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TBX2_MOUSE
ID   TBX2_MOUSE              Reviewed;         711 AA.
AC   Q60707; Q5SSP7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=T-box transcription factor TBX2;
DE            Short=T-box protein 2;
GN   Name=Tbx2;
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], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=7920656; DOI=10.1038/ng0794-383;
RA   Bollag R.J., Siegfried Z., Cebra-Thomas J.A., Garvey N., Davison E.M.,
RA   Silver L.M.;
RT   "An ancient family of embryonically expressed mouse genes sharing a
RT   conserved protein motif with the T locus.";
RL   Nat. Genet. 7:383-389(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10770922; DOI=10.1074/jbc.m000035200;
RA   Carreira S., Liu B., Goding C.R.;
RT   "The gene encoding the T-box Factor Tbx2 is a target for the
RT   microphthalmia-associated transcription factor in melanocytes.";
RL   J. Biol. Chem. 275:21920-21927(2000).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=8853987;
RX   DOI=10.1002/(sici)1097-0177(199608)206:4<379::aid-aja4>3.0.co;2-f;
RA   Chapman D.L., Garvey N., Hancock S., Alexiou M., Agulnik S.I.,
RA   Gibson-Brown J.J., Cebra-Thomas J., Bollag R.J., Silver L.M.,
RA   Papaioannou V.E.;
RT   "Expression of the T-box family genes, Tbx1-Tbx5, during early mouse
RT   development.";
RL   Dev. Dyn. 206:379-390(1996).
RN   [7]
RP   FUNCTION.
RX   PubMed=9710594; DOI=10.1128/mcb.18.9.5099;
RA   Carreira S., Dexter T.J., Yavuzer U., Easty D.J., Goding C.R.;
RT   "Brachyury-related transcription factor Tbx2 and repression of the
RT   melanocyte-specific TRP-1 promoter.";
RL   Mol. Cell. Biol. 18:5099-5108(1998).
RN   [8]
RP   FUNCTION.
RX   PubMed=11867218; DOI=10.1016/s0378-1119(01)00878-2;
RA   Paxton C., Zhao H., Chin Y., Langner K., Reecy J.;
RT   "Murine Tbx2 contains domains that activate and repress gene
RT   transcription.";
RL   Gene 283:117-124(2002).
RN   [9]
RP   FUNCTION.
RX   PubMed=12023302; DOI=10.1101/gad.222902;
RA   Habets P.E., Moorman A.F., Clout D.E., van Roon M.A., Lingbeek M.,
RA   van Lohuizen M., Campione M., Christoffels V.M.;
RT   "Cooperative action of Tbx2 and Nkx2.5 inhibits ANF expression in the
RT   atrioventricular canal: implications for cardiac chamber formation.";
RL   Genes Dev. 16:1234-1246(2002).
RN   [10]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=15459098; DOI=10.1242/dev.01378;
RA   Harrelson Z., Kelly R.G., Goldin S.N., Gibson-Brown J.J., Bollag R.J.,
RA   Silver L.M., Papaioannou V.E.;
RT   "Tbx2 is essential for patterning the atrioventricular canal and for
RT   morphogenesis of the outflow tract during heart development.";
RL   Development 131:5041-5052(2004).
RN   [11]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16222716; DOI=10.1002/dvdy.20575;
RA   Jerome-Majewska L.A., Jenkins G.P., Ernstoff E., Zindy F., Sherr C.J.,
RA   Papaioannou V.E.;
RT   "Tbx3, the ulnar-mammary syndrome gene, and Tbx2 interact in mammary gland
RT   development through a p19Arf/p53-independent pathway.";
RL   Dev. Dyn. 234:922-933(2005).
RN   [12]
RP   FUNCTION, MUTAGENESIS OF SER-336; SER-623 AND SER-675, AND PHOSPHORYLATION
RP   AT SER-336; SER-623 AND SER-675.
