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Protein

Transcription factor PDR1

Gene

PDR1

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

Positive regulator of proteins involved in permeability. PDR1 and PDR3 jointly control the transcription level of both SNQ2 and PDR5.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi46 – 7227Zn(2)-C6 fungal-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • positive regulation of cellular response to drug Source: SGD
  • positive regulation of transcription from RNA polymerase II promoter Source: SGD
  • transcription from RNA polymerase II promoter Source: GOC
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-30534-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor PDR1
Alternative name(s):
Pleiotropic drug resistance protein 1
Gene namesi
Name:PDR1
Synonyms:AMY1, ANT1, BOR2, CYH3, NRA2, SMR2, TIL1, TPE1, TPE3
Ordered Locus Names:YGL013C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL013C.
SGDiS000002981. PDR1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10681068Transcription factor PDR1PRO_0000114961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei930 – 9301PhosphoserineCombined sources
Modified residuei942 – 9421PhosphoserineCombined sources
Modified residuei948 – 9481PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP12383.
PeptideAtlasiP12383.

PTM databases

iPTMnetiP12383.

Interactioni

Protein-protein interaction databases

BioGridi33233. 132 interactions.
DIPiDIP-978N.
IntActiP12383. 13 interactions.
MINTiMINT-562805.

Structurei

3D structure databases

ProteinModelPortaliP12383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00530000069211.
HOGENOMiHOG000115482.
InParanoidiP12383.
OMAiRRNLWWK.
OrthoDBiEOG7D2FQ4.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF04082. Fungal_trans. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12383-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGLTPKNGV HIETGPDTES SADSSNFSTG FSGKIRKPRS KVSKACDNCR
60 70 80 90 100
KRKIKCNGKF PCASCEIYSC ECTFSTRQGG ARIKNLHKTS LEGTTVQVKE
110 120 130 140 150
ETDSSSTSFS NPQRCTDGPC AVEQPTKFFE NFKLGGRSSG DNSGSDGKND
160 170 180 190 200
DDVNRNGFYE DDSESQATLT SLQTTLKNLK EMAHLGTHVT SAIESIELQI
210 220 230 240 250
SDLLKRWEPK VRTKELATTK FYPNKSIETQ LMKNKYCDVV HLTRYAAWSN
260 270 280 290 300
NKKDQDTSSQ PLIDEIFGLY SPFQFLSLQG IGKCFQNYRS KSKCEIFPRT
310 320 330 340 350
AKETIYIMLR FFDVCFHHIN QGCVSIANPL ENYLQKMNLL PSTPSSISSA
360 370 380 390 400
GSPNTAHTKS HVALVINHLP QPFVRNITGI SNSELLSEMN NDISMFGILL
410 420 430 440 450
KMLDMHKNSY QNFLMEITSN PSVAKNTQSI DVLQEFIHYC QAGEALIALC
460 470 480 490 500
YSYYNSTLYN YVDFTCDITH LEQLLYFLDL LFWLSEIYGF EKVLNVAVHF
510 520 530 540 550
VSRVGLSRWE FYVGLDENFA ERRRNLWWKA FYFEKTLASK LGYPSNIDDS
560 570 580 590 600
KINCLLPKNF RDVGFLDNRD FIENVHLVRR SEAFDNMCIS DLKYYGELAV
610 620 630 640 650
LQIVSHFSSS VLFNEKFTSI RNTSKPSVVR EKLLFEVLEI FNETEMKYDA
660 670 680 690 700
IKEQTGKLFD IAFSKDSTEL KVSREDKIMA SKFVLFYEHH FCRMVNESDN
710 720 730 740 750
IVARLCVHRR PSILIENLKI YLHKIYKSWT DMNKILLDFD NDYSVYRSFA
760 770 780 790 800
HYSISCIILV SQAFSVAEFI KVNDVVNMIR VFKRFLDIKI FSENETNEHV
810 820 830 840 850
FNSQSFKDYT RAFSFLTIVT RIMLLAYGES SSTNLDVISK YIDENAPDLK
860 870 880 890 900
GIIELVLDTN SCAYRFLLEP VQKSGFHLTV SQMLKNRKFQ EPLMSNEDNK
910 920 930 940 950
QMKHNSGKNL NPDLPSLKTG TSCLLNGIES PQLPFNGRSA PSPVRNNSLP
960 970 980 990 1000
EFAQLPSFRS LSVSDMINPD YAQPTNGQNN TQVQSNKPIN AQQQIPTSVQ
1010 1020 1030 1040 1050
VPFMNTNEIN NNNNNNNNNK NNINNINNNN SNNFSATSFN LGTLDEFVNN
1060
GDLEDLYSIL WSDVYPDS
Length:1,068
Mass (Da):121,794
Last modified:June 10, 2008 - v2
Checksum:i391BA6C52770436C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111Q → K in AAA34849 (PubMed:3316228).Curated
Sequence conflicti411 – 4111Q → K in AAD13897 (PubMed:1882553).Curated
Sequence conflicti530 – 5301A → R in AAD13897 (PubMed:1882553).Curated
Sequence conflicti820 – 8201T → A in AAA34849 (PubMed:3316228).Curated
Sequence conflicti820 – 8201T → A in AAD13897 (PubMed:1882553).Curated
Sequence conflicti921 – 9211T → I in AAA34849 (PubMed:3316228).Curated
Sequence conflicti921 – 9211T → I in AAD13897 (PubMed:1882553).Curated
Sequence conflicti981 – 9811T → S in AAA34849 (PubMed:3316228).Curated
Sequence conflicti981 – 9811T → S in AAD13897 (PubMed:1882553).Curated
Sequence conflicti1015 – 10195Missing in AAA34849 (PubMed:3316228).Curated
Sequence conflicti1015 – 10195Missing in AAD13897 (PubMed:1882553).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03487 Genomic DNA. Translation: AAA34849.1.
S58126 Genomic DNA. Translation: AAD13897.2.
Z72535 Genomic DNA. Translation: CAA96713.1.
BK006941 Genomic DNA. Translation: DAA08085.1.
PIRiS64015.
RefSeqiNP_011502.1. NM_001180878.1.

