TBR1_MOUSE
ID TBR1_MOUSE Reviewed; 681 AA.
AC Q64336; Q7TSY9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=T-box brain protein 1;
DE Short=T-brain-1;
DE Short=TBR-1;
DE AltName: Full=TES-56;
GN Name=Tbr1;
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].
RC STRAIN=BALB/cJ; TISSUE=Fetal brain;
RX PubMed=7619531; DOI=10.1016/0896-6273(95)90065-9;
RA Bulfone A., Smiga S.M., Shimamura K., Peterson A., Puelles L.,
RA Rubenstein J.L.R.;
RT "T-brain-1: a homolog of Brachyury whose expression defines molecularly
RT distinct domains within the cerebral cortex.";
RL Neuron 15:63-78(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=9883721; DOI=10.1016/s0896-6273(00)80647-9;
RA Bulfone A., Wang F., Hevner R., Anderson S., Cutforth T., Chen S.,
RA Meneses J., Pedersen R., Axel R., Rubenstein J.L.;
RT "An olfactory sensory map develops in the absence of normal projection
RT neurons or GABAergic interneurons.";
RL Neuron 21:1273-1282(1998).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11239428; DOI=10.1016/s0896-6273(01)00211-2;
RA Hevner R.F., Shi L., Justice N., Hsueh Y., Sheng M., Smiga S., Bulfone A.,
RA Goffinet A.M., Campagnoni A.T., Rubenstein J.L.;
RT "Tbr1 regulates differentiation of the preplate and layer 6.";
RL Neuron 29:353-366(2001).
RN [7]
RP IDENTIFICATION IN COMPLEX WITH CASK AND TBR1.
RC STRAIN=C57BL/6J;
RX PubMed=15066269; DOI=10.1016/s0896-6273(04)00139-4;
RA Wang G.-S., Hong C.-J., Yen T.-Y., Huang H.-Y., Ou Y., Huang T.-N.,
RA Jung W.-G., Kuo T.-Y., Sheng M., Wang T.-F., Hsueh Y.-P.;
RT "Transcriptional modification by a CASK-interacting nucleosome assembly
RT protein.";
RL Neuron 42:113-128(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-408; SER-410; SER-594 AND
RP SER-640, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION.
RX PubMed=21285371; DOI=10.1073/pnas.1016723108;
RA Han W., Kwan K.Y., Shim S., Lam M.M., Shin Y., Xu X., Zhu Y., Li M.,
RA Sestan N.;
RT "TBR1 directly represses Fezf2 to control the laminar origin and
RT development of the corticospinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:3041-3046(2011).
CC -!- FUNCTION: Transcriptional repressor involved in multiple aspects of
CC cortical development, including neuronal migration, laminar and areal
CC identity, and axonal projection (PubMed:9883721, PubMed:11239428,
CC PubMed:21285371). As transcriptional repressor of FEZF2, it blocks the
CC formation of the corticospinal (CS) tract from layer 6 projection
CC neurons, thereby restricting the origin of CS axons specifically to
CC layer 5 neurons (PubMed:21285371). {ECO:0000269|PubMed:11239428,
CC ECO:0000269|PubMed:21285371, ECO:0000269|PubMed:9883721}.
CC -!- SUBUNIT: Homodimer (By similarity). Part of a complex containing CASK,
CC TBR1 and TSPYL2; may modulate gene expression in response to neuronal
CC synaptic activity (PubMed:15066269). Forms homodimers (By similarity).
CC Interacts with FOXP2 (By similarity). Interacts with FOXP1 (By
CC similarity). Interacts with BCL11A (By similarity).
CC {ECO:0000250|UniProtKB:Q16650, ECO:0000269|PubMed:15066269}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q16650}.
CC -!- TISSUE SPECIFICITY: Expressed in the developing and adult cortex
CC (PubMed:11239428). Expressed in the olfactory bulbs (PubMed:9883721).
CC {ECO:0000269|PubMed:11239428, ECO:0000269|PubMed:9883721}.
CC -!- DEVELOPMENTAL STAGE: First detected around day 10 of embryonic
CC development in the preplate, at day 12.5, in the cortical plate and
CC intermediate zone, and from day 16.5 to 18.5, in a rostro-caudal
CC gradient in the subplate. In the thalamus, expression is first observed
CC at postnatal stage, P7, and weak expression continues in later
CC postnatal and adult stages.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutant mice do not nurse and die
CC between postnatal days 1 and 3 (PubMed:9883721, PubMed:11239428).
