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Resistance to glucose repression protein 1 (Protein HEX2) (Second-site suppressor of the rna1-1 mutation 1)

 REG1_YEAST              Reviewed;        1014 AA.
Q00816; D6VS13;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-APR-1993, sequence version 1.
13-FEB-2019, entry version 172.
RecName: Full=Resistance to glucose repression protein 1;
AltName: Full=Protein HEX2;
AltName: Full=Second-site suppressor of the rna1-1 mutation 1;
Name=REG1; Synonyms=HEX2, PZF240, SPP43, SRN1;
OrderedLocusNames=YDR028C; ORFNames=YD9813.06C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1889400; DOI=10.1111/j.1432-1033.1991.tb16187.x;
Niederacher D., Entian K.-D.;
"Characterization of Hex2 protein, a negative regulatory element
necessary for glucose repression in yeast.";
Eur. J. Biochem. 200:311-319(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1588964; DOI=10.1128/MCB.12.6.2673;
Tung K.-S., Norbeck L.L., Nolan S.L., Atkinson N.S., Hopper A.K.;
"SRN1, a yeast gene involved in RNA processing, is identical to
HEX2/REG1, a negative regulator in glucose repression.";
Mol. Cell. Biol. 12:2673-2680(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1014.
PubMed=8896275;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1085::AID-YEA9>3.3.CO;2-S;
Eide L.G., Sander C., Prydz H.;
"Sequencing and analysis of a 35.4 kb region on the right arm of
chromosome IV from Saccharomyces cerevisiae reveal 23 open reading
frames.";
Yeast 12:1085-1090(1996).
[6]
INTERACTION WITH PP1.
PubMed=8846786;
Tu J.L., Carlson M.;
"REG1 binds to protein phosphatase type 1 and regulates glucose
repression in Saccharomyces cerevisiae.";
EMBO J. 14:5939-5946(1995).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-75, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-421; SER-572 AND
SER-576, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-73; SER-75; TYR-480 AND
SER-490, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-254; SER-311;
SER-421; SER-576 AND SER-680, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-242; SER-421;
SER-570; SER-572; SER-576; SER-610; SER-614; THR-896; SER-898 AND
SER-980, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[13]
FUNCTION, AND INTERACTION WITH SAK1.
PubMed=21216941; DOI=10.1128/EC.00291-10;
Liu Y., Xu X., Carlson M.;
"Interaction of SNF1 protein kinase with its activating kinase Sak1.";
Eukaryot. Cell 10:313-319(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Involved in RNA processing and negative regulation of
glucose repression. Regulates the level of two antigens, P43 and
P70. Binds to protein phosphatase type 1. Functions with REG2 and
SNF1 protein kinase to regulate growth. Might regulate SNF1
directly or indirectly. {ECO:0000269|PubMed:21216941}.
-!- SUBUNIT: Interacts with SAK1. {ECO:0000269|PubMed:21216941,
ECO:0000269|PubMed:8846786}.
-!- INTERACTION:
P32598:GLC7; NbExp=4; IntAct=EBI-8270, EBI-13715;
P06782:SNF1; NbExp=7; IntAct=EBI-8270, EBI-17516;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: Present with 2560 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M33703; AAA34670.1; -; Genomic_DNA.
EMBL; M90540; AAB59326.1; -; Genomic_DNA.
EMBL; Z47814; CAA87807.1; -; Genomic_DNA.
EMBL; Z74324; CAA98850.1; -; Genomic_DNA.
EMBL; X95966; CAA65223.1; -; Genomic_DNA.
EMBL; BK006938; DAA11873.1; -; Genomic_DNA.
PIR; S32613; S32613.
RefSeq; NP_010311.1; NM_001180336.1.
ProteinModelPortal; Q00816; -.
SMR; Q00816; -.
BioGrid; 32078; 138.
ComplexPortal; CPX-1266; REG1-GLC7 phosphatase complex.
DIP; DIP-2513N; -.
ELM; Q00816; -.
