GCN4_YEAST
ID GCN4_YEAST Reviewed; 281 AA.
AC P03069; D3DLN9; P03068; Q70D88; Q70D91; Q70D96; Q70D99; Q70DA0; Q96UT3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=General control transcription factor GCN4;
DE AltName: Full=Amino acid biosynthesis regulatory protein;
DE AltName: Full=General control protein GCN4;
GN Name=GCN4 {ECO:0000303|PubMed:6387704, ECO:0000312|SGD:S000000735};
GN Synonyms=AAS101 {ECO:0000303|PubMed:6433345, ECO:0000312|SGD:S000000735},
GN AAS3 {ECO:0000312|SGD:S000000735}, ARG9 {ECO:0000312|SGD:S000000735};
GN OrderedLocusNames=YEL009C;
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], AND INDUCTION.
RX PubMed=6387704; DOI=10.1073/pnas.81.20.6442;
RA Hinnebusch A.G.;
RT "Evidence for translational regulation of the activator of general amino
RT acid control in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=6433345; DOI=10.1073/pnas.81.16.5096;
RA Thireos G., Penn M.D., Greer H.;
RT "5' untranslated sequences are required for the translational control of a
RT yeast regulatory gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-24; SER-62; ALA-82;
RP ALA-91; ALA-125 AND GLU-196.
RC STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
RX PubMed=15087486; DOI=10.1093/nar/gkh529;
RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA Souciet J.-L.;
RT "Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and
RT implication of recombination in phylogeny.";
RL Nucleic Acids Res. 32:2069-2078(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 249-281.
RX PubMed=11896344; DOI=10.1046/j.1537-2995.2002.00018.x;
RA Czerwinski M., Krop-Watorek A., Lisowska E., Spitalnik S.L.;
RT "Construction of dimeric F(ab) useful in blood group serology.";
RL Transfusion 42:257-264(2002).
RN [7]
RP INDUCTION.
RX PubMed=3516411; DOI=10.1016/0092-8674(86)90384-3;
RA Mueller P.P., Hinnebusch A.G.;
RT "Multiple upstream AUG codons mediate translational control of GCN4.";
RL Cell 45:201-207(1986).
RN [8]
RP FUNCTION, AND DOMAINS.
RX PubMed=3530496; DOI=10.1016/0092-8674(86)90070-x;
RA Hope I.A., Struhl K.;
RT "Functional dissection of a eukaryotic transcriptional activator protein,
RT GCN4 of yeast.";
RL Cell 46:885-894(1986).
RN [9]
RP FUNCTION.
RX PubMed=3532321; DOI=10.1126/science.3532321;
RA Hill D.E., Hope I.A., Macke J.P., Struhl K.;
RT "Saturation mutagenesis of the yeast his3 regulatory site: requirements for
RT transcriptional induction and for binding by GCN4 activator protein.";
RL Science 234:451-457(1986).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=3678204; DOI=10.1002/j.1460-2075.1987.tb02573.x;
RA Hope I.A., Struhl K.;
RT "GCN4, a eukaryotic transcriptional activator protein, binds as a dimer to
RT target DNA.";
RL EMBO J. 6:2781-2784(1987).
RN [11]
RP INDUCTION.
RX PubMed=2676723; DOI=10.1101/gad.3.8.1217;
RA Miller P.F., Hinnebusch A.G.;
RT "Sequences that surround the stop codons of upstream open reading frames in
RT GCN4 mRNA determine their distinct functions in translational control.";
RL Genes Dev. 3:1217-1225(1989).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=2204805; DOI=10.1128/mcb.10.10.5077-5086.1990;
RA Sellers J.W., Vincent A.C., Struhl K.;
RT "Mutations that define the optimal half-site for binding yeast GCN4
RT activator protein and identify an ATF/CREB-like repressor that recognizes
RT similar DNA sites.";
RL Mol. Cell. Biol. 10:5077-5086(1990).
RN [13]
RP FUNCTION.
RX PubMed=2277632; DOI=10.1007/bf00259451;
RA Schmidheini T., Moesch H.U., Graf R., Braus G.H.;
RT "A GCN4 protein recognition element is not sufficient for GCN4-dependent
RT regulation of transcription in the ARO7 promoter of Saccharomyces
RT cerevisiae.";
RL Mol. Gen. Genet. 224:57-64(1990).
RN [14]
RP FUNCTION.
RX PubMed=1939099; DOI=10.1016/s0021-9258(18)54945-0;
RA Moesch H.U., Scheier B., Lahti R., Maentsaela P., Braus G.H.;
RT "Transcriptional activation of yeast nucleotide biosynthetic gene ADE4 by
RT GCN4.";
RL J. Biol. Chem. 266:20453-20456(1991).
RN [15]
RP INDUCTION.
RX PubMed=1986242; DOI=10.1128/mcb.11.1.486-496.1991;
RA Abastado J.P., Miller P.F., Jackson B.M., Hinnebusch A.G.;
RT "Suppression of ribosomal reinitiation at upstream open reading frames in
RT amino acid-starved cells forms the basis for GCN4 translational control.";
RL Mol. Cell. Biol. 11:486-496(1991).
RN [16]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=8336737; DOI=10.1128/mcb.13.8.5099-5111.1993;
RA Rolfes R.J., Hinnebusch A.G.;
RT "Translation of the yeast transcriptional activator GCN4 is stimulated by
RT purine limitation: implications for activation of the protein kinase
RT GCN2.";
RL Mol. Cell. Biol. 13:5099-5111(1993).