RX   PubMed=18025091; DOI=10.1074/jbc.m705651200;
RA   Abrahams A., Mowla S., Parker M.I., Goding C.R., Prince S.;
RT   "UV-mediated regulation of the anti-senescence factor Tbx2.";
RL   J. Biol. Chem. 283:2223-2230(2008).
RN   [13]
RP   FUNCTION.
RX   PubMed=22186728; DOI=10.1242/dev.067058;
RA   Sakabe M., Kokubo H., Nakajima Y., Saga Y.;
RT   "Ectopic retinoic acid signaling affects outflow tract cushion development
RT   through suppression of the myocardial Tbx2-Tgfbeta2 pathway.";
RL   Development 139:385-395(2012).
RN   [14]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=26486273; DOI=10.1111/cpr.12227;
RA   Pan L., Ma X., Wen B., Su Z., Zheng X., Liu Y., Li H., Chen Y., Wang J.,
RA   Lu F., Qu J., Hou L.;
RT   "Microphthalmia-associated transcription factor/T-box factor-2 axis acts
RT   through Cyclin D1 to regulate melanocyte proliferation.";
RL   Cell Prolif. 48:631-642(2015).
RN   [15]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27720610; DOI=10.1016/j.devcel.2016.08.007;
RA   Luedtke T.H., Rudat C., Wojahn I., Weiss A.C., Kleppa M.J., Kurz J.,
RA   Farin H.F., Moon A., Christoffels V.M., Kispert A.;
RT   "Tbx2 and Tbx3 Act Downstream of Shh to Maintain Canonical Wnt Signaling
RT   during Branching Morphogenesis of the Murine Lung.";
RL   Dev. Cell 39:239-253(2016).
RN   [16]
RP   FUNCTION.
RX   PubMed=26971330; DOI=10.1007/s11010-016-2680-7;
RA   Chen Y., Pan L., Su Z., Wang J., Li H., Ma X., Liu Y., Lu F., Qu J.,
RA   Hou L.;
RT   "The transcription factor TBX2 regulates melanogenesis in melanocytes by
RT   repressing Oca2.";
RL   Mol. Cell. Biochem. 415:103-109(2016).
RN   [17]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=28910203; DOI=10.1080/02713683.2017.1338351;
RA   Wang J., Liu Y., Su Z., Pan L., Lu F., Qu J., Hou L.;
RT   "The T-Box Transcription Factor TBX2 Regulates Cell Proliferation in the
RT   Retinal Pigment Epithelium.";
RL   Curr. Eye Res. 42:1537-1544(2017).
RN   [18]
RP   FUNCTION, AND MUTAGENESIS OF 132-ARG-ARG-133.
RX   PubMed=30599067; DOI=10.1007/s00018-018-2998-2;
RA   Reinhardt S., Schuck F., Stoye N., Hartmann T., Grimm M.O.W.,
RA   Pflugfelder G., Endres K.;
RT   "Transcriptional repression of the ectodomain sheddase ADAM10 by TBX2 and
RT   potential implication for Alzheimer's disease.";
RL   Cell. Mol. Life Sci. 76:1005-1025(2019).
RN   [19]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=33795231; DOI=10.1242/dev.195651;
RA   Kaiser M., Wojahn I., Rudat C., Luedtke T.H., Christoffels V.M., Moon A.,
RA   Kispert A., Trowe M.O.;
RT   "Regulation of otocyst patterning by Tbx2 and Tbx3 is required for inner
RT   ear morphogenesis in the mouse.";
RL   Development 148:0-0(2021).
RN   [20]
RP   FUNCTION, INTERACTION WITH CHD4; HDAC1; HDAC2; CBX3; HMGB2 AND PBX1,
RP   SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=33731112; DOI=10.1186/s12931-021-01679-y;
RA   Luedtke T.H., Wojahn I., Kleppa M.J., Schierstaedt J., Christoffels V.M.,
RA   Kuenzler P., Kispert A.;
RT   "Combined genomic and proteomic approaches reveal DNA binding sites and
RT   interaction partners of TBX2 in the developing lung.";
RL   Respir. Res. 22:85-85(2021).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; SER-342 AND SER-360, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Lung;
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).
