Tbx21
entrez
57765
canonical
uniprot
Q9JKD8
canonical
ensembl
ENSMUSG00000001444
resolver
ensp
ENSMUSP00000001484
resolver
enst
ENSMUST00000001484
resolver
genesymbol
Tbx21
resolver
genesymbol_syn
Tbet
resolver
genesymbol_syn
Tblym
resolver
uniprot
Q3U150
resolver
uniprot
Q9R0A6
resolver
uniprot_entry
TBX21_MOUSE
resolver
uniprot_sec
Q3U150
resolver
uniprot_sec
Q9R0A6
resolver
amino_acid_sequence
MGIVEPGCGDMLTGTEPMPSDEGRGPGADQQHRFFYPEPGAQDPTDRRAGSSLGTPYSGGALVPAAPGRFLGSFAYPPRAQVAGFPGPGEFFPPPAGAEGYPPVDGYPAPDPRAGLYPGPREDYALPAGLEVSGKLRVALSNHLLWSKFNQHQTEMIITKQGRRMFPFLSFTVAGLEPTSHYRMFVDVVLVDQHHWRYQSGKWVQCGKAEGSMPGNRLYVHPDSPNTGAHWMRQEVSFGKLKLTNNKGASNNVTQMIVLQSLHKYQPRLHIVEVNDGEPEAACSASNTHVFTFQETQFIAVTAYQNAEITQLKIDNNPFAKGFRENFESMYASVDTSVPSPPGPNCQLLGGDPFSPLLSNQYPVPSRFYPDLPGQPKDMISQPYWLGTPREHSYEAEFRAVSMKPTLLPSAPGPTVPYYRGQDVLAPGAGWPVAPQYPPKMSPAGWFRPMRTLPMDPGLGSSEEQGSSPSLWPEVTSLQPEPSDSGLGEGDTKRRRISPYPSSGDSSSPAGAPSPFDKETEGQFYNYFPN
uniprot
proteins
function
FUNCTION: Lineage-defining transcription factor which initiates Th1 lineage development from naive Th precursor cells both by activating Th1 genetic programs and by repressing the opposing Th2 and Th17 genetic programs. Activates transcription of a set of genes important for Th1 cell function, including those encoding IFN-gamma and the chemokine receptor CXCR3. Activates IFNG and CXCR3 genes in part by recruiting chromatin remodeling complexes including KDM6B, a SMARCA4-containing SWI/SNF-complex, and an H3K4me2-methyltransferase complex to their promoters and all of these complexes serve to establish a more permissive chromatin state conducive with transcriptional activation (PubMed:10761931, PubMed:17923685, PubMed:21095589). Can activate Th1 genes also via recruitment of Mediator complex and P-TEFb (composed of CDK9 and CCNT1/cyclin-T1) in the form of the super elongation complex (SEC) to super-enhancers and associated genes in activated Th1 cells (PubMed:27292648). Inhibits the Th17 cell lineage commitment by blocking RUNX1-mediated transactivation of Th17 cell-specific transcriptinal regulator RORC (PubMed:21151104). Inhibits the Th2 cell lineage commitment by suppressing the production of Th2 cytokines, such as IL-4, IL-5, and IL- 13, via repression of transcriptional regulators GATA3 and NFATC2 (PubMed:15662016, PubMed:21690296, PubMed:23616576). Protects Th1 cells from amplifying aberrant type-I IFN response in an IFN-gamma abundant microenvironment by acting as a repressor of type-I IFN transcription factors and type-I IFN- stimulated genes (PubMed:28623086). Acts as a regulator of antiviral B-cell responses; controls chronic viral infection by promoting the antiviral antibody IgG2a isotype switching and via regulation of a broad antiviral gene expression program (PubMed:27430722). {ECO:0000269|PubMed:10761931, ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:17923685, ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:27292648, ECO:0000269|PubMed:27430722, ECO:0000269|PubMed:28607488, ECO:0000269|PubMed:28623086}.