IntAct; Q00816; 24.
MINT; Q00816; -.
STRING; 4932.YDR028C; -.
iPTMnet; Q00816; -.
MaxQB; Q00816; -.
PaxDb; Q00816; -.
PRIDE; Q00816; -.
EnsemblFungi; YDR028C_mRNA; YDR028C_mRNA; YDR028C.
GeneID; 851592; -.
KEGG; sce:YDR028C; -.
EuPathDB; FungiDB:YDR028C; -.
SGD; S000002435; REG1.
InParanoid; Q00816; -.
OMA; WKYIILK; -.
BioCyc; YEAST:G3O-29644-MONOMER; -.
PRO; PR:Q00816; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000164; C:protein phosphatase type 1 complex; TAS:SGD.
GO; GO:0005773; C:vacuole; IEA:GOC.
GO; GO:0019888; F:protein phosphatase regulator activity; TAS:SGD.
GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
GO; GO:0005977; P:glycogen metabolic process; TAS:SGD.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:SGD.
GO; GO:0007039; P:protein catabolic process in the vacuole; IDA:SGD.
GO; GO:0006109; P:regulation of carbohydrate metabolic process; IGI:SGD.
GO; GO:0006986; P:response to unfolded protein; IMP:SGD.
GO; GO:0061587; P:transfer RNA gene-mediated silencing; IMP:SGD.
InterPro; IPR013860; AreA_GATA.
Pfam; PF08550; DUF1752; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
CHAIN 2 1014 Resistance to glucose repression protein
1.
/FTId=PRO_0000083953.
MOTIF 277 283 Nuclear localization signal.
{ECO:0000255}.
MOTIF 595 599 Nuclear localization signal.
{ECO:0000255}.
MOTIF 873 879 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 543 552 Ser-rich.
COMPBIAS 742 760 Asp/Glu-rich (acidic).
COMPBIAS 834 844 Asp/Glu-rich (acidic).
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:22814378}.
MOD_RES 73 73 Phosphothreonine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 254 254 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 480 480 Phosphotyrosine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000244|PubMed:17287358}.
MOD_RES 570 570 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 576 576 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 896 896 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 898 898 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 980 980 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CONFLICT 376 377 DK -> EE (in Ref. 1; AAA34670).
{ECO:0000305}.
CONFLICT 534 534 N -> K (in Ref. 1; AAA34670).
{ECO:0000305}.
CONFLICT 657 657 D -> H (in Ref. 1; AAA34670).
{ECO:0000305}.
CONFLICT 889 889 S -> T (in Ref. 1; AAA34670).
{ECO:0000305}.
CONFLICT 988 1014 ARGMASKYLHSWKKSDVKPQENGNDSS -> QEVWQASTCT
LGKRVTSSHKKMEMTAVRRKNFEVNMKRK (in Ref.
1). {ECO:0000305}.
