GIS1_YEAST
ID GIS1_YEAST Reviewed; 894 AA.
AC Q03833; D6VS81;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Transcriptional activator/repressor GIS1;
GN Name=GIS1; OrderedLocusNames=YDR096W; ORFNames=YD8557.01;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP DOMAIN ATYPICAL ZINC-FINGER.
RX PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA Boehm S., Frishman D., Mewes H.-W.;
RT "Variations of the C2H2 zinc finger motif in the yeast genome and
RT classification of yeast zinc finger proteins.";
RL Nucleic Acids Res. 25:2464-2469(1997).
RN [4]
RP FUNCTION IN TRANSCRIPTIONAL ACTIVATION.
RX PubMed=10628841; DOI=10.1007/s004380051121;
RA Balciunas D., Ronne H.;
RT "Yeast genes GIS1-4: multicopy suppressors of the Gal- phenotype of snf1
RT mig1 srb8/10/11 cells.";
RL Mol. Gen. Genet. 262:589-599(1999).
RN [5]
RP FUNCTION IN TRANSCRIPTIONAL REPRESSION.
RX PubMed=10523651; DOI=10.1128/mcb.19.11.7630;
RA Jang Y.K., Wang L., Sancar G.B.;
RT "RPH1 and GIS1 are damage-responsive repressors of PHR1.";
RL Mol. Cell. Biol. 19:7630-7638(1999).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=10835355; DOI=10.1093/emboj/19.11.2569;
RA Pedruzzi I., Buerckert N., Egger P., De Virgilio C.;
RT "Saccharomyces cerevisiae Ras/cAMP pathway controls post-diauxic shift
RT element-dependent transcription through the zinc finger protein Gis1.";
RL EMBO J. 19:2569-2579(2000).
RN [7]
RP FUNCTION, AND REPRESSION OF DPP1 EXPRESSION.
RX PubMed=12799368; DOI=10.1074/jbc.m305452200;
RA Oshiro J., Han G.-S., Iwanyshyn W.M., Conover K., Carman G.M.;
RT "Regulation of the yeast DPP1-encoded diacylglycerol pyrophosphate
RT phosphatase by transcription factor Gis1p.";
RL J. Biol. Chem. 278:31495-31503(2003).
RN [8]
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 [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-696 AND SER-747, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-690; SER-694;
RP SER-696 AND SER-734, 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).
CC -!- FUNCTION: Transcription factor involved in the regulation of gene
CC expression upon nutrient starvation. Recognizes and binds to the post-
CC diauxic-shift element 5'-T[AT]AGGGAT-3' in the promoter region. Can act
CC as a transcriptional activator (e.g. of stress genes like SSA3, HSP12
CC and HSP26) as well as a repressor (e.g. of pyrophosphate phosphatase
CC DPP1). GIS1 also acts as a DNA damage-responsive transcriptional
CC repressor of photolyase PHR1. {ECO:0000269|PubMed:10523651,
CC ECO:0000269|PubMed:10628841, ECO:0000269|PubMed:10835355,
CC ECO:0000269|PubMed:12799368}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Induced upon nutrient starvation.
CC {ECO:0000269|PubMed:10835355, ECO:0000269|PubMed:12799368}.
CC -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z47746; CAA87670.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11941.1; -; Genomic_DNA.
DR PIR; S51245; S51245.
DR RefSeq; NP_010381.1; NM_001180404.1.
DR AlphaFoldDB; Q03833; -.
DR SMR; Q03833; -.
DR BioGRID; 32151; 291.
DR IntAct; Q03833; 33.
DR MINT; Q03833; -.
DR STRING; 4932.YDR096W; -.
DR iPTMnet; Q03833; -.
DR MaxQB; Q03833; -.
DR PaxDb; Q03833; -.
DR PRIDE; Q03833; -.
DR EnsemblFungi; YDR096W_mRNA; YDR096W; YDR096W.
DR GeneID; 851670; -.
DR KEGG; sce:YDR096W; -.
DR SGD; S000002503; GIS1.
DR VEuPathDB; FungiDB:YDR096W; -.
DR eggNOG; KOG0958; Eukaryota.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_008557_0_0_1; -.
DR BioCyc; YEAST:G3O-29699-MON; -.
DR Reactome; R-SCE-3214842; HDMs demethylate histones.
DR Reactome; R-SCE-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR PRO; PR:Q03833; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03833; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IC:SGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IMP:SGD.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0071071; P:regulation of phospholipid biosynthetic process; IMP:SGD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..894
FT /note="Transcriptional activator/repressor GIS1"
FT /id="PRO_0000046806"
FT DOMAIN 12..53
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 170..324
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 828..851
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 857..882
FT /note="C2H2-type 2; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 324..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 90..110
FT /evidence="ECO:0000255"
FT COILED 361..385
FT /evidence="ECO:0000255"
FT MOTIF 316..332
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 336..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 734
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 894 AA; 99481 MW; 06F9F2B7F485DF88 CRC64;
MEIKPVEVID GVPVFKPSMM EFANFQYFID EITKFGIENG IVKVIPPKEW LELLEGSPPA
ESLKTIQLDS PIQQQAKRWD KHENGVFSIE NEYDNKSYNL TQWKNLAESL DSRISQGDFN
DKTLKENCRV DSQQDCYDLA QLQILESDFW KTIAFSKPFY AVDENSSIFP YDLTLWNLNN
LPDSINSSNR RLLTGQSKCI FPWHLDEQNK CSINYLHFGA PKQWYSIPSA NTDQFLKILS
KEPSSNKENC PAFIRHQNII TSPDFLRKNN IKFNRVVQFQ HEFIITFPYC MYSGFNYGYN
FGESIEFILD QQAVVRKQPL KCGCGNKKEE RKSGPFSNLS YDSNESEQRG SITDNDNDLF
QKVRSFDELL NHSSQELQNL EDNKNPLFSN INMNRPQSSS LRSTTPNGVN QFLNMNQTTI
SRISSPLLSR MMDLSNIVEP TLDDPGSKFK RKVLTPQLPQ MNIPSNSSNF GTPSLTNTNS
LLSNITATST NPSTTTNGSQ NHNNVNANGI NTSAAASINN NISSTNNSAN NSSSNNNVST
VPSSMMHSST LNGTSGLGGD NDDNMLALSL ATLANSATAS PRLTLPPLSS PMNPNGHTSY
NGNMMNNNSG NGSNGSNSYS NGVTTAAATT TSAPHNLSIV SPNPTYSPNP LSLYLTNSKN
PLNSGLAPLS PSTSNIPFLK RNNVVTLNIS REASKSPISS FVNDYRSPLG VSNPLMYSST
INDYSNGTGI RQNSNNINPL DAGPSFSPLH KKPKILNGND NSNLDSNNFD YSFTGNKQES
NPSILNNNTN NNDNYRTSSM NNNGNNYQAH SSKFGENEVI MSDHGKIYIC RECNRQFSSG
HHLTRHKKSV HSGEKPHSCP RCGKRFKRRD HVLQHLNKKI PCTQEMENTK LAES
