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General control protein GCN4 (Amino acid biosynthesis regulatory protein)

 GCN4_YEAST              Reviewed;         281 AA.
P03069; D3DLN9; P03068; Q70D88; Q70D91; Q70D96; Q70D99; Q70DA0;
Q96UT3;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 194.
RecName: Full=General control protein GCN4;
AltName: Full=Amino acid biosynthesis regulatory protein;
Name=GCN4; Synonyms=AAS3, ARG9; OrderedLocusNames=YEL009C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6387704; DOI=10.1073/pnas.81.20.6442;
Hinnebusch A.G.;
"Evidence for translational regulation of the activator of general
amino acid control in yeast.";
Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6433345; DOI=10.1073/pnas.81.16.5096;
Thireos G., Penn M.D., Greer H.;
"5' untranslated sequences are required for the translational control
of a yeast regulatory gene.";
Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-24; SER-62;
ALA-82; ALA-91; ALA-125 AND GLU-196.
STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
PubMed=15087486; DOI=10.1093/nar/gkh529;
Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
Souciet J.-L.;
"Differential evolution of the Saccharomyces cerevisiae DUP240
paralogs and implication of recombination in phylogeny.";
Nucleic Acids Res. 32:2069-2078(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169868;
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
Nature 387:78-81(1997).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 249-281.
PubMed=11896344; DOI=10.1046/j.1537-2995.2002.00018.x;
Czerwinski M., Krop-Watorek A., Lisowska E., Spitalnik S.L.;
"Construction of dimeric F(ab) useful in blood group serology.";
Transfusion 42:257-264(2002).
[7]
DOMAINS.
PubMed=3530496; DOI=10.1016/0092-8674(86)90070-X;
Hope I.A., Struhl K.;
"Functional dissection of a eukaryotic transcriptional activator
protein, GCN4 of yeast.";
Cell 46:885-894(1986).
[8]
DOMAINS, AND MUTAGENESIS OF 97-PHE-PHE-98; MET-107; TYR-110; LEU-113
AND 120-TRP--PHE-124.
PubMed=7862116; DOI=10.1128/MCB.15.3.1220;
Drysdale C.M., Duenas E., Jackson B.M., Reusser U., Braus G.H.,
Hinnebusch A.G.;
"The transcriptional activator GCN4 contains multiple activation
domains that are critically dependent on hydrophobic amino acids.";
Mol. Cell. Biol. 15:1220-1233(1995).
[9]
PHOSPHORYLATION AT THR-165.
PubMed=12101234; DOI=10.1128/MCB.22.15.5395-5404.2002;
Shemer R., Meimoun A., Holtzman T., Kornitzer D.;
"Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5.";
Mol. Cell. Biol. 22:5395-5404(2002).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-218, 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).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281.
PubMed=1948029; DOI=10.1126/science.1948029;
O'Shea E.K., Klemm J.D., Kim P.S., Alber T.;
"X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel
coiled coil.";
Science 254:539-544(1991).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281.
PubMed=1473154; DOI=10.1016/S0092-8674(05)80070-4;
Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C.;
"The GCN4 basic region leucine zipper binds DNA as a dimer of
uninterrupted alpha helices: crystal structure of the protein-DNA
complex.";
Cell 71:1223-1237(1992).
[13]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281.
PubMed=9837709; DOI=10.1006/jmbi.1998.2214;
Eckert D.M., Malashkevich V.N., Kim P.S.;
"Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried
polar residues.";
J. Mol. Biol. 284:859-865(1998).
[14]
STRUCTURE BY NMR OF 237-281.
PubMed=1891459; DOI=10.1093/protein/4.5.519;
Saudek V., Pastore A., Morelli M.A., Frank R., Gausepohl H.,
Gibson T.;
"The solution structure of a leucine-zipper motif peptide.";
Protein Eng. 4:519-529(1991).
