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Protein

Regulatory protein GAL4

Gene

GAL4

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

This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which code for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of these genes.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111Zinc 1
Metal bindingi11 – 111Zinc 2
Metal bindingi14 – 141Zinc 1
Metal bindingi21 – 211Zinc 1
Metal bindingi28 – 281Zinc 1
Metal bindingi28 – 281Zinc 2
Metal bindingi31 – 311Zinc 2
Metal bindingi38 – 381Zinc 2

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi11 – 3828Zn(2)-C6 fungal-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • galactose metabolic process Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter by galactose Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Carbohydrate metabolism, Galactose metabolism, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-34134-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein GAL4
Gene namesi
Name:GAL4
Ordered Locus Names:YPL248C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XVI

Organism-specific databases

CYGDiYPL248c.
EuPathDBiFungiDB:YPL248C.
SGDiS000006169. GAL4.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261P → L: Loss of DNA-binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 881881Regulatory protein GAL4PRO_0000114951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei694 – 6941Phosphotyrosine1 Publication
Modified residuei696 – 6961Phosphoserine1 Publication
Modified residuei699 – 6991Phosphoserine1 Publication
Modified residuei703 – 7031Phosphoserine1 Publication
Modified residuei712 – 7121Phosphoserine1 Publication

Post-translational modificationi

Association between GAL11 and GAL4 may serve to expedite phosphorylation of GAL4.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP04386.
PeptideAtlasiP04386.

Interactioni

Subunit structurei

Binds DNA as a homodimer. Interacts directly with the mediator subunits GAL11/MED15 and SRB4/MED17.2 Publications

Protein-protein interaction databases

BioGridi35915. 88 interactions.
DIPiDIP-593N.
IntActiP04386. 5 interactions.
MINTiMINT-1510289.
STRINGi4932.YPL248C.

Structurei

Secondary structure

1
881
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 176Combined sources
Beta strandi25 – 273Combined sources
Helixi29 – 335Combined sources
Helixi51 – 7121Combined sources
Beta strandi73 – 753Combined sources
Helixi77 – 826Combined sources
Helixi86 – 938Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AW6NMR-A1-43[»]
1D66X-ray2.70A/B1-65[»]
1HBWNMR-A/B50-106[»]
3BTSX-ray2.70E/F854-874[»]
3COQX-ray2.40A/B8-96[»]
ProteinModelPortaliP04386.
SMRiP04386. Positions 8-96.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04386.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi862 – 87099aaTAD

Domaini

the 9aaTAD motif (residues 862 to 870) is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

Sequence similaritiesi

Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG85363.
HOGENOMiHOG000112689.
InParanoidiP04386.
KOiK09241.
OMAiFRYILWE.
OrthoDBiEOG7J44JV.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR005600. Gal4_dimer_dom.
IPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF04082. Fungal_trans. 1 hit.
PF03902. Gal4_dimer. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04386-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLSSIEQA CDICRLKKLK CSKEKPKCAK CLKNNWECRY SPKTKRSPLT
60 70 80 90 100
RAHLTEVESR LERLEQLFLL IFPREDLDMI LKMDSLQDIK ALLTGLFVQD
110 120 130 140 150
NVNKDAVTDR LASVETDMPL TLRQHRISAT SSSEESSNKG QRQLTVSIDS
160 170 180 190 200
AAHHDNSTIP LDFMPRDALH GFDWSEEDDM SDGLPFLKTD PNNNGFFGDG
210 220 230 240 250
SLLCILRSIG FKPENYTNSN VNRLPTMITD RYTLASRSTT SRLLQSYLNN
260 270 280 290 300
FHPYCPIVHS PTLMMLYNNQ IEIASKDQWQ ILFNCILAIG AWCIEGESTD
310 320 330 340 350
IDVFYYQNAK SHLTSKVFES GSIILVTALH LLSRYTQWRQ KTNTSYNFHS
360 370 380 390 400
FSIRMAISLG LNRDLPSSFS DSSILEQRRR IWWSVYSWEI QLSLLYGRSI
410 420 430 440 450
QLSQNTISFP SSVDDVQRTT TGPTIYHGII ETARLLQVFT KIYELDKTVT
460 470 480 490 500
AEKSPICAKK CLMICNEIEE VSRQAPKFLQ MDISTTALTN LLKEHPWLSF
510 520 530 540 550
TRFELKWKQL SLIIYVLRDF FTNFTQKKSQ LEQDQNDHQS YEVKRCSIML
560 570 580 590 600
SDAAQRTVMS VSSYMDNHNV TPYFAWNCSY YLFNAVLVPI KTLLSNSKSN
610 620 630 640 650
AENNETAQLL QQINTVLMLL KKLATFKIQT CEKYIQVLEE VCAPFLLSQC
660 670 680 690 700
AIPLPHISYN NSNGSAIKNI VGSATIAQYP TLPEENVNNI SVKYVSPGSV
710 720 730 740 750
GPSPVPLKSG ASFSDLVKLL SNRPPSRNSP VTIPRSTPSH RSVTPFLGQQ
760 770 780 790 800
QQLQSLVPLT PSALFGGANF NQSGNIADSS LSFTFTNSSN GPNLITTQTN
810 820 830 840 850
SQALSQPIAS SNVHDNFMNN EITASKIDDG NNSKPLSPGW TDQTAYNAFG
860 870 880
ITTGMFNTTT MDDVYNYLFD DEDTPPNPKK E
Length:881
Mass (Da):99,403
Last modified:November 1, 1995 - v2
Checksum:i29D7FF68B0B05880
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01486 Genomic DNA. Translation: AAA34626.1.
Z67751 Genomic DNA. Translation: CAA91596.1.
Z73604 Genomic DNA. Translation: CAA97969.1.
BK006949 Genomic DNA. Translation: DAA11189.1.
PIRiA05022. RGBYG4.
RefSeqiNP_015076.1. NM_001184062.1.

