ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P04386


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name GAL4_YEAST
Primary accession number P04386
Secondary accession numbers None
Integrated into Swiss-Prot on March 20, 1987
Sequence was last modified on November 1, 1995 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 109)
Name and origin of the protein
Protein name Regulatory protein GAL4
Synonyms None
Gene name
Name: GAL4
OrderedLocusNames: YPL248C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6366516 [NCBI, ExPASy, EBI, Israel, Japan]
Laughon A., Gesteland R.F.;
"Primary structure of the Saccharomyces cerevisiae GAL4 gene.";
Mol. Cell. Biol. 4:260-267(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
MUTAGENESIS, AND ZINC REQUIREMENT.
DOI=10.1038/328353a0; PubMed=3299106 [NCBI, ExPASy, EBI, Israel, Japan]
Johnston M.;
"Genetic evidence that zinc is an essential co-factor in the DNA binding domain of GAL4 protein.";
Nature 328:353-355(1987).
[4]
INTERACTION WITH SRB4.
DOI=10.1016/S1097-2765(00)80088-X; PubMed=9660972 [NCBI, ExPASy, EBI, Israel, Japan]
Koh S.S., Ansari A.Z., Ptashne M., Young R.A.;
"An activator target in the RNA polymerase II holoenzyme.";
Mol. Cell 1:895-904(1998).
[5]
INTERACTION WITH GAL11.
DOI=10.1021/bi010011k; PubMed=11478912 [NCBI, ExPASy, EBI, Israel, Japan]
Jeong C.-J., Yang S.-H., Xie Y., Zhang L., Johnston S.A., Kodadek T.;
"Evidence that Gal11 protein is a target of the Gal4 activation domain in the mediator.";
Biochemistry 40:9421-9427(2001).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[8]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-65.
DOI=10.1038/356408a0; PubMed=1557122 [NCBI, ExPASy, EBI, Israel, Japan]
Marmorstein R., Carey M., Ptashne M., Harrison S.C.;
"DNA recognition by GAL4: structure of a protein-DNA complex.";
Nature 356:408-414(1992).
[9]
STRUCTURE BY NMR OF ZINC-BINDING REGION.
DOI=10.1073/pnas.87.6.2077; PubMed=2107541 [NCBI, ExPASy, EBI, Israel, Japan]
Pan T., Coleman J.E.;
"GAL4 transcription factor is not a 'zinc finger' but forms a Zn(II)2Cys6 binuclear cluster.";
Proc. Natl. Acad. Sci. U.S.A. 87:2077-2081(1990).
[10]
STRUCTURE BY NMR OF ZINC-BINDING REGION.
DOI=10.1021/bi00231a016; PubMed=2021614 [NCBI, ExPASy, EBI, Israel, Japan]
Pan T., Coleman J.E.;
"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.";
Biochemistry 30:4212-4222(1991).
[11]
STRUCTURE BY NMR OF ZINC-BINDING REGION.
DOI=10.1016/0014-5793(90)80504-C; PubMed=2265711 [NCBI, ExPASy, EBI, Israel, Japan]
Gadhavi P.L., Raine A.R.C., Alefounder P.R., Laue E.D.;
"Complete assignment of the 1H NMR spectrum and secondary structure of the DNA binding domain of GAL4.";
FEBS Lett. 276:49-53(1990).
[12]
STRUCTURE BY NMR OF ZINC-BINDING REGION.
DOI=10.1038/356448a0; PubMed=1557129 [NCBI, ExPASy, EBI, Israel, Japan]
Kraulis P.J., Raine A.R.C., Gadhavi P.L., Laue E.D.;
"Structure of the DNA-binding domain of zinc GAL4.";
Nature 356:448-450(1992).
[13]
STRUCTURE BY NMR OF ZINC-BINDING REGION.
DOI=10.1038/356450a0; PubMed=1557130 [NCBI, ExPASy, EBI, Israel, Japan]
Baleja J.D., Marmorstein R., Harrison S.C., Wagner G.;
"Solution structure of the DNA-binding domain of Cd2-GAL4 from S. cerevisiae.";
Nature 356:450-453(1992).
Comments
  • FUNCTION: This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which encode 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.
  • SUBUNIT: Binds DNA as a homodimer. Interacts directly with the mediator subunits GAL11/MED15 and SRB4/MED17.
  • SUBCELLULAR LOCATION: Nucleus.
  • PTM: Association between GAL11 and GAL4 may serve to expedite phosphorylation of GAL4.
  • MISCELLANEOUS: Present with 166 molecules/cell in log phase SD medium.
  • SIMILARITY: Contains 1 Zn(2)-C6 fungal-type DNA-binding domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K01486; AAA34626.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z67751; CAA91596.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z73604; CAA97969.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A05022; RGBYG4.
RefSeq NP_015076.1; -.
3D structure databases
PDB
1AW6; NMR; -; A=1-43.[ExPASy / RCSB / EBI]
1D66; X-ray; 2.70 A; A/B=1-65.[ExPASy / RCSB / EBI]
1HBW; NMR; -; A/B=50-106.[ExPASy / RCSB / EBI]
3BTS; X-ray; 2.70 A; E/F=854-874.[ExPASy / RCSB / EBI]
3COQ; X-ray; 2.40 A; A/B=8-96.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AW6; -.
1D66; -.
1HBW; -.
3BTS; -.
3COQ; -.
ModBase P04386.
Protein-protein interaction databases
DIP DIP:593N; -.
Organism-specific databases
CYGD YPL248c; -.
SGD S000006169; GAL4.
Yeast-GFP YPL248C.
Gene expression databases
ArrayExpress P04386; -.
GermOnline YPL248C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0043565; Molecular function: sequence-specific DNA binding (inferred from direct assay from SGD).
GO:0016563; Molecular function: transcription activator activity (inferred from direct assay from SGD).
GO:0003700; Molecular function: transcription factor activity (inferred from direct assay from SGD).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006012; Biological process: galactose metabolic process (inferred from mutant phenotype from SGD).
GO:0000411; Biological process: positive regulation of transcription by galactose (inferred from direct assay from SGD).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR007219; Fungal_trans.
IPR001138; Fungi_Trscrp_N.
IPR005600; Gal4_dimer.
Graphical view of domain structure.
Pfam PF04082; Fungal_trans; 1.
PF03902; Gal4_dimer; 1.
PF00172; Zn_clus; 1.
Pfam graphical view of domain structure.
SMART SM00066; GAL4; 1.
SMART graphical view of domain structure.
PROSITE PS00463; ZN2_CY6_FUNGAL_1; 1.
PS50048; ZN2_CY6_FUNGAL_2; 1.
PROSITE graphical view of domain structure (profiles).
Other
SWISS-3DIMAGE P04386.
Proteomic databases
PeptideAtlas P04386; -.
PRIDE P04386; -.
Genome annotation databases
Ensembl YPL248C; Saccharomyces cerevisiae. [Contig view]
GeneID 855828; -.
GenomeReviews U00094_GR; YPL248C.
KEGG sce:YPL248C; -.
NMPDR fig|4932.3.peg.6203; -.
Phylogenomic databases
HOGENOM P04386; -.
OMA P04386; IYESELT.
Other
NextBio 980383; -.
ProtoNet P04386.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Activator; Carbohydrate metabolism; Complete proteome; DNA-binding; Galactose metabolism; Metal-binding; Nucleus; Phosphoprotein; Transcription; Transcription regulation; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   881  881     Regulatory protein GAL4. PRO_0000114951
DNA_BIND   11    38  28     Zn(2)-C6 fungal-type. 
METAL   11    11        Zinc 1. 
METAL   11    11        Zinc 2. 
METAL   14    14        Zinc 1. 
METAL   21    21        Zinc 1. 
METAL   28    28        Zinc 1. 
METAL   28    28        Zinc 2. 
METAL   31    31        Zinc 2. 
METAL   38    38        Zinc 2. 
MOD_RES   712   712        Phosphoserine. 
MUTAGEN   26    26        P->L: Loss of DNA-binding. 
HELIX   12    17  6      
STRAND   25    27  3      
HELIX   29    33  5      
HELIX   51    71  21      
STRAND   73    75  3      
HELIX   77    82  6      
HELIX   86    93  8      
Sequence information
Length: 881 AA [This is the length of the unprocessed precursor] Molecular weight: 99403 Da [This is the MW of the unprocessed precursor] CRC64: 29D7FF68B0B05880 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKLLSSIEQA CDICRLKKLK CSKEKPKCAK CLKNNWECRY SPKTKRSPLT RAHLTEVESR 

