WHI2_YEAST
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 03-AUG-2022, entry version 162.
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; 381.
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 iPTMnet; P12611; -.
DR MaxQB; P12611; -.
DR PaxDb; P12611; -.
DR PRIDE; P12611; -.
DR EnsemblFungi; YOR043W_mRNA; YOR043W; YOR043W.
DR GeneID; 854208; -.
DR KEGG; sce:YOR043W; -.
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 BioCyc; YEAST:G3O-33587-MON; -.
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:0000422; P:autophagy of mitochondrion; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; 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:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; 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 Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR SUPFAM; SSF54695; SSF54695; 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
