CHA4_YEAST
ID CHA4_YEAST Reviewed; 648 AA.
AC P43634; D6VY98;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Activatory protein CHA4;
GN Name=CHA4; Synonyms=SIL2, SIL3; OrderedLocusNames=YLR098C;
GN ORFNames=L8004.8;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8889513; DOI=10.1093/genetics/144.2.467;
RA Holmberg S., Schjerling P.;
RT "Cha4p of Saccharomyces cerevisiae activates transcription via
RT serine/threonine response elements.";
RL Genetics 144:467-478(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION BY
RP 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164 AND SER-166, 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: Activates the CHA1 gene for L-serine dehydratase. Binds to
CC the DNA sequence 5'-GVGGARAYRTRATTCCRC-3'.
CC {ECO:0000269|PubMed:8889513}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49975; CAA90276.1; -; Genomic_DNA.
DR EMBL; U53876; AAB67542.1; -; Genomic_DNA.
DR EMBL; Z73270; CAA97662.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09414.1; -; Genomic_DNA.
DR PIR; S59723; S59723.
DR RefSeq; NP_013199.1; NM_001181985.1.
DR AlphaFoldDB; P43634; -.
DR SMR; P43634; -.
DR BioGRID; 31371; 127.
DR DIP; DIP-1798N; -.
DR IntAct; P43634; 11.
DR MINT; P43634; -.
DR STRING; 4932.YLR098C; -.
DR iPTMnet; P43634; -.
DR MaxQB; P43634; -.
DR PaxDb; P43634; -.
DR PRIDE; P43634; -.
DR EnsemblFungi; YLR098C_mRNA; YLR098C; YLR098C.
DR GeneID; 850787; -.
DR KEGG; sce:YLR098C; -.
DR SGD; S000004088; CHA4.
DR VEuPathDB; FungiDB:YLR098C; -.
DR eggNOG; ENOG502QTSE; Eukaryota.
DR HOGENOM; CLU_015811_0_0_1; -.
DR InParanoid; P43634; -.
DR OMA; YNFDFTL; -.
DR BioCyc; YEAST:G3O-32248-MON; -.
DR PRO; PR:P43634; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P43634; protein.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IMP:SGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..648
FT /note="Activatory protein CHA4"
FT /id="PRO_0000114942"
FT DNA_BIND 44..70
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 648 AA; 74393 MW; CF3381B4C0356F82 CRC64;
MMLEPSPPPL TTTVTPSLPS SLKKSVTDND QNNNNVPRKR KLACQNCRRR RRKCNMEKPC
SNCIKFRTEC VFTQQDLRNK RYSTTYVEAL QSQIRSLKEQ LQILSSSSST IASNALSSLK
NNSDHGDAPN EKILKYGETA QSALPSSESN DENESDAFTK KMPSESPPPV GTNSIYPSNS
LSIIKKKTDG STRYQQQQVS LKNLSRSPLI LRSLSLFFKW LYPGHYLFIH RETFLSAFFG
DTNTKSYYCS EELVFAIAAL GSLISYKSET ELFQQSEVFY QRAKTIVLKK IFQLEDSSLA
ESSSSSKLAI IQTLLCLAFY DIGSGENPMA WYLSGLAFRI AHEIGLHLNP EAWSNVYEDE
LSIMDFEVRS RIYWGCYIAD HLIAILFGRS TSLRLSNSTV PETDELPEIE TGIEEYIYDP
KVILSTANPL KKLIVLSRIT EIFASKIFSP NETLLQRSEY LAKFNLEVYN WRRDLPPELQ
WTKRSLMEMT DFNPTIAYVW FHYYIVLISY NKPFIYEIKQ SRELVEGYVD ELYYLLKVWK
NKFKTFEKAT IYMIYSAILA IQCMKSNLIK KDRKQDFLNF LSAPTLNYEL ARKFIENSED
ALHNSETMDL LGTLSHGNDF ALEYNFDFTL LNEIDMLIGG NTNDGLSK