CC   -!- FUNCTION: Transcription factor which acts as a transcriptional
CC       repressor (PubMed:22186728, PubMed:11867218, PubMed:18025091,
CC       PubMed:12023302). May also function as a transcriptional activator
CC       (PubMed:26486273, PubMed:22186728, PubMed:11867218). Binds to the
CC       palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-
CC       site, which are present in the regulatory region of several genes
CC       (PubMed:9710594, PubMed:26971330, PubMed:12023302, PubMed:33731112,
CC       PubMed:27720610). Required for cardiac atrioventricular canal formation
CC       (PubMed:15459098). May cooperate with NKX2.5 to negatively modulate
CC       expression of NPPA/ANF in the atrioventricular canal (PubMed:12023302).
CC       May play a role as a positive regulator of TGFB2 expression, perhaps
CC       acting in concert with GATA4 in the developing outflow tract myocardium
CC       (PubMed:22186728). Plays a role in limb pattern formation
CC       (PubMed:15459098). Acts as a transcriptional repressor of ADAM10 gene
CC       expression, perhaps in concert with histone deacetylase HDAC1 as
CC       cofactor (PubMed:30599067). Involved in branching morphogenesis in both
CC       developing lungs and adult mammary glands, via negative modulation of
CC       target genes; acting redundantly with TBX3 (PubMed:27720610,
CC       PubMed:16222716). Required, together with TBX3, to maintain cell
CC       proliferation in the embryonic lung mesenchyme; perhaps acting
CC       downstream of SHH, BMP and TGFbeta signaling (PubMed:27720610).
CC       Involved in modulating early inner ear development, acting
CC       independently of, and also redundantly with TBX3, in different
CC       subregions of the developing ear (PubMed:33795231). Acts as a negative
CC       regulator of PML function in cellular senescence (By similarity). Acts
CC       as a negative regulator of expression of CDKN1A/p21, IL33 and CCN4;
CC       repression of CDKN1A is enhanced in response to UV-induced stress,
CC       perhaps as a result of phosphorylation by p38 MAPK (PubMed:18025091,
CC       PubMed:33731112). Negatively modulates expression of CDKN2A/p19ARF and
CC       CDH1/E-cadherin (By similarity). Plays a role in induction of the
CC       epithelial-mesenchymal transition (EMT) (By similarity). Plays a role
CC       in melanocyte proliferation, perhaps via regulation of cyclin CCND1
CC       (PubMed:26486273). Involved in melanogenesis, acting via negative
CC       modulation of expression of DHICA oxidase/TYRP1 and P protein/OCA2
CC       (PubMed:26971330, PubMed:9710594). Involved in regulating retinal
CC       pigment epithelium (RPE) cell proliferation, perhaps via negatively
CC       modulating transcription of the transcription factor CEBPD
CC       (PubMed:28910203). {ECO:0000250|UniProtKB:Q13207,
CC       ECO:0000269|PubMed:11867218, ECO:0000269|PubMed:12023302,
CC       ECO:0000269|PubMed:15459098, ECO:0000269|PubMed:16222716,
CC       ECO:0000269|PubMed:18025091, ECO:0000269|PubMed:22186728,
CC       ECO:0000269|PubMed:26486273, ECO:0000269|PubMed:26971330,
CC       ECO:0000269|PubMed:27720610, ECO:0000269|PubMed:28910203,
CC       ECO:0000269|PubMed:30599067, ECO:0000269|PubMed:33731112,
CC       ECO:0000269|PubMed:33795231, ECO:0000269|PubMed:9710594}.
CC   -!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with CHD4,
CC       HDAC1 and HDAC2, perhaps as components of a NuRD-like complex
CC       (PubMed:33731112). Interacts with CBX3, HMGB2 and PBX1
CC       (PubMed:33731112). Interacts with PML (By similarity).
