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Down-regulator of invasive growth 1 (Regulator of STE12 protein 1) (Regulator of sterile twelve 1)

 DIG1_YEAST              Reviewed;         452 AA.
Q03063; D6W3W5;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 140.
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;
P14681:KSS1; NbExp=5; IntAct=EBI-29752, EBI-9945;
P13574:STE12; NbExp=6; IntAct=EBI-29752, EBI-18264;
-!- 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; 197.
DIP; DIP-1291N; -.
IntAct; Q03063; 64.
MINT; MINT-393786; -.
STRING; 4932.YPL049C; -.
iPTMnet; Q03063; -.
MaxQB; 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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