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P19880

- YAP1_YEAST

UniProt

P19880 - YAP1_YEAST

Protein

AP-1-like transcription factor YAP1

Gene

YAP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Transcription activator involved in oxidative stress response and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including the thioredoxin system (TRX2, TRR1), the glutaredoxin system (GSH1, GLR1), superoxide dismutase (SOD1, SOD2), glutathione peroxidase (GPX2), and thiol-specific peroxidases (TSA1, AHP1). The induction of some of these genes requires the cooperative action of both, YAP1 and SKN7. YAP1 preferentially binds to promoters with the core binding site 5'-TTA[CG]TAA-3'. Activity of YAP1 is controlled through oxidation of specific cysteine residues resulting in the alteration of its subcellular location. Oxidative stress (as well as carbon stress, but not increased temperature, acidic pH, or ionic stress) induces nuclear accumulation and as a result YAP1 transcriptional activity. Nuclear export is restored when disulfide bonds are reduced by thioredoxin (TRX2), whose expression is controlled by YAP1, providing a mechanism for negative autoregulation. When overexpressed, YAP1 confers pleiotropic drug-resistance and increases cellular tolerance to cadmium, iron chelators and zinc.13 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. sequence-specific DNA binding Source: InterPro
    3. sequence-specific DNA binding transcription factor activity Source: SGD

    GO - Biological processi

    1. regulation of transcription from RNA polymerase II promoter in response to oxidative stress Source: SGD
    2. response to cadmium ion Source: UniProtKB-KW
    3. response to drug Source: SGD
    4. response to heat Source: SGD
    5. response to metal ion Source: SGD
    6. response to singlet oxygen Source: SGD
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Cadmium resistance, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32612-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AP-1-like transcription factor YAP1
    Alternative name(s):
    Phenanthroline resistance protein PAR1
    Pleiotropic drug resistance protein PDR4
    Gene namesi
    Name:YAP1
    Synonyms:PAR1, PDR4, SNQ3
    Ordered Locus Names:YML007W
    ORF Names:YM9571.12
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYML007w.
    SGDiS000004466. YAP1.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Oxidized YAP1 is found predominantly in the nucleus, while reduced YAP1 is continuously exported to the cytoplasm by CRM1. Nuclear import requires the karyopherin PSE1/KAP121 and is independent on YAP1 oxidation state.

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781Q → A: Dominant negative transcription activator. 1 Publication
    Mutagenesisi620 – 6201C → T: Constitutive nuclear location and transcription activation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 650650AP-1-like transcription factor YAP1PRO_0000076521Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei9 – 91Phosphoserine1 Publication
    Modified residuei14 – 141Phosphoserine3 Publications
    Modified residuei17 – 171Phosphoserine1 Publication
    Modified residuei165 – 1651Phosphothreonine1 Publication
    Modified residuei204 – 2041Phosphoserine1 Publication
    Disulfide bondi303 ↔ 598In nuclear retained form; alternate1 Publication
    Disulfide bondi310 ↔ 629In nuclear retained form; alternate1 Publication
    Modified residuei372 – 3721Phosphoserine1 Publication
    Modified residuei528 – 5281Phosphoserine3 Publications
    Disulfide bondi598 ↔ 629In nuclear retained form; alternate1 Publication
    Disulfide bondi598 ↔ 620In nuclear retained form; alternate1 Publication
    Disulfide bondi598 – 598Interchain (with C-36 in HYR1); transient; in linked form1 Publication
    Disulfide bondi620 ↔ 629In nuclear retained form; alternate1 Publication

    Post-translational modificationi

    Depending on the oxidative stress inducing agent, YAP1 can undergo two distinct conformational changes, both involving disulfide bond formation, and both masking the nuclear export signal, thus abolishing nuclear export by CRM1. The disulfide stress-inducing agent diamide leads to the formation of one of three possible disulfide bonds in the c-CRD. Whereas, peroxide stress induces the formation of a disulfide bond between Cys-303 and Cys-598 (and the possibly stabilizing bond between Cys-310 and Cys-629) which is dependent on the hydroperoxide sensing peroxiredoxin HYR1/GPX3/ORP1 and YBP1.2 Publications

    Keywords - PTMi

    Disulfide bond, Oxidation, Phosphoprotein

    Proteomic databases

    MaxQBiP19880.
    PaxDbiP19880.

    Expressioni

    Inductioni

    YAP1 expression is at least partially regulated at the level of translation. A small upstream open reading frame (uORF) retains the 40S ribosomal subunit. By leaky scanning it then proceeds and reinitiates at the functional YAP1 ORF.