        70         80         90        100        110        120 
LERLEQLFLL IFPREDLDMI LKMDSLQDIK ALLTGLFVQD NVNKDAVTDR LASVETDMPL 

       130        140        150        160        170        180 
TLRQHRISAT SSSEESSNKG QRQLTVSIDS AAHHDNSTIP LDFMPRDALH GFDWSEEDDM 

       190        200        210        220        230        240 
SDGLPFLKTD PNNNGFFGDG SLLCILRSIG FKPENYTNSN VNRLPTMITD RYTLASRSTT 

       250        260        270        280        290        300 
SRLLQSYLNN FHPYCPIVHS PTLMMLYNNQ IEIASKDQWQ ILFNCILAIG AWCIEGESTD 

       310        320        330        340        350        360 
IDVFYYQNAK SHLTSKVFES GSIILVTALH LLSRYTQWRQ KTNTSYNFHS FSIRMAISLG 

       370        380        390        400        410        420 
LNRDLPSSFS DSSILEQRRR IWWSVYSWEI QLSLLYGRSI QLSQNTISFP SSVDDVQRTT 

       430        440        450        460        470        480 
TGPTIYHGII ETARLLQVFT KIYELDKTVT AEKSPICAKK CLMICNEIEE VSRQAPKFLQ 

       490        500        510        520        530        540 
MDISTTALTN LLKEHPWLSF TRFELKWKQL SLIIYVLRDF FTNFTQKKSQ LEQDQNDHQS 

       550        560        570        580        590        600 
YEVKRCSIML SDAAQRTVMS VSSYMDNHNV TPYFAWNCSY YLFNAVLVPI KTLLSNSKSN 

       610        620        630        640        650        660 
AENNETAQLL QQINTVLMLL KKLATFKIQT CEKYIQVLEE VCAPFLLSQC AIPLPHISYN 

       670        680        690        700        710        720 
NSNGSAIKNI VGSATIAQYP TLPEENVNNI SVKYVSPGSV GPSPVPLKSG ASFSDLVKLL 

       730        740        750        760        770        780 
SNRPPSRNSP VTIPRSTPSH RSVTPFLGQQ QQLQSLVPLT PSALFGGANF NQSGNIADSS 

       790        800        810        820        830        840 
LSFTFTNSSN GPNLITTQTN SQALSQPIAS SNVHDNFMNN EITASKIDDG NNSKPLSPGW 

       850        860        870        880 
TDQTAYNAFG ITTGMFNTTT MDDVYNYLFD DEDTPPNPKK E 

P04386 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!