TBX2_CANLF
ID TBX2_CANLF Reviewed; 712 AA.
AC Q863A2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=T-box transcription factor TBX2;
DE Short=T-box protein 2;
GN Name=TBX2;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Andelfinger G., Etter L., Dyment M., Hitte C., Galibert F., Kirkness E.,
RA Benson D.W.;
RT "Molecular cloning of canine Tbx2 and Tbx4: exclusion as candidates for
RT canine tricuspid valve malformation.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor which acts as a transcriptional
CC repressor (By similarity). May also function as a transcriptional
CC activator (By similarity). Binds to the palindromic T site 5'-
CC TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present
CC in the regulatory region of several genes. Required for cardiac
CC atrioventricular canal formation (By similarity). May cooperate with
CC NKX2.5 to negatively modulate expression of NPPA/ANF in the
CC atrioventricular canal. May play a role as a positive regulator of
CC TGFB2 expression, perhaps acting in concert with GATA4 in the
CC developing outflow tract myocardium (By similarity). Plays a role in
CC limb pattern formation. Acts as a transcriptional repressor of ADAM10
CC gene expression, perhaps in concert with histone deacetylase HDAC1 as
CC cofactor (By similarity). Involved in branching morphogenesis in both
CC developing lungs and adult mammary glands, via negative modulation of
CC target genes; acting redundantly with TBX3. Required, together with
CC TBX3, to maintain cell proliferation in the embryonic lung mesenchyme;
CC perhaps acting downstream of SHH, BMP and TGFbeta signaling. 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 (By similarity). 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. Plays a role in
CC induction of the epithelial-mesenchymal transition (EMT) (By
CC similarity). Plays a role in melanocyte proliferation, perhaps via
CC regulation of cyclin CCND1. Involved in melanogenesis, acting via
CC negative modulation of expression of DHICA oxidase/TYRP1 and P
CC protein/OCA2 (By similarity). Involved in regulating retinal pigment
CC epithelium (RPE) cell proliferation, perhaps via negatively modulating
CC transcription of the transcription factor CEBPD (By similarity).
CC {ECO:0000250|UniProtKB:Q13207, ECO:0000250|UniProtKB:Q60707}.
CC -!- SUBUNIT: Binds DNA as a monomer. Interacts with PML (isoform PML-2,
CC isoform PML-3 and isoform PML-4). {ECO:0000250|UniProtKB:Q13207}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13207}.
CC -!- DOMAIN: Repression domain 1 (RD1) is involved in transcriptional
CC repression. RD1 is necessary for its interaction with PML.
CC {ECO:0000250|UniProtKB:Q13207}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO24699.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY192802; AAO24699.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY192798; AAO24699.1; JOINED; Genomic_DNA.
DR EMBL; AY192799; AAO24699.1; JOINED; Genomic_DNA.
DR EMBL; AY192800; AAO24699.1; JOINED; Genomic_DNA.
DR EMBL; AY192801; AAO24699.1; JOINED; Genomic_DNA.
DR AlphaFoldDB; Q863A2; -.
DR SMR; Q863A2; -.
DR STRING; 9615.ENSCAFP00000037090; -.
DR Ensembl; ENSCAFT00000049492; ENSCAFP00000037090; ENSCAFG00000017745.
DR Ensembl; ENSCAFT00030045972; ENSCAFP00030040164; ENSCAFG00030024923.
DR Ensembl; ENSCAFT00845048190; ENSCAFP00845037798; ENSCAFG00845027360.
DR VEuPathDB; HostDB:ENSCAFG00845027360; -.
DR VGNC; VGNC:47171; TBX2.
DR GeneTree; ENSGT00940000158439; -.
DR InParanoid; Q863A2; -.
DR Proteomes; UP000002254; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0035909; P:aorta morphogenesis; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR GO; GO:1905222; P:atrioventricular canal morphogenesis; IEA:Ensembl.
DR GO; GO:1905072; P:cardiac jelly development; IEA:Ensembl.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IEA:Ensembl.
DR GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0090398; P:cellular senescence; ISS: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; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0035050; P:embryonic heart tube development; ISS:UniProtKB.
DR GO; GO:0003272; P:endocardial cushion formation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1901211; P:negative regulation of cardiac chamber formation; IEA:Ensembl.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
DR GO; GO:1901208; P:negative regulation of heart looping; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IEA:Ensembl.
DR GO; GO:0060465; P:pharynx development; IEA:Ensembl.
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; IEA:Ensembl.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..712
FT /note="T-box transcription factor TBX2"
FT /id="PRO_0000184425"
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 517..601
FT /note="Repression domain 1 (RD1)"
FT /evidence="ECO:0000250"
FT REGION 642..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..442
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 359
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:0000250|UniProtKB:Q13207"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13207"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60707"
SQ SEQUENCE 712 AA; 74900 MW; A8AC367FE34AE025 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 DASSCDPAPA REPPASPGSA PSPLRLHRTR ADEKCAADSD
PEPERLSEER AGPALGRSPG LDGGSPPRLT EPERARERRS PERGKEPAES GGDGPFGLRS
LEKERAEARR KDDGRKEAGE GKEPGLAPLV VQTDSASPLG AGHLPGLAFS GHLHGQQFFG
PLGAGQPLFL HPGQFAMGPG AFSAMGMGHL LASVAGGGGG GGGGGPGTAT GLDAGGLGPA
ASAASTPAPF PFHLSQHMLA SQGIPMPTFG GLFPYPYTYM AAAAAAASAL PATSAAAAAA
AAAGSLSRSH FLGSARPRLR FSPYQIPVTI PPSTSLLTTG LAAEGSKAAG SNSREPSPLP
ELALRKVGAP SRGALSPSGS AKEAASELQS IQRLVSGLEN QRALSPGRES PK
