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P03069

- GCN4_YEAST

UniProt

P03069 - GCN4_YEAST

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Protein
General control protein GCN4
Gene
GCN4, AAS3, ARG9, YEL009C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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'.

GO - Molecular functioni

  1. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: SGD
  2. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: SGD
  3. RNA polymerase II transcription factor recruiting transcription factor activity Source: SGD
  4. TFIID-class binding transcription factor activity Source: SGD
  5. chromatin binding Source: SGD
  6. identical protein binding Source: IntAct
  7. protein binding Source: IntAct
  8. sequence-specific DNA binding Source: SGD
  9. sequence-specific DNA binding transcription factor activity Source: SGD

GO - Biological processi

  1. cellular amino acid biosynthetic process Source: UniProtKB-KW
  2. negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels Source: SGD
  3. negative regulation of transcription from RNA polymerase II promoter Source: SGD
  4. nitrogen catabolite activation of transcription from RNA polymerase II promoter Source: SGD
  5. positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  6. positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
  7. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Amino-acid biosynthesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30137-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
General control protein GCN4
Alternative name(s):
Amino acid biosynthesis regulatory protein
Gene namesi
Name:GCN4
Synonyms:AAS3, ARG9
Ordered Locus Names:YEL009C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYEL009c.
SGDiS000000735. GCN4.

Subcellular locationi

GO - Cellular componenti

  1. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi97 – 982FF → AA: Reduces transcriptional activation activity; when associated with A-107; A-110; A-113; A-120; A-123 and A-124.
Mutagenesisi107 – 1071M → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-110; A-113; A-120; A-123 and A-124. 1 Publication
Mutagenesisi110 – 1101Y → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-113; A-120; A-123 and A-124. 1 Publication
Mutagenesisi113 – 1131L → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-110; A-120; A-123 and A-124. 1 Publication
Mutagenesisi120 – 1245WTSLF → ATSAA: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-110 and A-113. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281General control protein GCN4
PRO_0000076490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine1 Publication
Modified residuei165 – 1651Phosphothreonine; by PHO851 Publication
Modified residuei218 – 2181Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase complex SCF(Cdc4).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP03069.
PaxDbiP03069.

Expressioni

Gene expression databases

GenevestigatoriP03069.

Interactioni

Subunit structurei

Binds DNA as a dimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-7450,EBI-7450
RAP1P119385EBI-7450,EBI-14821

Protein-protein interaction databases

BioGridi36723. 99 interactions.
DIPiDIP-591N.
IntActiP03069. 8 interactions.
MINTiMINT-395967.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi118 – 1214
Helixi122 – 1243
Helixi250 – 2534
Turni264 – 2674
Helixi268 – 2758
Turni276 – 2783

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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/F258-276[»]
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[»]
DisProtiDP00083.
ProteinModelPortaliP03069.
SMRiP03069. Positions 101-134, 229-277.

Miscellaneous databases

EvolutionaryTraceiP03069.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini225 – 28157bZIP
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni89 – 10012Required for transcriptional activation
Add
BLAST
Regioni106 – 12520Required for transcriptional activation
Add
BLAST
Regioni231 – 25121Basic motif By similarity
Add
BLAST
Regioni253 – 27422Leucine-zipper By similarity
Add
BLAST

Domaini

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.2 Publications

Sequence similaritiesi

Belongs to the bZIP family. GCN4 subfamily.

Phylogenomic databases

eggNOGiNOG329891.
KOiK09464.
OrthoDBiEOG75QRD1.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF00170. bZIP_1. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P03069-1 [UniParc]FASTAAdd to Basket

« Hide

MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK    50
TEEDPIIKQD TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS 100
STDSTPMFEY ENLEDNSKEW TSLFDNDIPV TTDDVSLADK AIESTEEVSL 150
VPSNLEVSTT SFLPTPVLED AKLTQTRKVK KPNSVVKKSH HVGKDDESRL 200
DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR RSRARKLQRM 250
KQLEDKVEEL LSKNYHLENE VARLKKLVGE R 281
Length:281
Mass (Da):31,310
Last modified:July 21, 1986 - v1
Checksum:i2ED1B8E35D509578
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241S → P in strain: CLIB 219. 1 Publication
Natural varianti62 – 621P → S in strain: CLIB 630 haplotype Ha2. 1 Publication
Natural varianti82 – 821T → A in strain: CLIB 556 haplotype Ha1. 1 Publication
Natural varianti91 – 911D → 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. 1 Publication
Natural varianti125 – 1251D → A in strain: CLIB 556 haplotype Ha1. 1 Publication
Natural varianti196 – 1961D → E in strain: CLIB 388, CLIB 410, CLIB 413, CLIB 630 haplotype Ha1, K1, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 28143ARRSR…LVGER → PGVLVRESCKE in AAA65521. 1 Publication
Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA03605. RGBYA2.
RefSeqiNP_010907.3. NM_001178824.3.

