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UniProtKB/Swiss-Prot entry P03069


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GCN4_YEAST
Primary accession number P03069
Secondary accession numbers P03068 Q70D88 Q70D91 Q70D96 Q70D99 Q70DA0 Q96UT3
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 105)
Name and origin of the protein
Protein name General control protein GCN4
Synonym Amino acid biosynthesis regulatory protein
Gene name
Name: GCN4
Synonyms: AAS3, ARG9
OrderedLocusNames: YEL009C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1073/pnas.81.20.6442; PubMed=6387704 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1073/pnas.81.16.5096; PubMed=6433345 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1093/nar/gkh529; PubMed=15087486 [NCBI, ExPASy, EBI, Israel, Japan]
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 204511 / S288c / AB972;
PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan]
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 249-281.
DOI=10.1046/j.1537-2995.2002.00018.x; PubMed=11896344 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
DOMAINS.
DOI=10.1016/0092-8674(86)90070-X; PubMed=3530496 [NCBI, ExPASy, EBI, Israel, Japan]
Hope I.A., Struhl K.;
"Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast.";
Cell 46:885-894(1986).
[7]
DOMAINS, AND MUTAGENESIS OF 97-PHE-PHE-98; MET-107; TYR-110; LEU-113 AND 120-TRP--PHE-124.
PubMed=7862116 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PHOSPHORYLATION AT THR-165.
DOI=10.1128/MCB.22.15.5395-5404.2002; PubMed=12101234 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-165 AND SER-218, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281.
DOI=10.1126/science.1948029; PubMed=1948029 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281.
DOI=10.1016/S0092-8674(05)80070-4; PubMed=1473154 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281.
DOI=10.1006/jmbi.1998.2214; PubMed=9837709 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
STRUCTURE BY NMR OF 237-281.
DOI=10.1093/protein/4.5.519; PubMed=1891459 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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.
  • 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.
  • PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase complex SCF(Cdc4).
  • SIMILARITY: Belongs to the bZIP family. GCN4 subfamily.
  • SIMILARITY: Contains 1 bZIP domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K02205; AAA34640.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K02649; AAA65521.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585686; CAE52206.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585687; CAE52207.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585688; CAE52208.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585689; CAE52209.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585690; CAE52210.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585691; CAE52211.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585692; CAE52212.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585693; CAE52213.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585694; CAE52214.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585695; CAE52215.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585696; CAE52216.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585697; CAE52217.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585698; CAE52218.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585699; CAE52219.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585700; CAE52220.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585701; CAE52221.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585702; CAE52222.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585703; CAE52223.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ585704; CAE52224.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF416613; AAL09032.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U18530; AAB64486.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A03605; RGBYA2.
RefSeq NP_010907.1; -.
3D structure databases
PDB
1CE9; X-ray; 1.80 A; A/B/C/D=251-281.[ExPASy / RCSB / EBI]
1DGC; X-ray; 3.00 A; A=220-281.[ExPASy / RCSB / EBI]
1ENV; X-ray; 2.60 A; A=254-280.[ExPASy / RCSB / EBI]
1FAV; X-ray; 3.00 A; A=-.[ExPASy / RCSB / EBI]
1FMH; NMR; -; A=264-272, B=274-276.[ExPASy / RCSB / EBI]
1GCL; X-ray; 2.10 A; A/B/C/D=249-281.[ExPASy / RCSB / EBI]
