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P03069

- GCN4_YEAST

UniProt

P03069 - GCN4_YEAST

Protein

General control protein GCN4

Gene

GCN4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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. chromatin binding Source: SGD
    2. identical protein binding Source: IntAct
    3. protein binding Source: IntAct
    4. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: SGD
    5. RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription Source: SGD
    6. RNA polymerase II transcription factor recruiting transcription factor activity Source: SGD
    7. sequence-specific DNA binding Source: SGD
    8. sequence-specific DNA binding transcription factor activity Source: SGD
    9. TFIID-class 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

    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

    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.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 281281General control protein GCN4PRO_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).2 Publications

    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

    1
    281
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03069.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini225 – 28157bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni89 – 10012Required for transcriptional activationAdd
    BLAST
    Regioni106 – 12520Required for transcriptional activationAdd
    BLAST
    Regioni231 – 25121Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni253 – 27422Leucine-zipperPROSITE-ProRule annotationAdd
    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.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti239 – 28143ARRSR…LVGER → PGVLVRESCKE in AAA65521. (PubMed:6433345)CuratedAdd
    BLAST

    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 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

    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: October 1, 2014
    This is version 161 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