GENTAUR Molecular Products.

 DIG1_YEAST              Reviewed;         452 AA.
 Q03063; D6W3W5;
 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
 01-NOV-1996, sequence version 1.
 28-MAR-2018, entry version 143.
 RecName: Full=Down-regulator of invasive growth 1;
 AltName: Full=Regulator of STE12 protein 1;
 AltName: Full=Regulator of sterile twelve 1;
 Name=DIG1; Synonyms=RST1; OrderedLocusNames=YPL049C;
 ORFNames=P7102.02;
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
 Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
 Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
 NCBI_TaxID=559292;
 [1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=ATCC 204508 / S288c;
 PubMed=9169875;
 Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
 Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
 Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
 Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
 Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
 Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
 Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
 Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
 Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
 Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
 Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
 Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
 Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
 Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
 Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
 Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
 Zollner A., Vo D.H., Hani J.;
 "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
 Nature 387:103-105(1997).
 [2]
 GENOME REANNOTATION.
 STRAIN=ATCC 204508 / S288c;
 PubMed=24374639; DOI=10.1534/g3.113.008995;
 Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
 Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
 Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
 Cherry J.M.;
 "The reference genome sequence of Saccharomyces cerevisiae: Then and
 now.";
 G3 (Bethesda) 4:389-398(2014).
 [3]
 FUNCTION, INTERACTION WITH STE12 AND KSS1, AND PHOSPHORYLATION BY
 KSS1.
 PubMed=8918885; DOI=10.1101/gad.10.22.2831;
 Cook J.G., Bardwell L., Kron S.J., Thorner J.;
 "Two novel targets of the MAP kinase Kss1 are negative regulators of
 invasive growth in the yeast Saccharomyces cerevisiae.";
 Genes Dev. 10:2831-2848(1996).
 [4]
 FUNCTION, COMPLEX WITH DIG2; FUS3 AND STE12, AND INTERACTION WITH CLN1
 AND CLN2.
 PubMed=9094309; DOI=10.1016/S0960-9822(06)00118-7;
 Tedford K., Kim S., Sa D., Stevens K., Tyers M.;
 "Regulation of the mating pheromone and invasive growth responses in
 yeast by two MAP kinase substrates.";
 Curr. Biol. 7:228-238(1997).
 [5]
 FUNCTION, AND COMPLEX WITH DIG2; KSS1 AND STE12.
 PubMed=9744865; DOI=10.1101/gad.12.18.2887;
 Bardwell L., Cook J.G., Voora D., Baggott D.M., Martinez A.R.,
 Thorner J.;
 "Repression of yeast Ste12 transcription factor by direct binding of
 unphosphorylated Kss1 MAPK and its regulation by the Ste7 MEK.";
 Genes Dev. 12:2887-2898(1998).
 [6]
 FUNCTION.
 PubMed=9860980; DOI=10.1073/pnas.95.26.15400;
 Bardwell L., Cook J.G., Zhu-Shimoni J.X., Voora D., Thorner J.;
 "Differential regulation of transcription: repression by unactivated
 mitogen-activated protein kinase Kss1 requires the Dig1 and Dig2
 proteins.";
 Proc. Natl. Acad. Sci. U.S.A. 95:15400-15405(1998).
 [7]
 FUNCTION, AND INTERACTION WITH STE12.
 PubMed=10825185; DOI=10.1128/MCB.20.12.4199-4209.2000;
 Olson K.A., Nelson C., Tai G., Hung W., Yong C., Astell C.,
 Sadowski I.;
 "Two regulators of Ste12p inhibit pheromone-responsive transcription
 by separate mechanisms.";
 Mol. Cell. Biol. 20:4199-4209(2000).
 [8]
 FUNCTION, PHOSPHORYLATION BY FUS3, AND REPRESSION OF HAPLOID SPECIFIC
 AND A-SPECIFIC GENES.
 PubMed=12410840; DOI=10.1046/j.1365-2958.2002.03213.x;
 Gelli A.;
 "Rst1 and Rst2 are required for the a/alpha diploid cell type in
 yeast.";
 Mol. Microbiol. 46:845-854(2002).
 [9]
 FUNCTION, AND INTERACTION WITH STE12.