Genome annotation databases

EnsemblFungiiYEL009C; YEL009C; YEL009C.
GeneIDi856709.
KEGGisce:YEL009C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A03605. RGBYA2.
RefSeqi NP_010907.3. NM_001178824.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CE9 X-ray 1.80 A/B/C/D 251-281 [» ]
1DGC X-ray 3.00 A 220-281 [» ]
1ENV X-ray 2.60 A 252-280 [» ]
1FAV X-ray 3.00 A 252-280 [» ]
1FMH NMR - A/B 249-279 [» ]
1GCL X-ray 2.10 A/B/C/D 249-281 [» ]
1GCM X-ray 1.80 A/B/C 249-281 [» ]
1GK6 X-ray 1.90 A/B 249-279 [» ]
1GZL X-ray 1.80 A/B 249-276 [» ]
1IHQ NMR - A/B 264-281 [» ]
1IJ0 X-ray 1.86 A/B/C 249-281 [» ]
1IJ1 X-ray 1.86 A/B/C 249-281 [» ]
1IJ2 X-ray 1.70 A/B/C 249-281 [» ]
1IJ3 X-ray 1.80 A/B/C 249-281 [» ]
1KQL X-ray 2.70 A/B 255-278 [» ]
1LD4 electron microscopy 11.40 E/F/G/H/I/J/K/L 225-281 [» ]
1LLM X-ray 1.50 C/D 253-281 [» ]
1NKN X-ray 2.50 A/B/C/D 248-281 [» ]
1PIQ X-ray 1.80 A 249-279 [» ]
1RB4 X-ray 1.90 A/B/C 249-281 [» ]
1RB5 X-ray 1.90 A/B/C 249-281 [» ]
1RB6 X-ray 1.90 A/B/C 249-281 [» ]
1SWI X-ray 2.60 A/B/C 249-281 [» ]
1TMZ NMR - A/B 264-281 [» ]
1UNT X-ray 2.07 A/B 249-281 [» ]
1UNU X-ray 2.07 A/B 249-281 [» ]
1UNV X-ray 2.14 A/B 249-281 [» ]
1UNW X-ray 2.20 A/B 249-281 [» ]
1UNX X-ray 2.40 A/B 249-281 [» ]
1UNY X-ray 2.30 A/B 249-281 [» ]
1UNZ X-ray 2.30 A/B 249-281 [» ]
1UO0 X-ray 2.40 A/B 249-281 [» ]
1UO1 X-ray 2.50 A/B 249-281 [» ]
1UO2 X-ray 1.99 A/B 249-281 [» ]
1UO3 X-ray 1.92 A/B 249-281 [» ]
1UO4 X-ray 1.70 A/B 249-281 [» ]
1UO5 X-ray 2.07 A/B 249-281 [» ]
1W5G X-ray 2.16 A/B 249-281 [» ]
1W5H X-ray 2.50 A/B 249-281 [» ]
1W5I X-ray 2.30 A/B 249-281 [» ]
1W5J X-ray 2.20 A/B/C/D 249-281 [» ]
1W5K X-ray 1.92 A/B/C/D 249-281 [» ]
1W5L X-ray 2.17 A/B 249-281 [» ]
1YSA X-ray 2.90 C/D 226-281 [» ]
1ZII X-ray 1.80 A/B 249-281 [» ]
1ZIJ X-ray 2.00 A/B/C 249-281 [» ]
1ZIK X-ray 1.80 A/B 249-281 [» ]
1ZIL X-ray 2.25 A/B 249-281 [» ]
1ZIM X-ray 2.00 A/B/C 249-281 [» ]
1ZTA NMR - A 247-281 [» ]
2AHP X-ray 2.00 A/B 249-281 [» ]
2B1F X-ray 1.50 A/B/C/D 251-281 [» ]
2B22 X-ray 2.00 A 251-281 [» ]
2BNI X-ray 1.50 A/B/C/D 249-281 [» ]
2CCE X-ray 1.90 A/B 249-281 [» ]
2CCF X-ray 1.70 A/B 249-281 [» ]
2CCN X-ray 1.60 A/B 249-281 [» ]
2D3E X-ray 2.60 A/B/C/D 254-277 [» ]
2DGC X-ray 2.20 A 220-281 [» ]
2EFR X-ray 1.80 A/B/C/D 249-277 [» ]
2EFS X-ray 2.00 A/B/C/D 249-277 [» ]
2G9J NMR - A/B 264-281 [» ]
2HY6 X-ray 1.25 A/B/C/D/E/F/G 251-281 [» ]
2IPZ X-ray 1.35 A/B/C/D 251-281 [» ]
2K8X NMR - A/B 264-281 [» ]
2LPB NMR - B 101-134 [» ]
2NRN X-ray 1.40 A/B/C/D 251-281 [» ]
2O7H X-ray 1.86 A/B/C/D/E/F 249-281 [» ]
2OVN NMR - A 264-280 [» ]
