AP1_YEAST
ID AP1_YEAST Reviewed; 650 AA.
AC P19880; D6VZG8; P22631; Q06840;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=AP-1-like transcription factor YAP1 {ECO:0000305};
DE AltName: Full=Phenanthroline resistance protein PAR1 {ECO:0000303|PubMed:1889413};
DE AltName: Full=Pleiotropic drug resistance protein PDR4 {ECO:0000303|PubMed:2060792};
GN Name=YAP1 {ECO:0000303|PubMed:2542125};
GN Synonyms=PAR1 {ECO:0000303|PubMed:1889413},
GN PDR4 {ECO:0000303|PubMed:2060792}, SNQ3 {ECO:0000303|PubMed:1878996};
GN OrderedLocusNames=YML007W {ECO:0000312|SGD:S000004466}; ORFNames=YM9571.12;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2542125; DOI=10.1101/gad.3.3.283;
RA Moye-Rowley W.S., Harshman K.D., Parker C.S.;
RT "Yeast YAP1 encodes a novel form of the jun family of transcriptional
RT activator proteins.";
RL Genes Dev. 3:283-292(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2060792; DOI=10.1016/0378-1119(91)90238-7;
RA Hussain M., Lenard J.;
RT "Characterization of PDR4, a Saccharomyces cerevisiae gene that confers
RT pleiotropic drug resistance in high-copy number: identity with YAP1,
RT encoding a transcriptional activator.";
RL Gene 101:149-152(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1878996; DOI=10.1007/bf00312733;
RA Hertle K., Haase E., Brendel M.;
RT "The SNQ3 gene of Saccharomyces cerevisiae confers hyper-resistance to
RT several functionally unrelated chemicals.";
RL Curr. Genet. 19:429-433(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1889413; DOI=10.1111/j.1432-1033.1991.tb16209.x;
RA Schnell N., Entian K.-D.;
RT "Identification and characterization of a Saccharomyces cerevisiae gene
RT (PAR1) conferring resistance to iron chelators.";
RL Eur. J. Biochem. 200:487-493(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [7]
RP FUNCTION.
RX PubMed=1525853; DOI=10.1007/bf00351681;
RA Schnell N., Krems B., Entian K.-D.;
RT "The PAR1 (YAP1/SNQ3) gene of Saccharomyces cerevisiae, a c-jun homologue,
RT is involved in oxygen metabolism.";
RL Curr. Genet. 21:269-273(1992).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLN-78.
RX PubMed=8182076; DOI=10.1016/s0021-9258(17)36680-2;
RA Wemmie J.A., Wu A.L., Harshman K.D., Parker C.S., Moye-Rowley W.S.;
RT "Transcriptional activation mediated by the yeast AP-1 protein is required
RT for normal cadmium tolerance.";
RL J. Biol. Chem. 269:14690-14697(1994).
RN [9]
RP MUTAGENESIS OF CYS-598; CYS-620 AND CYS-629, AND SUBCELLULAR LOCATION.
RX PubMed=9130715; DOI=10.1093/emboj/16.7.1710;
RA Kuge S., Jones N., Nomoto A.;
RT "Regulation of yAP-1 nuclear localization in response to oxidative
RT stress.";
RL EMBO J. 16:1710-1720(1997).
RN [10]
RP FUNCTION.
RX PubMed=9065458; DOI=10.1074/jbc.272.12.7908;
RA Wemmie J.A., Steggerda S.M., Moye-Rowley W.S.;
RT "The Saccharomyces cerevisiae AP-1 protein discriminates between oxidative
RT stress elicited by the oxidants H2O2 and diamide.";
RL J. Biol. Chem. 272:7908-7914(1997).
RN [11]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=9372930; DOI=10.1128/mcb.17.12.6982;
RA Fernandes L., Rodrigues-Pousada C., Struhl K.;
RT "Yap, a novel family of eight bZIP proteins in Saccharomyces cerevisiae
RT with distinct biological functions.";
RL Mol. Cell. Biol. 17:6982-6993(1997).
RN [12]
RP FUNCTION, NUCLEAR EXPORT BY CRM1, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=9857197; DOI=10.1093/emboj/17.24.7416;
RA Yan C., Lee L.H., Davis L.I.;
RT "Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription
RT factor.";
RL EMBO J. 17:7416-7429(1998).
