GCR2_YEAST
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 03-AUG-2022, entry version 163.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 370.
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; Q01722; -.
DR PRIDE; Q01722; -.
DR EnsemblFungi; YNL199C_mRNA; YNL199C; YNL199C.
DR GeneID; 855522; -.
DR KEGG; sce:YNL199C; -.
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 BioCyc; YEAST:G3O-33208-MON; -.
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; IC: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; IC: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
