CSR2_YEAST
ID CSR2_YEAST Reviewed; 1121 AA.
AC Q12734; D6W440;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transcription factor CSR2;
DE AltName: Full=CHS5 SPA2 rescue protein 2;
GN Name=CSR2; Synonyms=MRG19; OrderedLocusNames=YPR030W; ORFNames=YP9367.10;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 FUNCTION.
RX PubMed=10660072; DOI=10.1007/pl00008654;
RA Kabir M.A., Khanday F.A., Mehta D.V., Bhat P.J.;
RT "Multiple copies of MRG19 suppress transcription of the GAL1 promoter in a
RT GAL80-dependent manner in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 262:1113-1122(2000).
RN [4]
RP FUNCTION.
RX PubMed=10679005; DOI=10.1091/mbc.11.2.435;
RA Santos B., Snyder M.;
RT "Sbe2p and sbe22p, two homologous Golgi proteins involved in yeast cell
RT wall formation.";
RL Mol. Biol. Cell 11:435-452(2000).
RN [5]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12444972; DOI=10.1046/j.1432-1033.2002.03303.x;
RA Khanday F.A., Saha M., Bhat P.J.;
RT "Molecular characterization of MRG19 of Saccharomyces cerevisiae.
RT Implication in the regulation of galactose and nonfermentable carbon source
RT utilization.";
RL Eur. J. Biochem. 269:5840-5850(2002).
RN [6]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=14574415; DOI=10.1038/nature02062;
RA Ubersax J.A., Woodbury E.L., Quang P.N., Paraz M., Blethrow J.D., Shah K.,
RA Shokat K.M., Morgan D.O.;
RT "Targets of the cyclin-dependent kinase Cdk1.";
RL Nature 425:859-864(2003).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-841, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [8]
RP FUNCTION.
RX PubMed=16336970; DOI=10.1016/j.febslet.2005.11.017;
RA Kharade S.V., Mittal N., Das S.P., Sinha P., Roy N.;
RT "Mrg19 depletion increases S. cerevisiae lifespan by augmenting ROS
RT defence.";
RL FEBS Lett. 579:6809-6813(2005).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=15632429; DOI=10.1099/mic.0.27347-0;
RA Das M., Bhat P.J.;
RT "Disruption of MRG19 results in altered nitrogen metabolic status and
RT defective pseudohyphal development in Saccharomyces cerevisiae.";
RL Microbiology 151:91-98(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-46; SER-127; SER-327
RP AND SER-987, 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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Transcription factor involved in the regulation of
CC fermentation and aerobic oxidation. Acts as a repressor of CYC1, which
CC is involved in electron flow through the mitochondria under aerobic
CC condition. Required for pseudohyphal formation upon nitrogen
CC starvation. May be involved in viability at stationary phase and aging.
CC {ECO:0000269|PubMed:10660072, ECO:0000269|PubMed:10679005,
CC ECO:0000269|PubMed:12444972, ECO:0000269|PubMed:15632429,
CC ECO:0000269|PubMed:16336970}.
CC -!- INTERACTION:
CC Q12734; P39940: RSP5; NbExp=2; IntAct=EBI-32379, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12444972}. Nucleus
CC {ECO:0000269|PubMed:12444972}.
CC -!- INDUCTION: Repressed by glucose and increased expression upon nitrogen
CC depletion. {ECO:0000269|PubMed:12444972, ECO:0000269|PubMed:15632429}.
CC -!- PTM: Phosphorylated by CDC28. {ECO:0000269|PubMed:14574415}.
CC -!- SIMILARITY: Belongs to the CSR2 family. {ECO:0000305}.
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DR EMBL; Z71255; CAA95026.1; -; Genomic_DNA.
DR EMBL; Z49274; CAA89284.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11456.1; -; Genomic_DNA.
DR PIR; S54504; S54504.
DR RefSeq; NP_015355.1; NM_001184127.1.
DR AlphaFoldDB; Q12734; -.
DR BioGRID; 36208; 160.
DR DIP; DIP-3911N; -.