RN [13]
RP FUNCTION, AND POST-TRANSCRIPTIONAL EXPRESSION CONTROL.
RX PubMed=9469820; DOI=10.1093/nar/26.5.1150;
RA Vilela C., Linz B., Rodrigues-Pousada C., McCarthy J.E.;
RT "The yeast transcription factor genes YAP1 and YAP2 are subject to
RT differential control at the levels of both translation and mRNA
RT stability.";
RL Nucleic Acids Res. 26:1150-1159(1998).
RN [14]
RP FUNCTION, COOPERATIVITY WITH SKN7, AND YAP1 DEPENDENT GENES.
RX PubMed=10347154; DOI=10.1074/jbc.274.23.16040;
RA Lee J., Godon C., Lagniel G., Spector D., Garin J., Labarre J.,
RA Toledano M.B.;
RT "Yap1 and Skn7 control two specialized oxidative stress response regulons
RT in yeast.";
RL J. Biol. Chem. 274:16040-16046(1999).
RN [15]
RP FUNCTION, AND REDUCTION BY THIOREDOXINS.
RX PubMed=11013218; DOI=10.1093/emboj/19.19.5157;
RA Delaunay A., Isnard A.D., Toledano M.B.;
RT "H2O2 sensing through oxidation of the Yap1 transcription factor.";
RL EMBO J. 19:5157-5166(2000).
RN [16]
RP TRANSCRIPTION PROFILING.
RX PubMed=11102521; DOI=10.1091/mbc.11.12.4241;
RA Gasch A.P., Spellman P.T., Kao C.M., Carmel-Harel O., Eisen M.B., Storz G.,
RA Botstein D., Brown P.O.;
RT "Genomic expression programs in the response of yeast cells to
RT environmental changes.";
RL Mol. Biol. Cell 11:4241-4257(2000).
RN [17]
RP TRANSCRIPTION PROFILING.
RX PubMed=10844671; DOI=10.1046/j.1365-2958.2000.01845.x;
RA Dumond H., Danielou N., Pinto M., Bolotin-Fukuhara M.;
RT "A large-scale study of Yap1p-dependent genes in normal aerobic and H2O2-
RT stress conditions: the role of Yap1p in cell proliferation control in
RT yeast.";
RL Mol. Microbiol. 36:830-845(2000).
RN [18]
RP FUNCTION, NUCLEAR IMPORT, AND INTERACTION WITH PSE1.
RX PubMed=11274141; DOI=10.1074/jbc.m009258200;
RA Isoyama T., Murayama A., Nomoto A., Kuge S.;
RT "Nuclear import of the yeast AP-1-like transcription factor Yap1p is
RT mediated by transport receptor Pse1p, and this import step is not affected
RT by oxidative stress.";
RL J. Biol. Chem. 276:21863-21869(2001).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11509657; DOI=10.1128/mcb.21.18.6139-6150.2001;
RA Kuge S., Arita M., Murayama A., Maeta K., Izawa S., Inoue Y., Nomoto A.;
RT "Regulation of the yeast Yap1p nuclear export signal is mediated by redox
RT signal-induced reversible disulfide bond formation.";
RL Mol. Cell. Biol. 21:6139-6150(2001).
RN [20]
RP FUNCTION, AND OXIDATION BY HYR1/GPX3.
RX PubMed=12437921; DOI=10.1016/s0092-8674(02)01048-6;
RA Delaunay A., Pflieger D., Barrault M.-B., Vinh J., Toledano M.B.;
RT "A thiol peroxidase is an H2O2 receptor and redox-transducer in gene
RT activation.";
RL Cell 111:471-481(2002).
RN [21]
RP TRANSCRIPTION PROFILING.
RX PubMed=12006656; DOI=10.1091/mbc.01-10-0472;
RA Cohen B.A., Pilpel Y., Mitra R.D., Church G.M.;
RT "Discrimination between paralogs using microarray analysis: application to
RT the Yap1p and Yap2p transcriptional networks.";
RL Mol. Biol. Cell 13:1608-1614(2002).
RN [22]
RP FUNCTION, OXIDATION, AND DISULFIDE BONDS.
RX PubMed=14556629; DOI=10.1021/bi035003d;
RA Wood M.J., Andrade E.C., Storz G.;
RT "The redox domain of the Yap1p transcription factor contains two disulfide
RT bonds.";
RL Biochemistry 42:11982-11991(2003).
