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Protein

Regulatory protein ADR1

Gene

ADR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2).

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri104 – 126C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri132 – 155C2H2-type 2PROSITE-ProRule annotationAdd BLAST24

GO - Molecular functioni

GO - Biological processi

  • cellular response to oleic acid Source: SGD
  • chromatin organization Source: SGD
  • negative regulation of chromatin silencing Source: SGD
  • peroxisome organization Source: SGD
  • positive regulation of ethanol catabolic process by positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of fatty acid beta-oxidation by positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of peroxisome organization by positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter by oleic acid Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter in response to ethanol Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29797-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory protein ADR1
Gene namesi
Name:ADR1
Ordered Locus Names:YDR216W
ORF Names:YD8142.16, YD8142B.08
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR216W.
SGDiS000002624. ADR1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106C → Y: Suppresses activity. 1
Mutagenesisi109C → Y: Suppresses activity. 1
Mutagenesisi114A → V: Lowers activity. 1
Mutagenesisi118H → Y: Suppresses activity. 1
Mutagenesisi122H → Y: Suppresses activity. 1
Mutagenesisi134C → Y: Suppresses activity. 1
Mutagenesisi142T → I: Lowers activity. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000468011 – 1323Regulatory protein ADR1Add BLAST1323

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54PhosphoserineCombined sources1
Modified residuei188PhosphothreonineCombined sources1
Modified residuei193PhosphothreonineCombined sources1
Modified residuei230Phosphoserine; by PKA; in vitroCombined sources1 Publication1
Modified residuei258PhosphoserineCombined sources1
Modified residuei259PhosphothreonineCombined sources1
Modified residuei299PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Modified residuei325PhosphoserineCombined sources1
Modified residuei327PhosphothreonineCombined sources1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07248.
PRIDEiP07248.

PTM databases

iPTMnetiP07248.

Interactioni

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: SGD
  • TFIIB-class transcription factor binding Source: SGD
  • TFIID-class transcription factor binding Source: SGD

Protein-protein interaction databases

BioGridi32269. 102 interactors.
DIPiDIP-7N.
IntActiP07248. 26 interactors.
MINTiMINT-406601.

Structurei

Secondary structure

11323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi104 – 106Combined sources3
Turni107 – 109Combined sources3
Beta strandi111 – 115Combined sources5
Helixi116 – 126Combined sources11
Beta strandi131 – 133Combined sources3
Turni135 – 137Combined sources3
Beta strandi142 – 144Combined sources3
Helixi145 – 151Combined sources7
Turni152 – 154Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ARDNMR-A102-130[»]
1ARENMR-A102-130[»]
1ARFNMR-A102-130[»]
1PAANMR-A130-159[»]
2ADRNMR-A102-161[»]
5A7Uelectron microscopy4.80A130-158[»]
DisProtiDP00077.
ProteinModelPortaliP07248.
SMRiP07248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07248.

Family & Domainsi

Sequence similaritiesi

Contains 2 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri104 – 126C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri132 – 155C2H2-type 2PROSITE-ProRule annotationAdd BLAST24