2WG5 X-ray 2.10 A/B/C/D/E/F/G/H/I/J/K/L 249-272 [» ]
2WG6 X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L 249-272 [» ]
2WPY X-ray 1.75 A 249-281 [» ]
2WPZ X-ray 1.25 A/B/C 249-281 [» ]
2WQ0 X-ray 1.12 A 249-281 [» ]
2WQ1 X-ray 1.08 A 249-281 [» ]
2WQ2 X-ray 1.36 A 249-281 [» ]
2WQ3 X-ray 1.22 A 249-281 [» ]
2YNY X-ray 1.35 A/B/C 250-278 [» ]
2YNZ X-ray 1.40 A/B/C 250-278 [» ]
2YO0 X-ray 2.80 A 250-278 [» ]
2YO1 X-ray 3.10 A/B/C 250-278 [» ]
2YO2 X-ray 2.00 A 250-278 [» ]
2YO3 X-ray 2.00 A/B/C 250-278 [» ]
2Z5H X-ray 2.89 A/B/C/D/E/F/G/H 259-278 [» ]
I 267-278 [» ]
2Z5I X-ray 2.10 A/B/C/D/E/F/G/H 259-278 [» ]
I/J 267-278 [» ]
2ZTA X-ray 1.80 A/B 249-281 [» ]
3AZD X-ray 0.98 A/B 264-281 [» ]
3BAS X-ray 2.30 A/B 250-281 [» ]
3BAT X-ray 2.30 A/B/C/D 250-281 [» ]
3CK4 X-ray 1.70 A/B/C/D/E/F/G/H/I/J/K/L 251-281 [» ]
3CRP X-ray 1.70 A/B/C/D/E 251-281 [» ]
3G9R X-ray 2.00 A/B/C/D/E/F 258-276 [» ]
3GJP X-ray 2.00 A/B/C 249-281 [» ]
3I1G X-ray 1.60 A 249-281 [» ]
3I5C X-ray 1.94 A/B 249-278 [» ]
3K7Z X-ray 1.90 A/B/C 249-281 [» ]
3M48 X-ray 1.45 A 249-281 [» ]
3P8M X-ray 2.90 C/D 250-281 [» ]
3ZMF X-ray 1.85 A/B/C 250-278 [» ]
4C46 X-ray 1.95 A/B/C 250-278 [» ]
4DMD X-ray 2.00 A/B 249-281 [» ]
4G2K X-ray 1.90 A/B/C 250-279 [» ]
4HU5 X-ray 2.30 A/B 249-281 [» ]
4HU6 X-ray 2.30 A/B/C/D 260-281 [» ]
DisProti DP00083.
ProteinModelPortali P03069.
SMRi P03069. Positions 101-134, 229-277.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36723. 99 interactions.
DIPi DIP-591N.
IntActi P03069. 8 interactions.
MINTi MINT-395967.

Proteomic databases

MaxQBi P03069.
PaxDbi P03069.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YEL009C ; YEL009C ; YEL009C .
GeneIDi 856709.
KEGGi sce:YEL009C.

Organism-specific databases

CYGDi YEL009c.
SGDi S000000735. GCN4.

Phylogenomic databases

eggNOGi NOG329891.
KOi K09464.
OrthoDBi EOG75QRD1.

Enzyme and pathway databases

BioCyci YEAST:G3O-30137-MONOMER.

Miscellaneous databases

EvolutionaryTracei P03069.
NextBioi 982781.

Gene expression databases

Genevestigatori P03069.

Family and domain databases

InterProi IPR004827. bZIP.
[Graphical view ]
Pfami PF00170. bZIP_1. 1 hit.
[Graphical view ]
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. 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.

Entry informationi

Entry nameiGCN4_YEAST
AccessioniPrimary (citable) accession number: P03069
Secondary accession number(s): D3DLN9
, P03068, Q70D88, Q70D91, Q70D96, Q70D99, Q70DA0, Q96UT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

External Data

Dasty 3

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