YAP4_YEAST
ID YAP4_YEAST Reviewed; 295 AA.
AC P40917; D6W294;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=AP-1-like transcription factor YAP4;
DE AltName: Full=Chromosome instability protein 5;
DE AltName: Full=Transcription activator CIN5;
GN Name=CIN5; Synonyms=HAL6, SDS15, YAP4; OrderedLocusNames=YOR028C;
GN ORFNames=OR26.18;
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].
RC STRAIN=ATCC 204508 / S288c;
RA Hoyt M.;
RT "A putative transcriptional activator required for normal microtubule
RT function.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP FUNCTION, AND ISOLATION OF YAP FAMILY PROTEINS.
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 [5]
RP FUNCTION, AND RESISTANCE TO ANTIMALARIAL DRUGS.
RX PubMed=9593122; DOI=10.1128/aac.42.5.1034;
RA Delling U., Raymond M., Schurr E.;
RT "Identification of Saccharomyces cerevisiae genes conferring resistance to
RT quinoline ring-containing antimalarial drugs.";
RL Antimicrob. Agents Chemother. 42:1034-1041(1998).
RN [6]
RP FUNCTION, AND SALT TOLERANCE.
RX PubMed=9559673; DOI=10.1016/s0014-5793(98)00249-x;
RA Mendizabal I., Rios G., Mulet J.M., Serrano R., de Larrinoa I.F.;
RT "Yeast putative transcription factors involved in salt tolerance.";
RL FEBS Lett. 425:323-328(1998).
RN [7]
RP FUNCTION, AND PLEIOTROPIC DRUG-RESISTANCE.
RX PubMed=11179441; DOI=10.1124/mol.59.3.470;
RA Furuchi T., Ishikawa H., Miura N., Ishizuka M., Kajiya K., Kuge S.,
RA Naganuma A.;
RT "Two nuclear proteins, Cin5 and Ydr259c, confer resistance to cisplatin in
RT Saccharomyces cerevisiae.";
RL Mol. Pharmacol. 59:470-474(2001).
RN [8]
RP FUNCTION, AND PROMOTER BINDING.
RX PubMed=12399584; DOI=10.1126/science.1075090;
RA Lee T.I., Rinaldi N.J., Robert F., Odom D.T., Bar-Joseph Z., Gerber G.K.,
RA Hannett N.M., Harbison C.T., Thompson C.M., Simon I., Zeitlinger J.,
RA Jennings E.G., Murray H.L., Gordon D.B., Ren B., Wyrick J.J., Tagne J.B.,
RA Volkert T.L., Fraenkel E., Gifford D.K., Young R.A.;
RT "Transcriptional regulatory networks in Saccharomyces cerevisiae.";
RL Science 298:799-804(2002).
RN [9]
RP FUNCTION, AND REGULATORY TRANSCRIPTION MODULES.
RX PubMed=14555958; DOI=10.1038/nbt890;
RA Bar-Joseph Z., Gerber G.K., Lee T.I., Rinaldi N.J., Yoo J.Y., Robert F.,
RA Gordon D.B., Fraenkel E., Jaakkola T.S., Young R.A., Gifford D.K.;
RT "Computational discovery of gene modules and regulatory networks.";
RL Nat. Biotechnol. 21:1337-1342(2003).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND SER-196, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Transcription activator involved in the regulation of genes
CC expressed in response to environmental changes and metabolic
CC requirements. According to genome-wide promoter binding and gene
CC expression studies it regulates, among others, genes involved in
CC ribosome biogenesis, and protein synthesis. It may also be involved in
CC pleiotropic drug resistance. When overexpressed it confers increased
CC resistance to cisplatin, the DNA-alkylating agents
CC methylmethanosulfonate, and mitomycin C, the antimalarial drugs
CC quinidine, mefloquine, and chloroquine, and increases cellular
CC tolerance to sodium and lithium. Preferentially binds 5'-TTACTAA-3'.
CC {ECO:0000269|PubMed:11179441, ECO:0000269|PubMed:12399584,
CC ECO:0000269|PubMed:14555958, ECO:0000269|PubMed:9372930,
CC ECO:0000269|PubMed:9559673, ECO:0000269|PubMed:9593122}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
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 -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; U16780; AAA52752.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60744.1; -; Genomic_DNA.
DR EMBL; Z74936; CAA99218.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10810.1; -; Genomic_DNA.
DR PIR; S50316; S50316.
DR RefSeq; NP_014671.1; NM_001183447.1.
DR AlphaFoldDB; P40917; -.
DR SMR; P40917; -.
DR BioGRID; 34431; 135.
DR DIP; DIP-4351N; -.
DR IntAct; P40917; 5.
DR MINT; P40917; -.
DR STRING; 4932.YOR028C; -.
DR iPTMnet; P40917; -.
DR PaxDb; P40917; -.
DR PRIDE; P40917; -.
DR EnsemblFungi; YOR028C_mRNA; YOR028C; YOR028C.
DR GeneID; 854193; -.
DR KEGG; sce:YOR028C; -.
DR SGD; S000005554; CIN5.
DR VEuPathDB; FungiDB:YOR028C; -.
DR eggNOG; ENOG502SC5V; Eukaryota.
DR GeneTree; ENSGT00940000176707; -.
DR HOGENOM; CLU_1103509_0_0_1; -.
DR InParanoid; P40917; -.
DR OMA; FESSYTT; -.
DR BioCyc; YEAST:G3O-33575-MON; -.
DR PRO; PR:P40917; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P40917; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
DR GO; GO:0042538; P:hyperosmotic salinity response; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISA:SGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..295
FT /note="AP-1-like transcription factor YAP4"
FT /id="PRO_0000076524"
FT DOMAIN 237..295
FT /note="bZIP"
FT REGION 181..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..260
FT /note="Basic motif"
FT /evidence="ECO:0000250"
FT REGION 262..271
FT /note="Leucine-zipper"
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 295 AA; 32975 MW; D80BF21505267548 CRC64;
MLMQIKMDNH PFNFQPILAS HSMTRDSTKP KKMTDTAFVP SPPVGFIKEE NKADLHTISV
VASNVTLPQI QLPKIATLEE PGYESRTGSL TDLSGRRNSV NIGALCEDVP NTAGPHIARP
VTINNLIPPS LPRLNTYQLR PQLSDTHLNC HFNSNPYTTA SHAPFESSYT TASTFTSQPA
ASYFPSNSTP ATRKNSATTN LPSEERRRVS VSLSEQVFNE GERYNNDGQL IGKTGKPLRN
TKRAAQNRSA QKAFRQRREK YIKNLEEKSK LFDGLMKENS ELKKMIESLK SKLKE
