ID   GCR2_YEAST              Reviewed;         534 AA.
AC   Q01722; D6W0Y9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   27-MAR-2024, entry version 170.
DE   RecName: Full=Glycolytic genes transcriptional activator GCR2;
GN   Name=GCR2; OrderedLocusNames=YNL199C; ORFNames=N1374;
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], FUNCTION, AND INTERACTION WITH GCR1.
RX   PubMed=1508187; DOI=10.1128/mcb.12.9.3834-3842.1992;
RA   Uemura H., Jigami Y.;
RT   "Role of GCR2 in transcriptional activation of yeast glycolytic genes.";
RL   Mol. Cell. Biol. 12:3834-3842(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=7725799; DOI=10.1002/yea.320101213;
RA   Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
RT   "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
RT   WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8
RT   new open reading frames of unknown function.";
RL   Yeast 10:1639-1645(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [5]
RP   FUNCTION.
RX   PubMed=9335588; DOI=10.1093/genetics/147.2.493;
RA   Zeng X., Deminoff S.J., Santangelo G.M.;
RT   "Specialized Rap1p/Gcr1p transcriptional activation through Gcr1p DNA
RT   contacts requires Gcr2p, as does hyperphosphorylation of Gcr1p.";
RL   Genetics 147:493-505(1997).
RN   [6]
RP   FUNCTION, AND HOMODIMERIZATION.
RX   PubMed=11333224; DOI=10.1093/genetics/158.1.133;
RA   Deminoff S.J., Santangelo G.M.;
RT   "Rap1p requires Gcr1p and Gcr2p homodimers to activate ribosomal protein
RT   and glycolytic genes, respectively.";
RL   Genetics 158:133-143(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-409, 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 required for the expression of
CC       glycolytic genes. Enhances the CT box-dependent transcriptional
CC       activation of a RAP1-GCR1 complex. Required for GCR1 phosphorylation.
CC       {ECO:0000269|PubMed:11333224, ECO:0000269|PubMed:1508187,
CC       ECO:0000269|PubMed:9335588}.
CC   -!- SUBUNIT: Homodimer via the leucine-zipper domain. Forms a complex with
CC       a GCR1 homodimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; D10104; BAA00985.1; -; Genomic_DNA.
DR   EMBL; X78898; CAA55509.1; -; Genomic_DNA.
DR   EMBL; Z71475; CAA96097.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10355.1; -; Genomic_DNA.
DR   PIR; S31300; S31300.
DR   RefSeq; NP_014200.1; NM_001183037.1.
DR   AlphaFoldDB; Q01722; -.
DR   SMR; Q01722; -.
DR   BioGRID; 35635; 377.
DR   ComplexPortal; CPX-1229; RAP1-GCR1-GCR2 transcription activation complex.
DR   DIP; DIP-732N; -.
DR   IntAct; Q01722; 14.
DR   MINT; Q01722; -.
DR   STRING; 4932.YNL199C; -.
DR   iPTMnet; Q01722; -.
DR   MaxQB; Q01722; -.
DR   PaxDb; 4932-YNL199C; -.
DR   PeptideAtlas; Q01722; -.
DR   EnsemblFungi; YNL199C_mRNA; YNL199C; YNL199C.
DR   GeneID; 855522; -.
DR   KEGG; sce:YNL199C; -.
DR   AGR; SGD:S000005143; -.
DR   SGD; S000005143; GCR2.
DR   VEuPathDB; FungiDB:YNL199C; -.
DR   eggNOG; ENOG502QU4I; Eukaryota.
DR   HOGENOM; CLU_023702_0_0_1; -.
DR   InParanoid; Q01722; -.
DR   OMA; AGIMHHQ; -.
DR   OrthoDB; 2025195at2759; -.
DR   BioCyc; YEAST:G3O-33208-MONOMER; -.
DR   BioGRID-ORCS; 855522; 8 hits in 10 CRISPR screens.
DR   PRO; PR:Q01722; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; Q01722; Protein.
DR   GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005667; C:transcription regulator complex; NAS:ComplexPortal.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR   GO; GO:0003712; F:transcription coregulator activity; IGI:SGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR   GO; GO:0060196; P:positive regulation of antisense RNA transcription; IDA:SGD.
DR   GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006110; P:regulation of glycolytic process; NAS:ComplexPortal.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..534
FT                   /note="Glycolytic genes transcriptional activator GCR2"
FT                   /id="PRO_0000087446"
FT   REGION          29..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..534
FT                   /note="Leucine-zipper"
FT   MOTIF           281..288
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        29..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   534 AA;  58062 MW;  958D4A9393255B1B CRC64;
     MHHQTKLDVF IIRAYNLLSN ESVISGASLQ SVTNSPQTTT NTPSGMVNGA VGTGIANPTG
     LMGSDSTPNI DEIITSTGSN ALTKTNSDSA NGTPNGNSSS TSAISNASNP ATTGNNASSS
     ATSNGIYTQA QYSQLFAKIS KLYNATLSSG SIDDRSTSPK SAIELYQRFQ QMIKELELSF
     DASPYAKYFR RLDGRLWQIK TDSELENDEL WRLVSMSIFT VFDPQTGQIL TQGRRKGNSL
     NTSTKGSPSD LQGINNGNNN GNNGNIGNGS NIKNYGNKNM PNNRTKKRGT RVAKNAKNGK
     NNKNSNKERN GITDTSAFSN TTISNPGTNM LFDPSLSQQL QKRLQTLSQD VNSRSLTGYY
     TQPTSPGSGG FEFGLSHADL NPNASSNTMG YNTMSNNGSH SWKRRSLGSL DVNTLDDEAV
     EELLQLTNTS KRQRPMTTAA EGALINDGPD TNLNANNTQM KVDLNPSNSM GPIDTEAVIR
     PLKEAYDAII SEKGQRIVQL ERELELQRQE TQWLRKMLIE DMGCVRSMLR DLQR
//