DR IntAct; Q12734; 7.
DR MINT; Q12734; -.
DR STRING; 4932.YPR030W; -.
DR iPTMnet; Q12734; -.
DR PaxDb; Q12734; -.
DR PRIDE; Q12734; -.
DR EnsemblFungi; YPR030W_mRNA; YPR030W; YPR030W.
DR GeneID; 856142; -.
DR KEGG; sce:YPR030W; -.
DR SGD; S000006234; CSR2.
DR VEuPathDB; FungiDB:YPR030W; -.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000176445; -.
DR HOGENOM; CLU_006239_0_0_1; -.
DR InParanoid; Q12734; -.
DR OMA; FITHHAS; -.
DR BioCyc; YEAST:G3O-34189-MON; -.
DR PRO; PR:Q12734; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12734; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; ISA:SGD.
DR Gene3D; 2.60.40.640; -; 1.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011022; Arrestin_C-like.
DR Pfam; PF02752; Arrestin_C; 1.
DR SMART; SM01017; Arrestin_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1121
FT /note="Transcription factor CSR2"
FT /id="PRO_0000228156"
FT REGION 273..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 841
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
SQ SEQUENCE 1121 AA; 124849 MW; 31F958BB8DB0B7E8 CRC64;
MQSTVPIAIA SNGNKRDVVQ NVSAGDEGDI LQRLARNREM ISTSLSPQKS SGFSGRRRSS
SVRDALSSFF GTGNSPTSSM DDYSNLMNRN YSTASTAMCR GNSFPSDVGT KAYNITGSYQ
PDRHRNSVPY TTIDQLHTRQ DTGLRRESDP VAAKQISSNN DIVRSFITHH ASNSTMFINR
VLSDYLADRG FIKQTPLYNK KSVLEISIAT SAESVFLPTT KSDETEYLSL IHGSLNQART
QPVGSTNTAE SDFLPSCPTM DTLNENNDLS LFPLHTQRTS PSNTARTGNA MDTSNSDRAS
PASNNNTTDA DSFVASGNNN PMNNNNSPAR NRHPNSHSRS LPNAWNSQMP SFSFALIFSL
NKSTTLSDIK VELTSNVRVV WFNGLPPTKN VNEECYNIGS LDWTLNADNF NLFIPQGAKS
PLDIVENHSN NRKLKVLQKL SMRKRRSFSN KAVLRENILN NLNASNSTNK LNAGVYVFTI
PIVLASRIPE SLYYPSARVS YSLRLATKLK DEHTQLVASR PRSSSISSPQ KLRSYSCSDS
YEYSQIDDTI EGETYNNDKN STGKIAFPSS WLKSAKGRLK RNNSNGRSDN NGASSSGLAM
QHDSEDTINL QYPLNLVRTP PEISVTTANK PLYINKVWEN CLSYEISFAQ KYVPLNGEIP
ITIKVAPLVK SLSVKRIRVS CREKISYRSK DYQYDFDQLD PLASDPCNPY HMRYLVRKKK
DRSLPLFEVA SKCTSGPSIR EEVVTNTVDD NLLAYTSSKE NNKDIPFSES FTVKTKLKFP
KYCEVDATKA ASLPPYGIDL FDPIKDPTQS ENTSNNGNVL GFLVGRPNRA SKTVHKIPQD
KNHNEVNDTN GNSNTSLQTS SNVPIQHYTR LNKPRRGLYL DSMHFKNIQC SHKLEIVLRV
SKTDSGSSKI IRHYEVIVDT PIYLISDLCN TSNIDLPTYD MATTESSKVL PPTFEEATSV
SASPRSSVSY YPDDISMQQL NLSRSTSLAN GYLSTLHPKT TAVSDSSNGA PIRDQQEQQA
RPLRTEDYAL QMGNENNAYS NMDGLLSQDI FEQETAATLF KRDIVTMNFN NNIFTPRYSP
RTFTNTDYNY NDNDNNDNDT EGPGPIIHPG PEPPRYDEIS S