CC       {ECO:0000250|UniProtKB:Q13207, ECO:0000269|PubMed:33731112}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26486273,
CC       ECO:0000269|PubMed:33731112}.
CC   -!- TISSUE SPECIFICITY: In adults, highest levels in lung. Also found in
CC       heart, kidney, and ovary.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the otic placode at 8.5 dpc (at
CC       protein level) (PubMed:33795231). Between 10.5-12.0 dpc, expressed in
CC       various regions of the developing ear, including the cochlear duct,
CC       endolymphatic duct and the vestibule, but not in the region which gives
CC       rise to the posterior and anterior semicircular canals (at protein
CC       level) (PubMed:33795231). Expressed at 8.5 dpc in the cardiac crescent,
CC       the atrium and the inflow tract (IFT) (PubMed:15459098). Expressed at
CC       9.5 dpc in the otic and optic vesicles, facial region, septum
CC       transversum, bilateral nephrogenic mesodermal cords, ventral body wall
CC       mesoderm caudal to the forelimbs, pharyngeal arch mesenchyme that
CC       contains neural crest cells, including those migrating into the outflow
CC       tract (OFT), septum OFT, inner curvature, atrioventricular canal (AVC)
CC       and IFT of the heart (PubMed:7920656, PubMed:8853987, PubMed:15459098,
CC       PubMed:33795231). Expressed in a continuous stripe of mesenchyme in the
CC       ventro-lateral body wall between the fore and hind limb buds at day
CC       10.5-11.5 dpc (PubMed:16222716). At 12.5 dpc, expressed in the
CC       trigeminal ganglia, facial regions, retina and limb bud mesenchyme
CC       (PubMed:8853987). In later stages, found in ear pinnae, the milk line,
CC       lung mesenchyme, body wall, genital ridge and developing nervous system
CC       (PubMed:8853987, PubMed:33731112). Expressed in proliferating retinal
CC       pigment epithelium (RPE) cells at 14.5 dpc, and continues after birth,
CC       but diminishes by postnatal day 90 (PubMed:28910203). Expressed in
CC       melanocytes of postnatal day 3 hair follicles (PubMed:26486273).
CC       {ECO:0000269|PubMed:15459098, ECO:0000269|PubMed:16222716,
CC       ECO:0000269|PubMed:26486273, ECO:0000269|PubMed:28910203,
CC       ECO:0000269|PubMed:33731112, ECO:0000269|PubMed:33795231,
CC       ECO:0000269|PubMed:7920656, ECO:0000269|PubMed:8853987}.
CC   -!- DOMAIN: Repression domain 1 (RD1) is involved in transcriptional
CC       repression (By similarity). RD1 is necessary for its interaction with
CC       PML (By similarity). {ECO:0000250|UniProtKB:Q13207}.
CC   -!- PTM: Phosphorylated (PubMed:18025091). May be phosphorylated by p38
CC       MAPK in response to UV irradiation stress (PubMed:18025091).
CC       {ECO:0000269|PubMed:18025091}.
CC   -!- DISRUPTION PHENOTYPE: Knockouts do not survive beyond embryonic 14.5
CC       dpc (PubMed:15459098). Abnormal atrioventricular morphology at 9.5-10.5
CC       dpc and outflow tract (OFT) septation defects in those surviving to
CC       12.5 dpc (PubMed:15459098). Hindlimb digit duplication at 14.5 dpc
CC       (PubMed:15459098). Increased expression of CDKN1A, FRZB, IL33, SHISA3,
CC       and CCN4/WISP1 in lung mesenchyme between 12.5-14.5 dpc
CC       (PubMed:33731112). Conditional knockdown targeted mainly to lung
CC       mesenchyme causes lung hypoplasia at 18.5 dpc (PubMed:27720610).