RN [17]
RP FUNCTION, DOMAINS, AND MUTAGENESIS OF 97-PHE-PHE-98; MET-107; TYR-110;
RP LEU-113 AND 120-TRP--PHE-124.
RX PubMed=7862116; DOI=10.1128/mcb.15.3.1220;
RA Drysdale C.M., Duenas E., Jackson B.M., Reusser U., Braus G.H.,
RA Hinnebusch A.G.;
RT "The transcriptional activator GCN4 contains multiple activation domains
RT that are critically dependent on hydrophobic amino acids.";
RL Mol. Cell. Biol. 15:1220-1233(1995).
RN [18]
RP FUNCTION, AND SUBUNIT.
RX PubMed=7664107; DOI=10.1038/nsb0695-450;
RA Stanojevic D., Verdine G.L.;
RT "Deconstruction of GCN4/GCRE into a monomeric peptide-DNA complex.";
RL Nat. Struct. Biol. 2:450-457(1995).
RN [19]
RP INDUCTION.
RX PubMed=9582292; DOI=10.1074/jbc.273.21.12696;
RA Albrecht G., Moesch H.U., Hoffmann B., Reusser U., Braus G.H.;
RT "Monitoring the Gcn4 protein-mediated response in the yeast Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 273:12696-12702(1998).
RN [20]
RP FUNCTION, AND INTERACTION WITH THE MEDIATOR COMPLEX AND THE SAGA COMPLEX.
RX PubMed=9488488; DOI=10.1128/mcb.18.3.1711;
RA Drysdale C.M., Jackson B.M., McVeigh R., Klebanow E.R., Bai Y., Kokubo T.,
RA Swanson M., Nakatani Y., Weil P.A., Hinnebusch A.G.;
RT "The Gcn4p activation domain interacts specifically in vitro with RNA
RT polymerase II holoenzyme, TFIID, and the Adap-Gcn5p coactivator complex.";
RL Mol. Cell. Biol. 18:1711-1724(1998).
RN [21]
RP FUNCTION, INTERACTION WITH THE MEDIATOR COMPLEX; THE SAGA COMPLEX AND THE
RP SWI/SNF COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=10549298; DOI=10.1016/s1097-2765(00)80217-8;
RA Natarajan K., Jackson B.M., Zhou H., Winston F., Hinnebusch A.G.;
RT "Transcriptional activation by Gcn4p involves independent interactions with
RT the SWI/SNF complex and the SRB/mediator.";
RL Mol. Cell 4:657-664(1999).
RN [22]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10733573; DOI=10.1128/mcb.20.8.2706-2717.2000;
RA Yang R., Wek S.A., Wek R.C.;
RT "Glucose limitation induces GCN4 translation by activation of Gcn2 protein
RT kinase.";
RL Mol. Cell. Biol. 20:2706-2717(2000).
RN [23]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11390663; DOI=10.1128/mcb.21.13.4347-4368.2001;
RA Natarajan K., Meyer M.R., Jackson B.M., Slade D., Roberts C.,
RA Hinnebusch A.G., Marton M.J.;
RT "Transcriptional profiling shows that Gcn4p is a master regulator of gene
RT expression during amino acid starvation in yeast.";
RL Mol. Cell. Biol. 21:4347-4368(2001).
RN [24]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:12455686};
RX PubMed=12455686; DOI=10.1128/ec.1.5.663-672.2002;
RA Pries R., Boemeke K., Irniger S., Grundmann O., Braus G.H.;
RT "Amino acid-dependent Gcn4p stability regulation occurs exclusively in the
RT yeast nucleus.";
RL Eukaryot. Cell 1:663-672(2002).
RN [25]
RP PHOSPHORYLATION AT THR-165.
RX PubMed=12101234; DOI=10.1128/mcb.22.15.5395-5404.2002;
RA Shemer R., Meimoun A., Holtzman T., Kornitzer D.;
RT "Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5.";
RL Mol. Cell. Biol. 22:5395-5404(2002).
RN [26]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:14648200};
RX PubMed=14648200; DOI=10.1007/s00438-003-0955-7;
RA Pries R., Boemeke K., Draht O., Kuenzler M., Braus G.H.;
RT "Nuclear import of yeast Gcn4p requires karyopherins Srp1p and Kap95p.";
RL Mol. Genet. Genomics 271:257-266(2004).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-218, 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 [28]
RP FUNCTION, INTERACTION WITH GAL11/MED15; THE SAGA COMPLEX AND THE SWI/SNF
RP COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=19940160; DOI=10.1074/jbc.m109.071589;
RA Jedidi I., Zhang F., Qiu H., Stahl S.J., Palmer I., Kaufman J.D.,
RA Nadaud P.S., Mukherjee S., Wingfield P.T., Jaroniec C.P., Hinnebusch A.G.;
RT "Activator Gcn4 employs multiple segments of Med15/Gal11, including the KIX
RT domain, to recruit mediator to target genes in vivo.";
RL J. Biol. Chem. 285:2438-2455(2010).
RN [29]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29628310; DOI=10.1016/j.molcel.2018.03.007;
RA Rawal Y., Chereji R.V., Valabhoju V., Qiu H., Ocampo J., Clark D.J.,
RA Hinnebusch A.G.;
RT "Gcn4 Binding in Coding Regions Can Activate Internal and Canonical 5'
RT Promoters in Yeast.";
RL Mol. Cell 70:297-311(2018).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281.
