TBF1_YEAST
ID TBF1_YEAST Reviewed; 562 AA.
AC Q02457; D6W3N9;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Protein TBF1;
DE AltName: Full=TBF-alpha;
DE AltName: Full=TTAGGG repeat-binding factor 1;
GN Name=TBF1; OrderedLocusNames=YPL128C; ORFNames=LPI16C;
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].
RC STRAIN=LN224;
RX PubMed=8423796; DOI=10.1128/mcb.13.2.1306-1314.1993;
RA Brigati C., Kurtz S., Balderes D., Vidali G., Shore D.M.;
RT "An essential yeast gene encoding a TTAGGG repeat-binding protein.";
RL Mol. Cell. Biol. 13:1306-1314(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 FUNCTION.
RX PubMed=8614633; DOI=10.1093/nar/24.7.1294;
RA Bilaud T., Koering C.E., Binet-Brasselet E., Ancelin K., Pollice A.,
RA Gasser S.M., Gilson E.;
RT "The telobox, a Myb-related telomeric DNA binding motif found in proteins
RT from yeast, plants and human.";
RL Nucleic Acids Res. 24:1294-1303(1996).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10871401; DOI=10.1093/nar/28.13.2519;
RA Koering C.E., Fourel G., Binet-Brasselet E., Laroche T., Klein F.,
RA Gilson E.;
RT "Identification of high affinity Tbf1p-binding sites within the budding
RT yeast genome.";
RL Nucleic Acids Res. 28:2519-2526(2000).
RN [6]
RP FUNCTION.
RX PubMed=11258704; DOI=10.1093/embo-reports/kve024;
RA Fourel G., Boscheron C., Revardel E., Lebrun E., Hu Y.-F., Simmen K.C.,
RA Mueller K., Li R., Mermod N., Gilson E.;
RT "An activation-independent role of transcription factors in insulator
RT function.";
RL EMBO Rep. 2:124-132(2001).
RN [7]
RP FUNCTION.
RX PubMed=12200417; DOI=10.1074/jbc.m202578200;
RA Fourel G., Miyake T., Defossez P.-A., Li R., Gilson E.;
RT "General regulatory factors (GRFs) as genome partitioners.";
RL J. Biol. Chem. 277:41736-41743(2002).
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 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Binds the telomeric double-stranded TTAGGG repeat and
CC negatively regulates telomere length. Involved in the regulation of
CC gene expression. 52 binding sites have been identified, distributed
CC over 15 chromosomes. A member of the general regulatory factors (GRFs)
CC which act as genome partitioners. Acts as a chromatin insulator which
CC are known as STARs (Subtelomeric anti-silencing region). STARs prevent
CC negative or positive transcription influence by extending across
CC chromatin to a promoter. {ECO:0000269|PubMed:10871401,
CC ECO:0000269|PubMed:11258704, ECO:0000269|PubMed:12200417,
CC ECO:0000269|PubMed:8614633}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- INTERACTION:
CC Q02457; Q05934: VID22; NbExp=2; IntAct=EBI-19005, EBI-30350;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:10871401}. Chromosome, telomere
CC {ECO:0000269|PubMed:10871401}. Note=Localizes to synapsed chromosomes
CC during meiosis.
CC -!- MISCELLANEOUS: Present with 6380 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X69394; CAA49191.1; -; Genomic_DNA.
DR EMBL; U43703; AAB68230.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11305.1; -; Genomic_DNA.
DR PIR; S69055; S69055.
DR RefSeq; NP_015197.1; NM_001183942.1.
DR AlphaFoldDB; Q02457; -.
DR SMR; Q02457; -.
DR BioGRID; 36053; 301.
DR DIP; DIP-1918N; -.
DR IntAct; Q02457; 23.
DR MINT; Q02457; -.
DR STRING; 4932.YPL128C; -.
DR iPTMnet; Q02457; -.
DR MaxQB; Q02457; -.
DR PaxDb; Q02457; -.
DR PRIDE; Q02457; -.
DR EnsemblFungi; YPL128C_mRNA; YPL128C; YPL128C.
DR GeneID; 855975; -.
DR KEGG; sce:YPL128C; -.
DR SGD; S000006049; TBF1.
DR VEuPathDB; FungiDB:YPL128C; -.
DR eggNOG; ENOG502QRT9; Eukaryota.
DR HOGENOM; CLU_008791_4_0_1; -.
DR InParanoid; Q02457; -.
DR OMA; IFCPNTL; -.
DR BioCyc; YEAST:G3O-34027-MON; -.
DR PRO; PR:Q02457; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02457; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IGI:SGD.
DR GO; GO:0001015; P:snoRNA transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IDA:SGD.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF08558; TRF; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; DNA-binding; Nucleus; Reference proteome; Telomere;
KW Transcription; Transcription regulation.
FT CHAIN 1..562
FT /note="Protein TBF1"
FT /id="PRO_0000197125"
FT DOMAIN 404..460
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 431..456
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 376..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 71
FT /note="E -> R (in Ref. 1; CAA49191)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..373
FT /note="DAA -> ERR (in Ref. 1; CAA49191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 562 AA; 62824 MW; 2340F086468EC54F CRC64;
MDSQVPNNNE SLNRFNDIIQ SLPARTRLTI CSLCLLDNIS TQLLRFLILN ANSPNIIAVL
TDQTAFLSSG ETEIFQTLVK LFKQIRMIYH TRSPLLSVHD VAPGLWFPNS PPPLILRGHE
AFIITAIRKA NLLTFLLTSL NCLNYGFELL QSIFLDIFCP NTNTVGNNSL EQSGKFLKSQ
AILYLDLKTQ AYIAGLKEFQ DETNEISLEK KQELLDLIFP SNLADILVQR RTGDSGDITL
LTPSEKDFVE RCDRRRENLK IVQDFNSLTQ SYEWAQFIRE LLDYCNKNMG LIIWGRKGRG
KSPLYDFDVN EFDPQVLFST GTRTVEFMDD QNQPSSASAF LSTARPNHYS THTPTTDVSS
KNPAITQSIV DAAVAASMSN SSSGPHSSHN NSSNSNNNGS IGLRKPKAKR TWSKEEEEAL
VEGLKEVGPS WSKILDLYGP GGKITENLKN RTQVQLKDKA RNWKLQYLKS GKPLPDYLIK
VTGNLEKIYK AKKKFSQSPN SSTIMEQNLS QHPSSAASAT EDTQTHQEDS HGQNSDNMPS
NGLFGNSTSD NTGFDPHLED GM
