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 27-MAR-2024, entry version 220. 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}, PDR4 GN {ECO:0000303|PubMed:2060792}, SNQ3 {ECO:0000303|PubMed:1878996}; GN OrderedLocusNames=YML007W {ECO:0000312|SGD:S000004466}; GN 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 267. DR DIP; DIP-1752N; -. DR IntAct; P19880; 39. DR MINT; P19880; -. DR STRING; 4932.YML007W; -. DR iPTMnet; P19880; -. DR MaxQB; P19880; -. DR PaxDb; 4932-YML007W; -. DR PeptideAtlas; P19880; -. DR EnsemblFungi; YML007W_mRNA; YML007W; YML007W. DR GeneID; 855005; -. DR KEGG; sce:YML007W; -. DR AGR; SGD:S000004466; -. 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 OrthoDB; 1363150at2759; -. DR BioCyc; YEAST:G3O-32612-MONOMER; -. DR BioGRID-ORCS; 855005; 6 hits in 13 CRISPR screens. 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:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; HMP:SGD. DR GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:SGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; 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 CDD; cd14688; bZIP_YAP; 1. DR DisProt; DP01584; -. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.10.238.100; YAP1 redox domain. Chain B; 1. DR InterPro; IPR004827; bZIP. DR InterPro; IPR046347; bZIP_sf. DR InterPro; IPR013910; TF_PAP1. DR InterPro; IPR023167; Yap1_redox_dom_sf. DR PANTHER; PTHR40621:SF6; AP-1-LIKE TRANSCRIPTION FACTOR YAP1-RELATED; 1. DR PANTHER; PTHR40621; TRANSCRIPTION FACTOR KAPC-RELATED; 1. DR Pfam; PF00170; bZIP_1; 1. DR Pfam; PF08601; PAP1; 1. DR SMART; SM00338; BRLZ; 1. DR SUPFAM; SSF57959; Leucine zipper domain; 1. DR SUPFAM; SSF111430; YAP1 redox domain; 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 //