RX PubMed=1948029; DOI=10.1126/science.1948029;
RA O'Shea E.K., Klemm J.D., Kim P.S., Alber T.;
RT "X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel
RT coiled coil.";
RL Science 254:539-544(1991).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281 IN COMPLEX WITH DNA,
RP FUNCTION, AND SUBUNIT.
RX PubMed=1473154; DOI=10.1016/s0092-8674(05)80070-4;
RA Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C.;
RT "The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted
RT alpha helices: crystal structure of the protein-DNA complex.";
RL Cell 71:1223-1237(1992).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281.
RX PubMed=9837709; DOI=10.1006/jmbi.1998.2214;
RA Eckert D.M., Malashkevich V.N., Kim P.S.;
RT "Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar
RT residues.";
RL J. Mol. Biol. 284:859-865(1998).
RN [33]
RP STRUCTURE BY NMR OF 237-281.
RX PubMed=1891459; DOI=10.1093/protein/4.5.519;
RA Saudek V., Pastore A., Morelli M.A., Frank R., Gausepohl H., Gibson T.;
RT "The solution structure of a leucine-zipper motif peptide.";
RL Protein Eng. 4:519-529(1991).
CC -!- FUNCTION: Master transcriptional regulator that mediates the response
CC to amino acid starvation (PubMed:11390663, PubMed:29628310). Binds
CC variations of the DNA sequence 5'-ATGA[CG]TCAT-3' in canonical
CC nucleosome-depleted 5'-positioned promoters, and also within coding
CC sequences and 3' non-coding regions (PubMed:29628310, PubMed:11390663,
CC PubMed:1473154, PubMed:2277632, PubMed:1939099, PubMed:7664107,
CC PubMed:2204805, PubMed:3678204, PubMed:3532321, PubMed:3530496). During
CC nutrient starvation (low or poor amino acid, carbon or purine sources),
CC it activates genes required for amino acid biosynthesis and transport,
CC autophagy, cofactor biosynthesis and transport, mitochondrial
CC transport, and additional downstream transcription factors
CC (PubMed:11390663, PubMed:29628310, PubMed:8336737, PubMed:1939099,
CC PubMed:10733573, PubMed:7862116). Activates transcription by recruiting
CC multiple coactivators, including the mediator complex, the SAGA
CC complex, and the SWI/SNF complex, to enable assembly of the pre-
CC initiation complex at core promoters (PubMed:19940160, PubMed:9488488,
CC PubMed:10549298). {ECO:0000269|PubMed:10549298,
CC ECO:0000269|PubMed:10733573, ECO:0000269|PubMed:11390663,
CC ECO:0000269|PubMed:1473154, ECO:0000269|PubMed:1939099,
CC ECO:0000269|PubMed:19940160, ECO:0000269|PubMed:2204805,
CC ECO:0000269|PubMed:2277632, ECO:0000269|PubMed:29628310,
CC ECO:0000269|PubMed:3530496, ECO:0000269|PubMed:3532321,
CC ECO:0000269|PubMed:3678204, ECO:0000269|PubMed:7664107,
CC ECO:0000269|PubMed:7862116, ECO:0000269|PubMed:8336737,
CC ECO:0000269|PubMed:9488488}.
CC -!- SUBUNIT: Homodimer (PubMed:1473154, PubMed:3678204). Each subunit binds
CC overlapping and non-identical half-sites that flank the central CG
CC base-pair in the pseudo-palindromic motif 5'-ATGA[CG]TCAT-3'
CC (PubMed:1473154, PubMed:7664107, PubMed:2204805, PubMed:3678204).
CC Interacts with the mediator tail; the interaction with GAL11/MED15 is
CC direct (PubMed:19940160, PubMed:9488488, PubMed:10549298). Interacts
CC with the SAGA histone acetyltransferase complex (PubMed:19940160,
CC PubMed:9488488, PubMed:10549298). Interacts with the SWI/SNF chromatin
CC remodeling complex (PubMed:19940160, PubMed:10549298).
CC {ECO:0000269|PubMed:10549298, ECO:0000269|PubMed:1473154,
CC ECO:0000269|PubMed:19940160, ECO:0000269|PubMed:2204805,
CC ECO:0000269|PubMed:3678204, ECO:0000269|PubMed:7664107,
CC ECO:0000269|PubMed:9488488}.
CC -!- INTERACTION:
CC P03069; P03069: GCN4; NbExp=15; IntAct=EBI-7450, EBI-7450;
CC P03069; P11938: RAP1; NbExp=5; IntAct=EBI-7450, EBI-14821;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12455686,
CC ECO:0000269|PubMed:14648200}. Note=Localizes to the nucleus
CC independently of cellular amino acid levels.
CC {ECO:0000269|PubMed:12455686}.
CC -!- INDUCTION: Translation is induced by amino acid or purine starvation,
CC or during growth in low or poor carbon sources (PubMed:6387704,
CC PubMed:6433345, PubMed:8336737, PubMed:10733573, PubMed:9582292).
CC Translational repression during nutrient-rich conditions is dependent
CC on four uORFs (upstream open reading frames) present in the 5'-UTR of
CC the mRNA; these promote ribosome dissociation (PubMed:6387704,
CC PubMed:6433345, PubMed:3516411, PubMed:2676723, PubMed:8336737,
CC PubMed:9582292). Translational induction occurs in conditions reducing
CC translation machinery efficiency, leading to ribosomes scanning over
CC the uORFs, and increased translation of the mRNA (PubMed:1986242). The
CC rapid translational induction is followed by transcriptional induction
CC at later time-points, independently of the uORF sequences
CC (PubMed:9582292). {ECO:0000269|PubMed:10733573,
CC ECO:0000269|PubMed:1986242, ECO:0000269|PubMed:2676723,
CC ECO:0000269|PubMed:3516411, ECO:0000269|PubMed:6387704,
CC ECO:0000269|PubMed:6433345, ECO:0000269|PubMed:8336737,
CC ECO:0000269|PubMed:9582292}.
