TBS1_YEAST
ID TBS1_YEAST Reviewed; 1094 AA.
AC P38114; D6VQE5; E9PAD3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Uncharacterized transcriptional regulatory protein TBS1;
DE AltName: Full=Thiabendazole sensitive protein 1;
GN Name=TBS1; OrderedLocusNames=YBR150C; ORFNames=YBR1133;
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=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 [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=10628851; DOI=10.1007/pl00013817;
RA Entian K.-D., Schuster T., Hegemann J.H., Becher D., Feldmann H.,
RA Gueldener U., Goetz R., Hansen M., Hollenberg C.P., Jansen G., Kramer W.,
RA Klein S., Koetter P., Kricke J., Launhardt H., Mannhaupt G., Maierl A.,
RA Meyer P., Mewes W., Munder T., Niedenthal R.K., Ramezani Rad M.,
RA Roehmer A., Roemer A., Rose M., Schaefer B., Siegler M.-L., Vetter J.,
RA Wilhelm N., Wolf K., Zimmermann F.K., Zollner A., Hinnen A.;
RT "Functional analysis of 150 deletion mutants in Saccharomyces cerevisiae by
RT a systematic approach.";
RL Mol. Gen. Genet. 262:683-702(1999).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP IDENTIFICATION BY 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 [8]
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: Involved in tolerance to thiabendazole.
CC {ECO:0000269|PubMed:10628851}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane; Single-pass membrane protein.
CC Mitochondrion membrane; Single-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 573 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z36019; CAA85108.1; -; Genomic_DNA.
DR EMBL; Z36020; CAA85110.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07265.1; -; Genomic_DNA.
DR PIR; S46021; S46021.
DR RefSeq; NP_009708.1; NM_001178498.1.
DR AlphaFoldDB; P38114; -.
DR SMR; P38114; -.
DR BioGRID; 32849; 92.
DR DIP; DIP-6485N; -.
DR IntAct; P38114; 5.
DR MINT; P38114; -.
DR STRING; 4932.YBR150C; -.
DR iPTMnet; P38114; -.
DR MaxQB; P38114; -.
DR PaxDb; P38114; -.
DR PRIDE; P38114; -.
DR EnsemblFungi; YBR150C_mRNA; YBR150C; YBR150C.
DR GeneID; 852447; -.
DR KEGG; sce:YBR150C; -.
DR SGD; S000000354; TBS1.
DR VEuPathDB; FungiDB:YBR150C; -.
DR eggNOG; ENOG502QZJZ; Eukaryota.
DR GeneTree; ENSGT00940000176304; -.
DR HOGENOM; CLU_008153_0_0_1; -.
DR InParanoid; P38114; -.
DR BioCyc; YEAST:G3O-29101-MON; -.
DR PRO; PR:P38114; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38114; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA: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:0006351; P:transcription, DNA-templated; IEA:InterPro.
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 DNA-binding; Membrane; Metal-binding; Mitochondrion; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..1094
FT /note="Uncharacterized transcriptional regulatory protein
FT TBS1"
FT /id="PRO_0000114992"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DNA_BIND 107..137
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00227"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1032
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 126904 MW; 3C08F83F5879D14F CRC64;
MNMDSGITSS HGSMDKTQKQ SSEWAANQKH NQRVENTRVL MGPAVPAMPP VPSNFPPVPT
GTIMSPQLSP FPDHRLRHHP LAHMMPADKN FLAYNMESFK SRVTKACDYC RKRKIRCTEI
EPISGKCRNC IKYNKDCTFH FHEELKRRRE EALNNKGNGK SVKKPRLDKE NKFKDENFDI
AVRSRNTSST DSSPKLHTNL SQEYIGVSAG KSASDKEDTW PDFVPIDRTV LEKIELNHTK
VAGKVFVLEE ICKNMKGTIE KLAEKSKIDV IDKEYMKRPK RKQYSKALLT KQKMFHFRQN
VLSHLTDEEF LSPINEMFTT TFKYSILQTK LVLDFSFRSA SSPSSDNILY PLPRLAIAKR
LLKNIKCPSL ASLLHIVDVD QCLQFADVHF DPAKGRLTSS QAFLLNICLC LGATVTNFEE
KQELVDEDNH ETYYFEKFEL WRLRSFTFLN SVYYYHKLSV ARADMTALKA LLLLAKFAQQ
KISASSAVKV LSVAIKVALD LRLNLHSTYE DLELDEIIKR RRLWCYCFST DKFFSVVLSR
PPFLKEENTD VLTDESYVEL FRDKILPNLS IKYDDSKLEG VKDIVSVVNL LANHLEYVPY
IQSYFLSRLS LIESQIYYSC FSIRTTLDDT LDEIIENVLE NQKALDRMRD DLPTILSLEN
YKENMRILSL DSSKLDFEVS CCTTILLHLR WYHQKITLSL FVISIIGDNL DQRESSRHDI
AEIIRRSRLD FKRNCIEVLN ILKDFEYYPT VQNEFLYFSL TTVFSMFLYL SEIMVNDEHA
METGYIIGLL RDTHTRMLGS EERCLSVHNL KWQTSLFFYT FFLRSTMEKF NLTSKYAKFY
AFDSNYYEGV LNRLVKHTRE SKDDMVELLK TSFINKEKMA AFGSFVTEDQ EKMEVSFNIF
NEITIQDLNF LQFSSIPKLW ENKTLEPGEE YHHSNGTNTD NNETTGADDT DDNNNNNNNN
NKNGNNSSST INNNNNNYSN SNNNDNDNNI NDDDDDDDDD DDDDDDDDDD DDNDDDYSNN
GADDDEEDDD YDRSLFPTGL ASLLDASYPE RTANDYRDEN EQSNKLFEKI EGHLEHGVFF
YDRDFFFKNV CVKM