-!- FUNCTION: Is a transcription factor that is responsible for the
activation of more than 30 genes required for amino acid or for
purine biosynthesis in response to amino acid or purine
starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-
3'.
-!- SUBUNIT: Binds DNA as a dimer.
-!- INTERACTION:
Self; NbExp=14; IntAct=EBI-7450, EBI-7450;
P11938:RAP1; NbExp=5; IntAct=EBI-7450, EBI-14821;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- DOMAIN: Residues 89 to 100 and 106 to 125 define the N-terminal
activation domain (NTAD) and the central acidic activation domain
(CAAD) respectively, which can function independently to promote
high-level transcription of the target genes.
{ECO:0000269|PubMed:3530496, ECO:0000269|PubMed:7862116}.
-!- PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation
of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase
complex SCF(Cdc4). {ECO:0000269|PubMed:12101234}.
-!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily.
{ECO:0000305}.
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EMBL; K02205; AAA34640.1; -; Genomic_DNA.
EMBL; K02649; AAA65521.1; -; Genomic_DNA.
EMBL; AJ585686; CAE52206.1; -; Genomic_DNA.
EMBL; AJ585687; CAE52207.1; -; Genomic_DNA.
EMBL; AJ585688; CAE52208.1; -; Genomic_DNA.
EMBL; AJ585689; CAE52209.1; -; Genomic_DNA.
EMBL; AJ585690; CAE52210.1; -; Genomic_DNA.
EMBL; AJ585691; CAE52211.1; -; Genomic_DNA.
EMBL; AJ585692; CAE52212.1; -; Genomic_DNA.
EMBL; AJ585693; CAE52213.1; -; Genomic_DNA.
EMBL; AJ585694; CAE52214.1; -; Genomic_DNA.
EMBL; AJ585695; CAE52215.1; -; Genomic_DNA.
EMBL; AJ585696; CAE52216.1; -; Genomic_DNA.
EMBL; AJ585697; CAE52217.1; -; Genomic_DNA.
EMBL; AJ585698; CAE52218.1; -; Genomic_DNA.
EMBL; AJ585699; CAE52219.1; -; Genomic_DNA.
EMBL; AJ585700; CAE52220.1; -; Genomic_DNA.
EMBL; AJ585701; CAE52221.1; -; Genomic_DNA.
EMBL; AJ585702; CAE52222.1; -; Genomic_DNA.
EMBL; AJ585703; CAE52223.1; -; Genomic_DNA.
EMBL; AJ585704; CAE52224.1; -; Genomic_DNA.
EMBL; AF416613; AAL09032.1; -; mRNA.
EMBL; U18530; AAB64486.1; -; Genomic_DNA.
EMBL; BK006939; DAA07643.1; -; Genomic_DNA.
PIR; A03605; RGBYA2.
RefSeq; NP_010907.3; NM_001178824.3.
PDB; 1CE9; X-ray; 1.80 A; A/B/C/D=251-281.
PDB; 1DGC; X-ray; 3.00 A; A=220-281.
PDB; 1ENV; X-ray; 2.60 A; A=252-280.
PDB; 1FAV; X-ray; 3.00 A; A=252-280.
PDB; 1FMH; NMR; -; A/B=249-279.
PDB; 1GCL; X-ray; 2.10 A; A/B/C/D=249-281.
PDB; 1GCM; X-ray; 1.80 A; A/B/C=249-281.
PDB; 1GK6; X-ray; 1.90 A; A/B=249-279.
PDB; 1GZL; X-ray; 1.80 A; A/B=249-276.
PDB; 1IHQ; NMR; -; A/B=264-281.
PDB; 1IJ0; X-ray; 1.86 A; A/B/C=249-281.
PDB; 1IJ1; X-ray; 1.86 A; A/B/C=249-281.
PDB; 1IJ2; X-ray; 1.70 A; A/B/C=249-281.