CC -!- DOMAIN: Residues 89 to 100 and 106 to 125 define the N-terminal
CC activation domain (NTAD) and the central acidic activation domain
CC (CAAD) respectively, which can function independently to promote high-
CC level transcription of the target genes. {ECO:0000269|PubMed:3530496,
CC ECO:0000269|PubMed:7862116}.
CC -!- PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation of
CC Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase complex
CC SCF(Cdc4). {ECO:0000269|PubMed:12101234}.
CC -!- DISRUPTION PHENOTYPE: Abolishes recruitment of the mediator complex to
CC the upstream activating sequence (UAS) of amino-acid starvation
CC responsive genes (PubMed:19940160). Decreases RNA level of genes
CC involved in amino acid biosynthesis and cofactor biosynthesis during
CC amino acid starvation or methyl methanesulfonate stress
CC (PubMed:11390663, PubMed:8336737, PubMed:29628310). Growth dependent on
CC amino acid supplementation (PubMed:10733573). Sensitive to amino acid
CC starvation (PubMed:10549298). Sensitive to purine starvation
CC (PubMed:8336737). Decreases cellular glycogen levels during glucose
CC starvation (PubMed:10733573). {ECO:0000269|PubMed:10549298,
CC ECO:0000269|PubMed:10733573, ECO:0000269|PubMed:11390663,
CC ECO:0000269|PubMed:19940160, ECO:0000269|PubMed:29628310,
CC ECO:0000269|PubMed:8336737}.
CC -!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily. {ECO:0000305}.
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DR EMBL; K02205; AAA34640.1; -; Genomic_DNA.
DR EMBL; K02649; AAA65521.1; -; Genomic_DNA.
DR EMBL; AJ585686; CAE52206.1; -; Genomic_DNA.
DR EMBL; AJ585687; CAE52207.1; -; Genomic_DNA.
DR EMBL; AJ585688; CAE52208.1; -; Genomic_DNA.
DR EMBL; AJ585689; CAE52209.1; -; Genomic_DNA.
DR EMBL; AJ585690; CAE52210.1; -; Genomic_DNA.
DR EMBL; AJ585691; CAE52211.1; -; Genomic_DNA.
DR EMBL; AJ585692; CAE52212.1; -; Genomic_DNA.
DR EMBL; AJ585693; CAE52213.1; -; Genomic_DNA.
DR EMBL; AJ585694; CAE52214.1; -; Genomic_DNA.
DR EMBL; AJ585695; CAE52215.1; -; Genomic_DNA.
DR EMBL; AJ585696; CAE52216.1; -; Genomic_DNA.
DR EMBL; AJ585697; CAE52217.1; -; Genomic_DNA.
DR EMBL; AJ585698; CAE52218.1; -; Genomic_DNA.
DR EMBL; AJ585699; CAE52219.1; -; Genomic_DNA.
DR EMBL; AJ585700; CAE52220.1; -; Genomic_DNA.
DR EMBL; AJ585701; CAE52221.1; -; Genomic_DNA.
DR EMBL; AJ585702; CAE52222.1; -; Genomic_DNA.
DR EMBL; AJ585703; CAE52223.1; -; Genomic_DNA.
DR EMBL; AJ585704; CAE52224.1; -; Genomic_DNA.
DR EMBL; AF416613; AAL09032.1; -; mRNA.
DR EMBL; U18530; AAB64486.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07643.1; -; Genomic_DNA.
DR PIR; A03605; RGBYA2.
DR RefSeq; NP_010907.3; NM_001178824.3.
DR PDB; 1CE9; X-ray; 1.80 A; A/B/C/D=251-281.
DR PDB; 1DGC; X-ray; 3.00 A; A=220-281.
DR PDB; 1ENV; X-ray; 2.60 A; A=252-280.
DR PDB; 1FAV; X-ray; 3.00 A; A=252-280.
DR PDB; 1FMH; NMR; -; A/B=249-279.
DR PDB; 1GCL; X-ray; 2.10 A; A/B/C/D=249-281.
DR PDB; 1GCM; X-ray; 1.80 A; A/B/C=249-281.
DR PDB; 1GK6; X-ray; 1.90 A; A/B=249-279.
DR PDB; 1GZL; X-ray; 1.80 A; A/B=249-276.
DR PDB; 1IHQ; NMR; -; A/B=264-281.
DR PDB; 1IJ0; X-ray; 1.86 A; A/B/C=249-281.
DR PDB; 1IJ1; X-ray; 1.86 A; A/B/C=249-281.
DR PDB; 1IJ2; X-ray; 1.70 A; A/B/C=249-281.
DR PDB; 1IJ3; X-ray; 1.80 A; A/B/C=249-281.
DR PDB; 1KQL; X-ray; 2.70 A; A/B=255-278.
DR PDB; 1LD4; EM; 11.40 A; E/F/G/H/I/J/K/L=225-281.
DR PDB; 1LLM; X-ray; 1.50 A; C/D=253-281.
DR PDB; 1NKN; X-ray; 2.50 A; A/B/C/D=250-281.
