Reviewed, UniProtKB/Swiss-Prot P07248 (ADR1_YEAST)

Names and origin

Protein names

Recommended name:
    Regulatory protein ADR1

Gene names

Name:	ADR1
Ordered Locus Names:	YDR216W
ORF Names:	YD8142.16, YD8142B.08

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	1323 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).
Subcellular location	Nucleus.
Post-translational modification	Phosphorylation at Ser-230 by cAMP-dependent protein kinase A does not affect DNA binding but appears to prevent transcription of ADH2 during glucose repression.
Sequence similarities	Contains 2 C2H2-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	negative regulation of transcription from RNA polymerase II promoter by glucose Inferred from mutant phenotype. Source: SGD peroxisome organization Inferred from mutant phenotype. Source: SGD regulation of carbohydrate metabolic process Inferred from genetic interaction. Source: SGD transcription Inferred from genetic interaction. Source: SGD
Cellular component	nucleus Inferred from direct assay. Source: SGD
Molecular function	sequence-specific DNA binding Inferred from direct assay. Source: SGD transcription factor activity Inferred from physical interaction. 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 – 1323

1323

Regulatory protein ADR1

PRO_0000046801

Regions

Zinc finger

104 – 126

23

C2H2-type 1

Zinc finger

132 – 155

24

C2H2-type 2

Amino acid modifications

Modified residue

193

1

Phosphothreonine Ref.5

Modified residue

212

1

Phosphoserine Ref.5

Modified residue

230

1

Phosphoserine; by PKA; in vitro Ref.5 Ref.12

Modified residue

232

1

Phosphoserine Ref.4

Modified residue

259

1

Phosphothreonine Ref.5 Ref.3

Modified residue

301

1

Phosphoserine Ref.5

Modified residue

322

1

Phosphoserine Ref.5

Modified residue

323

1

Phosphoserine Ref.5

Modified residue

327

1

Phosphothreonine Ref.5

Modified residue

400

1

Phosphoserine Ref.5

Modified residue

401

1

Phosphoserine Ref.5

Modified residue

475

1

Phosphoserine Ref.5

Modified residue

1248

1

Phosphothreonine Ref.5

Modified residue

1250

1

Phosphoserine Ref.5

Experimental info

Mutagenesis

106

1

C → Y: Suppresses activity.

Mutagenesis

109

1

C → Y: Suppresses activity.

Mutagenesis

114

1

A → V: Lowers activity.

Mutagenesis

118

1

H → Y: Suppresses activity.

Mutagenesis

122

1

H → Y: Suppresses activity.

Mutagenesis

134

1

C → Y: Suppresses activity.

Mutagenesis

142

1

T → I: Lowers activity.

Sequence conflict

1216

1

D → H in AAA73863. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

1323

Helix Strand Turn

Details...