PDB; 1IJ3; X-ray; 1.80 A; A/B/C=249-281.
PDB; 1KQL; X-ray; 2.70 A; A/B=255-278.
PDB; 1LD4; EM; 11.40 A; E/F/G/H/I/J/K/L=225-281.
PDB; 1LLM; X-ray; 1.50 A; C/D=253-281.
PDB; 1NKN; X-ray; 2.50 A; A/B/C/D=250-281.
PDB; 1PIQ; X-ray; 1.80 A; A=249-279.
PDB; 1RB4; X-ray; 1.90 A; A/B/C=249-281.
PDB; 1RB5; X-ray; 1.90 A; A/B/C=249-281.
PDB; 1RB6; X-ray; 1.90 A; A/B/C=249-281.
PDB; 1SWI; X-ray; 2.60 A; A/B/C=249-281.
PDB; 1TMZ; NMR; -; A/B=264-281.
PDB; 1UNT; X-ray; 2.07 A; A/B=249-281.
PDB; 1UNU; X-ray; 2.07 A; A/B=249-281.
PDB; 1UNV; X-ray; 2.14 A; A/B=249-281.
PDB; 1UNW; X-ray; 2.20 A; A/B=249-281.
PDB; 1UNX; X-ray; 2.40 A; A/B=249-281.
PDB; 1UNY; X-ray; 2.30 A; A/B=249-281.
PDB; 1UNZ; X-ray; 2.30 A; A/B=249-281.
PDB; 1UO0; X-ray; 2.40 A; A/B=249-281.
PDB; 1UO1; X-ray; 2.50 A; A/B=249-281.
PDB; 1UO2; X-ray; 1.99 A; A/B=249-281.
PDB; 1UO3; X-ray; 1.92 A; A/B=249-281.
PDB; 1UO4; X-ray; 1.70 A; A/B=249-281.
PDB; 1UO5; X-ray; 2.07 A; A/B=249-281.
PDB; 1W5G; X-ray; 2.16 A; A/B=249-281.
PDB; 1W5H; X-ray; 2.50 A; A/B=249-281.
PDB; 1W5I; X-ray; 2.30 A; A/B=249-281.
PDB; 1W5J; X-ray; 2.20 A; A/B/C/D=249-281.
PDB; 1W5K; X-ray; 1.92 A; A/B/C/D=249-281.
PDB; 1W5L; X-ray; 2.17 A; A/B=249-281.
PDB; 1YSA; X-ray; 2.90 A; C/D=226-281.
PDB; 1ZII; X-ray; 1.80 A; A/B=249-281.
PDB; 1ZIJ; X-ray; 2.00 A; A/B/C=249-281.
PDB; 1ZIK; X-ray; 1.80 A; A/B=249-281.
PDB; 1ZIL; X-ray; 2.25 A; A/B=249-281.
PDB; 1ZIM; X-ray; 2.00 A; A/B/C=249-281.
PDB; 1ZTA; NMR; -; A=247-281.
PDB; 2AHP; X-ray; 2.00 A; A/B=249-281.
PDB; 2B1F; X-ray; 1.50 A; A/B/C/D=251-281.
PDB; 2B22; X-ray; 2.00 A; A=251-281.
PDB; 2BNI; X-ray; 1.50 A; A/B/C/D=249-281.
PDB; 2CCE; X-ray; 1.90 A; A/B=249-281.
PDB; 2CCF; X-ray; 1.70 A; A/B=249-281.
PDB; 2CCN; X-ray; 1.60 A; A/B=249-281.
PDB; 2D3E; X-ray; 2.60 A; A/B/C/D=254-277.
PDB; 2DGC; X-ray; 2.20 A; A=220-281.
PDB; 2EFR; X-ray; 1.80 A; A/B/C/D=249-277.
PDB; 2EFS; X-ray; 2.00 A; A/B/C/D=249-277.
PDB; 2G9J; NMR; -; A/B=264-281.