DR PDB; 1PIQ; X-ray; 1.80 A; A=249-279.
DR PDB; 1RB4; X-ray; 1.90 A; A/B/C=249-281.
DR PDB; 1RB5; X-ray; 1.90 A; A/B/C=249-281.
DR PDB; 1RB6; X-ray; 1.90 A; A/B/C=249-281.
DR PDB; 1SWI; X-ray; 2.60 A; A/B/C=249-281.
DR PDB; 1TMZ; NMR; -; A/B=264-281.
DR PDB; 1UNT; X-ray; 2.07 A; A/B=249-281.
DR PDB; 1UNU; X-ray; 2.07 A; A/B=249-281.
DR PDB; 1UNV; X-ray; 2.14 A; A/B=249-281.
DR PDB; 1UNW; X-ray; 2.20 A; A/B=249-281.
DR PDB; 1UNX; X-ray; 2.40 A; A/B=249-281.
DR PDB; 1UNY; X-ray; 2.30 A; A/B=249-281.
DR PDB; 1UNZ; X-ray; 2.30 A; A/B=249-281.
DR PDB; 1UO0; X-ray; 2.40 A; A/B=249-281.
DR PDB; 1UO1; X-ray; 2.50 A; A/B=249-281.
DR PDB; 1UO2; X-ray; 1.99 A; A/B=249-281.
DR PDB; 1UO3; X-ray; 1.92 A; A/B=249-281.
DR PDB; 1UO4; X-ray; 1.70 A; A/B=249-281.
DR PDB; 1UO5; X-ray; 2.07 A; A/B=249-281.
DR PDB; 1W5G; X-ray; 2.16 A; A/B=249-281.
DR PDB; 1W5H; X-ray; 2.50 A; A/B=249-281.
DR PDB; 1W5I; X-ray; 2.30 A; A/B=249-281.
DR PDB; 1W5J; X-ray; 2.20 A; A/B/C/D=249-281.
DR PDB; 1W5K; X-ray; 1.92 A; A/B/C/D=249-281.
DR PDB; 1W5L; X-ray; 2.17 A; A/B=249-281.
DR PDB; 1YSA; X-ray; 2.90 A; C/D=226-281.
DR PDB; 1ZII; X-ray; 1.80 A; A/B=249-281.
DR PDB; 1ZIJ; X-ray; 2.00 A; A/B/C=249-281.
DR PDB; 1ZIK; X-ray; 1.80 A; A/B=249-281.
DR PDB; 1ZIL; X-ray; 2.25 A; A/B=249-281.
DR PDB; 1ZIM; X-ray; 2.00 A; A/B/C=249-281.
DR PDB; 1ZTA; NMR; -; A=247-281.
DR PDB; 2AHP; X-ray; 2.00 A; A/B=249-281.
DR PDB; 2B1F; X-ray; 1.50 A; A/B/C/D=251-281.
DR PDB; 2B22; X-ray; 2.00 A; A=251-281.
DR PDB; 2BNI; X-ray; 1.50 A; A/B/C/D=249-281.
DR PDB; 2CCE; X-ray; 1.90 A; A/B=249-281.
DR PDB; 2CCF; X-ray; 1.70 A; A/B=249-281.
DR PDB; 2CCN; X-ray; 1.60 A; A/B=249-281.
DR PDB; 2D3E; X-ray; 2.60 A; A/B/C/D=254-277.
DR PDB; 2DGC; X-ray; 2.20 A; A=220-281.
DR PDB; 2EFR; X-ray; 1.80 A; A/B/C/D=249-277.
DR PDB; 2EFS; X-ray; 2.00 A; A/B/C/D=249-277.
DR PDB; 2G9J; NMR; -; A/B=264-281.
DR PDB; 2HY6; X-ray; 1.25 A; A/B/C/D/E/F/G=251-281.
DR PDB; 2IPZ; X-ray; 1.35 A; A/B/C/D=251-281.
DR PDB; 2K8X; NMR; -; A/B=264-281.
DR PDB; 2LPB; NMR; -; B=101-134.
DR PDB; 2N9B; NMR; -; A/B=253-280.
DR PDB; 2NRN; X-ray; 1.40 A; A/B/C/D=251-281.
DR PDB; 2O7H; X-ray; 1.86 A; A/B/C/D/E/F=249-281.
DR PDB; 2OVN; NMR; -; A=264-280.
DR PDB; 2VKY; X-ray; 2.05 A; B=256-280.
DR PDB; 2VNL; X-ray; 1.80 A; A=252-280.
DR PDB; 2WG5; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272.
DR PDB; 2WG6; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272.
DR PDB; 2WPY; X-ray; 1.75 A; A=249-281.
DR PDB; 2WPZ; X-ray; 1.25 A; A/B/C=249-281.
DR PDB; 2WQ0; X-ray; 1.12 A; A=249-281.
DR PDB; 2WQ1; X-ray; 1.08 A; A=249-281.
DR PDB; 2WQ2; X-ray; 1.36 A; A=249-281.
DR PDB; 2WQ3; X-ray; 1.22 A; A=249-281.
DR PDB; 2YNY; X-ray; 1.35 A; A/B/C=250-278.
DR PDB; 2YNZ; X-ray; 1.40 A; A/B/C=250-278.
DR PDB; 2YO0; X-ray; 2.80 A; A=250-278.
DR PDB; 2YO1; X-ray; 3.10 A; A/B/C=250-278.
DR PDB; 2YO2; X-ray; 2.00 A; A=250-278.
DR PDB; 2YO3; X-ray; 2.00 A; A/B/C=250-278.