1GCM; X-ray; 1.80 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1GK6; X-ray; 1.90 A; A/B=249-280.[ExPASy / RCSB / EBI]
1GZL; X-ray; 1.80 A; A/B=249-276.[ExPASy / RCSB / EBI]
1IHQ; NMR; -; A/B=264-281.[ExPASy / RCSB / EBI]
1IJ0; X-ray; 1.86 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1IJ1; X-ray; 1.86 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1IJ2; X-ray; 1.70 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1IJ3; X-ray; 1.80 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1KQL; X-ray; 2.70 A; A/B=255-281.[ExPASy / RCSB / EBI]
1LD4; EM; 11.40 A; E/F/G/H/I/J/K/L=225-281.[ExPASy / RCSB / EBI]
1LLM; X-ray; 1.50 A; C/D=253-281.[ExPASy / RCSB / EBI]
1NKN; X-ray; 2.50 A; A/B/C/D=250-281.[ExPASy / RCSB / EBI]
1PIQ; X-ray; 1.80 A; A=249-279.[ExPASy / RCSB / EBI]
1RB1; X-ray; 1.90 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1RB4; X-ray; 1.90 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1RB5; X-ray; 1.90 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1RB6; X-ray; 1.90 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1SWI; X-ray; 2.60 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1TMZ; NMR; -; A/B=264-281.[ExPASy / RCSB / EBI]
1UNT; X-ray; 2.07 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UNU; X-ray; 2.07 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UNV; X-ray; 2.14 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UNW; X-ray; 2.20 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UNX; X-ray; 2.40 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UNY; X-ray; 2.30 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UNZ; X-ray; 2.30 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UO0; X-ray; 2.40 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UO1; X-ray; 2.50 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UO2; X-ray; 1.99 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UO3; X-ray; 1.92 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UO4; X-ray; 1.70 A; A/B=249-281.[ExPASy / RCSB / EBI]
1UO5; X-ray; 2.07 A; A/B=249-281.[ExPASy / RCSB / EBI]
1W5G; X-ray; 2.16 A; A/B=249-281.[ExPASy / RCSB / EBI]
1W5H; X-ray; 2.50 A; A/B=249-281.[ExPASy / RCSB / EBI]
1W5I; X-ray; 2.30 A; A/B=249-281.[ExPASy / RCSB / EBI]
1W5J; X-ray; 2.20 A; A/B/C/D=249-281.[ExPASy / RCSB / EBI]
1W5K; X-ray; 1.92 A; A/B/C/D=249-281.[ExPASy / RCSB / EBI]
1W5L; X-ray; 2.17 A; A/B=249-281.[ExPASy / RCSB / EBI]
1YSA; X-ray; 2.90 A; C/D=226-281.[ExPASy / RCSB / EBI]
1ZII; X-ray; 1.80 A; A/B=249-281.[ExPASy / RCSB / EBI]
1ZIJ; X-ray; 2.00 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1ZIK; X-ray; 1.80 A; A/B=249-281.[ExPASy / RCSB / EBI]
1ZIL; X-ray; 2.25 A; A/B=249-281.[ExPASy / RCSB / EBI]
1ZIM; X-ray; 2.00 A; A/B/C=249-281.[ExPASy / RCSB / EBI]
1ZTA; NMR; -; A=247-281.[ExPASy / RCSB / EBI]
2AHP; X-ray; 2.00 A; A/B=249-281.[ExPASy / RCSB / EBI]
2B1F; X-ray; 1.50 A; A/B/C/D=251-281.[ExPASy / RCSB / EBI]
2B22; X-ray; 2.00 A; A=251-281.[ExPASy / RCSB / EBI]
2BNI; X-ray; 1.50 A; A/B/C/D=249-281.[ExPASy / RCSB / EBI]
2CCE; X-ray; 1.90 A; A/B=249-281.[ExPASy / RCSB / EBI]
2CCF; X-ray; 1.70 A; A/B=249-281.[ExPASy / RCSB / EBI]
2CCN; X-ray; 1.60 A; A/B=249-281.[ExPASy / RCSB / EBI]
2D3E; X-ray; 2.60 A; A/B/C/D=253-278.[ExPASy / RCSB / EBI]
2DGC; X-ray; 2.20 A; A=220-281.[ExPASy / RCSB / EBI]
2EFR; X-ray; 1.80 A; A/B/C/D=248-277.[ExPASy / RCSB / EBI]
2EFS; X-ray; 2.00 A; A/B/C/D=248-277.[ExPASy / RCSB / EBI]
2G9J; NMR; -; A/B=264-281.[ExPASy / RCSB / EBI]
2HY6; X-ray; 1.25 A; A/B/C/D/E/F/G=251-281.[ExPASy / RCSB / EBI]
2IPZ; X-ray; 1.35 A; A=251-281.[ExPASy / RCSB / EBI]
2NRN; X-ray; 1.40 A; A/B/C/D=251-281.[ExPASy / RCSB / EBI]
2O7H; X-ray; 1.86 A; A/B/C/D/E/F=249-281.[ExPASy / RCSB / EBI]
2OVN; NMR; -; A=264-280.[ExPASy / RCSB / EBI]
2WG5; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272.[ExPASy / RCSB / EBI]
2WG6; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272.[ExPASy / RCSB / EBI]
2Z5H; X-ray; 2.89 A; A/B/C/D/E/F/G/H=259-278, I=267-278.[ExPASy / RCSB / EBI]
2Z5I; X-ray; 2.10 A; A/B/C/D/E/F/G/H=259-278, I/J=267-278.[ExPASy / RCSB / EBI]
2ZTA; X-ray; 1.80 A; A/B=249-281.[ExPASy / RCSB / EBI]
3CK4; X-ray; 1.70 A; A/D/E/H/I/L=251-281, B/C/F/G/J/K=251-281.[ExPASy / RCSB / EBI]
3CRP; X-ray; 1.70 A; A/D=251-281, B/C/E=251-281.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CE9; -.
1DGC; -.
1ENV; -.
1FAV; -.
1FMH; -.
1GCL; -.
1GCM; -.
1GK6; -.
1GZL; -.
1IHQ; -.
1IJ0; -.
1IJ1; -.
1IJ2; -.
1IJ3; -.
1KQL; -.
1LD4; -.
1LLM; -.
1NKN; -.
