ID   WHI2_YEAST              Reviewed;         486 AA.
AC   P12611; D6W2A9; Q08413;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Growth regulation protein;
GN   Name=WHI2; OrderedLocusNames=YOR043W;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=3049245; DOI=10.1016/0378-1119(88)90357-5;
RA   Kelly D.E., Trevethick J., Mountain H., Sudbery P.E.;
RT   "Transcript characterisation, gene disruption and nucleotide sequence of
RT   the Saccharomyces cerevisiae WH12 gene.";
RL   Gene 66:205-213(1988).
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   FUNCTION, AND INTERACTION WITH PSR1 AND MSN2.
RX   PubMed=12090248; DOI=10.1046/j.1365-2443.2002.00538.x;
RA   Kaida D., Yashiroda H., Toh-e A., Kikuchi Y.;
RT   "Yeast Whi2 and Psr1-phosphatase form a complex and regulate STRE-mediated
RT   gene expression.";
RL   Genes Cells 7:543-552(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   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).
CC   -!- FUNCTION: Plays a role in the coordination of growth and proliferation.
CC       Required for entry into G0 phase under conditions of carbon limitation.
CC       Involved in the general stress response; acts together with PSR1 to
CC       activate stress response element (STRE)-mediated gene expression,
CC       possibly through dephosphorylation of MSN2.
CC       {ECO:0000269|PubMed:12090248, ECO:0000269|PubMed:3049245}.
CC   -!- SUBUNIT: Interacts with MSN2 and PSR1. {ECO:0000269|PubMed:12090248}.
CC   -!- INTERACTION:
CC       P12611; Q07800: PSR1; NbExp=4; IntAct=EBI-20530, EBI-31129;
CC   -!- DISRUPTION PHENOTYPE: Negative mutants fail to enter the G0 phase under
CC       conditions of carbon limitation. {ECO:0000269|PubMed:3049245}.
CC   -!- MISCELLANEOUS: Present with 1800 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the WHI2 family. {ECO:0000305}.
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DR   EMBL; M21089; AAA35218.1; -; Genomic_DNA.
DR   EMBL; Z74951; CAA99234.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10825.1; -; Genomic_DNA.
DR   PIR; S66917; COBYW2.
DR   RefSeq; NP_014686.1; NM_001183462.1.
DR   AlphaFoldDB; P12611; -.
DR   BioGRID; 34444; 385.
DR   ComplexPortal; CPX-1317; WHI2-PSR1 phosphatase complex.
DR   ComplexPortal; CPX-1318; WHI2-PSR2 phosphatase complex.
DR   DIP; DIP-2573N; -.
DR   IntAct; P12611; 13.
DR   MINT; P12611; -.
DR   STRING; 4932.YOR043W; -.
DR   CarbonylDB; P12611; -.
DR   GlyGen; P12611; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; P12611; -.
DR   MaxQB; P12611; -.
DR   PaxDb; 4932-YOR043W; -.
DR   PeptideAtlas; P12611; -.
DR   EnsemblFungi; YOR043W_mRNA; YOR043W; YOR043W.
DR   GeneID; 854208; -.
DR   KEGG; sce:YOR043W; -.
DR   AGR; SGD:S000005569; -.
DR   SGD; S000005569; WHI2.
DR   VEuPathDB; FungiDB:YOR043W; -.
DR   eggNOG; ENOG502RXS0; Eukaryota.
DR   GeneTree; ENSGT00390000007074; -.
DR   HOGENOM; CLU_028899_0_1_1; -.
DR   InParanoid; P12611; -.
DR   OMA; IHLNIRG; -.
DR   OrthoDB; 1356419at2759; -.
DR   BioCyc; YEAST:G3O-33587-MONOMER; -.
DR   BioGRID-ORCS; 854208; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P12611; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P12611; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1903293; C:phosphatase complex; IDA:UniProtKB.
DR   GO; GO:0019903; F:protein phosphatase binding; IDA:SGD.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IMP:SGD.
DR   GO; GO:0000423; P:mitophagy; IMP:SGD.
DR   GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:SGD.
DR   GO; GO:1903452; P:positive regulation of G1 to G0 transition; IMP:SGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006470; P:protein dephosphorylation; IMP:UniProtKB.
DR   GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   SUPFAM; SSF54695; POZ domain; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Reference proteome.
FT   CHAIN           1..486
FT                   /note="Growth regulation protein"
FT                   /id="PRO_0000065967"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        216
FT                   /note="F -> L (in Ref. 1; AAA35218)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   486 AA;  55346 MW;  105419D6180207F2 CRC64;
     MDDIITQVSP DNAESAPILQ EQQQQQNSQY EGNEEDYGDS LIHLNIQENH YFITRDQLMS
     LPESLLLCLF PSGVFLDRCG QVITNLTRDD EVYIVNFPPD CFEYIMEIYT KAHDDLYNHP
     VEKFFDRPSS SFVSNAKGFF GLSSNNSISS NNEQDILHQK PAIIVLREDL DYYCVPQEEF
     QFDSTNEENN EDLLRHFMAQ VKMAAGSYLT SKTSIFQGLY SSNRLKQQQQ QQKIEKGSNS
     SSNTKSTSKK LGPAEQHLMD MLCSSGFTKE TCWGNRTQET GKTVISSLSL CRLANETTEG
     FRQKFNEAKA KWEAEHKPSQ DNFITPMQSN ISINSLSASK SNSTISTARN LTSGSTAPAT
     ARDKRKSRLS KLADNVRSHS SSRHSSQTRS KPPELPKLYD LVPKPNINAK LLLFWRKPAR
     KCWWGEEDIE LEVEVFGSWK DESKKIIELI LPTNVDPEAE LHKIIVPVRL HIRRVWTLEL
     SVIGVQ
//