DR PDB; 2Z5H; X-ray; 2.89 A; A/B/C/D/E/F/G/H=259-278, I=267-278.
DR PDB; 2Z5I; X-ray; 2.10 A; A/B/C/D/E/F/G/H=259-278, I/J=267-278.
DR PDB; 2ZTA; X-ray; 1.80 A; A/B=249-281.
DR PDB; 3AZD; X-ray; 0.98 A; A/B=264-281.
DR PDB; 3BAS; X-ray; 2.30 A; A/B=250-281.
DR PDB; 3BAT; X-ray; 2.30 A; A/B/C/D=250-281.
DR PDB; 3CK4; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=251-281.
DR PDB; 3CRP; X-ray; 1.70 A; A/B/C/D/E=251-281.
DR PDB; 3G9R; X-ray; 2.00 A; A/B/C/D/E/F=258-276.
DR PDB; 3GJP; X-ray; 2.00 A; A/B/C=249-281.
DR PDB; 3I1G; X-ray; 1.60 A; A=249-281.
DR PDB; 3I5C; X-ray; 1.94 A; A/B=249-278.
DR PDB; 3K7Z; X-ray; 1.90 A; A/B/C=249-281.
DR PDB; 3M48; X-ray; 1.45 A; A=249-281.
DR PDB; 3P8M; X-ray; 2.90 A; C/D=250-281.
DR PDB; 3ZMF; X-ray; 1.85 A; A/B/C=250-278.
DR PDB; 4C46; X-ray; 1.95 A; A/B/C=250-278.
DR PDB; 4DMD; X-ray; 2.00 A; A/B=249-281.
DR PDB; 4G2K; X-ray; 1.90 A; A/B/C=250-279.
DR PDB; 4HU5; X-ray; 2.30 A; A/B=249-281.
DR PDB; 4HU6; X-ray; 2.30 A; A/B/C/D=260-281.
DR PDB; 4NIZ; X-ray; 2.00 A; A/B=249-281.
DR PDB; 4NJ0; X-ray; 1.90 A; A/B=249-281.
DR PDB; 4NJ1; X-ray; 2.00 A; A/B=249-281.
DR PDB; 4NJ2; X-ray; 2.20 A; A/B=249-281.
DR PDB; 4OWI; X-ray; 1.20 A; A/B=249-278.
DR PDB; 4TL1; X-ray; 1.80 A; A/B=249-281.
DR PDB; 5APP; X-ray; 2.30 A; A/B/C=250-276.
DR PDB; 5APQ; X-ray; 2.10 A; A/B/C=250-281.
DR PDB; 5APS; X-ray; 1.37 A; A=250-281.
DR PDB; 5APT; X-ray; 1.80 A; A/B/C=250-281.
DR PDB; 5APU; X-ray; 1.35 A; A/B/C=250-281.
DR PDB; 5APV; X-ray; 2.00 A; A/B/C/D/E/F=250-281.
DR PDB; 5APW; X-ray; 1.60 A; A/B/C=250-281.
DR PDB; 5APX; X-ray; 1.80 A; A/B/C=250-281.
DR PDB; 5APY; X-ray; 2.00 A; A/B/C=250-281.
DR PDB; 5APZ; X-ray; 1.60 A; A=250-279.
DR PDB; 5IEW; NMR; -; A/B=250-280.
DR PDB; 5IIR; NMR; -; A/B=250-280.
DR PDB; 5IIV; NMR; -; A/B=250-280.
DR PDB; 5KHT; X-ray; 1.50 A; A/B/C/D=264-281.
DR PDB; 6E52; X-ray; 1.93 A; A/B=250-275.
DR PDB; 6E95; X-ray; 2.25 A; A/B=250-275.
DR PDB; 6H9M; X-ray; 2.10 A; A/B/C=251-281.
DR PDB; 6HN4; EM; 4.20 A; E/F=249-281.
DR PDB; 6HN5; EM; 3.20 A; E/F=249-281.
DR PDB; 6O2E; X-ray; 1.90 A; A=249-279.
DR PDB; 6O2F; X-ray; 1.80 A; A=249-279.
DR PDB; 6PSA; X-ray; 1.30 A; A=249-277.
DR PDB; 6UT2; NMR; -; B/C=264-281.
DR PDB; 6VWG; EM; 3.21 A; A/B=249-281.
DR PDB; 6VWH; EM; 4.26 A; A/B=249-281.
DR PDB; 6VWI; EM; 3.70 A; A/B=249-281.
DR PDB; 6VWJ; EM; 4.21 A; A/B=249-281.
DR PDB; 6XNE; X-ray; 1.96 A; A/B/C=249-278.
DR PDB; 6XNF; X-ray; 2.00 A; A/B/C=249-278.
DR PDB; 6XNL; X-ray; 2.20 A; A/B/C=249-278.
DR PDB; 6XNM; X-ray; 2.25 A; A/B/C=249-278.
DR PDB; 7A4T; X-ray; 2.12 A; B/C=252-279.
DR PDBsum; 1CE9; -.
DR PDBsum; 1DGC; -.
DR PDBsum; 1ENV; -.
DR PDBsum; 1FAV; -.
DR PDBsum; 1FMH; -.
DR PDBsum; 1GCL; -.
DR PDBsum; 1GCM; -.
DR PDBsum; 1GK6; -.
DR PDBsum; 1GZL; -.
DR PDBsum; 1IHQ; -.
DR PDBsum; 1IJ0; -.