1PIQ; -.
1RB1; -.
1RB4; -.
1RB5; -.
1RB6; -.
1SWI; -.
1TMZ; -.
1UNT; -.
1UNU; -.
1UNV; -.
1UNW; -.
1UNX; -.
1UNY; -.
1UNZ; -.
1UO0; -.
1UO1; -.
1UO2; -.
1UO3; -.
1UO4; -.
1UO5; -.
1W5G; -.
1W5H; -.
1W5I; -.
1W5J; -.
1W5K; -.
1W5L; -.
1YSA; -.
1ZII; -.
1ZIJ; -.
1ZIK; -.
1ZIL; -.
1ZIM; -.
1ZTA; -.
2AHP; -.
2B1F; -.
2B22; -.
2BNI; -.
2CCE; -.
2CCF; -.
2CCN; -.
2D3E; -.
2DGC; -.
2EFR; -.
2EFS; -.
2G9J; -.
2HY6; -.
2IPZ; -.
2NRN; -.
2O7H; -.
2OVN; -.
2WG5; -.
2WG6; -.
2Z5H; -.
2Z5I; -.
2ZTA; -.
3CK4; -.
3CRP; -.
DisProt DP00083; -.
ModBase P03069.
Protein-protein interaction databases
DIP DIP:591N; -.
IntAct P03069; 7.
Organism-specific databases
CYGD YEL009c; -.
SGD S000000735; GCN4.
Yeast-GFP YEL009C.
Gene expression databases
ArrayExpress P03069; -.
GermOnline YEL009C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from physical interaction from SGD).
GO:0046983; Molecular function: protein dimerization activity (inferred from electronic annotation from InterPro).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from direct assay from SGD).
GO:0003700; Molecular function: transcription factor activity (inferred from direct assay from SGD).
GO:0008652; Biological process: cellular amino acid biosynthetic process (traceable author statement from SGD).
GO:0006990; Biological process: positive regulation of gene-specific transcription involved in unfolded protein response (inferred from mutant phenotype from SGD).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR011616; bZIP_1.
IPR004827; TF_bZIP.
Graphical view of domain structure.
Pfam PF00170; bZIP_1; 1.
Pfam graphical view of domain structure.
SMART SM00338; BRLZ; 1.
SMART graphical view of domain structure.
PROSITE PS50217; BZIP; 1.
PS00036; BZIP_BASIC; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl YEL009C; Saccharomyces cerevisiae. [Contig view]
GeneID 856709; -.
GenomeReviews U00092_GR; YEL009C.
KEGG sce:YEL009C; -.
NMPDR fig|4932.3.peg.1964; -.
Phylogenomic databases
OMA P03069; ARKLQRM.
Other
NextBio 982781; -.
ProtoNet P03069.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Activator; Amino-acid biosynthesis; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   281  281     General control protein GCN4. PRO_0000076490
DOMAIN   253   274  22     Leucine-zipper. 
DNA_BIND   231   249  19     Basic motif. 
REGION   89   100  12     Required for transcriptional activation. 
REGION   106   125  20     Required for transcriptional activation. 
MOD_RES   17    17        Phosphoserine. 
MOD_RES   165   165        Phosphothreonine; by PHO85. 
MOD_RES   218   218        Phosphoserine. 
VARIANT   24    24  1     S -> P (in strain: CLIB 219). 
VARIANT   62    62  1     P -> S (in strain: CLIB 630 haplotype Ha2). 
VARIANT   82    82  1     T -> A (in strain: CLIB 556 haplotype Ha1). 
VARIANT   91    91  1     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). 
VARIANT   125   125  1     D -> A (in strain: CLIB 556 haplotype Ha1). 
VARIANT   196   196  1     D -> E (in strain: CLIB 388, CLIB 410, CLIB 413, CLIB 630 haplotype Ha1, K1, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1). 
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. 
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. 
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. 
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. 
MUTAGEN   120   124        WTSLF->ATSAA: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-110 and A-113. 
CONFLICT   239   281        ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKK LVGER -> PGVLVRESCKE (in Ref. 2; AAA65521). 
HELIX   230   248  19      
HELIX   251   280  30      
Sequence information
Length: 281 AA [This is the length of the unprocessed precursor] Molecular weight: 31310 Da [This is the MW of the unprocessed precursor] CRC64: 2ED1B8E35D509578 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK TEEDPIIKQD 

        70         80         90        100        110        120 
TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS STDSTPMFEY ENLEDNSKEW 

       130        140        150        160        170        180 
TSLFDNDIPV TTDDVSLADK AIESTEEVSL VPSNLEVSTT SFLPTPVLED AKLTQTRKVK 

       190        200        210        220        230        240 
KPNSVVKKSH HVGKDDESRL DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR 

       250        260        270        280 
RSRARKLQRM KQLEDKVEEL LSKNYHLENE VARLKKLVGE R 

P03069 in FASTA format

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