ACA2_YEAST
ID ACA2_YEAST Reviewed; 587 AA.
AC P40535; D6VVP6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=ATF/CREB activator 2;
DE AltName: Full=Chromosome stability protein CST6;
GN Name=CST6; Synonyms=ACA2; OrderedLocusNames=YIL036W;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 IDENTIFICATION.
RX PubMed=10454593; DOI=10.1093/nar/27.15.3001;
RA Ouspenski I.I., Elledge S.J., Brinkley B.R.;
RT "New yeast genes important for chromosome integrity and segregation
RT identified by dosage effects on genome stability.";
RL Nucleic Acids Res. 27:3001-3008(1999).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10825197; DOI=10.1128/mcb.20.12.4340-4349.2000;
RA Garcia-Gimeno M.A., Struhl K.;
RT "Aca1 and Aca2, ATF/CREB activators in Saccharomyces cerevisiae, are
RT important for carbon source utilization but not the response to stress.";
RL Mol. Cell. Biol. 20:4340-4349(2000).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557 AND THR-559, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399 AND THR-559, AND
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-557 AND THR-559, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-557 AND THR-559, 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: Transcriptional activator of promoters containing ATF/CREB
CC sites. Can independently stimulate transcription through ATF/CREB
CC sites. Important for a variety of biological functions including growth
CC on non-optimal carbon sources.
CC -!- INTERACTION:
CC P40535; P39970: ACA1; NbExp=2; IntAct=EBI-2052, EBI-22524;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 1240 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; Z46861; CAA86915.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08512.1; -; Genomic_DNA.
DR PIR; S49942; S49942.
DR RefSeq; NP_012228.1; NM_001179386.1.
DR AlphaFoldDB; P40535; -.
DR SMR; P40535; -.
DR BioGRID; 34954; 189.
DR IntAct; P40535; 3.
DR MINT; P40535; -.
DR STRING; 4932.YIL036W; -.
DR iPTMnet; P40535; -.
DR MaxQB; P40535; -.
DR PaxDb; P40535; -.
DR PRIDE; P40535; -.
DR EnsemblFungi; YIL036W_mRNA; YIL036W; YIL036W.
DR GeneID; 854775; -.
DR KEGG; sce:YIL036W; -.
DR SGD; S000001298; CST6.
DR VEuPathDB; FungiDB:YIL036W; -.
DR eggNOG; KOG1414; Eukaryota.
DR GeneTree; ENSGT00940000176485; -.
DR HOGENOM; CLU_033100_0_0_1; -.
DR InParanoid; P40535; -.
DR OMA; AHLPMTN; -.
DR BioCyc; YEAST:G3O-31308-MON; -.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-450341; Activation of the AP-1 family of transcription factors.
DR PRO; PR:P40535; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40535; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0071244; P:cellular response to carbon dioxide; IMP:SGD.
DR GO; GO:0071400; P:cellular response to oleic acid; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0061429; P:positive regulation of transcription from RNA polymerase II promoter by oleic acid; IMP:SGD.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IDA:SGD.
DR InterPro; IPR029810; Aca1/Aca2.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR PANTHER; PTHR19304:SF40; PTHR19304:SF40; 2.
DR Pfam; PF00170; bZIP_1; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
DR PROSITE; PS00036; BZIP_BASIC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..587
FT /note="ATF/CREB activator 2"
FT /id="PRO_0000076530"
FT DOMAIN 425..488
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..447
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 453..467
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 552..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 559
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 587 AA; 65264 MW; 1B98DC38BC8CAE94 CRC64;
MFTGQEYHSV DSNSNKQKDN NKRGIDDTSK ILNNKIPHSV SDTSAAATTT STMNNSALSR
SLDPTDINYS TNMAGVVDQI HDYTTSNRNS LTPQYSIAAG NVNSHDRVVK PSANSNYQQA
AYLRQQQQQD QRQQSPSMKT EEESQLYGDI LMNSGVVQDM HQNLATHTNL SQLSSTRKSA
PNDSTTAPTN ASNIANTASV NKQMYFMNMN MNNNPHALND PSILETLSPF FQPFGVDVAH
LPMTNPPIFQ SSLPGCDEPI RRRRISISNG QISQLGEDIE TLENLHNTQP PPMPNFHNYN
GLSQTRNVSN KPVFNQAVPV SSIPQYNAKK VINPTKDSAL GDQSVIYSKS QQRNFVNAPS
KNTPAESISD LEGMTTFAPT TGGENRGKSA LRESHSNPSF TPKSQGSHLN LAANTQGNPI
PGTTAWKRAR LLERNRIAAS KCRQRKKVAQ LQLQKEFNEI KDENRILLKK LNYYEKLISK
FKKFSKIHLR EHEKLNKDSD NNVNGTNSSN KNESMTVDSL KIIEELLMID SDVTEVDKDT
GKIIAIKHEP YSQRFGSDTD DDDIDLKPVE GGKDPDNQSL PNSEKIK
