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P04386 (GAL4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Regulatory protein GAL4
Gene names
Name:GAL4
Ordered Locus Names:YPL248C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length881 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 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.

Subunit structure

Binds DNA as a homodimer. Interacts directly with the mediator subunits GAL11/MED15 and SRB4/MED17. Ref.5 Ref.6

Subcellular location

Nucleus.

Domain

the 9aaTAD motif (residues 862 to 870) is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.8

Post-translational modification

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

Miscellaneous

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

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 881881Regulatory protein GAL4
PRO_0000114951

Regions

DNA binding11 – 3828Zn(2)-C6 fungal-type
Motif862 – 87099aaTAD

Sites

Metal binding111Zinc 1
Metal binding111Zinc 2
Metal binding141Zinc 1
Metal binding211Zinc 1
Metal binding281Zinc 1
Metal binding281Zinc 2
Metal binding311Zinc 2
Metal binding381Zinc 2

Amino acid modifications

Modified residue6941Phosphotyrosine Ref.10
Modified residue6961Phosphoserine Ref.10
Modified residue6991Phosphoserine Ref.10
Modified residue7031Phosphoserine Ref.10
Modified residue7121Phosphoserine Ref.9

Experimental info

Mutagenesis261P → L: Loss of DNA-binding.

Secondary structure

............... 881
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04386 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 29D7FF68B0B05880

FASTA88199,403
        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K01486 Genomic DNA. Translation: AAA34626.1.
Z67751 Genomic DNA. Translation: CAA91596.1.
Z73604 Genomic DNA. Translation: CAA97969.1.
BK006949 Genomic DNA. Translation: DAA11189.1.
PIRRGBYG4. A05022.
RefSeqNP_015076.1. NM_001184062.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP04386.
SMRP04386. Positions 8-96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35915. 87 interactions.
DIPDIP-593N.
IntActP04386. 5 interactions.
MINTMINT-1510289.
STRING4932.YPL248C.

Proteomic databases

PaxDbP04386.
PeptideAtlasP04386.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL248C; YPL248C; YPL248C.
GeneID855828.
KEGGsce:YPL248C.

Organism-specific databases

CYGDYPL248c.
SGDS000006169. GAL4.

Phylogenomic databases

eggNOGNOG85363.
HOGENOMHOG000112689.
KOK09241.
OMAIYESELT.
OrthoDBEOG7J44JV.

Enzyme and pathway databases

BioCycYEAST:G3O-34134-MONOMER.

Gene expression databases

GenevestigatorP04386.

Family and domain databases

Gene3D4.10.240.10. 1 hit.
InterProIPR005600. Gal4_dimer_dom.
IPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamPF04082. Fungal_trans. 1 hit.
PF03902. Gal4_dimer. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMSSF57701. SSF57701. 1 hit.
PROSITEPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04386.
NextBio980383.

Entry information

Entry nameGAL4_YEAST
AccessionPrimary (citable) accession number: P04386
Secondary accession number(s): D6W3C3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: November 1, 1995
Last modified: March 19, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references