    Gene expression databases

    GenevestigatoriP19880.

    Interactioni

    Subunit structurei

    Homodimer By similarity. YAP1 interacts independent of oxidation state in the cytoplasm with the karyopherin PSE1/KAP121 (and less strongly with KAP123). The reduced form of YAP1 interacts in the nucleus with the nuclear export protein CRM1, and in the cytoplasm with YBP1 and the peroxiredoxin HYR1/GPX3/ORP1. Interacts with RBG1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CNB1P252962EBI-31265,EBI-3968
    YBP1P383154EBI-31265,EBI-20985

    Protein-protein interaction databases

    BioGridi35163. 177 interactions.
    DIPiDIP-1752N.
    IntActiP19880. 41 interactions.
    MINTiMINT-505627.

    Structurei

    Secondary structure

    1
    650
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi289 – 2913
    Beta strandi292 – 2943
    Beta strandi298 – 3003
    Helixi301 – 3088
    Helixi598 – 6069
    Helixi616 – 6238
    Turni624 – 6263
    Helixi638 – 6469

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SSENMR-A279-313[»]
    B565-650[»]
    ProteinModelPortaliP19880.
    SMRiP19880. Positions 63-125, 279-313, 565-650.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19880.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini64 – 12764bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni67 – 9024Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni92 – 12029Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST
    Regioni220 – 378159Transcription activation 1 (PubMed:8182076)1 PublicationAdd
    BLAST
    Regioni430 – 537108Transcription activation 2 (PubMed:8182076)1 PublicationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi5 – 1612Nuclear localization signalAdd
    BLAST
    Motifi50 – 5910Nuclear localization signal
    Motifi614 – 6218Nuclear export signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi411 – 4144Poly-Asn
    Compositional biasi517 – 5215Poly-Asp

    Domaini

    YAP1 contains two cysteine rich domains (CRD), referred to as the N- and C-terminal CRD's, n-CRD (Cys-303, Cys-310 and Cys-315) and c-CRD (Cys-598, Cys-620 and Cys-629), respectively. Cys-315 is not conserved in orthologs in other yeast species. A nuclear export signal is embedded in the c-CRD, with which the nuclear export protein CRM1 interacts only in the absence of disulfide bonds within the c-CRD or between the c-CRD and the n-CRD.

    Sequence similaritiesi

    Belongs to the bZIP family. YAP subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG72873.
    GeneTreeiENSGT00530000069148.
    HOGENOMiHOG000142347.
    KOiK09043.
    OMAiRCSEIWD.
    OrthoDBiEOG7GFBHK.

    Family and domain databases

    Gene3Di1.10.238.100. 1 hit.
    InterProiIPR004827. bZIP.
    IPR013910. TF_PAP1.
    IPR023167. Yap1_redox_dom.
    [Graphical view]
    PfamiPF00170. bZIP_1. 1 hit.
    PF08601. PAP1. 1 hit.
    [Graphical view]
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19880-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVSTAKRSL DVVSPGSLAE FEGSKSRHDE IENEHRRTGT RDGEDSEQPK    50
    KKGSKTSKKQ DLDPETKQKR TAQNRAAQRA FRERKERKMK ELEKKVQSLE 100
    SIQQQNEVEA TFLRDQLITL VNELKKYRPE TRNDSKVLEY LARRDPNLHF 150
    SKNNVNHSNS EPIDTPNDDI QENVKQKMNF TFQYPLDNDN DNDNSKNVGK 200
    QLPSPNDPSH SAPMPINQTQ KKLSDATDSS SATLDSLSNS NDVLNNTPNS 250
    STSMDWLDNV IYTNRFVSGD DGSNSKTKNL DSNMFSNDFN FENQFDEQVS 300
    EFCSKMNQVC GTRQCPIPKK PISALDKEVF ASSSILSSNS PALTNTWESH 350
    SNITDNTPAN VIATDATKYE NSFSGFGRLG FDMSANHYVV NDNSTGSTDS 400
    TGSTGNKNKK NNNNSDDVLP FISESPFDMN QVTNFFSPGS TGIGNNAASN 450
    TNPSLLQSSK EDIPFINANL AFPDDNSTNI QLQPFSESQS QNKFDYDMFF 500
    RDSSKEGNNL FGEFLEDDDD DKKAANMSDD ESSLIKNQLI NEEPELPKQY 550
    LQSVPGNESE ISQKNGSSLQ NADKINNGND NDNDNDVVPS KEGSLLRCSE 600
    IWDRITTHPK YSDIDVDGLC SELMAKAKCS ERGVVINAED VQLALNKHMN 650
    Length:650
    Mass (Da):72,533
    Last modified:October 1, 1993 - v2
    Checksum:i192F20FA71027688
    GO

