TEA1_YEAST
ID TEA1_YEAST Reviewed; 759 AA.
AC P47988; D6W332;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=TY1 enhancer activator;
GN Name=TEA1; OrderedLocusNames=YOR337W; ORFNames=O6257;
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=8524314; DOI=10.1128/mcb.16.1.347;
RA Gray W.M., Fassler J.S.;
RT "Isolation and analysis of the yeast TEA1 gene, which encodes a zinc
RT cluster Ty enhancer-binding protein.";
RL Mol. Cell. Biol. 16:347-358(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896263;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<999::aid-yea976>3.0.co;2-e;
RA Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
RT "Sequence of 29 kb around the PDR10 locus on the right arm of Saccharomyces
RT cerevisiae chromosome XV: similarity to part of chromosome I.";
RL Yeast 12:999-1004(1996).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 476-759.
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 [6]
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 [7]
RP DOMAIN.
RX PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT "Nine-amino-acid transactivation domain: establishment and prediction
RT utilities.";
RL Genomics 89:756-768(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-755, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-755, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-22 AND THR-755, 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: TY1 element enhancer binding protein. Binds to the DNA
CC sequence 5'-TCGGTGGTATTATTCCGA-3'.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:17467953}.
CC -!- MISCELLANEOUS: Present with 736 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U37696; AAA96753.1; -; Genomic_DNA.
DR EMBL; Z49821; CAA89982.1; -; Genomic_DNA.
DR EMBL; X95720; CAA65025.1; -; Genomic_DNA.
DR EMBL; Z75245; CAA99660.1; -; Genomic_DNA.
DR EMBL; Z75246; CAA99662.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11098.1; -; Genomic_DNA.
DR PIR; S62067; S62067.
DR RefSeq; NP_014982.3; NM_001183757.3.
DR AlphaFoldDB; P47988; -.
DR BioGRID; 34720; 91.
DR IntAct; P47988; 4.
DR STRING; 4932.YOR337W; -.
DR iPTMnet; P47988; -.
DR MaxQB; P47988; -.
DR PaxDb; P47988; -.
DR PRIDE; P47988; -.
DR EnsemblFungi; YOR337W_mRNA; YOR337W; YOR337W.
DR GeneID; 854515; -.
DR KEGG; sce:YOR337W; -.
DR SGD; S000005864; TEA1.
DR VEuPathDB; FungiDB:YOR337W; -.
DR eggNOG; ENOG502QU3W; Eukaryota.
DR HOGENOM; CLU_015811_0_0_1; -.
DR InParanoid; P47988; -.
DR OMA; CYIADHF; -.
DR BioCyc; YEAST:G3O-33812-MON; -.
DR PRO; PR:P47988; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P47988; protein.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 4.10.240.10; -; 1.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR001138; Zn2-C6_fun-type_DNA-bd.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00906; Fungal_trans; 1.
DR SMART; SM00066; GAL4; 1.
DR SUPFAM; SSF57701; SSF57701; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..759
FT /note="TY1 enhancer activator"
FT /id="PRO_0000114982"
FT DNA_BIND 70..96
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 744..752
FT /note="9aaTAD"
FT COMPBIAS 19..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 755
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 501..502
FT /note="SV -> RL (in Ref. 1; AAA96753)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="T -> A (in Ref. 1; AAA96753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 759 AA; 86833 MW; C1F7892182D1ADC2 CRC64;
MTAPLWPNKN EKNHTVKRAL STDMTSNILS STNASSNEEN SRSSSAANVR SGTGANTLTN
GGSTRKRLAC TNCRNRRKKC DLGFPCGNCS RLELVCNVND EDLRKKRYTN KYVKSLESHI
AQLETNLKNL VQKIYPDDEQ ILNRMMVGDV LSALPDSSQV SINYTDQTPS LPIPATRGTF
IIENDKVSQP LSSFNQQTEP STLNSGIFNT QKQNFEESLD DQLLLRRSLT PQGEKKKKPL
VKGSLYPEGP VSYKRKHPVK SDSLLPVSSL TAATDPSTFS DGITAGNSVL VNGELKKRIS
DLKTTVIVRG LNDDNPNSIN NDPRILKSLS NFYKWLYPGY FIFVHRESFL YGFFNHSKNN
YEDSSYCSVE LIYAMCAVGS RLTPDLQEYS EVYYQRSKKT LLQLVFDEQS TARITTVQAL
FCLAFYELGK GNNQLGWYFS GLAIRVGYDM GFQLDPKVWY VDDNNLQLTQ SELEIRSRIY
WGCYIADHFI CLMLGRTSTL SVSNSTMPES DELPEVNGTE EFRFIGRHVL QISLPLKNLI
ILSRLVQIFT SKIFIESEDI ARKLKYLNTF NSQVYNWRQS LPEFLQWSKT LIENDDVSTD
PTISYFWYCY YIVRLTFNKP FIEDSQESET VVIEIIDDLK TLLDNFGKKF GNYTKGNLYQ
LYSCLLAINC LKKLKEIRSS EQDSWNAQLD FFNHIFYTQL YPAYDLPKKL QEDTELETEQ
ENQMLNQVGN INYTHDFSLS HEIDDLIREL FGVGTPQKL
