TEC1_YEAST
ID TEC1_YEAST Reviewed; 486 AA.
AC P18412; D6VQ82;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Ty transcription activator TEC1;
GN Name=TEC1; Synonyms=ROC1; OrderedLocusNames=YBR083W; ORFNames=YBR0750;
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=2192259; DOI=10.1128/mcb.10.7.3541-3550.1990;
RA Laloux I., Dubois E., Dewerchin M., Jacobs E.;
RT "TEC1, a gene involved in the activation of Ty1 and Ty1-mediated gene
RT expression in Saccharomyces cerevisiae: cloning and molecular analysis.";
RL Mol. Cell. Biol. 10:3541-3550(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP DOMAIN TEA.
RX PubMed=2070413; DOI=10.1016/0092-8674(91)90132-i;
RA Buerglin T.R.;
RT "The TEA domain: a novel, highly conserved DNA-binding motif.";
RL Cell 66:11-12(1991).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: TEC1 is involved in the activation of TY1 and TY1-mediated
CC gene expression. It is not involved in mating or sporulation processes.
CC -!- INTERACTION:
CC P18412; P13574: STE12; NbExp=12; IntAct=EBI-19091, EBI-18264;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 530 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TEC1 family. {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; M32797; AAA35141.1; -; Genomic_DNA.
DR EMBL; Z35952; CAA85028.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07202.1; -; Genomic_DNA.
DR PIR; A35667; A35667.
DR RefSeq; NP_009639.3; NM_001178431.3.
DR AlphaFoldDB; P18412; -.
DR SMR; P18412; -.
DR BioGRID; 32787; 131.
DR ComplexPortal; CPX-576; Tec1/Ste12/Dig1 transcription regulation complex.
DR DIP; DIP-6311N; -.
DR IntAct; P18412; 9.
DR MINT; P18412; -.
DR STRING; 4932.YBR083W; -.
DR iPTMnet; P18412; -.
DR MaxQB; P18412; -.
DR PaxDb; P18412; -.
DR PRIDE; P18412; -.
DR EnsemblFungi; YBR083W_mRNA; YBR083W; YBR083W.
DR GeneID; 852377; -.
DR KEGG; sce:YBR083W; -.
DR SGD; S000000287; TEC1.
DR VEuPathDB; FungiDB:YBR083W; -.
DR eggNOG; KOG3841; Eukaryota.
DR GeneTree; ENSGT00950000182956; -.
DR HOGENOM; CLU_043980_0_0_1; -.
DR InParanoid; P18412; -.
DR OMA; ANFGRNE; -.
DR BioCyc; YEAST:G3O-29051-MON; -.
DR PRO; PR:P18412; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P18412; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:1990527; C:Tec1p-Ste12p-Dig1p complex; IDA:SGD.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IDA:SGD.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IDA:SGD.
DR GO; GO:0010527; P:positive regulation of transposition, RNA-mediated; IMP:SGD.
DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
DR GO; GO:0010570; P:regulation of filamentous growth; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 6.10.20.40; -; 1.
DR InterPro; IPR000818; TEA/ATTS_dom.
DR InterPro; IPR038096; TEA/ATTS_sf.
DR Pfam; PF01285; TEA; 1.
DR PRINTS; PR00065; TEADOMAIN.
DR SMART; SM00426; TEA; 1.
DR PROSITE; PS00554; TEA_1; 1.
DR PROSITE; PS51088; TEA_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..486
FT /note="Ty transcription activator TEC1"
FT /id="PRO_0000205941"
FT DNA_BIND 125..199
FT /note="TEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00505"
FT REGION 372..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 486 AA; 55157 MW; F247016D3E75C454 CRC64;
MSLKEDDFGK DNSRNIESYT GRIFDVYIQK DSYSQSALDD MFPEAVVSTA ACVKNEAEDN
INLIDTHPQF ELVNTGLGAK SDDLKSPSAK ATFTDKQRKN EVPNISVSNY FPGQSSETSS
TTESWTIGCD KWSEKVEEAF LEALRLIMKN GTTKIKIRNA NFGRNELISL YIKHKTNEFR
TKKQISSHIQ VWKKTIQNKI KDSLTLSSKE KELLHLIEHG AEQTTENSNL FYDIFEEIID
SLPSVSDSGS LTPKNLYVSN NSSGLSVHSK LLTPITASNE KKIENFIKTN AASQAKTPLI
YAKHIYENID GYKCVPSKRP LEQLSPTELH QGDRPNKASF SNKKAILESA KKIEIEQRKI
INKYQRISRI QEHESNPEFS SNSNSGSEYE SEEEVVPRSA TVTQLQSRPV PYYKNNGMPY
SLSKVRGRPM YPRPAEDAYN ANYIQGLPQY QTSYFSQLLL SSPQHYEHSP HQRNFTPSNQ
SHGNFY
