MSN2_YEAST
ID MSN2_YEAST Reviewed; 704 AA.
AC P33748; D6VZL2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Zinc finger protein MSN2;
DE AltName: Full=Multicopy suppressor of SNF1 protein 2;
GN Name=MSN2; OrderedLocusNames=YMR037C; ORFNames=YM9532.02C;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8321194; DOI=10.1128/mcb.13.7.3872-3881.1993;
RA Estruch F., Carlson M.;
RT "Two homologous zinc finger genes identified by multicopy suppression in a
RT SNF1 protein kinase mutant of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 13:3872-3881(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 CHARACTERIZATION.
RX PubMed=8641288; DOI=10.1002/j.1460-2075.1996.tb00576.x;
RA Martinez-Pastor M.T., Marchler G., Schueller C., Marchler-Bauer A.,
RA Ruis H., Estruch F.;
RT "The Saccharomyces cerevisiae zinc finger proteins Msn2p and Msn4p are
RT required for transcriptional induction through the stress response element
RT (STRE).";
RL EMBO J. 15:2227-2235(1996).
RN [5]
RP INTERACTION WITH WHI2, AND PHOSPHORYLATION.
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 [6]
RP NUCLEOCYTOPLASMIC SHUTTLING.
RX PubMed=12732613; DOI=10.1083/jcb.200303030;
RA Jacquet M., Renault G., Lallet S., De Mey J., Goldbeter A.;
RT "Oscillatory nucleocytoplasmic shuttling of the general stress response
RT transcriptional activators Msn2 and Msn4 in Saccharomyces cerevisiae.";
RL J. Cell Biol. 161:497-505(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-633, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288 AND SER-451, AND
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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-304; SER-451;
RP SER-582 AND SER-633, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [12]
RP DOMAIN.
RX PubMed=27618436; DOI=10.1371/journal.pone.0162842;
RA Piskacek M., Havelka M., Rezacova M., Knight A.;
RT "The 9aaTAD transactivation domains: From Gal4 to p53.";
RL PLoS ONE 11:E0162842-E0162842(2016).
CC -!- FUNCTION: Positive transcriptional factor that acts as a component of
CC the stress responsive system. Recognizes and binds to the stress
CC response element (STRE) which is involved in the response to various
CC forms of stress (heat, oxidative, osmotic, etc.). Involved in the
CC regulation of the CTT1, DDR2, HSP12 genes. May be regulated via WHI2-
CC PSR1 complex phosphatase activity.
CC -!- SUBUNIT: Interacts with WHI2. {ECO:0000269|PubMed:12090248}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: The 9aaTAD motif (residues 261 to 269) is a transactivation
CC domain present in a large number of yeast and animal transcription
CC factors. {ECO:0000305|PubMed:27618436}.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; L08838; AAA34806.1; -; Genomic_DNA.
DR EMBL; Z48502; CAA88403.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09936.1; -; Genomic_DNA.
DR PIR; S39004; S39004.
DR RefSeq; NP_013751.1; NM_001182534.1.
DR AlphaFoldDB; P33748; -.
DR SMR; P33748; -.
DR BioGRID; 35209; 186.
DR DIP; DIP-8185N; -.
DR IntAct; P33748; 64.
DR MINT; P33748; -.
DR STRING; 4932.YMR037C; -.
DR iPTMnet; P33748; -.
DR MaxQB; P33748; -.
DR PaxDb; P33748; -.
DR PRIDE; P33748; -.
DR EnsemblFungi; YMR037C_mRNA; YMR037C; YMR037C.
DR GeneID; 855053; -.
DR KEGG; sce:YMR037C; -.
DR SGD; S000004640; MSN2.
DR VEuPathDB; FungiDB:YMR037C; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000174779; -.
DR HOGENOM; CLU_024342_0_0_1; -.
DR InParanoid; P33748; -.
DR OMA; AIDINEM; -.
DR BioCyc; YEAST:G3O-32742-MON; -.
DR PRO; PR:P33748; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P33748; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0080144; P:amino acid homeostasis; IDA:SGD.
DR GO; GO:0071483; P:cellular response to blue light; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IGI:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0061402; P:positive regulation of transcription from RNA polymerase II promoter in response to acidic pH; IMP:SGD.
DR GO; GO:0061422; P:positive regulation of transcription from RNA polymerase II promoter in response to alkaline pH; IGI:SGD.
DR GO; GO:0061412; P:positive regulation of transcription from RNA polymerase II promoter in response to amino acid starvation; IGI:SGD.
DR GO; GO:0061395; P:positive regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance; IGI:SGD.
DR GO; GO:0061411; P:positive regulation of transcription from RNA polymerase II promoter in response to cold; IGI:SGD.
DR GO; GO:0061410; P:positive regulation of transcription from RNA polymerase II promoter in response to ethanol; IGI:SGD.
DR GO; GO:0061409; P:positive regulation of transcription from RNA polymerase II promoter in response to freezing; IGI:SGD.
DR GO; GO:0061406; P:positive regulation of transcription from RNA polymerase II promoter in response to glucose starvation; IGI:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
DR GO; GO:0061407; P:positive regulation of transcription from RNA polymerase II promoter in response to hydrogen peroxide; IMP:SGD.
DR GO; GO:0061405; P:positive regulation of transcription from RNA polymerase II promoter in response to hydrostatic pressure; IGI:SGD.
DR GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; IGI:SGD.
DR GO; GO:0061403; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrosative stress; IGI:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:SGD.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..704
FT /note="Zinc finger protein MSN2"
FT /id="PRO_0000046810"
FT ZN_FING 647..665
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 676..698
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 84..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 261..269
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:27618436"
FT COMPBIAS 94..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 704 AA; 77861 MW; EDF6F07446819DF1 CRC64;
MTVDHDFNSE DILFPIESMS SIQYVENNNP NNINNDVIPY SLDIKNTVLD SADLNDIQNQ
ETSLNLGLPP LSFDSPLPVT ETIPSTTDNS LHLKADSNKN RDARTIENDS EIKSTNNASG
SGANQYTTLT SPYPMNDILY NMNNPLQSPS PSSVPQNPTI NPPINTASNE TNLSPQTSNG
NETLISPRAQ QHTSIKDNRL SLPNGANSNL FIDTNPNNLN EKLRNQLNSD TNSYSNSISN
SNSNSTGNLN SSYFNSLNID SMLDDYVSSD LLLNDDDDDT NLSRRRFSDV ITNQFPSMTN
SRNSISHSLD LWNHPKINPS NRNTNLNITT NSTSSSNASP NTTTMNANAD SNIAGNPKNN
DATIDNELTQ ILNEYNMNFN DNLGTSTSGK NKSACPSSFD ANAMTKINPS QQLQQQLNRV
QHKQLTSSHN NSSTNMKSFN SDLYSRRQRA SLPIIDDSLS YDLVNKQDED PKNDMLPNSN
LSSSQQFIKP SMILSDNASV IAKVATTGLS NDMPFLTEEG EQNANSTPNF DLSITQMNMA
PLSPASSSST SLATNHFYHH FPQQGHHTMN SKIGSSLRRR KSAVPLMGTV PLTNQQNNIS
SSSVNSTGNG AGVTKERRPS YRRKSMTPSR RSSVVIESTK ELEEKPFHCH ICPKSFKRSE
HLKRHVRSVH SNERPFACHI CDKKFSRSDN LSQHIKTHKK HGDI
