TYE7_YEAST
ID TYE7_YEAST Reviewed; 291 AA.
AC P33122; D6W340;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Serine-rich protein TYE7;
DE AltName: Full=Basic-helix-loop-helix protein SGC1;
GN Name=TYE7; Synonyms=SGC1; OrderedLocusNames=YOR344C; ORFNames=O6233;
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].
RX PubMed=7900422; DOI=10.1002/yea.320101010;
RA Loehning C., Ciriacy M.;
RT "The TYE7 gene of Saccharomyces cerevisiae encodes a putative bHLH-LZ
RT transcription factor required for Ty1-mediated gene expression.";
RL Yeast 10:1329-1339(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Loehning C.;
RL Thesis (1993), Heinrich-Heine University / Duesseldorf, Germany.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
RX PubMed=7739544; DOI=10.1128/mcb.15.5.2646;
RA Nishi K., Park C.S., Pepper A.E., Eichinger G., Innis M.A., Holland M.J.;
RT "The GCR1 requirement for yeast glycolytic gene expression is suppressed by
RT dominant mutations in the SGC1 gene, which encodes a novel basic-helix-
RT loop-helix protein.";
RL Mol. Cell. Biol. 15:2646-2653(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90843 / S288c / FY73;
RX PubMed=8948102;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1475::aid-yea32>3.0.co;2-v;
RA Purnelle B., Goffeau A.;
RT "Nucleotide sequence analysis of a 40 kb segment on the right arm of yeast
RT chromosome XV reveals 18 open reading frames including a new pyruvate
RT kinase and three homologues to chromosome I genes.";
RL Yeast 12:1475-1481(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [6]
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 [7]
RP CHARACTERIZATION.
RX PubMed=10606743; DOI=10.1016/s0014-5793(99)01654-3;
RA Sato T., Lopez M.C., Sugioka S., Jigami Y., Baker H.V., Uemura H.;
RT "The E-box DNA binding protein Sgc1p suppresses the gcr2 mutation, which is
RT involved in transcriptional activation of glycolytic genes in Saccharomyces
RT cerevisiae.";
RL FEBS Lett. 463:307-311(1999).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, 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 [11]
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 glycolytic gene expression, such
CC as enolase genes (ENO1 and ENO2), glyceraldehyde-3-phosphate
CC dehydrogenase gene (TDH), phosphoglycerate kinase (PGK1),
CC phosphoglycerate mutase (PGM1), pyruvate kinase (PYK1) and
CC triosephosphate isomerase (TPI1) genes. Binds DNA on E-box motifs: 5'-
CC CANNTG-3'.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 486 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z14973; CAA78695.1; -; Genomic_DNA.
DR EMBL; L38594; AAA92865.1; -; Genomic_DNA.
DR EMBL; X95720; CAA65032.1; -; Genomic_DNA.
DR EMBL; Z75252; CAA99671.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11106.1; -; Genomic_DNA.
DR PIR; S48252; S48252.
DR RefSeq; NP_014989.3; NM_001183764.3.
DR PDB; 7F2F; X-ray; 2.55 A; A/B=165-291.
DR PDBsum; 7F2F; -.
DR AlphaFoldDB; P33122; -.
DR SMR; P33122; -.
DR BioGRID; 34729; 215.
DR DIP; DIP-4279N; -.
DR IntAct; P33122; 2.
DR STRING; 4932.YOR344C; -.
DR iPTMnet; P33122; -.
DR MaxQB; P33122; -.
DR PaxDb; P33122; -.
DR PRIDE; P33122; -.
DR EnsemblFungi; YOR344C_mRNA; YOR344C; YOR344C.
DR GeneID; 854525; -.
DR KEGG; sce:YOR344C; -.
DR SGD; S000005871; TYE7.
DR VEuPathDB; FungiDB:YOR344C; -.
DR eggNOG; KOG2588; Eukaryota.
DR HOGENOM; CLU_067895_0_0_1; -.
DR InParanoid; P33122; -.
DR OMA; IXSASSS; -.
DR BioCyc; YEAST:G3O-33818-MON; -.
DR PRO; PR:P33122; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P33122; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0045821; P:positive regulation of glycolytic process; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..291
FT /note="Serine-rich protein TYE7"
FT /id="PRO_0000127495"
FT DOMAIN 180..265
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 89..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MUTAGEN 189
FT /note="E->Q: In SGC1-1; suppresses transcriptional defect
FT caused by a GCR1 null mutation."
FT /evidence="ECO:0000269|PubMed:7739544"
FT MUTAGEN 210
FT /note="V->I: In SGC1-2/3/4; suppresses transcriptional
FT defect caused by a GCR1 null mutation."
FT /evidence="ECO:0000269|PubMed:7739544"
FT HELIX 179..205
FT /evidence="ECO:0007829|PDB:7F2F"
FT TURN 208..212
FT /evidence="ECO:0007829|PDB:7F2F"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:7F2F"
FT HELIX 251..287
FT /evidence="ECO:0007829|PDB:7F2F"
SQ SEQUENCE 291 AA; 32689 MW; 0B18F78C8AEEECA7 CRC64;
MNSILDRNVR SSETTLIKPE SEFDNWLSDE NDGASHINVN KDSSSVLSAS SSTWFEPLEN
IISSASSSSI GSPIEDQFIS SNNEESALFP TDQFFSNPSS YSHSPEVSSS IKREEDDNAL
SLADFEPASL QLMPNMINTD NNDDSTPLKN EIELNDSFIK TNLDAKETKK RAPRKRLTPF
QKQAHNKIEK RYRININTKI ARLQQIIPWV ASEQTAFEVG DSVKKQDEDG AETAATTPLP
SAAATSTKLN KSMILEKAVD YILYLQNNER LYEMEVQRLK SEIDTLKQDQ K
