Regulatory protein GAL4 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P04386 (GAL4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 144. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Regulatory protein GAL4

Gene names

Name:	GAL4
Ordered Locus Names:	YPL248C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	881 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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 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.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Galactose metabolism Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	galactose metabolic process Inferred from mutant phenotype PubMed 6350827. Source: SGD positive regulation of transcription from RNA polymerase II promoter by galactose Inferred from direct assay PubMed 3886158. Source: SGD
Cellular_component	nucleus Inferred from direct assay PubMed 6091123. Source: SGD
Molecular_function	RNA polymerase II core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 3886158. Source: SGD RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay PubMed 3080805. Source: SGD RNA polymerase II transcription factor binding Inferred from direct assay PubMed 14871930. Source: SGD sequence-specific transcription regulatory region DNA binding RNA polymerase II transcription factor recruiting transcription factor activity Inferred from mutant phenotype PubMed 14871930. Source: SGD zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 881

881

Regulatory protein GAL4

PRO_0000114951

Regions

DNA binding

11 – 38

Zn(2)-C6 fungal-type

Motif

862 – 870

9aaTAD

Sites

Metal binding

Zinc 1

Metal binding

Zinc 2

Metal binding

Zinc 1

Metal binding

Zinc 1

Metal binding

Zinc 1

Metal binding

Zinc 2

Metal binding

Zinc 2

Metal binding

Zinc 2

Amino acid modifications

Modified residue

712

Phosphoserine Ref.9

Experimental info

Mutagenesis

P → L: Loss of DNA-binding.

Secondary structure

881

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04386 [UniParc].

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

881

99,403

        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' referencesShow '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. Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[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, MASS SPECTROMETRY.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.

PIR

RGBYG4. A05022.

RefSeq

NP_015076.1. NM_001184062.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AW6	NMR	-	A	1-43	[»]
1D66	X-ray	2.70	A/B	1-65	[»]
1HBW	NMR	-	A/B	50-106	[»]
3BTS	X-ray	2.70	E/F	854-874	[»]
3COQ	X-ray	2.40	A/B	8-96	[»]

ProteinModelPortal

P04386.

SMR

P04386. Positions 8-96.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-593N.

IntAct

P04386. 4 interactions.

STRING

4932.YPL248C.

Proteomic databases

PaxDb

P04386.

PeptideAtlas

P04386.

PRIDE

P04386.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL248C; YPL248C; YPL248C.

GeneID

855828.

KEGG

sce:YPL248C.

Organism-specific databases

CYGD

YPL248c.

SGD

S000006169. GAL4.

Phylogenomic databases

eggNOG

NOG85363.

HOGENOM

HOG000112689.

K09241.

OMA

IYESELT.

OrthoDB

EOG4NS6MF.

Gene expression databases

Genevestigator

P04386.

GermOnline

YPL248C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

4.10.240.10. 1 hit.

InterPro

IPR005600. Gal4_dimer_dom.
IPR007219. Transcription_factor_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]

Pfam

PF04082. Fungal_trans. 1 hit.
PF03902. Gal4_dimer. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]

SMART

SM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]

SUPFAM

SSF57701. Fungi_TrN. 1 hit.

PROSITE

PS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P04386.

NextBio

980383.

Entry information

Entry name

GAL4_YEAST

Accession

Primary (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:	April 3, 2013
This is version 144 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XVI

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents