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P03069 (GCN4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
General control protein GCN4
Alternative name(s):
Amino acid biosynthesis regulatory protein
Gene names
Name:GCN4
Synonyms:AAS3, ARG9
Ordered Locus Names:YEL009C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 structure

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. Ref.7 Ref.8

Post-translational modification

Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase complex SCF(Cdc4). Ref.9

Sequence similarities

Belongs to the bZIP family. GCN4 subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular amino acid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels

Inferred from mutant phenotype PubMed 21183953. Source: SGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 15590823. Source: SGD

nitrogen catabolite activation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 21148207. Source: SGD

positive regulation of RNA polymerase II transcriptional preinitiation complex assembly

Inferred from direct assay PubMed 18794364. Source: SGD

positive regulation of transcription initiation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 1425591. Source: SGD

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19940160. Source: GOC

   Cellular_componentnucleus

Inferred from direct assay PubMed 12455686PubMed 14648200. Source: SGD

   Molecular_functionRNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription

Inferred from physical interaction PubMed 21183953. Source: SGD

RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 19940160. Source: SGD

RNA polymerase II transcription factor recruiting transcription factor activity

Inferred from direct assay PubMed 19940160. Source: SGD

TFIID-class binding transcription factor activity

Inferred from physical interaction PubMed 20308326. Source: SGD

chromatin binding

Inferred from direct assay PubMed 18794364. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 16844784PubMed 22157749PubMed 23348965. Source: IntAct

protein binding

Inferred from physical interaction PubMed 21183953. Source: IntAct

sequence-specific DNA binding

Inferred from direct assay PubMed 2204805PubMed 3290651PubMed 3464968Ref.7PubMed 3907851. Source: SGD

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 16581788. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-7450,EBI-7450
RAP1P119385EBI-7450,EBI-14821

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281General control protein GCN4
PRO_0000076490

Regions

Domain225 – 28157bZIP
Region89 – 10012Required for transcriptional activation
Region106 – 12520Required for transcriptional activation
Region231 – 25121Basic motif By similarity
Region253 – 27422Leucine-zipper By similarity

Amino acid modifications

Modified residue171Phosphoserine Ref.10
Modified residue1651Phosphothreonine; by PHO85 Ref.9
Modified residue2181Phosphoserine Ref.10

Natural variations

Natural variant241S → P in strain: CLIB 219. Ref.3
Natural variant621P → S in strain: CLIB 630 haplotype Ha2. Ref.3
Natural variant821T → A in strain: CLIB 556 haplotype Ha1. Ref.3
Natural variant911D → 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. Ref.3
Natural variant1251D → A in strain: CLIB 556 haplotype Ha1. Ref.3
Natural variant1961D → E in strain: CLIB 388, CLIB 410, CLIB 413, CLIB 630 haplotype Ha1, K1, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1. Ref.3

Experimental info

Mutagenesis97 – 982FF → AA: Reduces transcriptional activation activity; when associated with A-107; A-110; A-113; A-120; A-123 and A-124.
Mutagenesis1071M → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-110; A-113; A-120; A-123 and A-124. Ref.8
Mutagenesis1101Y → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-113; A-120; A-123 and A-124. Ref.8
Mutagenesis1131L → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-110; A-120; A-123 and A-124. Ref.8
Mutagenesis120 – 1245WTSLF → ATSAA: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-110 and A-113. Ref.8
Sequence conflict239 – 28143ARRSR…LVGER → PGVLVRESCKE in AAA65521. Ref.2

Secondary structure

.......... 281
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03069 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 2ED1B8E35D509578