RN [23]
RP FUNCTION.
RX PubMed=12582119; DOI=10.1128/ec.2.1.19-26.2003;
RA Wiatrowski H.A., Carlson M.;
RT "Yap1 accumulates in the nucleus in response to carbon stress in
RT Saccharomyces cerevisiae.";
RL Eukaryot. Cell 2:19-26(2003).
RN [24]
RP FUNCTION, AND ELICITOR SPECIFIC DISULFIDE BONDS.
RX PubMed=14556853; DOI=10.1016/s0891-5849(03)00434-9;
RA Azevedo D., Tacnet F., Delaunay A., Rodrigues-Pousada C., Toledano M.B.;
RT "Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals
RT signaling.";
RL Free Radic. Biol. Med. 35:889-900(2003).
RN [25]
RP FUNCTION, AND INTERACTION WITH YBP1.
RX PubMed=12743123; DOI=10.1074/jbc.m303542200;
RA Veal E.A., Ross S.J., Malakasi P., Peacock E., Morgan B.A.;
RT "Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1
RT transcription factor.";
RL J. Biol. Chem. 278:30896-30904(2003).
RN [26]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [28]
RP DISULFIDE BOND WITH HYR1.
RX PubMed=17720812; DOI=10.1074/jbc.m705953200;
RA Ma L.H., Takanishi C.L., Wood M.J.;
RT "Molecular mechanism of oxidative stress perception by the Orp1 protein.";
RL J. Biol. Chem. 282:31429-31436(2007).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [30]
RP DISULFIDE BONDS.
RX PubMed=17707237; DOI=10.1016/j.molcel.2007.06.035;
RA Okazaki S., Tachibana T., Naganuma A., Mano N., Kuge S.;
RT "Multistep disulfide bond formation in Yap1 is required for sensing and
RT transduction of H2O2 stress signal.";
RL Mol. Cell 27:675-688(2007).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372 AND SER-528, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [33]
RP INTERACTION WITH RBG1.
RX PubMed=19448108; DOI=10.1128/ec.00356-08;
RA Wout P.K., Sattlegger E., Sullivan S.M., Maddock J.R.;
RT "Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2
RT interact on polyribosomes with Gcn1.";
RL Eukaryot. Cell 8:1061-1071(2009).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-14; SER-17; THR-165;
RP SER-204 AND SER-528, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [35]
RP FUNCTION.
RX PubMed=20971184; DOI=10.1016/j.freeradbiomed.2010.10.697;
RA Ouyang X., Tran Q.T., Goodwin S., Wible R.S., Sutter C.H., Sutter T.R.;
RT "Yap1 activation by H2O2 or thiol-reactive chemicals elicits distinct
RT adaptive gene responses.";
RL Free Radic. Biol. Med. 50:1-13(2011).
RN [36] {ECO:0007744|PDB:1SSE}
RP STRUCTURE BY NMR OF 279-313 AND 565-650, AND DISULFIDE BONDS.
RX PubMed=15318225; DOI=10.1038/nature02790;
RA Wood M.J., Storz G., Tjandra N.;
RT "Structural basis for redox regulation of Yap1 transcription factor
RT localization.";
RL Nature 430:917-921(2004).