Turn

107 – 109

3

Helix

116 – 126

11

Turn

135 – 137

3

Beta strand

142 – 144

3

Helix

145 – 151

7

Sequences

	Sequence		Length	Mass (Da)
	P07248-1 [UniParc]. Last modified December 21, 2004. Version 2. Checksum: EE807290EA6CC5C2	FASTA	1,323	150,941
	10 20 30 40 50 60 MANVEKPNDC SGFPVVDLNS CFSNGFNNEK QEIEMETDDS PILLMSSSAS RENSNTFSVI 70 80 90 100 110 120 QRTPDGKIIT TNNNMNSKIN KQLDKLPENL RLNGRTPSGK LRSFVCEVCT RAFARQEHLK 130 140 150 160 170 180 RHYRSHTNEK PYPCGLCNRC FTRRDLLIRH AQKIHSGNLG ETISHTKKVS RTITKARKNS 190 200 210 220 230 240 ASSVKFQTPT YGTPDNGNFL NRTTANTRRK ASPEANVKRK YLKKLTRRAS FSAQSASSYA 250 260 270 280 290 300 LPDQSSLEQH PKDRVKFSTP ELVPLDLKNP ELDSSFDLNM NLDLNLNLDS NFNIALNRSD 310 320 330 340 350 360 SSGSTMNLDY KLPESANNYT YSSGSPTRAY VGANTNSKNA SFNDADLLSS SYWIKAYNDH 370 380 390 400 410 420 LFSVSESDET SPMNSELNDT KLIVPDFKST IHHLKDSRSS SWTVAIDNNS NNNKVSDNQP 430 440 450 460 470 480 DFVDFQELLD NDTLGNDLLE TTAVLKEFEL LHDDSVSATA TSNEIDLSHL NLSNSPISPH 490 500 510 520 530 540 KLIYKNKEGT NDDMLISFGL DHPSNREDDL DKLCNMTRDV QAIFSQYLKG EESKRSLEDF 550 560 570 580 590 600 LSTSNRKEKP DSGNYTFYGL DCLTLSKISR ALPASTVNNN QPSHSIESKL FNEPMRNMCI 610 620 630 640 650 660 KVLRYYEKFS HDSSESVMDS NPNLLSKELL MPAVSELNEY LDLFKNNFLP HFPIIHPSLL 670 680 690 700 710 720 DLDLDSLQRY TNEDGYDDAE NAQLFDRLSQ GTDKEYDYEH YQILSISKIV CLPLFMATFG 730 740 750 760 770 780 SLHKFGYKSQ TIELYEMSRR ILHSFLETKR RCRSTTVNDS YQNIWLMQSL ILSFMFALVA 790 800 810 820 830 840 DYLEKIDSSL MKRQLSALCS TIRSNCLPTI SANSEKSINN NNEPLTFGSP LQYIIFESKI 850 860 870 880 890 900 RCTLMAYDFC QFLKCFFHIK FDLSIKEKDV ETIYIPDNES KWASESIICN GHVVQKQNFY 910 920 930 940 950 960 DFRNFYYSFT YGHLHSIPEF LGSSMIYYEY DLRKGTKSHV FLDRIDTKRL ERSLDTSSYG 970 980 990 1000 1010 1020 NDNMAATNKN IAILIDDTII LKNNLMSMRF IKQIDRSFTE KVRKGQIAKI YDSFLNSVRL 1030 1040 1050 1060 1070 1080 NFLKNYSVEV LCEFLVALNF SIRNISSLYV EEESDCSQRM NSPELPRIHL NNQALSVFNL 1090 1100 1110 1120 1130 1140 QGYYYCFILI IKFLLDFEAT PNFKLLRIFI ELRSLANSIL LPTLSRLYPQ EFSGFPDVVF 1150 1160 1170 1180 1190 1200 TQQFINKDNG MLVPGLSANE HHNGASAAVK TKLAKKINVE GLAMFINEIL VNSFNDTSFL 1210 1220 1230 1240 1250 1260 NMEDPIRNEF SFDNGDRAVT DLPRSAHFLS DTGLEGINFS GLNDSHQTVS TLNLLRYGEN 1270 1280 1290 1300 1310 1320 HSSKHKNGGK GQGFAEKYQL SLKYVTIAKL FFTNVKENYI HCHMLDKMAS DFHTLENHLK GNS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence homology of the yeast regulatory protein ADR1 with Xenopus transcription factor TFIIIA." Hartshorne T.A., Blumberg H., Young E.T. Nature 320:283-287(1986) [PubMed: 3515197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-259, MASS SPECTROMETRY.
[4]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY.
[5]	"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 THR-193; SER-212; SER-230; THR-259; SER-301; SER-322; SER-323; THR-327; SER-400; SER-401; SER-475; THR-1248 AND SER-1250, MASS SPECTROMETRY.
[6]	"Zinc-dependent structure of a single-finger domain of yeast ADR1." Parraga G., Horvath S.J., Eisen A., Taylor W.E., Hood L., Young E.T., Klevit R.E. Science 241:1489-1492(1988) [PubMed: 3047872] [Abstract] Cited for: STRUCTURE BY NMR OF ZINC-FINGERS.
[7]	"ADR1a, a zinc finger peptide, exists in two folded conformations." Xu R.X., Horvath S.J., Klevit R.E. Biochemistry 30:3365-3371(1991) [PubMed: 2012802] [Abstract] Cited for: STRUCTURE BY NMR OF 131-159.
[8]	"A folding transition and novel zinc finger accessory domain in the transcription factor ADR1." Bowers P.M., Schaufler L.E., Klevit R.E. Nat. Struct. Biol. 6:478-485(1999) [PubMed: 10331877] [Abstract] Cited for: STRUCTURE BY NMR OF 102-161.
[9]	"Two zinc fingers of a yeast regulatory protein shown by genetic evidence to be essential for its function." Blumberg H., Eisen A., Sledziewski A., Bader D., Young E.T. Nature 328:443-445(1987) [PubMed: 3112579] [Abstract] Cited for: MUTAGENESIS.
[10]	"Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: residues that contact DNA and that transactivate." Thukral S.K., Morrison M.L., Young E.T. Proc. Natl. Acad. Sci. U.S.A. 88:9188-9192(1991) [PubMed: 1924382] [Abstract] Cited for: MUTAGENESIS.
[11]	"Mutations in the zinc fingers of ADR1 that change the specificity of DNA binding and transactivation." Thukral S.K., Morrison M.L., Young E.T. Mol. Cell. Biol. 12:2784-2792(1992) [PubMed: 1588970] [Abstract] Cited for: MUTAGENESIS.
[12]	"ADR1c mutations enhance the ability of ADR1 to activate transcription by a mechanism that is independent of effects on cyclic AMP-dependent protein kinase phosphorylation of Ser-230." Denis C.L., Fontaine S.C., Chase D., Kemp B.E., Bemis L.T. Mol. Cell. Biol. 12:1507-1514(1992) [PubMed: 1549108] [Abstract] Cited for: MUTAGENESIS, PHOSPHORYLATION AT SER-230.
[13]	"A mutation outside the two zinc fingers of ADR1 can suppress defects in either finger." Camier S., Kacherovsky N., Young E.T. Mol. Cell. Biol. 12:5758-5767(1992) [PubMed: 1448103] [Abstract] Cited for: MUTAGENESIS.
[14]	"Mutations in the zinc-finger region of the yeast regulatory protein ADR1 affect both DNA binding and transcriptional activation." Cook W.J., Mosley S.P., Audino D.C., Mullaney D.L., Rovelli A., Stewart G., Denis C.L. J. Biol. Chem. 269:9374-9379(1994) [PubMed: 8132676] [Abstract] Cited for: MUTAGENESIS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U28414 Genomic DNA. Translation: AAA73863.1.
Z48612 Genomic DNA. Translation: CAA88496.1.
Z68194 Genomic DNA. Translation: CAA92359.1.
Z68195 Genomic DNA. Translation: CAA92367.1.

