TEB1_SCHPO
ID TEB1_SCHPO Reviewed; 390 AA.
AC Q10274; P78793;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Telobox protein 1 {ECO:0000303|PubMed:10572167};
DE AltName: Full=Meiotically up-regulated gene 152 protein {ECO:0000303|PubMed:16303567};
GN Name=teb1 {ECO:0000303|PubMed:10572167};
GN Synonyms=mug152 {ECO:0000303|PubMed:16303567},
GN spX {ECO:0000303|PubMed:10606652};
GN ORFNames=SPAC13G7.10 {ECO:0000312|PomBase:SPAC13G7.10};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-390.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=10572167; DOI=10.1093/nar/27.24.4687;
RA Vassetzky N.S., Gaden F., Brun C., Gasser S.M., Gilson E.;
RT "Taz1p and Teb1p, two telobox proteins in Schizosaccharomyces pombe,
RT recognize different telomere-related DNA sequences.";
RL Nucleic Acids Res. 27:4687-4694(1999).
RN [4]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=10606652; DOI=10.1093/nar/28.2.527;
RA Spink K.G., Evans R.J., Chambers A.;
RT "Sequence-specific binding of Taz1p dimers to fission yeast telomeric
RT DNA.";
RL Nucleic Acids Res. 28:527-533(2000).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND DNA-BINDING.
RX PubMed=23314747; DOI=10.1038/emboj.2012.339;
RA Valente L.P., Dehe P.M., Klutstein M., Aligianni S., Watt S., Baehler J.,
RA Cooper J.P.;
RT "Myb-domain protein Teb1 controls histone levels and centromere assembly in
RT fission yeast.";
RL EMBO J. 32:450-460(2013).
CC -!- FUNCTION: General transcription factor with prominent roles in
CC controlling histone levels and stability. Binds and regulates the
CC activities of many promoters, including those controlling the
CC expression of all four types of canonical histones. Is also involved in
CC the centromeric loading of cnp1 and maintenance of centromere identity.
CC Moreover, regulates the expression of cdc2, a protease capable of
CC histone clipping. {ECO:0000269|PubMed:10572167,
CC ECO:0000269|PubMed:10606652, ECO:0000269|PubMed:23314747}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:23314747}.
CC -!- DISRUPTION PHENOTYPE: Leads to lethality.
CC {ECO:0000269|PubMed:16303567}.
CC -!- CAUTION: Was initially reported as a potential telomeric factor as it
CC harbors two helix-loop-helix dsDNA binding domains which are
CC recurrently found in telomeric proteins. However, teb1 was shown to
CC have higher affinity for the vertebrate telomere repeat, TTAGGG, than
CC to fission yeast telomere repeats in vitro.
CC {ECO:0000269|PubMed:10572167, ECO:0000269|PubMed:10606652}.
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DR EMBL; CU329670; CAA93598.1; -; Genomic_DNA.
DR EMBL; D89142; BAA13804.1; -; mRNA.
DR PIR; T37660; S67439.
DR RefSeq; NP_593712.1; NM_001019143.2.
DR AlphaFoldDB; Q10274; -.
DR BioGRID; 279267; 1.
DR STRING; 4896.SPAC13G7.10.1; -.
DR MaxQB; Q10274; -.
DR PaxDb; Q10274; -.
DR EnsemblFungi; SPAC13G7.10.1; SPAC13G7.10.1:pep; SPAC13G7.10.
DR GeneID; 2542820; -.
DR KEGG; spo:SPAC13G7.10; -.
DR PomBase; SPAC13G7.10; teb1.
DR VEuPathDB; FungiDB:SPAC13G7.10; -.
DR eggNOG; ENOG502S225; Eukaryota.
DR HOGENOM; CLU_708153_0_0_1; -.
DR InParanoid; Q10274; -.
DR OMA; CWTRISK; -.
DR PRO; PR:Q10274; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0003712; F:transcription coregulator activity; EXP:PomBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; EXP:PomBase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51294; HTH_MYB; 2.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..390
FT /note="Telobox protein 1"
FT /id="PRO_0000197147"
FT DOMAIN 50..109
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 135..193
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 78..105
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 162..189
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 30..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 312
FT /note="F -> V (in Ref. 2; BAA13804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43922 MW; 0718C86A44CA7DF1 CRC64;
MRSMKPPGFS SDLMDEHSVD LLNGSILAAE NPSKREVAQD VPGFERKPTK VRKPRVKWTE
KETNDLLRGC QIHGVGNWKK ILLDERFHFT NRSPNDLKDR FRTILPEDYK KFYPNAKTHM
GRPQKIPHTV GLSKSTRKER KQFTPEEDER LLEGFFLHGP CWTRISKDAN LGLQNRRSTD
LRDRFRNAFP ERYAAAGFKL KNNPGNRSKY YQNNMVNDAT TPNDSSTTEA AAAAVAAVAA
VAASNPNASP QQTTEQPASD ELLDWPHHNL PSQFFTSQRN PNYSTDSFLL GQSLSDPFNH
TLQSFHPYES LFSAGQPPSL PISPSTSQNS VQPFPFSIQQ PPLHLEPPLS SNTLNSSTLP
QPNSTDFNTF PPLPSTPRIS SEDIPWDNRG