CC       Conditional knockdown targeted mainly to the otic epithelium disrupts
CC       inner ear morphogenesis, which is exacerbated by simultaneous
CC       conditional knockdown of TBX3 (PubMed:33795231). Simultaneous
CC       conditional knockdown of TBX2 and TBX3 targeted mainly to lung
CC       mesenchyme causes severe bleeding from 10.5 dpc and embryos die shortly
CC       thereafter, perhaps as a result of knockdown in the developing heart
CC       (PubMed:27720610). {ECO:0000269|PubMed:15459098,
CC       ECO:0000269|PubMed:27720610, ECO:0000269|PubMed:33731112,
CC       ECO:0000269|PubMed:33795231}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52697.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U15566; AAC52697.1; ALT_FRAME; mRNA.
DR   EMBL; AF244917; AAF90050.1; -; Genomic_DNA.
DR   EMBL; AL596324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466556; EDL15775.1; -; Genomic_DNA.
DR   EMBL; BC156393; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS36266.1; -.
DR   PIR; S46458; S46458.
DR   RefSeq; NP_033350.2; NM_009324.2.
DR   AlphaFoldDB; Q60707; -.
DR   SMR; Q60707; -.
DR   BioGRID; 203987; 15.
DR   STRING; 10090.ENSMUSP00000000095; -.
DR   iPTMnet; Q60707; -.
DR   PhosphoSitePlus; Q60707; -.
DR   MaxQB; Q60707; -.
DR   PaxDb; Q60707; -.
DR   PRIDE; Q60707; -.
DR   ProteomicsDB; 263016; -.
DR   Antibodypedia; 1779; 326 antibodies from 36 providers.
DR   DNASU; 21385; -.
DR   Ensembl; ENSMUST00000000095; ENSMUSP00000000095; ENSMUSG00000000093.
DR   GeneID; 21385; -.
DR   KEGG; mmu:21385; -.
DR   UCSC; uc007ksb.1; mouse.
DR   CTD; 6909; -.
DR   MGI; MGI:98494; Tbx2.
DR   VEuPathDB; HostDB:ENSMUSG00000000093; -.
DR   eggNOG; KOG3585; Eukaryota.
DR   GeneTree; ENSGT00940000158439; -.
DR   HOGENOM; CLU_023038_1_0_1; -.
DR   InParanoid; Q60707; -.
DR   OMA; HQDERCT; -.
DR   OrthoDB; 301173at2759; -.
DR   PhylomeDB; Q60707; -.
DR   TreeFam; TF106341; -.
DR   BioGRID-ORCS; 21385; 4 hits in 74 CRISPR screens.
DR   PRO; PR:Q60707; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q60707; protein.
DR   Bgee; ENSMUSG00000000093; Expressed in urothelium of ureter and 213 other tissues.
DR   Genevisible; Q60707; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
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:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0035909; P:aorta morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR   GO; GO:0036302; P:atrioventricular canal development; IMP:BHF-UCL.
DR   GO; GO:1905222; P:atrioventricular canal morphogenesis; IGI:BHF-UCL.
DR   GO; GO:1905072; P:cardiac jelly development; ISO:MGI.
DR   GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IDA:BHF-UCL.
DR   GO; GO:0048738; P:cardiac muscle tissue development; IMP:MGI.
DR   GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR   GO; GO:0090398; P:cellular senescence; IDA:MGI.
DR   GO; GO:0090103; P:cochlea morphogenesis; IMP:UniProtKB.
DR   GO; GO:0060560; P:developmental growth involved in morphogenesis; IMP:MGI.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0035050; P:embryonic heart tube development; ISS:UniProtKB.
DR   GO; GO:0003272; P:endocardial cushion formation; ISO:MGI.
DR   GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IGI:UniProtKB.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0060596; P:mammary placode formation; IGI:MGI.
DR   GO; GO:0097325; P:melanocyte proliferation; IMP:UniProtKB.
DR   GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IMP:UniProtKB.
DR   GO; GO:0007521; P:muscle cell fate determination; IMP:MGI.
DR   GO; GO:1901211; P:negative regulation of cardiac chamber formation; IMP:BHF-UCL.