DR PDBsum; 1IJ1; -.
DR PDBsum; 1IJ2; -.
DR PDBsum; 1IJ3; -.
DR PDBsum; 1KQL; -.
DR PDBsum; 1LD4; -.
DR PDBsum; 1LLM; -.
DR PDBsum; 1NKN; -.
DR PDBsum; 1PIQ; -.
DR PDBsum; 1RB4; -.
DR PDBsum; 1RB5; -.
DR PDBsum; 1RB6; -.
DR PDBsum; 1SWI; -.
DR PDBsum; 1TMZ; -.
DR PDBsum; 1UNT; -.
DR PDBsum; 1UNU; -.
DR PDBsum; 1UNV; -.
DR PDBsum; 1UNW; -.
DR PDBsum; 1UNX; -.
DR PDBsum; 1UNY; -.
DR PDBsum; 1UNZ; -.
DR PDBsum; 1UO0; -.
DR PDBsum; 1UO1; -.
DR PDBsum; 1UO2; -.
DR PDBsum; 1UO3; -.
DR PDBsum; 1UO4; -.
DR PDBsum; 1UO5; -.
DR PDBsum; 1W5G; -.
DR PDBsum; 1W5H; -.
DR PDBsum; 1W5I; -.
DR PDBsum; 1W5J; -.
DR PDBsum; 1W5K; -.
DR PDBsum; 1W5L; -.
DR PDBsum; 1YSA; -.
DR PDBsum; 1ZII; -.
DR PDBsum; 1ZIJ; -.
DR PDBsum; 1ZIK; -.
DR PDBsum; 1ZIL; -.
DR PDBsum; 1ZIM; -.
DR PDBsum; 1ZTA; -.
DR PDBsum; 2AHP; -.
DR PDBsum; 2B1F; -.
DR PDBsum; 2B22; -.
DR PDBsum; 2BNI; -.
DR PDBsum; 2CCE; -.
DR PDBsum; 2CCF; -.
DR PDBsum; 2CCN; -.
DR PDBsum; 2D3E; -.
DR PDBsum; 2DGC; -.
DR PDBsum; 2EFR; -.
DR PDBsum; 2EFS; -.
DR PDBsum; 2G9J; -.
DR PDBsum; 2HY6; -.
DR PDBsum; 2IPZ; -.
DR PDBsum; 2K8X; -.
DR PDBsum; 2LPB; -.
DR PDBsum; 2N9B; -.
DR PDBsum; 2NRN; -.
DR PDBsum; 2O7H; -.
DR PDBsum; 2OVN; -.
DR PDBsum; 2VKY; -.
DR PDBsum; 2VNL; -.
DR PDBsum; 2WG5; -.
DR PDBsum; 2WG6; -.
DR PDBsum; 2WPY; -.
DR PDBsum; 2WPZ; -.
DR PDBsum; 2WQ0; -.
DR PDBsum; 2WQ1; -.
DR PDBsum; 2WQ2; -.
DR PDBsum; 2WQ3; -.
DR PDBsum; 2YNY; -.
DR PDBsum; 2YNZ; -.
DR PDBsum; 2YO0; -.
DR PDBsum; 2YO1; -.
DR PDBsum; 2YO2; -.
DR PDBsum; 2YO3; -.
DR PDBsum; 2Z5H; -.
DR PDBsum; 2Z5I; -.
DR PDBsum; 2ZTA; -.
DR PDBsum; 3AZD; -.
DR PDBsum; 3BAS; -.
DR PDBsum; 3BAT; -.
DR PDBsum; 3CK4; -.
DR PDBsum; 3CRP; -.
DR PDBsum; 3G9R; -.
DR PDBsum; 3GJP; -.
DR PDBsum; 3I1G; -.
DR PDBsum; 3I5C; -.
DR PDBsum; 3K7Z; -.
DR PDBsum; 3M48; -.
DR PDBsum; 3P8M; -.
DR PDBsum; 3ZMF; -.
DR PDBsum; 4C46; -.
DR PDBsum; 4DMD; -.
DR PDBsum; 4G2K; -.
DR PDBsum; 4HU5; -.
DR PDBsum; 4HU6; -.
DR PDBsum; 4NIZ; -.
DR PDBsum; 4NJ0; -.
DR PDBsum; 4NJ1; -.
DR PDBsum; 4NJ2; -.
DR PDBsum; 4OWI; -.
DR PDBsum; 4TL1; -.
DR PDBsum; 5APP; -.
DR PDBsum; 5APQ; -.
DR PDBsum; 5APS; -.
DR PDBsum; 5APT; -.
DR PDBsum; 5APU; -.
DR PDBsum; 5APV; -.
DR PDBsum; 5APW; -.
DR PDBsum; 5APX; -.
DR PDBsum; 5APY; -.
DR PDBsum; 5APZ; -.
DR PDBsum; 5IEW; -.
DR PDBsum; 5IIR; -.
DR PDBsum; 5IIV; -.
DR PDBsum; 5KHT; -.
DR PDBsum; 6E52; -.
DR PDBsum; 6E95; -.
DR PDBsum; 6H9M; -.
DR PDBsum; 6HN4; -.
DR PDBsum; 6HN5; -.
DR PDBsum; 6O2E; -.
DR PDBsum; 6O2F; -.
DR PDBsum; 6PSA; -.
DR PDBsum; 6UT2; -.
DR PDBsum; 6VWG; -.
DR PDBsum; 6VWH; -.
DR PDBsum; 6VWI; -.
DR PDBsum; 6VWJ; -.
