TBX15_MOUSE
ID TBX15_MOUSE Reviewed; 602 AA.
AC O70306; O54840; Q5GBG1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=T-box transcription factor TBX15;
DE Short=T-box protein 15;
DE AltName: Full=MmTBx8;
DE AltName: Full=T-box transcription factor TBX14;
DE Short=T-box protein 14;
GN Name=Tbx15; Synonyms=Tbx14, Tbx8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9693034; DOI=10.1006/geno.1998.5278;
RA Agulnik S.I., Papaioannou V.E., Silver L.M.;
RT "Cloning, mapping, and expression analysis of TBX15, a new member of the T-
RT Box gene family.";
RL Genomics 51:68-75(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=15652702; DOI=10.1016/j.mod.2004.10.011;
RA Singh M.K., Petry M., Haenig B., Lescher B., Leitges M., Kispert A.;
RT "The T-box transcription factor Tbx15 is required for skeletal
RT development.";
RL Mech. Dev. 122:131-144(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 44-602.
RX PubMed=9503012; DOI=10.1006/geno.1997.5150;
RA Wattler S., Russ A., Evans M., Nehls M.;
RT "A combined analysis of genomic and primary protein structure defines the
RT phylogenetic relationship of new members of the T-box family.";
RL Genomics 48:24-33(1998).
RN [6]
RP INTERACTION WITH TBX18.
RX PubMed=17584735; DOI=10.1074/jbc.m703724200;
RA Farin H.F., Bussen M., Schmidt M.K., Singh M.K., Schuster-Gossler K.,
RA Kispert A.;
RT "Transcriptional repression by the T-box proteins Tbx18 and Tbx15 depends
RT on Groucho corepressors.";
RL J. Biol. Chem. 282:25748-25759(2007).
CC -!- FUNCTION: Probable transcriptional regulator involved in the
CC development of the skeleton of the limb, vertebral column and head.
CC Acts by controlling the number of mesenchymal precursor cells and
CC chondrocytes.
CC -!- SUBUNIT: Can form a heterodimer with TBX18.
CC {ECO:0000269|PubMed:17584735}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
CC -!- DEVELOPMENTAL STAGE: Expressed during limb development, first in the
CC mesenchyme of the early limb bud, then during early endochondral bone
CC development in prehypertrophic chondrocytes of cartilaginous templates.
CC Expression is also found in mesenchymal precursor cells and
CC prehypertrophic chondrocytes, respectively, during development of
CC skeletal elements of the vertebral column and the head.
CC {ECO:0000269|PubMed:15652702}.
CC -!- DISRUPTION PHENOTYPE: Mice show a general reduction of bone size and
CC changes of bone shape. In the forelimb skeleton, the scapula lacks the
CC central region of the blade. Cartilaginous templates are already
CC reduced in size and show a transient delay in ossification in mutant
CC embryos. Mice show a significantly reduced proliferation of
CC prehypertrophic chondrocytes as well as of mesenchymal precursor cells.
CC {ECO:0000269|PubMed:15652702}.
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DR EMBL; AF041822; AAC32316.1; -; mRNA.
DR EMBL; AY662679; AAV80417.1; -; mRNA.
DR EMBL; AK132578; BAE21240.1; -; mRNA.
DR EMBL; AC080018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF013282; AAC40115.1; -; mRNA.
DR CCDS; CCDS17673.1; -.
DR RefSeq; NP_033349.2; NM_009323.2.
DR AlphaFoldDB; O70306; -.
DR SMR; O70306; -.
DR BioGRID; 203986; 1.
DR IntAct; O70306; 1.
DR STRING; 10090.ENSMUSP00000029462; -.
DR iPTMnet; O70306; -.
DR PhosphoSitePlus; O70306; -.
DR MaxQB; O70306; -.
DR PaxDb; O70306; -.
DR PRIDE; O70306; -.
DR ProteomicsDB; 263256; -.
DR Antibodypedia; 20199; 156 antibodies from 27 providers.
DR DNASU; 21384; -.
DR Ensembl; ENSMUST00000029462; ENSMUSP00000029462; ENSMUSG00000027868.
DR GeneID; 21384; -.
DR KEGG; mmu:21384; -.
DR UCSC; uc008qql.1; mouse.
DR CTD; 6913; -.
DR MGI; MGI:1277234; Tbx15.
DR VEuPathDB; HostDB:ENSMUSG00000027868; -.
DR eggNOG; KOG3586; Eukaryota.
DR GeneTree; ENSGT00940000159013; -.
DR HOGENOM; CLU_030727_0_0_1; -.
DR InParanoid; O70306; -.
DR OMA; QTANTCD; -.
DR OrthoDB; 828211at2759; -.
DR PhylomeDB; O70306; -.
DR TreeFam; TF106341; -.
DR BioGRID-ORCS; 21384; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Tbx15; mouse.
DR PRO; PR:O70306; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O70306; protein.
DR Bgee; ENSMUSG00000027868; Expressed in hindlimb stylopod muscle and 138 other tissues.
DR ExpressionAtlas; O70306; baseline and differential.
DR Genevisible; O70306; MM.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00182; TBOX; 1.
DR Gene3D; 2.60.40.820; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR046360; T-box_DNA-bd.
DR InterPro; IPR036960; T-box_sf.
DR InterPro; IPR001699; TF_T-box.
DR InterPro; IPR018186; TF_T-box_CS.
DR PANTHER; PTHR11267; PTHR11267; 1.
DR Pfam; PF00907; T-box; 1.
DR PRINTS; PR00937; TBOX.
DR SMART; SM00425; TBOX; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS01283; TBOX_1; 1.
DR PROSITE; PS01264; TBOX_2; 1.
DR PROSITE; PS50252; TBOX_3; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..602
FT /note="T-box transcription factor TBX15"
FT /id="PRO_0000184445"
FT DNA_BIND 122..304
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 43..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96SF7"
FT CONFLICT 100..102
FT /note="AGP -> RAT (in Ref. 1; AAC32316)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="R -> G (in Ref. 1; AAC32316)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 65802 MW; 8B476A8E61DA9223 CRC64;
MSERRRSAVA LSSRAHAFSV EALIGSNKKR KLRDWEEKGL DLSMEALSPA GPLGDTDDPA
THGLEPHPDS EQSTGSDSEV LTERTSCSFS THTDLASGAA GPVPAAMSSM EEIQVELQCA
DLWKRFHDIG TEMIITKAGR RMFPAMRVKI TGLDPHQQYY IAMDIVPVDN KRYRYVYHSS
KWMVAGNADS PVPPRVYIHP DSLASGDTWM RQVVSFDKLK LTNNELDDQG HIILHSMHKY
QPRVHVIRKD FSSDLSPTKP VPVGDGVKTF NFPETVFTTV TAYQNQQITR LKIDRNPFAK
GFRDSGRNRT GLEAIMETYA FWRPPVRTLT FEDFTTMQKQ QGGSTGTSPT TSSTGTPSPS
ASSHLLSPSC SPPTFHLAPN TFNVGCRESQ LCNLNLSDYP PCARSNMAAL QSYPGLSDSG
YNRLQSGTAS ATQPSETFMP QRTPSLISGI PTPPSLPSNS KMEAYGGQLG SFPTSQFQYV
MQAGNAASSS SSPHMFGGSH MQQSSYNAFS LHNPYNLYGY NFPTSPRLAA SPEKLSASQS
TLLCSSPSNG AFGERQYLPT GMEHSMHMIS PSTNNQQATN TCDGRQYGAV PGSASQMSVH
MV