SEQUENCE 1014 AA; 112616 MW; 0D4AAC75E111B346 CRC64;
MSTNLANYFA GKKDIENEHV NRNASHESNS KSDVKISGND NDNDEDMGPS VSMAVQAKND
DDFHKSTFNL KRTRSMGLLD EYIDPTKKLL GRSDDLYDND NEYYDNSSNN SSSNSSDDDY
DDGYQEHSTS VSPPPADNDS YLIPQDDNDV VVEPERHVDY LSHEWKESEI SNSWKYIILK
KKKRDVDLVN AARLENASWR TWAKARNNLK TVSPEVVNWS KDSDVTWLYG PIVRDSEGNA
QSEEEHDLER GYGSDDENSK RISMPTKNSK SIAAAPKPIL KKRTVTEIIE DNALWKLNEA
RKHMTEMKHA SVIMDPNGNK NVHDDFDALA AQVNAQYYHY PKESNSSVSL KSQHSDKKDN
STIPNPVGEN SNGGGDKGEE DLHLKSALHV QNNRSTAQSN KSILENSTND RKANLDQNLN
SPDNNRFPSS TSSSNRDNEN NSMGLSSILT SNPSEKSNKP TKNRHIHFND RVEQCMALRY
PASQSEDDES DDENKQYVDV NNNANVTTIN NNRTPLLAIQ HKSIPINSAT EHLNKNTSDD
DTSSQSSSSS HSDDEEHGGL YINARFSRRS DSGVHSPITD NSSVASSTTS RAHVRPIIKL
LPDTTLNYGS DEESDNGEFN GYGNAVSHNV NTSRGYDYIY DYNSVYTGDT SSFLPVDSCD
IVDVPEGMDL QTAIADDNAS NYEFNNAVES KEKHVPQLHK ASANNTTRQH GSHMLLYDDD
NYSSSSDSEQ QFIEDSQYNS SDDEEEEDDD DQEVDDNHDE GLSLRRTLSL GKSGSTNSLY
DLAQPSLSSA TPQQKNPTNF TGGKTDVDKD AQLAVRPYPL KRNSSSGNFI FNSDSEEESS
SEEEQRPLPA NSQLVNRSVL KGSVTPANIS SQKKKALPKQ PKASDSSQSF RIVNNTPSPA
EVGASDVAIE GYFSPRNESI KSVVSGGNMM DHQDHSEMDT LAKGFENCHI NNASKLKDKK
VDSVQTTRKE ASLTDSSNES LHKVVQNARG MASKYLHSWK KSDVKPQENG NDSS


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Pathways :
WP2199: Seed Development
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
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WP1676: Non-homologous end-joining

Related Genes :
[REG1 HEX2 PZF240 SPP43 SRN1 YDR028C YD9813.06C] Resistance to glucose repression protein 1 (Protein HEX2) (Second-site suppressor of the rna1-1 mutation 1)
[] RNA1 polyprotein (P1) [Cleaved into: Protein X1; Protein X2; Putative ATP-dependent helicase (EC 3.6.4.-) (Membrane-binding protein) (NTP-binding protein) (NTB); Viral genome-linked protein (VPg); Picornain 3C-like protease (3C-like protease) (PRO) (EC 3.4.22.-); RNA-directed RNA polymerase (POL) (EC 2.7.7.48)]
[] RNA1 polyprotein (P1) [Cleaved into: Protein X1; Protein X2; Putative ATP-dependent helicase (EC 3.6.4.-) (Membrane-binding protein) (NTP-binding protein) (NTB); Viral genome-linked protein (VPg); Picornain 3C-like protease (3C-like protease) (PRO) (EC 3.4.22.-); RNA-directed RNA polymerase (POL) (EC 2.7.7.48)]
[ribBA C5Y96_25100] Riboflavin biosynthesis protein RibBA [Includes: 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12); GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II)]
[PTO1279] 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) (EC 4.1.2.51) (2-dehydro-3-deoxy-galactonate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase) (EC 4.1.2.-) (EC 4.1.2.21)
[STD1 MSN3 SFS3 YOR047C] Protein STD1 (Glucose repression modulator MSN3) (Suppressor of Tbp deletion protein 1) (Suppressor of fluoride sensitivity 3)
[] 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC 4.1.2.55)
[dapB C5Y96_04595] 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8)
[CRY2 PHH1 SEL20 At1g04400 F19P19.14] Cryptochrome-2 (Atcry2) (Blue light photoreceptor) (Protein PHR homolog 1) (AtPHH1) (Protein SUPPRESSOR OF elf3 20)
[pyrG C5Y96_01415] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[coaX C5Y96_07410] Type III pantothenate kinase (EC 2.7.1.33) (PanK-III) (Pantothenic acid kinase)
[katG C5Y96_06795] Catalase-peroxidase (CP) (EC 1.11.1.21) (Peroxidase/catalase)
