ID   STE12_YEAST             Reviewed;         688 AA.
AC   P13574; D3DL35;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 197.
DE   RecName: Full=Protein STE12;
GN   Name=STE12; OrderedLocusNames=YHR084W;
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=2668945; DOI=10.1073/pnas.86.15.5703;
RA   Dolan J.W., Kirkman C., Fields S.;
RT   "The yeast STE12 protein binds to the DNA sequence mediating pheromone
RT   induction.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:5703-5707(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2558054; DOI=10.1101/gad.3.9.1349;
RA   Errede B., Ammerer G.;
RT   "STE12, a protein involved in cell-type-specific transcription and signal
RT   transduction in yeast, is part of protein-DNA complexes.";
RL   Genes Dev. 3:1349-1361(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [4]
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   [5]
RP   DNA-BINDING DOMAIN.
RX   PubMed=1944269; DOI=10.1128/mcb.11.12.5910-5918.1991;
RA   Yuan Y.-L., Fields S.;
RT   "Properties of the DNA-binding domain of the Saccharomyces cerevisiae STE12
RT   protein.";
RL   Mol. Cell. Biol. 11:5910-5918(1991).
RN   [6]
RP   INTERACTION WITH ALPHA1.
RX   PubMed=8339934; DOI=10.1101/gad.7.8.1584;
RA   Yuan Y.-L.O., Stroke I., Fields S.;
RT   "Coupling of cell identity to signal response in yeast: interaction between
RT   the alpha-1 and STE12 proteins.";
RL   Genes Dev. 7:1584-1597(1993).
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 THR-29; SER-226 AND SER-400, 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-29; SER-226 AND THR-289, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-226 AND SER-400, AND
RP   IDENTIFICATION 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).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Binds to the DNA sequence mediating pheromone induction
CC       (called the pheromone response element = PRE) which is found in the
CC       upstream control region of several a-, alpha- and haploid-specific
CC       genes. Involved in mating of haploids and in pseudohyphae formation in
CC       diploids.
CC   -!- SUBUNIT: Interacts with mating-type protein ALPHA1.
CC       {ECO:0000269|PubMed:8339934}.
CC   -!- INTERACTION:
CC       P13574; Q03063: DIG1; NbExp=6; IntAct=EBI-18264, EBI-29752;
CC       P13574; Q03373: DIG2; NbExp=9; IntAct=EBI-18264, EBI-34019;
CC       P13574; P14681: KSS1; NbExp=8; IntAct=EBI-18264, EBI-9945;
CC       P13574; P0CY06: MATALPHA1; NbExp=2; IntAct=EBI-18264, EBI-10438;
CC       P13574; Q00772: SLT2; NbExp=2; IntAct=EBI-18264, EBI-17372;
CC       P13574; P18412: TEC1; NbExp=12; IntAct=EBI-18264, EBI-19091;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: The DNA-binding domain seems to be involved in the suppression
CC       of pseudohyphae formation under nitrogen-rich conditions and in
CC       haploids. This region is also involved in the regulation of budding
CC       pattern of haploids.
CC   -!- PTM: Phosphorylated by the STE7, STE11 and STE20 kinases.
CC   -!- MISCELLANEOUS: Present with 1920 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the STE12 transcription factor family.
CC       {ECO:0000305}.
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DR   EMBL; X16112; CAA34246.1; -; Genomic_DNA.
DR   EMBL; M24502; AAA35109.1; -; Genomic_DNA.
DR   EMBL; U10556; AAB68884.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06779.1; -; Genomic_DNA.
DR   PIR; A33540; A33540.
DR   RefSeq; NP_011952.1; NM_001179214.1.
DR   PDB; 3W3W; X-ray; 2.20 A; B=581-649.
DR   PDBsum; 3W3W; -.
DR   AlphaFoldDB; P13574; -.
DR   SMR; P13574; -.
DR   BioGRID; 36519; 114.
DR   ComplexPortal; CPX-575; Ste12/Dig1/Dig2 transcription regulation complex.
DR   ComplexPortal; CPX-576; Tec1/Ste12/Dig1 transcription regulation complex.
DR   DIP; DIP-64N; -.
DR   IntAct; P13574; 24.
DR   MINT; P13574; -.