CC -!- FUNCTION: Transcription activator involved in oxidative stress response
CC and redox homeostasis. Regulates the transcription of genes encoding
CC antioxidant enzymes and components of the cellular thiol-reducing
CC pathways, including the thioredoxin system (TRX2, TRR1), the
CC glutaredoxin system (GSH1, GLR1), superoxide dismutase (SOD1, SOD2),
CC glutathione peroxidase (GPX2), and thiol-specific peroxidases (TSA1,
CC AHP1). The induction of some of these genes requires the cooperative
CC action of both, YAP1 and SKN7. Preferentially binds to promoters with
CC the core binding site 5'-TTA[CG]TAA-3'. Activity of the transcription
CC factor is controlled through oxidation of specific cysteine residues
CC resulting in the alteration of its subcellular location. Oxidative
CC stress (as well as carbon stress, but not increased temperature, acidic
CC pH, or ionic stress) induces nuclear accumulation and as a result YAP1
CC transcriptional activity. Activation by hydrogen peroxide or thiol-
CC reactive chemicals elicit distinct adaptive gene responses. Nuclear
CC export is restored when disulfide bonds are reduced by thioredoxin
CC (TRX2), whose expression is controlled by YAP1, providing a mechanism
CC for negative autoregulation. When overexpressed, YAP1 confers
CC pleiotropic drug-resistance and increases cellular tolerance to
CC cadmium, iron chelators and zinc. {ECO:0000269|PubMed:10347154,
CC ECO:0000269|PubMed:11013218, ECO:0000269|PubMed:11274141,
CC ECO:0000269|PubMed:11509657, ECO:0000269|PubMed:12006656,
CC ECO:0000269|PubMed:12437921, ECO:0000269|PubMed:12582119,
CC ECO:0000269|PubMed:12743123, ECO:0000269|PubMed:14556629,
CC ECO:0000269|PubMed:14556853, ECO:0000269|PubMed:1525853,
CC ECO:0000269|PubMed:20971184, ECO:0000269|PubMed:8182076,
CC ECO:0000269|PubMed:9065458, ECO:0000269|PubMed:9372930,
CC ECO:0000269|PubMed:9469820, ECO:0000269|PubMed:9857197}.
CC -!- SUBUNIT: Interacts independent of oxidation state in the cytoplasm with
CC the karyopherin PSE1/KAP121 (and less strongly with KAP123). The
CC reduced form of YAP1 interacts in the nucleus with the nuclear export
CC protein CRM1, and in the cytoplasm with YBP1 and the peroxiredoxin
CC HYR1/GPX3/ORP1. Interacts with RBG1. {ECO:0000250,
CC ECO:0000269|PubMed:11274141, ECO:0000269|PubMed:12743123,
CC ECO:0000269|PubMed:19448108}.
CC -!- INTERACTION:
CC P19880; P25296: CNB1; NbExp=2; IntAct=EBI-31265, EBI-3968;
CC P19880; P38315: YBP1; NbExp=3; IntAct=EBI-31265, EBI-20985;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11274141,
CC ECO:0000269|PubMed:9130715, ECO:0000269|PubMed:9857197}. Cytoplasm
CC {ECO:0000269|PubMed:11274141, ECO:0000269|PubMed:9130715,
CC ECO:0000269|PubMed:9857197}. Note=Oxidized YAP1 is found predominantly
CC in the nucleus, while reduced YAP1 is continuously exported to the
CC cytoplasm by CRM1/exportin 1. Nuclear import requires the karyopherin
CC PSE1/KAP121 and is independent on YAP1 oxidation state.
CC {ECO:0000269|PubMed:11274141, ECO:0000269|PubMed:9130715,
CC ECO:0000269|PubMed:9857197}.
CC -!- INDUCTION: YAP1 expression is at least partially regulated at the level
CC of translation. A small upstream open reading frame (uORF) retains the
CC 40S ribosomal subunit. By leaky scanning it then proceeds and
CC reinitiates at the functional YAP1 ORF. {ECO:0000269|PubMed:9469820}.
CC -!- DOMAIN: Contains two cysteine rich domains (CRD), referred to as the
CC N- and C-terminal CRD's, n-CRD (Cys-303, Cys-310 and Cys-315) and c-CRD
CC (Cys-598, Cys-620 and Cys-629), respectively. Cys-315 is not conserved
CC in orthologs in other yeast species. A nuclear export signal is
CC embedded in the c-CRD, with which the nuclear export protein
CC CRM1/exportin 1 interacts only in the absence of disulfide bonds (or
CC otherwise oxidized cysteines) within the c-CRD or between the c-CRD and
CC the n-CRD. {ECO:0000269|PubMed:14556853, ECO:0000269|PubMed:15318225,
CC ECO:0000269|PubMed:20971184}.
CC -!- PTM: Depending on the oxidative stress inducing agent, YAP1 can undergo
CC two distinct conformational changes, both involving disulfide bond
CC formation, and both masking the nuclear export signal, thus abolishing
CC nuclear export by CRM1/exportin 1. The disulfide stress-inducing agent
CC diamide leads to the formation of one of three possible disulfide bonds
CC in the c-CRD. Peroxide stress induces the formation of the
CC HYR1/GPX3- and YBP1-dependent interdomain disulfide bond between Cys-
CC 303 and Cys-598 (causing nuclear localization of YAP1), and the
CC possibly stabilizing bond between Cys-310 and Cys-629 (required for
CC full activity of YAP1). {ECO:0000269|PubMed:12437921,
CC ECO:0000269|PubMed:14556629, ECO:0000269|PubMed:14556853,
CC ECO:0000269|PubMed:17707237, ECO:0000305|PubMed:11013218}.