[TUP1 AAR1 AER2 AMM1 CYC9 FLK1 SFL2 UMR7 YCR084C YCR84C] General transcriptional corepressor TUP1 (Flocculation suppressor protein) (Glucose repression regulatory protein TUP1) (Repressor AER2)
[YIPF3 C6orf109 KLIP1] Protein YIPF3 (Killer lineage protein 1) (Natural killer cell-specific antigen KLIP1) (YIP1 family member 3) [Cleaved into: Protein YIPF3, 36 kDa form III]
[FMR1] Synaptic functional regulator FMR1 (Fragile X mental retardation protein 1) (FMRP) (Protein FMR-1)
[gad gnaD SSO3198] D-gluconate/D-galactonate dehydratase (GAD) (GNAD) (EC 4.2.1.140) (EC 4.2.1.39) (EC 4.2.1.6)
[] RNA2 polyprotein (Genome polyprotein M) (M RNA polyprotein) (Middle component RNA polyprotein) (P2) [Cleaved into: VP58 (P58); Movement protein (MP) (48 kDa protein); Large capsid protein (LCP) (Coat protein VP37) (L subunit) (Large coat protein); Small capsid protein precursor (S subunit); Mature small capsid protein (SCP) (Coat protein VP23) (Small capsid protein, N-terminus part) (Small coat protein, N-terminus part); Small capsid protein C-terminus part (Small coat protein C-terminus part)]
[TP53 P53] Cellular tumor antigen p53 (Antigen NY-CO-13) (Phosphoprotein p53) (Tumor suppressor p53)
[rbsK C5Y96_23360] Ribokinase (RK) (EC 2.7.1.15)
[PDR5 LEM1 STS1 YDR1 YOR153W] Pleiotropic ABC efflux transporter of multiple drugs (Pleiotropic drug resistance protein 5) (Suppressor of toxicity of sporidesmin)
[cheB C5Y96_04460] Protein-glutamate methylesterase/protein-glutamine glutaminase (EC 3.1.1.61) (EC 3.5.1.44)
[cheB C5Y96_10080] Protein-glutamate methylesterase/protein-glutamine glutaminase (EC 3.1.1.61) (EC 3.5.1.44)
[SHO1 SSU81 YER118C] High osmolarity signaling protein SHO1 (Osmosensor SHO1) (Suppressor of SUA8-1 mutation) (Synthetic high osmolarity-sensitive protein 1)
[nqrB C5Y96_03230] Na(+)-translocating NADH-quinone reductase subunit B (Na(+)-NQR subunit B) (Na(+)-translocating NQR subunit B) (EC 7.2.1.1) (NQR complex subunit B) (NQR-1 subunit B)
[gag-pol] Gag-Pol polyprotein (Pr160Gag-Pol) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Transframe peptide (TF); p6-pol (p6*); Protease (EC 3.4.23.16) (PR) (Retropepsin); Reverse transcriptase/ribonuclease H (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.13) (Exoribonuclease H) (EC 3.1.13.2) (p66 RT); p51 RT; p15; Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[aspA fumC C5Y96_14825] Fumarate hydratase class II (Fumarase C) (EC 4.2.1.2) (Aerobic fumarase) (Iron-independent fumarase)
[APEX1 APE APE1 APEX APX HAP1 REF1] DNA-(apurinic or apyrimidinic site) lyase (EC 3.1.-.-) (EC 4.2.99.18) (APEX nuclease) (APEN) (Apurinic-apyrimidinic endonuclease 1) (AP endonuclease 1) (APE-1) (REF-1) (Redox factor-1) [Cleaved into: DNA-(apurinic or apyrimidinic site) lyase, mitochondrial]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[NR3C1 GRL] Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)
[garL yhaF b3126 JW3095] 5-keto-4-deoxy-D-glucarate aldolase (KDGluc aldolase) (KDGlucA) (EC 4.1.2.20) (2-dehydro-3-deoxy-D-glucarate aldolase) (2-keto-3-deoxy-D-glucarate aldolase) (5-dehydro-4-deoxy-D-glucarate aldolase) (Alpha-keto-beta-deoxy-D-glucarate aldolase)

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