Reviewed, UniProtKB/Swiss-Prot P04386 (GAL4_YEAST)

Names and origin

Protein names

Recommended name:
    Regulatory protein GAL4

Gene names

Name:	GAL4
Ordered Locus Names:	YPL248C

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	881 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.4 Ref.5
Subcellular location	Nucleus.
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. Ref.6
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
Gene Ontology (GO)
Biological process	galactose metabolic process Inferred from mutant phenotype. Source: SGD positive regulation of transcription by galactose Inferred from direct assay. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: SGD
Molecular function	sequence-specific DNA binding Inferred from direct assay. Source: SGD transcription activator activity Inferred from direct assay. Source: SGD transcription factor activity Inferred from direct assay. Source: SGD zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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

28

Zn(2)-C6 fungal-type

Sites

Metal binding

11

1

Zinc 1

Metal binding

11

1

Zinc 2

Metal binding

14

1

Zinc 1

Metal binding

21

1

Zinc 1

Metal binding

28

1

Zinc 1

Metal binding

28

1

Zinc 2

Metal binding

31

1

Zinc 2

Metal binding

38

1

Zinc 2

Amino acid modifications

Modified residue

712

1

Phosphoserine Ref.7

Experimental info

Mutagenesis

26

1

P → L: Loss of DNA-binding.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

881

Helix Strand Turn

Details...

Helix

12 – 17

6

Beta strand

25 – 27

3

Helix

29 – 33

5

Helix

51 – 71

21

Beta strand

73 – 75

3

Helix

77 – 82

6

Helix

86 – 93

8

Sequences

	Sequence		Length	Mass (Da)
	P04386-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 29D7FF68B0B05880	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

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: 6366516] [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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 3299106] [Abstract] Cited for: MUTAGENESIS, ZINC REQUIREMENT.
[4]	"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: 9660972] [Abstract] Cited for: INTERACTION WITH SRB4.
[5]	"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: 11478912] [Abstract] Cited for: INTERACTION WITH GAL11.
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, MASS SPECTROMETRY.
[8]	"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: 1557122] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-65.
[9]	"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: 2107541] [Abstract] Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
[10]	"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: 2021614] [Abstract] Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
[11]	"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: 2265711] [Abstract] Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
[12]	"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: 1557129] [Abstract] Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
[13]	"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: 1557130] [Abstract] Cited for: STRUCTURE BY NMR OF ZINC-BINDING REGION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

K01486 Genomic DNA. Translation: AAA34626.1.
Z67751 Genomic DNA. Translation: CAA91596.1.
Z73604 Genomic DNA. Translation: CAA97969.1.

PIR

RGBYG4. A05022.

RefSeq

NP_015076.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:593N.

STRING

P04386.

Proteomic databases

PeptideAtlas

P04386.

Genome annotation databases

Ensembl

YPL248C; YPL248C; YPL248C; Saccharomyces cerevisiae. [Genome view]

GeneID

855828.

GenomeReviews

Gene locus YPL248C in contig U00094_GR.

KEGG

sce:YPL248C.

NMPDR

fig|4932.3.peg.6203.

Organism-specific databases

CYGD

YPL248c.

SGD

S000006169. GAL4.

Phylogenomic databases

OMA

IYESELT.

Gene expression databases

ArrayExpress

P04386.

Genevestigator

P04386.

GermOnline

YPL248C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR007219. Fungal_trans.
IPR001138. Fungi_Trscrp_N.
IPR005600. Gal4_dimer.
[Graphical view]

Pfam

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

SMART

SM00066. GAL4. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

980383.

Entry information

Entry name

GAL4_YEAST

Accession

Primary (citable) accession number: P04386

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	November 1, 1995
Last modified:	November 3, 2009
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)