uniprot
proteins
mass_dalton
57852
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="S->A: No loss in its ability to induce IFN-gamma. Significant reduction in its ability to induce IFN-gamma and reduced ability to promote addition of permissive chromatin-remodeling mark H3K4Me2 to the IFNG promoter region; when associated with A-76 and A-224."; /evidence="ECO:0000269|PubMed:28424242"; MUTAGEN 55; /note="T->A: No loss in its ability to induce IFN-gamma."; /evidence="ECO:0000269|PubMed:28424242"; MUTAGEN 76; /note="Y->A: No loss in its ability to induce IFN-gamma. Significant reduction in its ability to induce IFN-gamma and reduced ability to promote addition of permissive chromatin-remodeling mark H3K4Me2 to the IFNG promoter region; when associated with A-52 and A-224."; /evidence="ECO:0000269|PubMed:28424242"; MUTAGEN 117; /note="Y->A: No loss in its ability to induce IFN-gamma."; /evidence="ECO:0000269|PubMed:28424242"; MUTAGEN 208; /note="K->R: No effect on DNA-binding or its nuclear localization."; /evidence="ECO:0000269|PubMed:23616576"; MUTAGEN 219; /note="Y->F: Significant loss of ABL1-mediated phosphorylation and loss of transcriptional activator activity; when associated with F-225 and F-304."; /evidence="ECO:0000269|PubMed:21690296"; MUTAGEN 224; /note="S->A: No loss in its ability to induce IFN-gamma. Significant reduction in its ability to induce IFN-gamma and reduced ability to promote addition of permissive chromatin-remodeling mark H3K4Me2 to the IFNG promoter region; when associated with A-52 and A-76."; /evidence="ECO:0000269|PubMed:28424242"; MUTAGEN 265; /note="Y->F: No loss of interaction with RUNX1."; /evidence="ECO:0000269|PubMed:21151104"; MUTAGEN 265; /note="Y->F: Significant loss of ABL1-mediated phosphorylation and loss of transcriptional activator activity; when associated with F-219 and F-304."; /evidence="ECO:0000269|PubMed:21690296"; MUTAGEN 302; /note="T->A: Loss of phosphorylation and its ability to interact with NFATC2. Loss of its ability to suppress IL-2 and Th2 cytokine production. No loss of DNA-binding and no loss its ability to activate IFN-gamma transcription."; /evidence="ECO:0000269|PubMed:23616576"; MUTAGEN 304; /note="Y->F: Loss of interaction with RUNX1 and loss of its ability to inhibit RUNX1 transcriptional activity and suppress TH17 lineage development. Significant loss of ABL1-mediated phosphorylation and loss of transcriptional activator activity; when associated with F-219 and F-225."; /evidence="ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:21690296"; MUTAGEN 310; /note="T->A: No loss of phospshorylation."; /evidence="ECO:0000269|PubMed:23616576"; MUTAGEN 313; /note="K->R: Significant loss of ubiquitination. Loss of phosphorylation at T-302 causing loss of its ability to interact with NFATC2. Loss its ability to activate IFN-gamma transcription due to loss of DNA-binding activity. Loss of its ability to suppress IL-2 and Th2 cytokine production. Increased protein stability. Localization seen in both the nucleus and cytoplasm. No loss of interaction with GATA3 and RELA."; /evidence="ECO:0000269|PubMed:23616576"; MUTAGEN 321; /note="K->R: No effect on DNA-binding or its nuclear localization."; /evidence="ECO:0000269|PubMed:23616576"; MUTAGEN 437; /note="Y->F: No loss of interaction with ITK and GATA3."; /evidence="ECO:0000269|PubMed:15662016"; MUTAGEN 508; /note="S->A: No loss of interaction with RUNX1. No loss in its ability to induce IFN-gamma."; /evidence="ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:28424242"; MUTAGEN 525; /note="Y->F: No loss of interaction with RUNX1. Loss of interaction with ITK and GATA3."; /evidence="ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21151104
uniprot
proteins
post_translational_modification
PTM: Phosphorylations at Ser-52, Tyr-76, Ser-224 and Ser-508 are regulated by mTORC1 (PubMed:28424242). Phosphorylation at Tyr-525 is essential for its interaction GATA3 (PubMed:15662016). Phosphorylation at Tyr-219, Tyr-265 and Tyr-304 enhances its transcriptional activator activity (PubMed:21690296). Phosphorylation at Thr-302 is required for its interaction with NFATC2 (PubMed:23616576). {ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576, ECO:0000269|PubMed:28424242}.; PTM: Ubiquitinated at Lys-313, leading to its degradation by the proteasome. Ubiquitination is essential for controlling protein stability, binding to the T-box-binding element of the IFN-gamma promoter, and for interaction with NFATC2 through induction of phosphorylation at Thr-302 (PubMed:23616576). Deubiquitinated by USP10 leading to its stabilization (By similarity). {ECO:0000250|UniProtKB:Q9UL17, ECO:0000269|PubMed:23616576}.
uniprot
proteins
pubmed
10761931
uniprot
proteins
pubmed
11087660
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15662016
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17923685
uniprot
proteins
pubmed
21095589
uniprot
proteins
pubmed
21151104
uniprot
proteins
pubmed
21690296
uniprot
proteins
pubmed
23616576
uniprot
proteins
pubmed
27292648
uniprot
proteins
pubmed
27430722
uniprot
proteins
pubmed
28424242
uniprot
proteins
pubmed
28607488
uniprot
proteins
pubmed
28623086
uniprot
proteins
sequence_length
530
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10761931, ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576}.
uniprot
proteins