CC Brains are smaller than those of heterozygous or wild-type littermates,
CC olfactory bulbs are small and olfactory bulb projection neurons are
CC absent (PubMed:9883721). Mutant mice show severe defects of cortical
CC development (PubMed:11239428). {ECO:0000269|PubMed:11239428,
CC ECO:0000269|PubMed:9883721}.
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DR EMBL; U49251; AAA92011.1; -; mRNA.
DR EMBL; AL845291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL26982.1; -; Genomic_DNA.
DR EMBL; BC052737; AAH52737.1; -; mRNA.
DR EMBL; BC058399; AAH58399.1; -; mRNA.
DR CCDS; CCDS16063.1; -.
DR RefSeq; NP_033348.2; NM_009322.3.
DR RefSeq; XP_006499161.1; XM_006499098.3.
DR AlphaFoldDB; Q64336; -.
DR SMR; Q64336; -.
DR STRING; 10090.ENSMUSP00000046787; -.
DR iPTMnet; Q64336; -.
DR PhosphoSitePlus; Q64336; -.
DR PaxDb; Q64336; -.
DR PRIDE; Q64336; -.
DR ProteomicsDB; 263012; -.
DR Antibodypedia; 35331; 201 antibodies from 32 providers.
DR DNASU; 21375; -.
DR Ensembl; ENSMUST00000048934; ENSMUSP00000046787; ENSMUSG00000035033.
DR GeneID; 21375; -.
DR KEGG; mmu:21375; -.
DR UCSC; uc008jvd.1; mouse.
DR CTD; 10716; -.
DR MGI; MGI:107404; Tbr1.
DR VEuPathDB; HostDB:ENSMUSG00000035033; -.
DR eggNOG; KOG3585; Eukaryota.
DR GeneTree; ENSGT00940000156994; -.
DR HOGENOM; CLU_014430_8_1_1; -.
DR InParanoid; Q64336; -.
DR OMA; NRALGYY; -.
DR OrthoDB; 374561at2759; -.
DR PhylomeDB; Q64336; -.
DR TreeFam; TF106341; -.
DR BioGRID-ORCS; 21375; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Tbr1; mouse.
DR PRO; PR:Q64336; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64336; protein.
DR Bgee; ENSMUSG00000035033; Expressed in cortical plate and 107 other tissues.
DR ExpressionAtlas; Q64336; baseline and differential.
DR Genevisible; Q64336; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IC:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0021764; P:amygdala development; IMP:MGI.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; IGI:MGI.
DR GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0016575; P:histone deacetylation; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1902667; P:regulation of axon guidance; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010092; P:specification of animal organ identity; IMP:MGI.
DR CDD; cd00182; TBOX; 1.
DR Gene3D; 2.60.40.820; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR032385; T-box_assoc.
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 Pfam; PF16176; T-box_assoc; 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..681
FT /note="T-box brain protein 1"
FT /id="PRO_0000184458"
FT DNA_BIND 213..393
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 43..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 53
FT /note="K -> E (in Ref. 1; AAA92011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 681 AA; 73940 MW; 6932EDE5412D97BF CRC64;
MQLEHCLSPS IMLSKKFLNV SSSYPHSGGS ELVLHDHPII STTDNLERSS PLKKITRGMT
NQSDTDNFPD SKDSPGDVQR SKLSPVLDGV SELRHSFDGS AADRYLLSQS SQPQSAATAP
SAMFPYPSQH GPAHPAFSIG SPSRYMAHHP VITNGAYNSL LSNSSPQGYP TAGYPYPQQY
GHSYQGAPFY QFSSTQPGLV PGKAQVYLCN RPLWLKFHRH QTEMIITKQG RRMFPFLSFN
ISGLDPTAHY NIFVDVILAD PNHWRFQGGK WVPCGKADTN VQGNRVYMHP DSPNTGAHWM
RQEISFGKLK LTNNKGASNN NGQMVVLQSL HKYQPRLHVV EVNEDGTEDT SQPGRVQTFT
FPETQFIAVT AYQNTDITQL KIDHNPFAKG FRDNYDTIYT GCDMDRLTPS PNDSPRSQIV
PGARYAMAGS FLQDQFVSNY AKARFHPGAG AGPGPGTDRS VPHTNGLLSP QQAEDPGAPS
PQRWFVTPAN NRLDFAASAY DTATDFAGNA ATLLSYAAAG VKALPLQAAG CTGRPLGYYA
DPSGWGARSP PQYCGAKSGS VLPCWPNSAA AAARMAGANP YLGEEAEGLA AERSPLAPAA
EDAKPKDLSD SSWIETPSSI KSIDSSDSGI YEQAKRRRIS PADTPVSESS SPLKSEVLAQ
RDCEKNCAKD IGGYYGFYSH S