CC -!- MISCELLANEOUS: One of 8 closely related fungi-specific YAP proteins
CC (YAP1 to YAP8), which all seem to be transcription activators of the
CC environmental stress response and metabolism control pathways and to
CC have similar but not identical DNA binding specificities.
CC {ECO:0000305|PubMed:9372930}.
CC -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA37827.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X58693; CAA41536.1; -; Genomic_DNA.
DR EMBL; X53830; CAA37827.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X60780; CAA43195.1; -; Genomic_DNA.
DR EMBL; X63268; CAA44917.1; -; Genomic_DNA.
DR EMBL; Z49810; CAA89945.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09892.1; -; Genomic_DNA.
DR PIR; S16706; S16706.
DR RefSeq; NP_013707.1; NM_001182362.1.
DR PDB; 1SSE; NMR; -; A=279-313, B=565-650.
DR PDBsum; 1SSE; -.
DR AlphaFoldDB; P19880; -.
DR SMR; P19880; -.
DR BioGRID; 35163; 260.
DR DIP; DIP-1752N; -.
DR IntAct; P19880; 39.
DR MINT; P19880; -.
DR STRING; 4932.YML007W; -.
DR iPTMnet; P19880; -.
DR MaxQB; P19880; -.
DR PaxDb; P19880; -.
DR PRIDE; P19880; -.
DR EnsemblFungi; YML007W_mRNA; YML007W; YML007W.
DR GeneID; 855005; -.
DR KEGG; sce:YML007W; -.
DR SGD; S000004466; YAP1.
DR VEuPathDB; FungiDB:YML007W; -.
DR eggNOG; ENOG502RPD7; Eukaryota.
DR GeneTree; ENSGT00940000176699; -.
DR HOGENOM; CLU_032750_0_0_1; -.
DR InParanoid; P19880; -.
DR OMA; WESHSNI; -.
DR BioCyc; YEAST:G3O-32612-MON; -.
DR EvolutionaryTrace; P19880; -.
DR PHI-base; PHI:2811; -.
DR PRO; PR:P19880; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P19880; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0061395; P:positive regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance; HMP:SGD.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:SGD.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:SGD.
DR GO; GO:0046686; P:response to cadmium ion; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IMP:SGD.
DR GO; GO:0000304; P:response to singlet oxygen; IMP:SGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR DisProt; DP01584; -.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013910; TF_PAP1.
DR InterPro; IPR023167; Yap1_redox_dom_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR Pfam; PF08601; PAP1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF111430; SSF111430; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cadmium resistance; Cytoplasm; Disulfide bond;
KW DNA-binding; Nucleus; Oxidation; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..650
FT /note="AP-1-like transcription factor YAP1"
FT /id="PRO_0000076521"
FT DOMAIN 64..127
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..90
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 92..120
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 149..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..378
FT /note="Transcription activation 1"
FT /evidence="ECO:0000269|PubMed:8182076"
FT REGION 303..315
FT /note="n-CRD"
FT /evidence="ECO:0000305|PubMed:15318225"
FT REGION 392..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..537
FT /note="Transcription activation 2"
FT /evidence="ECO:0000269|PubMed:8182076"
FT REGION 510..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..629
FT /note="c-CRD"
FT /evidence="ECO:0000305|PubMed:15318225"
FT MOTIF 35..42
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 68..75
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 614..621
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305|PubMed:9857197"
FT COMPBIAS 22..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 165
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT DISULFID 303..598
FT /note="In peroxide stress-induced nuclear retained form;
FT alternate"
FT /evidence="ECO:0000269|PubMed:12437921,
FT ECO:0000269|PubMed:14556629, ECO:0000269|PubMed:15318225,
FT ECO:0000269|PubMed:17707237, ECO:0007744|PDB:1SSE"
FT DISULFID 310..629
FT /note="In peroxide stress-induced nuclear retained form;
FT alternate"
FT /evidence="ECO:0000269|PubMed:14556629,
FT ECO:0000269|PubMed:15318225, ECO:0000269|PubMed:17707237,
FT ECO:0007744|PDB:1SSE"
FT DISULFID 598..629
FT /note="In diamide-induced nuclear retained form; alternate"
FT /evidence="ECO:0000269|PubMed:11509657"
FT DISULFID 598..620
FT /note="In diamide-induced nuclear retained form"
FT /evidence="ECO:0000269|PubMed:11509657"
FT DISULFID 598
FT /note="Interchain (with C-36 in HYR1); transient;
FT alternate"
FT /evidence="ECO:0000269|PubMed:12437921,
FT ECO:0000269|PubMed:14556629, ECO:0000269|PubMed:17720812"
FT DISULFID 620..629
FT /note="In diamide-induced nuclear retained form"
FT /evidence="ECO:0000269|PubMed:11509657"
FT MUTAGEN 78
FT /note="Q->A: Dominant negative transcription activator."
