STE12_YEAST
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 03-AUG-2022, entry version 191.
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; 108.
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; P13574; -.
DR PRIDE; P13574; -.
DR EnsemblFungi; YHR084W_mRNA; YHR084W; YHR084W.
DR GeneID; 856484; -.
DR KEGG; sce:YHR084W; -.
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 BioCyc; YEAST:G3O-31131-MON; -.
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; IC: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; IC: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 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
