TBX2_HUMAN
ID TBX2_HUMAN Reviewed; 712 AA.
AC Q13207; Q16424; Q7Z647;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=T-box transcription factor TBX2;
DE Short=T-box protein 2;
GN Name=TBX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal kidney;
RX PubMed=8530034; DOI=10.1006/geno.1995.1139;
RA Campbell C., Goodrich K., Casey G., Beatty B.;
RT "Cloning and mapping of a human gene (TBX2) sharing a highly conserved
RT protein motif with the Drosophila omb gene.";
RL Genomics 28:255-260(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-255.
RC TISSUE=Fetal kidney;
RX PubMed=8597636; DOI=10.1007/bf00539006;
RA Law D.J., Gebuhr T., Garvey N., Agulnik S.I., Silver L.M.;
RT "Identification, characterization, and localization to chromosome 17q21-22
RT of the human TBX2 homolog, member of a conserved developmental gene
RT family.";
RL Mamm. Genome 6:793-797(1995).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-132.
RX PubMed=11111039; DOI=10.1016/s0378-1119(00)00417-0;
RA Sinha S., Abraham S., Gronostajski R.M., Campbell C.E.;
RT "Differential DNA binding and transcription modulation by three T-box
RT proteins, T, TBX1 and TBX2.";
RL Gene 258:15-29(2000).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=11062467; DOI=10.1038/81583;
RA Jacobs J.J., Keblusek P., Robanus-Maandag E., Kristel P., Lingbeek M.,
RA Nederlof P.M., van Welsem T., van de Vijver M.J., Koh E.Y., Daley G.Q.,
RA van Lohuizen M.;
RT "Senescence bypass screen identifies TBX2, which represses Cdkn2a
RT (p19(ARF)) and is amplified in a subset of human breast cancers.";
RL Nat. Genet. 26:291-299(2000).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF ARG-132; ARG-133 AND ALA-282.
RX PubMed=12000749; DOI=10.1074/jbc.m200403200;
RA Lingbeek M.E., Jacobs J.J., van Lohuizen M.;
RT "The T-box repressors TBX2 and TBX3 specifically regulate the tumor
RT suppressor gene p14ARF via a variant T-site in the initiator.";
RL J. Biol. Chem. 277:26120-26127(2002).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=21403123; DOI=10.1161/circulationaha.110.980607;
RA Sizarov A., Ya J., de Boer B.A., Lamers W.H., Christoffels V.M.,
RA Moorman A.F.;
RT "Formation of the building plan of the human heart: morphogenesis, growth,
RT and differentiation.";
RL Circulation 123:1125-1135(2011).
RN [9]
RP FUNCTION, INTERACTION WITH PML, AND DOMAIN RD1.
RX PubMed=22002537; DOI=10.1038/emboj.2011.370;
RA Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M.,
RA Dejean A., Bischof O.;
RT "Physical and functional interaction between PML and TBX2 in the
RT establishment of cellular senescence.";
RL EMBO J. 31:95-109(2012).
RN [10]
RP FUNCTION.
RX PubMed=22844464; DOI=10.1371/journal.pone.0041355;
RA Wang B., Lindley L.E., Fernandez-Vega V., Rieger M.E., Sims A.H.,
RA Briegel K.J.;
RT "The T box transcription factor TBX2 promotes epithelial-mesenchymal
RT transition and invasion of normal and malignant breast epithelial cells.";
RL PLoS ONE 7:e41355-e41355(2012).
RN [11]
RP FUNCTION.
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 [12]
RP FUNCTION, AND DOMAIN.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653 AND SER-657, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN VETD, VARIANTS VETD GLN-20
RP AND HIS-305, AND CHARACTERIZATION OF VARIANTS VETD GLN-20 AND HIS-305.
RX PubMed=29726930; DOI=10.1093/hmg/ddy146;
RG Undiagnosed Diseases Network (UDN);
RA Liu N., Schoch K., Luo X., Pena L.D.M., Bhavana V.H., Kukolich M.K.,
RA Stringer S., Powis Z., Radtke K., Mroske C., Deak K.L., McDonald M.T.,
RA McConkie-Rosell A., Markert M.L., Kranz P.G., Stong N., Need A.C., Bick D.,
RA Amaral M.D., Worthey E.A., Levy S., Wangler M.F., Bellen H.J., Shashi V.,
RA Yamamoto S.;
RT "Functional variants in TBX2 are associated with a syndromic cardiovascular
RT and skeletal developmental disorder.";
RL Hum. Mol. Genet. 27:2454-2465(2018).
CC -!- FUNCTION: Transcription factor which acts as a transcriptional
CC repressor (PubMed:11111039, PubMed:11062467, PubMed:12000749,
CC PubMed:22844464, PubMed:30599067). May also function as a
CC transcriptional activator (By similarity). Binds to the palindromic T
CC site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are
CC present in the regulatory region of several genes (PubMed:11111039,
CC PubMed:12000749, PubMed:22844464, PubMed:30599067). Required for
CC cardiac atrioventricular canal formation (PubMed:29726930). May
CC cooperate with NKX2.5 to negatively modulate expression of NPPA/ANF in
CC the atrioventricular canal (By similarity). May play a role as a
CC positive regulator of TGFB2 expression, perhaps acting in concert with
CC GATA4 in the developing outflow tract myocardium (By similarity). Plays
CC a role in limb pattern formation (PubMed:29726930). Acts as a
CC transcriptional repressor of ADAM10 gene expression, perhaps in concert
CC with histone deacetylase HDAC1 as cofactor (PubMed:30599067). Involved
CC in branching morphogenesis in both developing lungs and adult mammary
CC glands, via negative modulation of target genes; acting redundantly
CC with TBX3 (By similarity). Required, together with TBX3, to maintain
CC cell proliferation in the embryonic lung mesenchyme; perhaps acting
CC downstream of SHH, BMP and TGFbeta signaling (By similarity). Involved
CC in modulating early inner ear development, acting independently of, and
CC also redundantly with TBX3, in different subregions of the developing
CC ear (By similarity). Acts as a negative regulator of PML function in
CC cellular senescence (PubMed:22002537). Acts as a negative regulator of
CC expression of CDKN1A/p21, IL33 and CCN4; repression of CDKN1A is
CC enhanced in response to UV-induced stress, perhaps as a result of
CC phosphorylation by p38 MAPK (By similarity). Negatively modulates
CC expression of CDKN2A/p14ARF and CDH1/E-cadherin (PubMed:11062467,
CC PubMed:12000749, PubMed:22844464). Plays a role in induction of the
CC epithelial-mesenchymal transition (EMT) (PubMed:22844464). Plays a role
CC in melanocyte proliferation, perhaps via regulation of cyclin CCND1 (By
CC similarity). Involved in melanogenesis, acting via negative modulation
CC of expression of DHICA oxidase/TYRP1 and P protein/OCA2 (By
CC similarity). Involved in regulating retinal pigment epithelium (RPE)
CC cell proliferation, perhaps via negatively modulating transcription of
CC the transcription factor CEBPD (PubMed:28910203).
CC {ECO:0000250|UniProtKB:Q60707, ECO:0000269|PubMed:11062467,
CC ECO:0000269|PubMed:11111039, ECO:0000269|PubMed:12000749,
CC ECO:0000269|PubMed:22002537, ECO:0000269|PubMed:22844464,
CC ECO:0000269|PubMed:28910203, ECO:0000269|PubMed:29726930,
CC ECO:0000269|PubMed:30599067}.
CC -!- SUBUNIT: Binds DNA as a monomer (PubMed:11111039). Interacts with PML
CC (isoform PML-2, isoform PML-3 and isoform PML-4) (PubMed:22002537).
CC {ECO:0000269|PubMed:11111039, ECO:0000269|PubMed:22002537}.
CC -!- INTERACTION:
CC Q13207; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-2853051, EBI-8624731;
CC Q13207; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-2853051, EBI-7062247;
CC Q13207; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-2853051, EBI-743033;
CC Q13207; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2853051, EBI-3867333;
CC Q13207; P25791-3: LMO2; NbExp=3; IntAct=EBI-2853051, EBI-11959475;
CC Q13207; O14770-4: MEIS2; NbExp=3; IntAct=EBI-2853051, EBI-8025850;
CC Q13207; P29590: PML; NbExp=2; IntAct=EBI-2853051, EBI-295890;
CC Q13207; O14787-2: TNPO2; NbExp=3; IntAct=EBI-2853051, EBI-12076664;
CC Q13207; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-2853051, EBI-948354;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29726930,
CC ECO:0000305|PubMed:11111039}.
CC -!- TISSUE SPECIFICITY: Expressed primarily in adult in kidney, lung, and
CC placenta. Weak expression in heart and ovary.
CC -!- DEVELOPMENTAL STAGE: Expressed in the outflow tract and the
CC atrioventricular canal at embryonic stage 12 and gradually reduced by
CC stage 16 (at protein level). {ECO:0000269|PubMed:21403123}.