PDB; 2HY6; X-ray; 1.25 A; A/B/C/D/E/F/G=251-281.
PDB; 2IPZ; X-ray; 1.35 A; A/B/C/D=251-281.
PDB; 2K8X; NMR; -; A/B=264-281.
PDB; 2LPB; NMR; -; B=101-134.
PDB; 2N9B; NMR; -; A/B=253-280.
PDB; 2NRN; X-ray; 1.40 A; A/B/C/D=251-281.
PDB; 2O7H; X-ray; 1.86 A; A/B/C/D/E/F=249-281.
PDB; 2OVN; NMR; -; A=264-280.
PDB; 2VKY; X-ray; 2.05 A; B=256-280.
PDB; 2VNL; X-ray; 1.80 A; A=252-280.
PDB; 2WG5; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272.
PDB; 2WG6; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272.
PDB; 2WPY; X-ray; 1.75 A; A=249-281.
PDB; 2WPZ; X-ray; 1.25 A; A/B/C=249-281.
PDB; 2WQ0; X-ray; 1.12 A; A=249-281.
PDB; 2WQ1; X-ray; 1.08 A; A=249-281.
PDB; 2WQ2; X-ray; 1.36 A; A=249-281.
PDB; 2WQ3; X-ray; 1.22 A; A=249-281.
PDB; 2YNY; X-ray; 1.35 A; A/B/C=250-278.
PDB; 2YNZ; X-ray; 1.40 A; A/B/C=250-278.
PDB; 2YO0; X-ray; 2.80 A; A=250-278.
PDB; 2YO1; X-ray; 3.10 A; A/B/C=250-278.
PDB; 2YO2; X-ray; 2.00 A; A=250-278.
PDB; 2YO3; X-ray; 2.00 A; A/B/C=250-278.
PDB; 2Z5H; X-ray; 2.89 A; A/B/C/D/E/F/G/H=259-278, I=267-278.
PDB; 2Z5I; X-ray; 2.10 A; A/B/C/D/E/F/G/H=259-278, I/J=267-278.
PDB; 2ZTA; X-ray; 1.80 A; A/B=249-281.
PDB; 3AZD; X-ray; 0.98 A; A/B=264-281.
PDB; 3BAS; X-ray; 2.30 A; A/B=250-281.
PDB; 3BAT; X-ray; 2.30 A; A/B/C/D=250-281.
PDB; 3CK4; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=251-281.
PDB; 3CRP; X-ray; 1.70 A; A/B/C/D/E=251-281.
PDB; 3G9R; X-ray; 2.00 A; A/B/C/D/E/F=258-276.
PDB; 3GJP; X-ray; 2.00 A; A/B/C=249-281.
PDB; 3I1G; X-ray; 1.60 A; A=249-281.
PDB; 3I5C; X-ray; 1.94 A; A/B=249-278.
PDB; 3K7Z; X-ray; 1.90 A; A/B/C=249-281.
PDB; 3M48; X-ray; 1.45 A; A=249-281.
PDB; 3P8M; X-ray; 2.90 A; C/D=250-281.
PDB; 3ZMF; X-ray; 1.85 A; A/B/C=250-278.
PDB; 4C46; X-ray; 1.95 A; A/B/C=250-278.
PDB; 4DMD; X-ray; 2.00 A; A/B=249-281.
PDB; 4G2K; X-ray; 1.90 A; A/B/C=250-279.
PDB; 4HU5; X-ray; 2.30 A; A/B=249-281.
PDB; 4HU6; X-ray; 2.30 A; A/B/C/D=260-281.
PDB; 4NIZ; X-ray; 2.00 A; A/B=249-281.
PDB; 4NJ0; X-ray; 1.90 A; A/B=249-281.
PDB; 4NJ1; X-ray; 2.00 A; A/B=249-281.
PDB; 4NJ2; X-ray; 2.20 A; A/B=249-281.