    Sequence cautioni

    The sequence CAA37827.1 differs from that shown. Reason: Frameshift at positions 291 and 306.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti316 – 3161P → S in CAA43195. (PubMed:1889413)Curated
    Sequence conflicti586 – 5861D → E in CAA41536. (PubMed:2542125)Curated
    Sequence conflicti648 – 6481H → D in CAA37827. (PubMed:2060792)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58693 Genomic DNA. Translation: CAA41536.1.
    X53830 Genomic DNA. Translation: CAA37827.1. Frameshift.
    X60780 Genomic DNA. Translation: CAA43195.1.
    X63268 Genomic DNA. Translation: CAA44917.1.
    Z49810 Genomic DNA. Translation: CAA89945.1.
    BK006946 Genomic DNA. Translation: DAA09892.1.
    PIRiS16706.
    RefSeqiNP_013707.1. NM_001182362.1.

    Genome annotation databases

    EnsemblFungiiYML007W; YML007W; YML007W.
    GeneIDi855005.
    KEGGisce:YML007W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58693 Genomic DNA. Translation: CAA41536.1 .
    X53830 Genomic DNA. Translation: CAA37827.1 . Frameshift.
    X60780 Genomic DNA. Translation: CAA43195.1 .
    X63268 Genomic DNA. Translation: CAA44917.1 .
    Z49810 Genomic DNA. Translation: CAA89945.1 .
    BK006946 Genomic DNA. Translation: DAA09892.1 .
    PIRi S16706.
    RefSeqi NP_013707.1. NM_001182362.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SSE NMR - A 279-313 [» ]
    B 565-650 [» ]
    ProteinModelPortali P19880.
    SMRi P19880. Positions 63-125, 279-313, 565-650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35163. 177 interactions.
    DIPi DIP-1752N.
    IntActi P19880. 41 interactions.
    MINTi MINT-505627.

    Proteomic databases

    MaxQBi P19880.
    PaxDbi P19880.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YML007W ; YML007W ; YML007W .
    GeneIDi 855005.
    KEGGi sce:YML007W.

    Organism-specific databases

    CYGDi YML007w.
    SGDi S000004466. YAP1.

    Phylogenomic databases

    eggNOGi NOG72873.
    GeneTreei ENSGT00530000069148.
    HOGENOMi HOG000142347.
    KOi K09043.
    OMAi RCSEIWD.
    OrthoDBi EOG7GFBHK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32612-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P19880.
    NextBioi 978163.

    Gene expression databases

    Genevestigatori P19880.