DR   STRING; 4932.YHR084W; -.
DR   iPTMnet; P13574; -.
DR   MaxQB; P13574; -.
DR   PaxDb; 4932-YHR084W; -.
DR   PeptideAtlas; P13574; -.
DR   EnsemblFungi; YHR084W_mRNA; YHR084W; YHR084W.
DR   GeneID; 856484; -.
DR   KEGG; sce:YHR084W; -.
DR   AGR; SGD:S000001126; -.
DR   SGD; S000001126; STE12.
DR   VEuPathDB; FungiDB:YHR084W; -.
DR   eggNOG; ENOG502QTVR; Eukaryota.
DR   HOGENOM; CLU_019798_0_0_1; -.
DR   InParanoid; P13574; -.
DR   OMA; DIMREDA; -.
DR   OrthoDB; 3023033at2759; -.
DR   BioCyc; YEAST:G3O-31131-MONOMER; -.
DR   BioGRID-ORCS; 856484; 3 hits in 13 CRISPR screens.
DR   PRO; PR:P13574; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P13574; Protein.
DR   GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:1990526; C:Ste12p-Dig1p-Dig2p complex; IDA:SGD.
DR   GO; GO:1990527; C:Tec1p-Ste12p-Dig1p complex; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR   GO; GO:0000747; P:conjugation with cellular fusion; IDA:SGD.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR   GO; GO:0045894; P:negative regulation of mating-type specific transcription, DNA-templated; NAS:ComplexPortal.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR   GO; GO:0010570; P:regulation of filamentous growth; NAS:ComplexPortal.
DR   GO; GO:2000220; P:regulation of pseudohyphal growth; IBA:GO_Central.
DR   GO; GO:0019236; P:response to pheromone; IEA:UniProtKB-KW.
DR   GO; GO:0019953; P:sexual reproduction; IBA:GO_Central.
DR   InterPro; IPR003120; Ste12.
DR   PANTHER; PTHR47427; PROTEIN STE12; 1.
DR   PANTHER; PTHR47427:SF1; PROTEIN STE12; 1.
DR   Pfam; PF02200; STE; 1.
DR   SMART; SM00424; STE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Nucleus; Pheromone response;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..688
FT                   /note="Protein STE12"
FT                   /id="PRO_0000072262"
FT   DNA_BIND        57..167
FT   REGION          177..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          285..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..606
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         29
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         214
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         226
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         289
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         400
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   688 AA;  77867 MW;  EE7371F18BBC0337 CRC64;
     MKVQITNSRT EEILKVQANN ENDEVSKATP GEVEESLRLI GDLKFFLATA PVNWQENQII
     RRYYLNSGQG FVSCVFWNNL YYITGTDIVK CCLYRMQKFG REVVQKKKFE EGIFSDLRNL
     KCGIDATLEQ PKSEFLSFLF RNMCLKTQKK QKVFFWFSVA HDKLFADALE RDLKRESLNQ
     PSTTKPVNEP ALSFSYDSSS DKPLYDQLLQ HLDSRRPSST TKSDNSPPKL ESENFKDNEL
     VTVTNQPLLG VGLMDDDAPE SPSQINDFIP QKLIIEPNTL ELNGLTEETP HDLPKNTAKG
     RDEEDFPLDY FPVSVEYPTE ENAFDPFPPQ AFTPAAPSMP ISYDNVNERD SMPVNSLLNR
     YPYQLSVAPT FPVPPSSSRQ HFMTNRDFYS SNNNKEKLVS PSDPTSYMKY DEPVMDFDES
     RPNENCTNAK SHNSGQQTKQ HQLYSNNFQQ SYPNGMVPGY YPKMPYNPMG GDPLLDQAFY
     GADDFFFPPE GCDNNMLYPQ TATSWNVLPP QAMQPAPTYV GRPYTPNYRS TPGSAMFPYM
     QSSNSMQWNT AVSPYSSRAP STTAKNYPPS TFYSQNINQY PRRRTVGMKS SQGNVPTGNK
     QSVGKSAKIS KPLHIKTSAY QKQYKINLET KARPSAGDED SAHPDKNKEI SMPTPDSNTL
     VVQSEEGGAH SLEVDTNRRS DKNLPDAT
//