FT /evidence="ECO:0000269|PubMed:8182076"
FT MUTAGEN 598
FT /note="C->T: Does not alter nuclear location and
FT transcription activation. Constitutively cytoplasmic; when
FT associated with A-620 and T-629."
FT /evidence="ECO:0000269|PubMed:9130715"
FT MUTAGEN 620
FT /note="C->A: Does not alter nuclear location and
FT transcription activation. Constitutively cytoplasmic; when
FT associated with T-598 and T-629."
FT /evidence="ECO:0000269|PubMed:9130715"
FT MUTAGEN 620
FT /note="C->T: Constitutive nuclear location and
FT transcription activation."
FT /evidence="ECO:0000269|PubMed:9130715"
FT MUTAGEN 629
FT /note="C->T: Does not alter nuclear location and
FT transcription activation. Constitutively cytoplasmic; when
FT associated with T-598 and T-620."
FT /evidence="ECO:0000269|PubMed:9130715"
FT CONFLICT 316
FT /note="P -> S (in Ref. 4; CAA43195)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="D -> E (in Ref. 1; CAA41536)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="H -> D (in Ref. 2; CAA37827)"
FT /evidence="ECO:0000305"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1SSE"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:1SSE"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:1SSE"
FT HELIX 301..308
FT /evidence="ECO:0007829|PDB:1SSE"
FT HELIX 598..606
FT /evidence="ECO:0007829|PDB:1SSE"
FT HELIX 616..623
FT /evidence="ECO:0007829|PDB:1SSE"
FT TURN 624..626
FT /evidence="ECO:0007829|PDB:1SSE"
FT HELIX 638..646
FT /evidence="ECO:0007829|PDB:1SSE"
SQ SEQUENCE 650 AA; 72533 MW; 192F20FA71027688 CRC64;
MSVSTAKRSL DVVSPGSLAE FEGSKSRHDE IENEHRRTGT RDGEDSEQPK KKGSKTSKKQ
DLDPETKQKR TAQNRAAQRA FRERKERKMK ELEKKVQSLE SIQQQNEVEA TFLRDQLITL
VNELKKYRPE TRNDSKVLEY LARRDPNLHF SKNNVNHSNS EPIDTPNDDI QENVKQKMNF
TFQYPLDNDN DNDNSKNVGK QLPSPNDPSH SAPMPINQTQ KKLSDATDSS SATLDSLSNS
NDVLNNTPNS STSMDWLDNV IYTNRFVSGD DGSNSKTKNL DSNMFSNDFN FENQFDEQVS
EFCSKMNQVC GTRQCPIPKK PISALDKEVF ASSSILSSNS PALTNTWESH SNITDNTPAN
VIATDATKYE NSFSGFGRLG FDMSANHYVV NDNSTGSTDS TGSTGNKNKK NNNNSDDVLP
FISESPFDMN QVTNFFSPGS TGIGNNAASN TNPSLLQSSK EDIPFINANL AFPDDNSTNI
QLQPFSESQS QNKFDYDMFF RDSSKEGNNL FGEFLEDDDD DKKAANMSDD ESSLIKNQLI
NEEPELPKQY LQSVPGNESE ISQKNGSSLQ NADKINNGND NDNDNDVVPS KEGSLLRCSE
IWDRITTHPK YSDIDVDGLC SELMAKAKCS ERGVVINAED VQLALNKHMN