FASTA28131,310
        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 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for translational regulation of the activator of general amino acid control in yeast."
Hinnebusch A.G.
Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"5' untranslated sequences are required for the translational control of a yeast regulatory gene."
Thireos G., Penn M.D., Greer H.
Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and implication of recombination in phylogeny."
Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S., Souciet J.-L.
Nucleic Acids Res. 32:2069-2078(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
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. expand/collapse author list , 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.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
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.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Construction of dimeric F(ab) useful in blood group serology."
Czerwinski M., Krop-Watorek A., Lisowska E., Spitalnik S.L.
Transfusion 42:257-264(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 249-281.
[7]"Functional dissection of a eukaryotic transcriptional activator protein, GCN4 of yeast."
Hope I.A., Struhl K.
Cell 46:885-894(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS.
[8]"The transcriptional activator GCN4 contains multiple activation domains that are critically dependent on hydrophobic amino acids."
Drysdale C.M., Duenas E., Jackson B.M., Reusser U., Braus G.H., Hinnebusch A.G.
Mol. Cell. Biol. 15:1220-1233(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS, MUTAGENESIS OF 97-PHE-PHE-98; MET-107; TYR-110; LEU-113 AND 120-TRP--PHE-124.
[9]"Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5."
Shemer R., Meimoun A., Holtzman T., Kornitzer D.
Mol. Cell. Biol. 22:5395-5404(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-165.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil."
O'Shea E.K., Klemm J.D., Kim P.S., Alber T.
Science 254:539-544(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281.
[12]"The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex."
Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C.
Cell 71:1223-1237(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281.
[13]"Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues."
Eckert D.M., Malashkevich V.N., Kim P.S.
J. Mol. Biol. 284:859-865(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281.
[14]"The solution structure of a leucine-zipper motif peptide."
Saudek V., Pastore A., Morelli M.A., Frank R., Gausepohl H., Gibson T.
Protein Eng. 4:519-529(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 237-281.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02205 Genomic DNA. Translation: AAA34640.1.
K02649 Genomic DNA. Translation: AAA65521.1.
AJ585686 Genomic DNA. Translation: CAE52206.1.
AJ585687 Genomic DNA. Translation: CAE52207.1.
AJ585688 Genomic DNA. Translation: CAE52208.1.
AJ585689 Genomic DNA. Translation: CAE52209.1.
AJ585690 Genomic DNA. Translation: CAE52210.1.
AJ585691 Genomic DNA. Translation: CAE52211.1.
AJ585692 Genomic DNA. Translation: CAE52212.1.
AJ585693 Genomic DNA. Translation: CAE52213.1.
AJ585694 Genomic DNA. Translation: CAE52214.1.
AJ585695 Genomic DNA. Translation: CAE52215.1.
AJ585696 Genomic DNA. Translation: CAE52216.1.
AJ585697 Genomic DNA. Translation: CAE52217.1.
AJ585698 Genomic DNA. Translation: CAE52218.1.
AJ585699 Genomic DNA. Translation: CAE52219.1.
AJ585700 Genomic DNA. Translation: CAE52220.1.
AJ585701 Genomic DNA. Translation: CAE52221.1.
AJ585702 Genomic DNA. Translation: CAE52222.1.
AJ585703 Genomic DNA. Translation: CAE52223.1.
AJ585704 Genomic DNA. Translation: CAE52224.1.
AF416613 mRNA. Translation: AAL09032.1.
U18530 Genomic DNA. Translation: AAB64486.1.
BK006939 Genomic DNA. Translation: DAA07643.1.
PIRRGBYA2. A03605.
RefSeqNP_010907.3. NM_001178824.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CE9X-ray1.80A/B/C/D251-281[»]
