPR013734; TF_Nrm1/Whi5.
DR PANTHER; PTHR28246; PTHR28246; 2.
DR Pfam; PF08528; Whi5; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..295
FT /note="G1-specific transcriptional repressor WHI5"
FT /id="PRO_0000262757"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15210110"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15210110,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15210110,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15210110"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15210110"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 290
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 295 AA; 32901 MW; 013A41AC5DC1975F CRC64;
MSLRTPKRSR TSDEQEQEQE QEQVQNPDTH VNNEHQQRPG PTTLLSTPVR LKNGFGTPSP
PSPPGITKSI TKSRRRPSTT SLQGIFMSPV NKRRVGITAH GRVYDHNDDG HESESEDDEN
EEENENQKKY DGHVSMPLLP PTTPKSRRSE VFLSPSPRLR SPPTAARRST GERPIREISH
TLRTRLNYAL VKLQNGWTDK TLPELETELA PAVQTPPRRY HNRFPDSADA GTSAHTAFLQ
ALGGHPPREE ATAVETLMLL SSPTKKQQHR PVPATSAGEP TDETEPESDT EVETS