PDB; 4OWI; X-ray; 1.20 A; A/B=249-278.
PDB; 4TL1; X-ray; 1.80 A; A/B=249-281.
PDB; 5APP; X-ray; 2.30 A; A/B/C=250-276.
PDB; 5APQ; X-ray; 2.10 A; A/B/C=250-281.
PDB; 5APS; X-ray; 1.37 A; A=250-281.
PDB; 5APT; X-ray; 1.80 A; A/B/C=250-281.
PDB; 5APU; X-ray; 1.35 A; A/B/C=250-281.
PDB; 5APV; X-ray; 2.00 A; A/B/C/D/E/F=250-281.
PDB; 5APW; X-ray; 1.60 A; A/B/C=250-281.
PDB; 5APX; X-ray; 1.80 A; A/B/C=250-281.
PDB; 5APY; X-ray; 2.00 A; A/B/C=250-281.
PDB; 5APZ; X-ray; 1.60 A; A=250-279.
PDB; 5IEW; NMR; -; A/B=250-280.
PDB; 5IIR; NMR; -; A/B=250-280.
PDB; 5IIV; NMR; -; A/B=250-280.
PDB; 5KHT; X-ray; 1.50 A; A/B/C/D=264-281.
PDBsum; 1CE9; -.
PDBsum; 1DGC; -.
PDBsum; 1ENV; -.
PDBsum; 1FAV; -.
PDBsum; 1FMH; -.
PDBsum; 1GCL; -.
PDBsum; 1GCM; -.
PDBsum; 1GK6; -.
PDBsum; 1GZL; -.
PDBsum; 1IHQ; -.
PDBsum; 1IJ0; -.
PDBsum; 1IJ1; -.
PDBsum; 1IJ2; -.
PDBsum; 1IJ3; -.
PDBsum; 1KQL; -.
PDBsum; 1LD4; -.
PDBsum; 1LLM; -.
PDBsum; 1NKN; -.
PDBsum; 1PIQ; -.
PDBsum; 1RB4; -.
PDBsum; 1RB5; -.
PDBsum; 1RB6; -.
PDBsum; 1SWI; -.
PDBsum; 1TMZ; -.
PDBsum; 1UNT; -.
PDBsum; 1UNU; -.
PDBsum; 1UNV; -.
PDBsum; 1UNW; -.
PDBsum; 1UNX; -.
PDBsum; 1UNY; -.
PDBsum; 1UNZ; -.
PDBsum; 1UO0; -.
PDBsum; 1UO1; -.
PDBsum; 1UO2; -.
PDBsum; 1UO3; -.
PDBsum; 1UO4; -.
PDBsum; 1UO5; -.
PDBsum; 1W5G; -.
PDBsum; 1W5H; -.
PDBsum; 1W5I; -.
PDBsum; 1W5J; -.
PDBsum; 1W5K; -.
PDBsum; 1W5L; -.
PDBsum; 1YSA; -.
PDBsum; 1ZII; -.
PDBsum; 1ZIJ; -.
PDBsum; 1ZIK; -.
PDBsum; 1ZIL; -.
PDBsum; 1ZIM; -.
PDBsum; 1ZTA; -.
PDBsum; 2AHP; -.
PDBsum; 2B1F; -.
PDBsum; 2B22; -.
PDBsum; 2BNI; -.
PDBsum; 2CCE; -.
PDBsum; 2CCF; -.
PDBsum; 2CCN; -.
PDBsum; 2D3E; -.
PDBsum; 2DGC; -.
PDBsum; 2EFR; -.
PDBsum; 2EFS; -.
PDBsum; 2G9J; -.
PDBsum; 2HY6; -.
PDBsum; 2IPZ; -.
PDBsum; 2K8X; -.
PDBsum; 2LPB; -.
PDBsum; 2N9B; -.
PDBsum; 2NRN; -.
PDBsum; 2O7H; -.