Genome annotation databases

EnsemblFungiiYGL013C; YGL013C; YGL013C.
GeneIDi852871.
KEGGisce:YGL013C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03487 Genomic DNA. Translation: AAA34849.1.
S58126 Genomic DNA. Translation: AAD13897.2.
Z72535 Genomic DNA. Translation: CAA96713.1.
BK006941 Genomic DNA. Translation: DAA08085.1.
PIRiS64015.
RefSeqiNP_011502.1. NM_001180878.1.

3D structure databases

ProteinModelPortaliP12383.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33233. 132 interactions.
DIPiDIP-978N.
IntActiP12383. 13 interactions.
MINTiMINT-562805.

PTM databases

iPTMnetiP12383.

Proteomic databases

MaxQBiP12383.
PeptideAtlasiP12383.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL013C; YGL013C; YGL013C.
GeneIDi852871.
KEGGisce:YGL013C.

Organism-specific databases

EuPathDBiFungiDB:YGL013C.
SGDiS000002981. PDR1.

Phylogenomic databases

GeneTreeiENSGT00530000069211.
HOGENOMiHOG000115482.
InParanoidiP12383.
OMAiRRNLWWK.
OrthoDBiEOG7D2FQ4.

Enzyme and pathway databases

BioCyciYEAST:G3O-30534-MONOMER.

Miscellaneous databases

PROiP12383.

Family and domain databases

Gene3Di4.10.240.10. 1 hit.
InterProiIPR007219. Transcription_factor_dom_fun.
IPR001138. Zn2-C6_fun-type_DNA-bd.
[Graphical view]
PfamiPF04082. Fungal_trans. 1 hit.
PF00172. Zn_clus. 1 hit.
[Graphical view]
SMARTiSM00906. Fungal_trans. 1 hit.
SM00066. GAL4. 1 hit.
[Graphical view]
SUPFAMiSSF57701. SSF57701. 1 hit.
PROSITEiPS00463. ZN2_CY6_FUNGAL_1. 1 hit.
PS50048. ZN2_CY6_FUNGAL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The multidrug resistance gene PDR1 from Saccharomyces cerevisiae."
    Balzi E., Chen W., Ulaszewski S., Capieaux E., Goffeau A.
    J. Biol. Chem. 262:16871-16879(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 46191 / IL125-2B.
  2. "The DNA sequencing of the 17 kb HindIII fragment spanning the LEU1 and ATE1 loci on chromosome VII from Saccharomyces cerevisiae reveals the PDR6 gene, a new member of the genetic network controlling pleiotropic drug resistance."
    Chen W., Balzi E., Capieaux E., Choder M., Goffeau A.
    Yeast 7:287-299(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930 AND SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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 SER-21; SER-942 AND SER-948, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPDR1_YEAST
AccessioniPrimary (citable) accession number: P12383
Secondary accession number(s): D6VUC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: June 10, 2008
Last modified: June 8, 2016
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1300 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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