DR   GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
DR   GO; GO:1901208; P:negative regulation of heart looping; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IMP:UniProtKB.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0060465; P:pharynx development; IMP:BHF-UCL.
DR   GO; GO:0043474; P:pigment metabolic process involved in pigmentation; IMP:UniProtKB.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
DR   GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0008016; P:regulation of heart contraction; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:UniProtKB.
DR   GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IGI:MGI.
DR   GO; GO:0072105; P:ureteric peristalsis; IGI:MGI.
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; IPR022582; TBX2/3_TAD.
DR   InterPro; IPR002070; TF_Brachyury.
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; PF12598; TBX; 1.
DR   PRINTS; PR00938; BRACHYURY.
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   Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..711
FT                   /note="T-box transcription factor TBX2"
FT                   /id="PRO_0000184427"
FT   DNA_BIND        109..287
FT                   /note="T-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT   REGION          313..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..602
FT                   /note="Repression domain 1 (RD1)"
FT                   /evidence="ECO:0000250"
FT   REGION          640..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..341
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..443
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18025091,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         360
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         623
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18025091"
FT   MOD_RES         652
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13207"
FT   MOD_RES         656
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13207"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18025091"
FT   MUTAGEN         132..133
FT                   /note="RR->EE: Attenuated repression of Adam10
FT                   transcription."
FT                   /evidence="ECO:0000269|PubMed:30599067"
FT   MUTAGEN         336
FT                   /note="S->A: Abolishes phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:18025091"
FT   MUTAGEN         623
FT                   /note="S->A: Abolishes phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:18025091"
FT   MUTAGEN         675
FT                   /note="S->A: Abolishes phosphorylation."
FT                   /evidence="ECO:0000269|PubMed:18025091"
FT   CONFLICT        377
FT                   /note="G -> C (in Ref. 1; AAC52697 and 2; AAF90050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        486
FT                   /note="G -> C (in Ref. 1; AAC52697 and 2; AAF90050)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        689
FT                   /note="S -> R (in Ref. 1; AAC52697 and 2; AAF90050)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   711 AA;  75081 MW;  1C38BF1D25E1FF60 CRC64;
     MREPALAASA MAYHPFHAPR PADFPMSAFL AAAQPSFFPA LALPPGALGK PLPDPGLAGA
     AAAAAAAAAA AEAGLHVSAL GPHPPAAHLR SLKSLEPEDE VEDDPKVTLE AKELWDQFHK
     LGTEMVITKS GRRMFPPFKV RVSGLDKKAK YILLMDIVAA DDCRYKFHNS RWMVAGKADP
     EMPKRMYIHP DSPATGEQWM AKPVAFHKLK LTNNISDKHG FTILNSMHKY QPRFHIVRAN
     DILKLPYSTF RTYVFPETDF IAVTAYQNDK ITQLKIDNNP FAKGFRDTGN GRREKRKQLT
     LPTLRLYEEH CKPERDGAES DASSCDPPPA REPPPSPSAA PSPLRLHRAR AEEKPGAADS
     DPEPERTGEE RSAAPLGRSP SRDASPARLT EPERSRERRS PERCSKEPTE GGGDGPFSLR
     SLEKERPEAR RKDEGRKDVG EGKEPSLAPL VVQTDSASPL GAGHLPGLAF SSHLHGQQFF
     GPLGAGQPLF LHPGQFAMGP GAFSAMGMGH LLASVAGGSG SSGGAGPGTA AGLDAGGLGP
     AASAASTAAP FPFHLSQHML ASQGIPMPTF GGLFPYPYTY MAAAAAAASA LPATSAAAAA
     AAAAGSLSRS PFLGSARPRL RFSPYQIPVT IPPSTSLLTT GLAAEGSKGG NSREPSPLPE
     LALRKVGGPS RGALSPSGSA KEAASELQSI QRLVSGLESQ RALSPGRESP K
 
 
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