    Family and domain databases

    Gene3Di 1.10.238.100. 1 hit.
    InterProi IPR004827. bZIP.
    IPR013910. TF_PAP1.
    IPR023167. Yap1_redox_dom.
    [Graphical view ]
    Pfami PF00170. bZIP_1. 1 hit.
    PF08601. PAP1. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Yeast YAP1 encodes a novel form of the jun family of transcriptional activator proteins."
      Moye-Rowley W.S., Harshman K.D., Parker C.S.
      Genes Dev. 3:283-292(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Characterization of PDR4, a Saccharomyces cerevisiae gene that confers pleiotropic drug resistance in high-copy number: identity with YAP1, encoding a transcriptional activator."
      Hussain M., Lenard J.
      Gene 101:149-152(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The SNQ3 gene of Saccharomyces cerevisiae confers hyper-resistance to several functionally unrelated chemicals."
      Hertle K., Haase E., Brendel M.
      Curr. Genet. 19:429-433(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Identification and characterization of a Saccharomyces cerevisiae gene (PAR1) conferring resistance to iron chelators."
      Schnell N., Entian K.-D.
      Eur. J. Biochem. 200:487-493(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    7. "The PAR1 (YAP1/SNQ3) gene of Saccharomyces cerevisiae, a c-jun homologue, is involved in oxygen metabolism."
      Schnell N., Krems B., Entian K.-D.
      Curr. Genet. 21:269-273(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "Transcriptional activation mediated by the yeast AP-1 protein is required for normal cadmium tolerance."
      Wemmie J.A., Wu A.L., Harshman K.D., Parker C.S., Moye-Rowley W.S.
      J. Biol. Chem. 269:14690-14697(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLN-78.
    9. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    10. "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-14 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-372 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2 interact on polyribosomes with Gcn1."
      Wout P.K., Sattlegger E., Sullivan S.M., Maddock J.R.
      Eukaryot. Cell 8:1061-1071(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBG1.
    14. "Yap, a novel family of eight bZIP proteins in Saccharomyces cerevisiae with distinct biological functions."
      Fernandes L., Rodrigues-Pousada C., Struhl K.
      Mol. Cell. Biol. 17:6982-6993(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    15. "Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor."
      Yan C., Lee L.H., Davis L.I.
      EMBO J. 17:7416-7429(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUCLEAR EXPORT BY CRM1, NUCLEAR EXPORT SIGNAL.
    16. "The yeast transcription factor genes YAP1 and YAP2 are subject to differential control at the levels of both translation and mRNA stability."
      Vilela C., Linz B., Rodrigues-Pousada C., McCarthy J.E.
      Nucleic Acids Res. 26:1150-1159(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, POST-TRANSCRIPTIONAL EXPRESSION CONTROL.
    17. "Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast."
      Lee J., Godon C., Lagniel G., Spector D., Garin J., Labarre J., Toledano M.B.
      J. Biol. Chem. 274:16040-16046(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COOPERATIVITY WITH SKN7, YAP1 DEPENDENT GENES.
    18. "H2O2 sensing through oxidation of the Yap1 transcription factor."
      Delaunay A., Isnard A.D., Toledano M.B.
      EMBO J. 19:5157-5166(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, REDUCTION BY THIOREDOXINS.
    19. "Nuclear import of the yeast AP-1-like transcription factor Yap1p is mediated by transport receptor Pse1p, and this import step is not affected by oxidative stress."
      Isoyama T., Murayama A., Nomoto A., Kuge S.
      J. Biol. Chem. 276:21863-21869(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUCLEAR IMPORT, INTERACTION WITH PSE1.
    20. "Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation."
      Kuge S., Arita M., Murayama A., Maeta K., Izawa S., Inoue Y., Nomoto A.
      Mol. Cell. Biol. 21:6139-6150(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    21. "A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation."
      Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B.
      Cell 111:471-481(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, OXIDATION BY HYR1/GPX3.
    22. "Yap1 accumulates in the nucleus in response to carbon stress in Saccharomyces cerevisiae."
      Wiatrowski H.A., Carlson M.
      Eukaryot. Cell 2:19-26(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "The redox domain of the Yap1p transcription factor contains two disulfide bonds."
      Wood M.J., Andrade E.C., Storz G.
      Biochemistry 42:11982-11991(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, OXIDATION, DISULFIDE BONDS.
    24. "Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling."
      Azevedo D., Tacnet F., Delaunay A., Rodrigues-Pousada C., Toledano M.B.
      Free Radic. Biol. Med. 35:889-900(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ELICITOR SPECIFIC DISULFIDE BONDS.
    25. "Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1 transcription factor."
      Veal E.A., Ross S.J., Malakasi P., Peacock E., Morgan B.A.
      J. Biol. Chem. 278:30896-30904(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH YBP1.
    26. "Regulation of yAP-1 nuclear localization in response to oxidative stress."
      Kuge S., Jones N., Nomoto A.
      EMBO J. 16:1710-1720(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-620, SUBCELLULAR LOCATION.
    27. "A large-scale study of Yap1p-dependent genes in normal aerobic and H2O2-stress conditions: the role of Yap1p in cell proliferation control in yeast."
      Dumond H., Danielou N., Pinto M., Bolotin-Fukuhara M.
      Mol. Microbiol. 36:830-845(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTION PROFILING.
    28. "Genomic expression programs in the response of yeast cells to environmental changes."
      Gasch A.P., Spellman P.T., Kao C.M., Carmel-Harel O., Eisen M.B., Storz G., Botstein D., Brown P.O.
      Mol. Biol. Cell 11:4241-4257(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTION PROFILING.
    29. "Transcription factors regulating the response to oxidative stress in yeast."
      Moye-Rowley W.S.
      Antioxid. Redox Signal. 4:123-140(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    30. Cited for: REVIEW.
    31. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    32. "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-9; SER-14; SER-17; THR-165; SER-204 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiYAP1_YEAST
    AccessioniPrimary (citable) accession number: P19880
    Secondary accession number(s): D6VZG8, P22631, Q06840
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    One of 8 closely related fungi-specific YAP proteins (YAP1 to YAP8), which all seem to be transcription activators of the environmental stress response and metabolism control pathways and to have similar but not identical DNA binding specificities.
    Present with 1600 molecules/cell in log phase SD medium.1 Publication

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

    External Data

    Dasty 3