 PubMed=12732146; DOI=10.1016/S0092-8674(03)00301-5;
 Zeitlinger J., Simon I., Harbison C.T., Hannett N.M., Volkert T.L.,
 Fink G.R., Young R.A.;
 "Program-specific distribution of a transcription factor dependent on
 partner transcription factor and MAPK signaling.";
 Cell 113:395-404(2003).
 [10]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
 PubMed=14562106; DOI=10.1038/nature02046;
 Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
 Dephoure N., O'Shea E.K., Weissman J.S.;
 "Global analysis of protein expression in yeast.";
 Nature 425:737-741(2003).
 [11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION
 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 STRAIN=YAL6B;
 PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
 Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
 Mann M., Jensen O.N.;
 "Quantitative phosphoproteomics applied to the yeast pheromone
 signaling pathway.";
 Mol. Cell. Proteomics 4:310-327(2005).
 [12]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-275, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 STRAIN=ADR376;
 PubMed=17330950; DOI=10.1021/pr060559j;
 Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
 Elias J.E., Gygi S.P.;
 "Large-scale phosphorylation analysis of alpha-factor-arrested
 Saccharomyces cerevisiae.";
 J. Proteome Res. 6:1190-1197(2007).
 [13]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-272; SER-330
 AND SER-428, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
 Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
 "A multidimensional chromatography technology for in-depth
 phosphoproteome analysis.";
 Mol. Cell. Proteomics 7:1389-1396(2008).
 [14]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-126; SER-272 AND
 THR-379, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 PubMed=19779198; DOI=10.1126/science.1172867;
 Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
 "Global analysis of Cdk1 substrate phosphorylation sites provides
 insights into evolution.";
 Science 325:1682-1686(2009).
 -!- FUNCTION: DIG1 and DIG2 are negative regulators of the
     filamentation and pheromone induced mating program. DIG1 and DIG2
     inhibit the transcriptional activity of STE12 by direct protein-
     protein interaction. DIG1 colocalizes to promoters with STE12 and
     redistributes with it during induction of filamentation (by
     butanol) or mating (by pheromone) to program specific genes, but
     binding of DIG1 to STE12 is reduced by pheromone treatment.
     {ECO:0000269|PubMed:10825185, ECO:0000269|PubMed:12410840,
     ECO:0000269|PubMed:12732146, ECO:0000269|PubMed:8918885,
     ECO:0000269|PubMed:9094309, ECO:0000269|PubMed:9744865,
     ECO:0000269|PubMed:9860980}.
 -!- SUBUNIT: Forms a complex with DIG2, STE12 and either FUS3 or KSS1.
     The interaction of FUS3 with STE12 depends on the presence of both
     DIG1 and DIG2. STE12 is lost from FUS3/DIG1/DIG2 complex after
     pheromone treatment. DIG1 and DIG2 have also been reported to
     interact with CLN1 and CLN2.
 -!- INTERACTION:
     Q03373:DIG2; NbExp=5; IntAct=EBI-29752, EBI-34019;
     O14641:DVL2 (xeno); NbExp=3; IntAct=EBI-29752, EBI-740850;
     P14681:KSS1; NbExp=5; IntAct=EBI-29752, EBI-9945;
     P23497-2:SP100 (xeno); NbExp=3; IntAct=EBI-29752, EBI-6589365;
     P13574:STE12; NbExp=7; IntAct=EBI-29752, EBI-18264;
     P63279:UBE2I (xeno); NbExp=3; IntAct=EBI-29752, EBI-80168;
 -!- SUBCELLULAR LOCATION: Nucleus.
 -!- PTM: Phosphorylated by FUS3 and KSS1, in a pheromone-stimulated
     manner. Phosphorylation reduces the affinity for STE12.
     {ECO:0000269|PubMed:12410840, ECO:0000269|PubMed:8918885}.
 -!- MISCELLANEOUS: Present with 5000 molecules/cell in log phase SD
     medium (5480 according to TAP-tag study).
     {ECO:0000269|PubMed:14562106}.
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 EMBL; U44030; AAB68172.1; -; Genomic_DNA.
 EMBL; BK006949; DAA11381.1; -; Genomic_DNA.
 PIR; S62027; S62027.
 RefSeq; NP_015276.1; NM_001183863.1.
 ProteinModelPortal; Q03063; -.
 BioGrid; 36131; 199.
 DIP; DIP-1291N; -.