Genome annotation databases

EnsemblFungiiYPL248C; YPL248C; YPL248C.
GeneIDi855828.
KEGGisce:YPL248C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K01486 Genomic DNA. Translation: AAA34626.1.
Z67751 Genomic DNA. Translation: CAA91596.1.
Z73604 Genomic DNA. Translation: CAA97969.1.
BK006949 Genomic DNA. Translation: DAA11189.1.
PIRiA05022. RGBYG4.
RefSeqiNP_015076.1. NM_001184062.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AW6NMR-A1-43[»]
1D66X-ray2.70A/B1-65[»]
1HBWNMR-A/B50-106[»]
3BTSX-ray2.70E/F854-874[»]
3COQX-ray2.40A/B8-96[»]
ProteinModelPortaliP04386.
SMRiP04386. Positions 8-96.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35915. 88 interactions.
DIPiDIP-593N.
IntActiP04386. 5 interactions.
MINTiMINT-1510289.
STRINGi4932.YPL248C.

Proteomic databases

PaxDbiP04386.
PeptideAtlasiP04386.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL248C; YPL248C; YPL248C.
GeneIDi855828.
KEGGisce:YPL248C.

Organism-specific databases

CYGDiYPL248c.
EuPathDBiFungiDB:YPL248C.
SGDiS000006169. GAL4.

Phylogenomic databases

eggNOGiNOG85363.
HOGENOMiHOG000112689.
InParanoidiP04386.
KOiK09241.
OMAiFRYILWE.
OrthoDBiEOG7J44JV.

Enzyme and pathway databases

BioCyciYEAST:G3O-34134-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP04386.
NextBioi980383.
PROiP04386.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR005600. Gal4_dimer_dom.
IPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF04082. Fungal_trans. 1 hit.
PF03902. Gal4_dimer. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of the Saccharomyces cerevisiae GAL4 gene."
    Laughon A., Gesteland R.F.
    Mol. Cell. Biol. 4:260-267(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Genetic evidence that zinc is an essential co-factor in the DNA binding domain of GAL4 protein."
    Johnston M.
    Nature 328:353-355(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, ZINC REQUIREMENT.
  5. "An activator target in the RNA polymerase II holoenzyme."
    Koh S.S., Ansari A.Z., Ptashne M., Young R.A.
    Mol. Cell 1:895-904(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRB4.
  6. "Evidence that Gal11 protein is a target of the Gal4 activation domain in the mediator."
    Jeong C.-J., Yang S.-H., Xie Y., Zhang L., Johnston S.A., Kodadek T.
    Biochemistry 40:9421-9427(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GAL11.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Nine-amino-acid transactivation domain: establishment and prediction utilities."
    Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
    Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  9. "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-712, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-694; SER-696; SER-699 AND SER-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "DNA recognition by GAL4: structure of a protein-DNA complex."
    Marmorstein R., Carey M., Ptashne M., Harrison S.C.
    Nature 356:408-414(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-65.
  12. "GAL4 transcription factor is not a 'zinc finger' but forms a Zn(II)2Cys6 binuclear cluster."
    Pan T., Coleman J.E.
    Proc. Natl. Acad. Sci. U.S.A. 87:2077-2081(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
  13. "Sequential assignments of the 1H NMR resonances of Zn(II)2 and 113Cd(II)2 derivatives of the DNA-binding domain of the GAL4 transcription factor reveal a novel structural motif for specific DNA recognition."
    Pan T., Coleman J.E.
    Biochemistry 30:4212-4222(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
  14. "Complete assignment of the 1H NMR spectrum and secondary structure of the DNA binding domain of GAL4."
    Gadhavi P.L., Raine A.R.C., Alefounder P.R., Laue E.D.
    FEBS Lett. 276:49-53(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
  15. "Structure of the DNA-binding domain of zinc GAL4."
    Kraulis P.J., Raine A.R.C., Gadhavi P.L., Laue E.D.
    Nature 356:448-450(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
  16. "Solution structure of the DNA-binding domain of Cd2-GAL4 from S. cerevisiae."
    Baleja J.D., Marmorstein R., Harrison S.C., Wagner G.
    Nature 356:450-453(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.

Entry informationi

Entry nameiGAL4_YEAST
AccessioniPrimary (citable) accession number: P04386
Secondary accession number(s): D6W3C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 166 molecules/cell in log phase SD medium.1 Publication

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

External Data

Dasty 3

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 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.