DR PDBsum; 6XNE; -.
DR PDBsum; 6XNF; -.
DR PDBsum; 6XNL; -.
DR PDBsum; 6XNM; -.
DR PDBsum; 7A4T; -.
DR AlphaFoldDB; P03069; -.
DR BMRB; P03069; -.
DR SMR; P03069; -.
DR BioGRID; 36723; 291.
DR DIP; DIP-591N; -.
DR IntAct; P03069; 17.
DR MINT; P03069; -.
DR STRING; 4932.YEL009C; -.
DR MoonProt; P03069; -.
DR iPTMnet; P03069; -.
DR MaxQB; P03069; -.
DR PaxDb; P03069; -.
DR PRIDE; P03069; -.
DR ABCD; P03069; 3 sequenced antibodies.
DR EnsemblFungi; YEL009C_mRNA; YEL009C; YEL009C.
DR GeneID; 856709; -.
DR KEGG; sce:YEL009C; -.
DR SGD; S000000735; GCN4.
DR VEuPathDB; FungiDB:YEL009C; -.
DR eggNOG; KOG0837; Eukaryota.
DR HOGENOM; CLU_068501_1_0_1; -.
DR InParanoid; P03069; -.
DR OMA; PMFEYEN; -.
DR BioCyc; YEAST:G3O-30137-MON; -.
DR Reactome; R-SCE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-SCE-2871796; FCERI mediated MAPK activation.
DR Reactome; R-SCE-450341; Activation of the AP-1 family of transcription factors.
DR EvolutionaryTrace; P03069; -.
DR PRO; PR:P03069; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P03069; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043621; F:protein self-association; IPI:AgBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IMP:UniProtKB.
DR GO; GO:0010691; P:negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0010508; P:positive regulation of autophagy; IMP:SGD.
DR GO; GO:1903833; P:positive regulation of cellular response to amino acid starvation; IMP:SGD.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0061412; P:positive regulation of transcription from RNA polymerase II promoter in response to amino acid starvation; IMP:UniProtKB.
DR GO; GO:0036278; P:positive regulation of transcription from RNA polymerase II promoter in response to nitrogen starvation; IMP:SGD.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:1990139; P:protein localization to nuclear periphery; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1990928; P:response to amino acid starvation; IMP:UniProtKB.
DR DisProt; DP00083; -.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Amino-acid biosynthesis; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..281
FT /note="General control transcription factor GCN4"
FT /id="PRO_0000076490"
FT DOMAIN 225..281
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 89..100
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000269|PubMed:7862116"
FT REGION 106..125
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000269|PubMed:7862116"
FT REGION 217..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..251
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978,
FT ECO:0000269|PubMed:1473154"
FT REGION 253..274
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978,
FT ECO:0000269|PubMed:1473154"
FT MOTIF 167..200
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12455686"
FT MOTIF 231..249
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:12455686"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 165
FT /note="Phosphothreonine; by PHO85"
FT /evidence="ECO:0000269|PubMed:12101234"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT VARIANT 24
FT /note="S -> P (in strain: CLIB 219)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 62
FT /note="P -> S (in strain: CLIB 630 haplotype Ha2)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 82
FT /note="T -> A (in strain: CLIB 556 haplotype Ha1)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 91
FT /note="D -> A (in strain: CLIB 95, CLIB 219, CLIB 382, CLIB
FT 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13
FT haplotype Ha2, Sigma 1278B haplotype Ha1, YIIc12 and
FT YIIc17)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 125
FT /note="D -> A (in strain: CLIB 556 haplotype Ha1)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT VARIANT 196
FT /note="D -> E (in strain: CLIB 388, CLIB 410, CLIB 413,
FT CLIB 630 haplotype Ha1, K1, YIIc12 haplotype Ha2 and YIIc17
FT haplotype Ha1)"
FT /evidence="ECO:0000269|PubMed:15087486"
FT MUTAGEN 97..98
FT /note="FF->AA: Reduces transcriptional activation activity;
FT when associated with A-107; A-110; A-113; A-120; A-123 and
FT A-124."
FT /evidence="ECO:0000269|PubMed:7862116"
FT MUTAGEN 107
FT /note="M->A: Reduces transcriptional activation activity;
FT when associated with A-97; A-98; A-110; A-113; A-120; A-123
FT and A-124."
FT /evidence="ECO:0000269|PubMed:7862116"
FT MUTAGEN 110
FT /note="Y->A: Reduces transcriptional activation activity;
FT when associated with A-97; A-98; A-107; A-113; A-120; A-123
FT and A-124."
FT /evidence="ECO:0000269|PubMed:7862116"
FT MUTAGEN 113
FT /note="L->A: Reduces transcriptional activation activity;
FT when associated with A-97; A-98; A-107; A-110; A-120; A-123
FT and A-124."
FT /evidence="ECO:0000269|PubMed:7862116"
FT MUTAGEN 120..124
FT /note="WTSLF->ATSAA: Reduces transcriptional activation
FT activity; when associated with A-97; A-98; A-107; A-110 and
FT A-113."
FT /evidence="ECO:0000269|PubMed:7862116"
FT CONFLICT 239..281
FT /note="ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER -> PGVLV
FT RESCKE (in Ref. 2; AAA65521)"
FT /evidence="ECO:0000305"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:2LPB"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2LPB"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:5APP"
FT HELIX 217..239
FT /evidence="ECO:0007829|PDB:5APP"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:3AZD"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:3AZD"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:3AZD"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3AZD"
SQ 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