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00850000133113.
InParanoidiP07248.
KOiK09466.
OMAiRVLHVYL.
OrthoDBiEOG092C0B9L.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANVEKPNDC SGFPVVDLNS CFSNGFNNEK QEIEMETDDS PILLMSSSAS
60 70 80 90 100
RENSNTFSVI QRTPDGKIIT TNNNMNSKIN KQLDKLPENL RLNGRTPSGK
110 120 130 140 150
LRSFVCEVCT RAFARQEHLK RHYRSHTNEK PYPCGLCNRC FTRRDLLIRH
160 170 180 190 200
AQKIHSGNLG ETISHTKKVS RTITKARKNS ASSVKFQTPT YGTPDNGNFL
210 220 230 240 250
NRTTANTRRK ASPEANVKRK YLKKLTRRAS FSAQSASSYA LPDQSSLEQH
260 270 280 290 300
PKDRVKFSTP ELVPLDLKNP ELDSSFDLNM NLDLNLNLDS NFNIALNRSD
310 320 330 340 350
SSGSTMNLDY KLPESANNYT YSSGSPTRAY VGANTNSKNA SFNDADLLSS
360 370 380 390 400
SYWIKAYNDH LFSVSESDET SPMNSELNDT KLIVPDFKST IHHLKDSRSS
410 420 430 440 450
SWTVAIDNNS NNNKVSDNQP DFVDFQELLD NDTLGNDLLE TTAVLKEFEL
460 470 480 490 500
LHDDSVSATA TSNEIDLSHL NLSNSPISPH KLIYKNKEGT NDDMLISFGL
510 520 530 540 550
DHPSNREDDL DKLCNMTRDV QAIFSQYLKG EESKRSLEDF LSTSNRKEKP
560 570 580 590 600
DSGNYTFYGL DCLTLSKISR ALPASTVNNN QPSHSIESKL FNEPMRNMCI
610 620 630 640 650
KVLRYYEKFS HDSSESVMDS NPNLLSKELL MPAVSELNEY LDLFKNNFLP
660 670 680 690 700
HFPIIHPSLL DLDLDSLQRY TNEDGYDDAE NAQLFDRLSQ GTDKEYDYEH
710 720 730 740 750
YQILSISKIV CLPLFMATFG SLHKFGYKSQ TIELYEMSRR ILHSFLETKR
760 770 780 790 800
RCRSTTVNDS YQNIWLMQSL ILSFMFALVA DYLEKIDSSL MKRQLSALCS
810 820 830 840 850
TIRSNCLPTI SANSEKSINN NNEPLTFGSP LQYIIFESKI RCTLMAYDFC
860 870 880 890 900
QFLKCFFHIK FDLSIKEKDV ETIYIPDNES KWASESIICN GHVVQKQNFY
910 920 930 940 950
DFRNFYYSFT YGHLHSIPEF LGSSMIYYEY DLRKGTKSHV FLDRIDTKRL
960 970 980 990 1000
ERSLDTSSYG NDNMAATNKN IAILIDDTII LKNNLMSMRF IKQIDRSFTE
1010 1020 1030 1040 1050
KVRKGQIAKI YDSFLNSVRL NFLKNYSVEV LCEFLVALNF SIRNISSLYV
1060 1070 1080 1090 1100
EEESDCSQRM NSPELPRIHL NNQALSVFNL QGYYYCFILI IKFLLDFEAT
1110 1120 1130 1140 1150
PNFKLLRIFI ELRSLANSIL LPTLSRLYPQ EFSGFPDVVF TQQFINKDNG
1160 1170 1180 1190 1200
MLVPGLSANE HHNGASAAVK TKLAKKINVE GLAMFINEIL VNSFNDTSFL
1210 1220 1230 1240 1250
NMEDPIRNEF SFDNGDRAVT DLPRSAHFLS DTGLEGINFS GLNDSHQTVS
1260 1270 1280 1290 1300
TLNLLRYGEN HSSKHKNGGK GQGFAEKYQL SLKYVTIAKL FFTNVKENYI
1310 1320
HCHMLDKMAS DFHTLENHLK GNS
Length:1,323
Mass (Da):150,941
Last modified:December 21, 2004 - v2
Checksum:iEE807290EA6CC5C2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1216D → H in AAA73863 (PubMed:3515197).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28414 Genomic DNA. Translation: AAA73863.1.
Z48612 Genomic DNA. Translation: CAA88496.1.
Z68194 Genomic DNA. Translation: CAA92359.1.
Z68195 Genomic DNA. Translation: CAA92367.1.
BK006938 Genomic DNA. Translation: DAA12059.1.
PIRiA24534.
RefSeqiNP_010502.3. NM_001180524.3.

Genome annotation databases

EnsemblFungiiYDR216W; YDR216W; YDR216W.
GeneIDi851802.
KEGGisce:YDR216W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28414 Genomic DNA. Translation: AAA73863.1.
Z48612 Genomic DNA. Translation: CAA88496.1.
Z68194 Genomic DNA. Translation: CAA92359.1.
Z68195 Genomic DNA. Translation: CAA92367.1.
BK006938 Genomic DNA. Translation: DAA12059.1.
PIRiA24534.
RefSeqiNP_010502.3. NM_001180524.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ARDNMR-A102-130[»]
1ARENMR-A102-130[»]
1ARFNMR-A102-130[»]
1PAANMR-A130-159[»]
2ADRNMR-A102-161[»]
5A7Uelectron microscopy4.80A130-158[»]
DisProtiDP00077.
ProteinModelPortaliP07248.
SMRiP07248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32269. 102 interactors.
DIPiDIP-7N.
IntActiP07248. 26 interactors.
MINTiMINT-406601.

PTM databases

iPTMnetiP07248.

Proteomic databases

MaxQBiP07248.
PRIDEiP07248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR216W; YDR216W; YDR216W.
GeneIDi851802.
KEGGisce:YDR216W.

Organism-specific databases

EuPathDBiFungiDB:YDR216W.
SGDiS000002624. ADR1.

Phylogenomic databases

GeneTreeiENSGT00850000133113.
InParanoidiP07248.
KOiK09466.
OMAiRVLHVYL.
OrthoDBiEOG092C0B9L.

Enzyme and pathway databases

BioCyciYEAST:G3O-29797-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP07248.
PROiP07248.

Family and domain databases

Gene3Di3.30.160.60. 2 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 2 hits.
PS50157. ZINC_FINGER_C2H2_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiADR1_YEAST
AccessioniPrimary (citable) accession number: P07248
Secondary accession number(s): D6VSJ9, Q04919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 184 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.