1DGCX-ray3.00A220-281[»]
1ENVX-ray2.60A252-280[»]
1FAVX-ray3.00A252-280[»]
1FMHNMR-A/B249-279[»]
1GCLX-ray2.10A/B/C/D249-281[»]
1GCMX-ray1.80A/B/C249-281[»]
1GK6X-ray1.90A/B249-279[»]
1GZLX-ray1.80A/B249-276[»]
1IHQNMR-A/B264-281[»]
1IJ0X-ray1.86A/B/C249-281[»]
1IJ1X-ray1.86A/B/C249-281[»]
1IJ2X-ray1.70A/B/C249-281[»]
1IJ3X-ray1.80A/B/C249-281[»]
1KQLX-ray2.70A/B255-278[»]
1LD4electron microscopy11.40E/F/G/H/I/J/K/L225-281[»]
1LLMX-ray1.50C/D253-281[»]
1NKNX-ray2.50A/B/C/D248-281[»]
1PIQX-ray1.80A249-279[»]
1RB4X-ray1.90A/B/C249-281[»]
1RB5X-ray1.90A/B/C249-281[»]
1RB6X-ray1.90A/B/C249-281[»]
1SWIX-ray2.60A/B/C249-281[»]
1TMZNMR-A/B264-281[»]
1UNTX-ray2.07A/B249-281[»]
1UNUX-ray2.07A/B249-281[»]
1UNVX-ray2.14A/B249-281[»]
1UNWX-ray2.20A/B249-281[»]
1UNXX-ray2.40A/B249-281[»]
1UNYX-ray2.30A/B249-281[»]
1UNZX-ray2.30A/B249-281[»]
1UO0X-ray2.40A/B249-281[»]
1UO1X-ray2.50A/B249-281[»]
1UO2X-ray1.99A/B249-281[»]
1UO3X-ray1.92A/B249-281[»]
1UO4X-ray1.70A/B249-281[»]
1UO5X-ray2.07A/B249-281[»]
1W5GX-ray2.16A/B249-281[»]
1W5HX-ray2.50A/B249-281[»]
1W5IX-ray2.30A/B249-281[»]
1W5JX-ray2.20A/B/C/D249-281[»]
1W5KX-ray1.92A/B/C/D249-281[»]
1W5LX-ray2.17A/B249-281[»]
1YSAX-ray2.90C/D226-281[»]
1ZIIX-ray1.80A/B249-281[»]
1ZIJX-ray2.00A/B/C249-281[»]
1ZIKX-ray1.80A/B249-281[»]
1ZILX-ray2.25A/B249-281[»]
1ZIMX-ray2.00A/B/C249-281[»]
1ZTANMR-A247-281[»]
2AHPX-ray2.00A/B249-281[»]
2B1FX-ray1.50A/B/C/D251-281[»]
2B22X-ray2.00A251-281[»]
2BNIX-ray1.50A/B/C/D249-281[»]
2CCEX-ray1.90A/B249-281[»]
2CCFX-ray1.70A/B249-281[»]
2CCNX-ray1.60A/B249-281[»]
2D3EX-ray2.60A/B/C/D254-277[»]
2DGCX-ray2.20A220-281[»]
2EFRX-ray1.80A/B/C/D249-277[»]
2EFSX-ray2.00A/B/C/D249-277[»]
2G9JNMR-A/B264-281[»]
2HY6X-ray1.25A/B/C/D/E/F/G251-281[»]
2IPZX-ray1.35A/B/C/D251-281[»]
2K8XNMR-A/B264-281[»]
2LPBNMR-B101-134[»]
2NRNX-ray1.40A/B/C/D251-281[»]
2O7HX-ray1.86A/B/C/D/E/F249-281[»]
2OVNNMR-A264-280[»]
2WG5X-ray2.10A/B/C/D/E/F/G/H/I/J/K/L249-272[»]
2WG6X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L249-272[»]
2WPYX-ray1.75A249-281[»]
2WPZX-ray1.25A/B/C249-281[»]
2WQ0X-ray1.12A249-281[»]
2WQ1X-ray1.08A249-281[»]
2WQ2X-ray1.36A249-281[»]
2WQ3X-ray1.22A249-281[»]
2YNYX-ray1.35A/B/C250-278[»]
2YNZX-ray1.40A/B/C250-278[»]
2YO0X-ray2.80A250-278[»]
2YO1X-ray3.10A/B/C250-278[»]
2YO2X-ray2.00A250-278[»]
2YO3X-ray2.00A/B/C250-278[»]
2Z5HX-ray2.89A/B/C/D/E/F/G/H259-278[»]
I267-278[»]
2Z5IX-ray2.10A/B/C/D/E/F/G/H259-278[»]
I/J267-278[»]
2ZTAX-ray1.80A/B249-281[»]
3AZDX-ray0.98A/B264-281[»]
3BASX-ray2.30A/B250-281[»]
3BATX-ray2.30A/B/C/D250-281[»]
3CK4X-ray1.70A/B/C/D/E/F/G/H/I/J/K/L251-281[»]
3CRPX-ray1.70A/B/C/D/E251-281[»]
3G9RX-ray2.00A/B/C/D/E/F258-263[»]
3GJPX-ray2.00A/B/C249-281[»]
3I1GX-ray1.60A249-281[»]
3I5CX-ray1.94A/B249-278[»]
3K7ZX-ray1.90A/B/C249-281[»]
3M48X-ray1.45A249-281[»]
3P8MX-ray2.90C/D250-281[»]
3ZMFX-ray1.85A/B/C250-278[»]
4C46X-ray1.95A/B/C250-278[»]
4DMDX-ray2.00A/B249-281[»]
4G2KX-ray1.90A/B/C250-279[»]
4HU5X-ray2.30A/B249-281[»]
4HU6X-ray2.30A/B/C/D260-281[»]
DisProtDP00083.
ProteinModelPortalP03069.
SMRP03069. Positions 101-134, 229-277.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36723. 99 interactions.
DIPDIP-591N.
IntActP03069. 8 interactions.
MINTMINT-395967.

Proteomic databases

MaxQBP03069.
PaxDbP03069.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYEL009C; YEL009C; YEL009C.
GeneID856709.
KEGGsce:YEL009C.

Organism-specific databases

CYGDYEL009c.
SGDS000000735. GCN4.

Phylogenomic databases

eggNOGNOG329891.
KOK09464.
OrthoDBEOG75QRD1.

Enzyme and pathway databases

BioCycYEAST:G3O-30137-MONOMER.

Gene expression databases

GenevestigatorP03069.

Family and domain databases

InterProIPR004827. bZIP.
[Graphical view]
PfamPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP03069.
NextBio982781.

Entry information

Entry nameGCN4_YEAST
AccessionPrimary (citable) accession number: P03069
Secondary accession number(s): D3DLN9 expand/collapse secondary AC list , P03068, Q70D88, Q70D91, Q70D96, Q70D99, Q70DA0, Q96UT3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references