PIR

A24534.

RefSeq

NP_010502.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ARD	NMR	-	A	102-130	[»]
1ARE	NMR	-	A	102-130	[»]
1ARF	NMR	-	A	102-130	[»]
1PAA	NMR	-	A	134-159	[»]
2ADR	NMR	-	A	102-161	[»]

DisProt

DP00077.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-7N.

IntAct

P07248. 14 interactions.

STRING

P07248.

Proteomic databases

PeptideAtlas

P07248.

PRIDE

P07248.

Genome annotation databases

Ensembl

YDR216W; YDR216W; YDR216W; Saccharomyces cerevisiae. [Genome view]

GeneID

851802.

KEGG

sce:YDR216W.

NMPDR

fig|4932.3.peg.1259.

Organism-specific databases

CYGD

YDR216w.

SGD

S000002624. ADR1.

Phylogenomic databases

eggNOG

fuNOG08066.

OMA

AFARQEH.

OrthoDB

EOG9CG1RB.

PhylomeDB

P07248.

Gene expression databases

ArrayExpress

P07248.

Genevestigator

P07248.

GermOnline

YDR216W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Gene3D

G3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 1 hit.

Pfam

PF00096. zf-C2H2. 1 hit.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 2 hits.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

969641.

Entry information

Entry name

ADR1_YEAST

Accession

Primary (citable) accession number: P07248
Secondary accession number(s): Q04919

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	December 21, 2004
Last modified:	February 9, 2010
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)