 IntAct; Q03063; 72.
 MINT; Q03063; -.
 STRING; 4932.YPL049C; -.
 iPTMnet; Q03063; -.
 MaxQB; Q03063; -.
 PaxDb; Q03063; -.
 PRIDE; Q03063; -.
 EnsemblFungi; YPL049C; YPL049C; YPL049C.
 GeneID; 856058; -.
 KEGG; sce:YPL049C; -.
 EuPathDB; FungiDB:YPL049C; -.
 SGD; S000005970; DIG1.
 InParanoid; Q03063; -.
 KO; K11241; -.
 OMA; ADHEDSE; -.
 OrthoDB; EOG092C2EWD; -.
 BioCyc; YEAST:G3O-33962-MONOMER; -.
 PRO; PR:Q03063; -.
 Proteomes; UP000002311; Chromosome XVI.
 GO; GO:0005634; C:nucleus; IDA:SGD.
 GO; GO:1990526; C:Ste12p-Dig1p-Dig2p complex; IDA:SGD.
 GO; GO:1990527; C:Tec1p-Ste12p-Dig1p complex; IDA:SGD.
 GO; GO:0008134; F:transcription factor binding; IDA:SGD.
 GO; GO:2000218; P:negative regulation of invasive growth in response to glucose limitation; IGI:SGD.
 GO; GO:1900240; P:negative regulation of phenotypic switching; IMP:SGD.
 GO; GO:2000221; P:negative regulation of pseudohyphal growth; IGI:SGD.
 GO; GO:0046020; P:negative regulation of transcription from RNA polymerase II promoter by pheromones; IGI:SGD.
 1: Evidence at protein level;
 Complete proteome; Nucleus; Phosphoprotein; Reference proteome.
 CHAIN         1    452       Down-regulator of invasive growth 1.
                              /FTId=PRO_0000079897.
 REGION      212    452       Interaction with FUS3 and KSS1.
                              {ECO:0000269|PubMed:8918885}.
 MOD_RES      45     45       Phosphoserine.
                              {ECO:0000244|PubMed:19779198}.
 MOD_RES     126    126       Phosphoserine.
                              {ECO:0000244|PubMed:19779198}.
 MOD_RES     142    142       Phosphoserine.
                              {ECO:0000244|PubMed:18407956}.
 MOD_RES     272    272       Phosphoserine.
                              {ECO:0000244|PubMed:17330950,
                              ECO:0000244|PubMed:18407956,
                              ECO:0000244|PubMed:19779198}.
 MOD_RES     275    275       Phosphoserine.
                              {ECO:0000244|PubMed:17330950}.
 MOD_RES     330    330       Phosphoserine.
                              {ECO:0000244|PubMed:18407956}.
 MOD_RES     379    379       Phosphothreonine.
                              {ECO:0000244|PubMed:19779198}.
 MOD_RES     395    395       Phosphoserine.
                              {ECO:0000244|PubMed:15665377}.
 MOD_RES     428    428       Phosphoserine.
                              {ECO:0000244|PubMed:18407956}.
 SEQUENCE   452 AA;  49356 MW;  2D27F9878BFADD30 CRC64;
 MAVSARLRTT AEDTSIAKST QDPIGDTEIS VANAKGSSDS NIKNSPGGNS VGQESELEHV
 PEEDDSGDKE ADHEDSETAT AKKRKAQPLK NPKKSLKRGR VPAPLNLSDS NTNTHGGNIK
 DGNLASSNSA HFPPVANQNV KSAPAQVTQH SKFQPRVQYL GKASSRQSIQ VNNSSNSYGK
 PHMPSAGIMS AMNPYMPMNR YIMSPYYNPY GIPPPHMLNK PIMTPYVSYP YPMGPRTSIP
 YAMQGGNARP YEENEYSASN YRNKRVNDSY DSPLSGTAST GKTRRSEEGS RNSSVGSSAN
 AGPTQQRADL RPADMIPAEE YHFERDALLS ANTKARSAST STSTSTSTNR DRSSWHEAEP
 NKDEEEGTDL AIEDGAVPTP TFTTFQRTSQ PQQQSPSLLQ GEIRLSSHIF AFEFPLSSSN
 VDKKMFMSIC NKVWNESKEL TKKSSSHHRT GK

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