PDBsum; 2OVN; -.
PDBsum; 2VKY; -.
PDBsum; 2VNL; -.
PDBsum; 2WG5; -.
PDBsum; 2WG6; -.
PDBsum; 2WPY; -.
PDBsum; 2WPZ; -.
PDBsum; 2WQ0; -.
PDBsum; 2WQ1; -.
PDBsum; 2WQ2; -.
PDBsum; 2WQ3; -.
PDBsum; 2YNY; -.
PDBsum; 2YNZ; -.
PDBsum; 2YO0; -.
PDBsum; 2YO1; -.
PDBsum; 2YO2; -.
PDBsum; 2YO3; -.
PDBsum; 2Z5H; -.
PDBsum; 2Z5I; -.
PDBsum; 2ZTA; -.
PDBsum; 3AZD; -.
PDBsum; 3BAS; -.
PDBsum; 3BAT; -.
PDBsum; 3CK4; -.
PDBsum; 3CRP; -.
PDBsum; 3G9R; -.
PDBsum; 3GJP; -.
PDBsum; 3I1G; -.
PDBsum; 3I5C; -.
PDBsum; 3K7Z; -.
PDBsum; 3M48; -.
PDBsum; 3P8M; -.
PDBsum; 3ZMF; -.
PDBsum; 4C46; -.
PDBsum; 4DMD; -.
PDBsum; 4G2K; -.
PDBsum; 4HU5; -.
PDBsum; 4HU6; -.
PDBsum; 4NIZ; -.
PDBsum; 4NJ0; -.
PDBsum; 4NJ1; -.
PDBsum; 4NJ2; -.
PDBsum; 4OWI; -.
PDBsum; 4TL1; -.
PDBsum; 5APP; -.
PDBsum; 5APQ; -.
PDBsum; 5APS; -.
PDBsum; 5APT; -.
PDBsum; 5APU; -.
PDBsum; 5APV; -.
PDBsum; 5APW; -.
PDBsum; 5APX; -.
PDBsum; 5APY; -.
PDBsum; 5APZ; -.
PDBsum; 5IEW; -.
PDBsum; 5IIR; -.
PDBsum; 5IIV; -.
PDBsum; 5KHT; -.
DisProt; DP00083; -.
ProteinModelPortal; P03069; -.
SMR; P03069; -.
BioGrid; 36723; 279.
DIP; DIP-591N; -.
IntAct; P03069; 17.
MINT; MINT-395967; -.
STRING; 4932.YEL009C; -.
iPTMnet; P03069; -.
MaxQB; P03069; -.
PRIDE; P03069; -.
EnsemblFungi; YEL009C; YEL009C; YEL009C.
GeneID; 856709; -.
KEGG; sce:YEL009C; -.
EuPathDB; FungiDB:YEL009C; -.
SGD; S000000735; GCN4.
InParanoid; P03069; -.
KO; K09464; -.
OMA; RKLQRMN; -.
OrthoDB; EOG092C2P66; -.
BioCyc; YEAST:G3O-30137-MONOMER; -.
EvolutionaryTrace; P03069; -.
PRO; PR:P03069; -.
Proteomes; UP000002311; Chromosome V.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005667; C:transcription factor complex; IBA:GO_Central.
GO; GO:0003682; F:chromatin binding; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043621; F:protein self-association; IPI:AgBase.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
GO; GO:0001135; F:transcription factor activity, RNA polymerase II transcription factor recruiting; IDA:SGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:SGD.
GO; GO:0001084; F:transcription factor activity, TFIID-class binding; IPI:SGD.
GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IDA:SGD.
GO; GO:0001191; F:transcriptional repressor activity, RNA polymerase II transcription factor binding; IPI:SGD.
GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0010691; P:negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels; IMP:SGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:1903833; P:positive regulation of cellular response to amino acid starvation; IMP:SGD.
GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:SGD.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:SGD.
InterPro; IPR004827; bZIP.
Pfam; PF07716; bZIP_2; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
3D-structure; Activator; Amino-acid biosynthesis; Complete proteome;
DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 281 General control protein GCN4.
/FTId=PRO_0000076490.
DOMAIN 225 281 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 89 100 Required for transcriptional activation.
REGION 106 125 Required for transcriptional activation.
REGION 231 251 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 253 274 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 165 165 Phosphothreonine; by PHO85.
{ECO:0000269|PubMed:12101234}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
VARIANT 24 24 S -> P (in strain: CLIB 219).
{ECO:0000269|PubMed:15087486}.
VARIANT 62 62 P -> S (in strain: CLIB 630 haplotype
Ha2). {ECO:0000269|PubMed:15087486}.
VARIANT 82 82 T -> A (in strain: CLIB 556 haplotype
Ha1). {ECO:0000269|PubMed:15087486}.
VARIANT 91 91 D -> A (in strain: CLIB 95, CLIB 219,
CLIB 382, CLIB 388, CLIB 410, CLIB 413,
CLIB 556, CLIB 630, K1, R12, R13
haplotype Ha2, Sigma 1278B haplotype Ha1,
YIIc12 and YIIc17).
{ECO:0000269|PubMed:15087486}.
VARIANT 125 125 D -> A (in strain: CLIB 556 haplotype
Ha1). {ECO:0000269|PubMed:15087486}.
VARIANT 196 196 D -> E (in strain: CLIB 388, CLIB 410,
CLIB 413, CLIB 630 haplotype Ha1, K1,
YIIc12 haplotype Ha2 and YIIc17 haplotype
Ha1). {ECO:0000269|PubMed:15087486}.
MUTAGEN 97 98 FF->AA: Reduces transcriptional
activation activity; when associated with
A-107; A-110; A-113; A-120; A-123 and A-
124. {ECO:0000269|PubMed:7862116}.
MUTAGEN 107 107 M->A: Reduces transcriptional activation
activity; when associated with A-97; A-
98; A-110; A-113; A-120; A-123 and A-124.
{ECO:0000269|PubMed:7862116}.
MUTAGEN 110 110 Y->A: Reduces transcriptional activation
activity; when associated with A-97; A-
98; A-107; A-113; A-120; A-123 and A-124.
{ECO:0000269|PubMed:7862116}.
MUTAGEN 113 113 L->A: Reduces transcriptional activation
activity; when associated with A-97; A-
98; A-107; A-110; A-120; A-123 and A-124.
{ECO:0000269|PubMed:7862116}.
MUTAGEN 120 124 WTSLF->ATSAA: Reduces transcriptional
activation activity; when associated with
A-97; A-98; A-107; A-110 and A-113.
{ECO:0000269|PubMed:7862116}.
CONFLICT 239 281 ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVG
ER -> PGVLVRESCKE (in Ref. 2; AAA65521).
{ECO:0000305}.
HELIX 118 121 {ECO:0000244|PDB:2LPB}.
HELIX 122 124 {ECO:0000244|PDB:2LPB}.
HELIX 250 256 {ECO:0000244|PDB:4TL1}.
TURN 264 267 {ECO:0000244|PDB:3AZD}.
HELIX 268 275 {ECO:0000244|PDB:3AZD}.
TURN 276 278 {ECO:0000244|PDB:3AZD}.
SEQUENCE 281 AA; 31310 MW; 2ED1B8E35D509578 CRC64;
MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK TEEDPIIKQD
TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS STDSTPMFEY ENLEDNSKEW
TSLFDNDIPV TTDDVSLADK AIESTEEVSL VPSNLEVSTT SFLPTPVLED AKLTQTRKVK
KPNSVVKKSH HVGKDDESRL DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR
RSRARKLQRM KQLEDKVEEL LSKNYHLENE VARLKKLVGE R


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