CC -!- DOMAIN: Repression domain 1 (RD1) is involved in transcriptional
CC repression (PubMed:11062467, PubMed:30599067). RD1 is necessary for its
CC interaction with PML (PubMed:22002537). {ECO:0000269|PubMed:11062467,
CC ECO:0000269|PubMed:22002537, ECO:0000269|PubMed:30599067}.
CC -!- DISEASE: Vertebral anomalies and variable endocrine and T-cell
CC dysfunction (VETD) [MIM:618223]: An autosomal dominant syndrome
CC characterized by skeletal malformations primarily involving the
CC vertebrae, immunodeficiency, endocrine abnormalities such as
CC hypoparathyroidism and growth hormone deficiency, craniofacial
CC dysmorphism, congenital cardiac anomalies consisting of double-outlet
CC right ventricle, pulmonary valve stenosis and atrial septal defect, and
CC developmental impairments. {ECO:0000269|PubMed:29726930}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA73861.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH52566.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TBX2ID42485ch17q23.html";
CC -!- WEB RESOURCE: Name=Undiagnosed Disease Network; Note=TBX2;
CC URL="https://undiagnosed.hms.harvard.edu/updates/genes-of-interest/tbx2-gene/";
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DR EMBL; U28049; AAA73861.1; ALT_FRAME; mRNA.
DR EMBL; AC005746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052566; AAH52566.1; ALT_INIT; mRNA.
DR EMBL; S81264; AAB36216.1; -; mRNA.
DR CCDS; CCDS11627.2; -.
DR PIR; G01840; G01840.
DR RefSeq; NP_005985.3; NM_005994.3.
DR AlphaFoldDB; Q13207; -.
DR SMR; Q13207; -.
DR BioGRID; 112772; 21.
DR IntAct; Q13207; 16.
DR MINT; Q13207; -.
DR STRING; 9606.ENSP00000240328; -.
DR GlyGen; Q13207; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q13207; -.
DR PhosphoSitePlus; Q13207; -.
DR BioMuta; TBX2; -.
DR DMDM; 294862490; -.
DR jPOST; Q13207; -.
DR MassIVE; Q13207; -.
DR MaxQB; Q13207; -.
DR PaxDb; Q13207; -.
DR PeptideAtlas; Q13207; -.
DR PRIDE; Q13207; -.
DR ProteomicsDB; 59225; -.
DR Antibodypedia; 1779; 326 antibodies from 36 providers.
DR DNASU; 6909; -.
DR Ensembl; ENST00000240328.4; ENSP00000240328.3; ENSG00000121068.14.
DR GeneID; 6909; -.
DR KEGG; hsa:6909; -.
DR MANE-Select; ENST00000240328.4; ENSP00000240328.3; NM_005994.4; NP_005985.3.
DR UCSC; uc010wox.3; human.
DR CTD; 6909; -.
DR DisGeNET; 6909; -.
DR GeneCards; TBX2; -.
DR HGNC; HGNC:11597; TBX2.
DR HPA; ENSG00000121068; Tissue enhanced (lung).
DR MalaCards; TBX2; -.
DR MIM; 600747; gene.
DR MIM; 618223; phenotype.
DR neXtProt; NX_Q13207; -.
DR OpenTargets; ENSG00000121068; -.
DR PharmGKB; PA36360; -.
DR VEuPathDB; HostDB:ENSG00000121068; -.
DR eggNOG; KOG3585; Eukaryota.
DR GeneTree; ENSGT00940000158439; -.
DR HOGENOM; CLU_023038_1_0_1; -.
DR InParanoid; Q13207; -.
DR OMA; HQDERCT; -.
DR OrthoDB; 301173at2759; -.
DR PhylomeDB; Q13207; -.
DR TreeFam; TF106341; -.
DR PathwayCommons; Q13207; -.
DR SignaLink; Q13207; -.
DR SIGNOR; Q13207; -.
DR BioGRID-ORCS; 6909; 27 hits in 1096 CRISPR screens.
DR ChiTaRS; TBX2; human.
DR GeneWiki; TBX2; -.
DR GenomeRNAi; 6909; -.
DR Pharos; Q13207; Tbio.
DR PRO; PR:Q13207; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q13207; protein.
DR Bgee; ENSG00000121068; Expressed in right lung and 166 other tissues.
DR ExpressionAtlas; Q13207; baseline and differential.
DR Genevisible; Q13207; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0035909; P:aorta morphogenesis; ISS:BHF-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:0036302; P:atrioventricular canal development; ISS:BHF-UCL.
DR GO; GO:1905222; P:atrioventricular canal morphogenesis; ISS:BHF-UCL.
