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Protein

General control protein GCN4

Gene

GCN4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • cellular amino acid biosynthetic process Source: UniProtKB-KW
  • negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • nitrogen catabolite activation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of cellular response to amino acid starvation Source: SGD
  • positive regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: SGD
  • positive regulation of transcription initiation from RNA polymerase II promoter Source: SGD
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
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL009C.
SGDiS000000735. GCN4.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: GO_Central
  • nucleus Source: SGD
  • transcription factor complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97 – 98FF → AA: Reduces transcriptional activation activity; when associated with A-107; A-110; A-113; A-120; A-123 and A-124. 1 Publication2
Mutagenesisi107M → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-110; A-113; A-120; A-123 and A-124. 1 Publication1
Mutagenesisi110Y → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-113; A-120; A-123 and A-124. 1 Publication1
Mutagenesisi113L → A: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-110; A-120; A-123 and A-124. 1 Publication1
Mutagenesisi120 – 124WTSLF → ATSAA: Reduces transcriptional activation activity; when associated with A-97; A-98; A-107; A-110 and A-113. 1 Publication5

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000764901 – 281General control protein GCN4Add BLAST281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphoserineCombined sources1
Modified residuei165Phosphothreonine; by PHO851 Publication1
Modified residuei218PhosphoserineCombined sources1

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.
PRIDEiP03069.

PTM databases

iPTMnetiP03069.

Interactioni

Subunit structurei

Binds DNA as a dimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-7450,EBI-7450
RAP1P119385EBI-7450,EBI-14821

GO - Molecular functioni

  • protein self-association Source: AgBase

Protein-protein interaction databases

BioGridi36723. 106 interactors.
DIPiDIP-591N.
IntActiP03069. 15 interactors.
MINTiMINT-395967.

Structurei

Secondary structure

1281
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi118 – 121Combined sources4
Helixi122 – 124Combined sources3
Helixi250 – 256Combined sources7
Turni264 – 267Combined sources4
Helixi268 – 275Combined sources8
Turni276 – 278Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/D250-281[»]
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[»]
2N9BNMR-A/B253-280[»]
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[»]
4NIZX-ray2.00A/B249-281[»]
4NJ0X-ray1.90A/B249-281[»]
4NJ1X-ray2.00A/B249-281[»]
4NJ2X-ray2.20A/B249-281[»]
4OWIX-ray1.20A/B249-278[»]
4TL1X-ray1.80A/B249-281[»]
5APPX-ray2.30A/B/C250-276[»]
5APQX-ray2.10A/B/C250-281[»]
5APSX-ray1.37A250-281[»]
5APTX-ray1.80A/B/C250-281[»]
5APUX-ray1.35A/B/C250-281[»]
5APVX-ray2.00A/B/C/D/E/F250-281[»]
5APWX-ray1.60A/B/C250-281[»]
5APXX-ray1.80A/B/C250-281[»]
5APYX-ray2.00A/B/C250-281[»]
5APZX-ray1.60A250-279[»]
DisProtiDP00083.
ProteinModelPortaliP03069.
SMRiP03069.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03069.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 281bZIPPROSITE-ProRule annotationAdd BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni89 – 100Required for transcriptional activationAdd BLAST12
Regioni106 – 125Required for transcriptional activationAdd BLAST20
Regioni231 – 251Basic motifPROSITE-ProRule annotationAdd BLAST21
Regioni253 – 274Leucine-zipperPROSITE-ProRule annotationAdd BLAST22

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.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiP03069.
KOiK09464.
OMAiRKLQRMN.
OrthoDBiEOG092C2P66.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 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

        10         20         30         40         50
MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK
60 70 80 90 100
TEEDPIIKQD TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS
110 120 130 140 150
STDSTPMFEY ENLEDNSKEW TSLFDNDIPV TTDDVSLADK AIESTEEVSL
160 170 180 190 200
VPSNLEVSTT SFLPTPVLED AKLTQTRKVK KPNSVVKKSH HVGKDDESRL
210 220 230 240 250
DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR RSRARKLQRM
260 270 280
KQLEDKVEEL LSKNYHLENE VARLKKLVGE R
Length:281
Mass (Da):31,310
Last modified:July 21, 1986 - v1
Checksum:i2ED1B8E35D509578
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti239 – 281ARRSR…LVGER → PGVLVRESCKE in AAA65521 (PubMed:6433345).CuratedAdd BLAST43

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti24S → P in strain: CLIB 219. 1 Publication1
Natural varianti62P → S in strain: CLIB 630 haplotype Ha2. 1 Publication1
Natural varianti82T → A in strain: CLIB 556 haplotype Ha1. 1 Publication1
Natural varianti91D → 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 Publication1
Natural varianti125D → A in strain: CLIB 556 haplotype Ha1. 1 Publication1
Natural varianti196D → E in strain: CLIB 388, CLIB 410, CLIB 413, CLIB 630 haplotype Ha1, K1, YIIc12 haplotype Ha2 and YIIc17 haplotype Ha1. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/D250-281[»]
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[»]
2N9BNMR-A/B253-280[»]
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[»]
4NIZX-ray2.00A/B249-281[»]
4NJ0X-ray1.90A/B249-281[»]
4NJ1X-ray2.00A/B249-281[»]
4NJ2X-ray2.20A/B249-281[»]
4OWIX-ray1.20A/B249-278[»]
4TL1X-ray1.80A/B249-281[»]
5APPX-ray2.30A/B/C250-276[»]
5APQX-ray2.10A/B/C250-281[»]
5APSX-ray1.37A250-281[»]
5APTX-ray1.80A/B/C250-281[»]
5APUX-ray1.35A/B/C250-281[»]
5APVX-ray2.00A/B/C/D/E/F250-281[»]
5APWX-ray1.60A/B/C250-281[»]
5APXX-ray1.80A/B/C250-281[»]
5APYX-ray2.00A/B/C250-281[»]
5APZX-ray1.60A250-279[»]
DisProtiDP00083.
ProteinModelPortaliP03069.
SMRiP03069.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36723. 106 interactors.
DIPiDIP-591N.
IntActiP03069. 15 interactors.
MINTiMINT-395967.

PTM databases

iPTMnetiP03069.

Proteomic databases

MaxQBiP03069.
PRIDEiP03069.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YEL009C.
SGDiS000000735. GCN4.

Phylogenomic databases

InParanoidiP03069.
KOiK09464.
OMAiRKLQRMN.
OrthoDBiEOG092C2P66.

Enzyme and pathway databases

BioCyciYEAST:G3O-30137-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP03069.
PROiP03069.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 186 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.