DR GO; GO:1905072; P:cardiac jelly development; IMP:BHF-UCL.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IEA:Ensembl.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISS:BHF-UCL.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0090398; P:cellular senescence; IDA:UniProtKB.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0060560; P:developmental growth involved in morphogenesis; IEA:Ensembl.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; ISS:BHF-UCL.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISS:BHF-UCL.
DR GO; GO:0035050; P:embryonic heart tube development; ISS:UniProtKB.
DR GO; GO:0003272; P:endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; ISS:UniProtKB.
DR GO; GO:0060596; P:mammary placode formation; IEA:Ensembl.
DR GO; GO:0097325; P:melanocyte proliferation; IEA:Ensembl.
DR GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IEA:Ensembl.
DR GO; GO:0007521; P:muscle cell fate determination; ISS:BHF-UCL.
DR GO; GO:1901211; P:negative regulation of cardiac chamber formation; ISS:BHF-UCL.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IDA:UniProtKB.
DR GO; GO:1901208; P:negative regulation of heart looping; ISS: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:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060465; P:pharynx development; ISS:BHF-UCL.
DR GO; GO:0043474; P:pigment metabolic process involved in pigmentation; IEA:Ensembl.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0008016; P:regulation of heart contraction; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0072105; P:ureteric peristalsis; IEA:Ensembl.
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; Disease variant; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..712
FT /note="T-box transcription factor TBX2"
FT /id="PRO_0000184426"
FT DNA_BIND 109..287
FT /note="T-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 313..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..601
FT /note="Repression domain 1 (RD1)"
FT /evidence="ECO:0000269|PubMed:11062467,
FT ECO:0000269|PubMed:30599067"
FT REGION 637..687
FT /note="Disordered"
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 390..410
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:0000250|UniProtKB:Q60707"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60707"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60707"
FT MOD_RES 622
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60707"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60707"
FT VARIANT 20
FT /note="R -> Q (in VETD; unknown pathological significance;
FT decreased transcriptional regulatory activity; no effect on
FT localization to the nucleus; dbSNP:rs1364709483)"
FT /evidence="ECO:0000269|PubMed:29726930"
FT /id="VAR_081780"
FT VARIANT 305
FT /note="R -> H (in VETD; de novo variant; decreased
FT transcriptional regulatory activity; no effect on
FT localization to the nucleus; dbSNP:rs1555877071)"
FT /evidence="ECO:0000269|PubMed:29726930"
FT /id="VAR_081781"
FT MUTAGEN 132..133
FT /note="RR->EE: Abolishes repression of tumor suppressor
FT ARF/p14ARF expression."
FT /evidence="ECO:0000269|PubMed:12000749"
FT MUTAGEN 132
FT /note="R->A: Abolishes binding to T site 5'-
FT TTCACACCTAGGTGTGAA-3' DNA sequence."
FT /evidence="ECO:0000269|PubMed:11111039"
FT MUTAGEN 282
FT /note="A->E: Severely impairs repression of tumor
FT suppressor ARF/p14ARF expression."
FT /evidence="ECO:0000269|PubMed:12000749"
FT CONFLICT 7
FT /note="A -> T (in Ref. 1; AAA73861)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="Y -> D (in Ref. 4; AAB36216)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..178
FT /note="AGKA -> TDKT (in Ref. 4; AAB36216)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="G -> R (in Ref. 1; AAA73861)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="S -> C (in Ref. 1; AAA73861)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="A -> P (in Ref. 1; AAA73861)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="Q -> L (in Ref. 1; AAA73861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 75066 MW; 5C890DFC10FC3B68 CRC64;
MREPALAASA MAYHPFHAPR PADFPMSAFL AAAQPSFFPA LALPPGALAK 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
LPSLRLYEEH CKPERDGAES DASSCDPPPA REPPTSPGAA PSPLRLHRAR AEEKSCAADS
DPEPERLSEE RAGAPLGRSP APDSASPTRL TEPERARERR SPERGKEPAE SGGDGPFGLR
SLEKERAEAR RKDEGRKEAA EGKEQGLAPL VVQTDSASPL GAGHLPGLAF SSHLHGQQFF
GPLGAGQPLF LHPGQFTMGP GAFSAMGMGH LLASVAGGGN GGGGGPGTAA GLDAGGLGPA
ASAASTAAPF PFHLSQHMLA SQGIPMPTFG GLFPYPYTYM AAAAAAASAL PATSAAAAAA
AAAGSLSRSP FLGSARPRLR FSPYQIPVTI PPSTSLLTTG LASEGSKAAG GNSREPSPLP
ELALRKVGAP SRGALSPSGS AKEAANELQS IQRLVSGLES QRALSPGRES PK
