Batf
entrez
53314
canonical
uniprot
O35284
canonical
ensembl
ENSMUSG00000034266
resolver
ensp
ENSMUSP00000040706
resolver
enst
ENSMUST00000040536
resolver
genesymbol
Batf
resolver
uniprot
A2RT86
resolver
uniprot_entry
BATF_MOUSE
resolver
uniprot_sec
A2RT86
resolver
amino_acid_sequence
MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP
uniprot
proteins
function
FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the formation of a heterodimer with JUNB that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3'. The BATF-JUNB heterodimer also forms a complex with IRF4 (or IRF8) in immune cells, leading to recognition of AICE sequence (5'-TGAnTCA/GAAA-3'), an immune-specific regulatory element, followed by cooperative binding of BATF and IRF4 (or IRF8) and activation of genes. Controls differentiation of T-helper cells producing interleukin-17 (Th17 cells) by binding to Th17-associated gene promoters: regulates expression of the transcription factor RORC itself and RORC target genes such as IL17 (IL17A or IL17B). Also involved in differentiation of follicular T-helper cells (TfH) by directing expression of BCL6 and MAF. In B-cells, involved in class-switch recombination (CSR) by controlling the expression of both AICDA and of germline transcripts of the intervening heavy-chain region and constant heavy-chain region (I(H)-C(H)). Following infection, can participate in CD8(+) dendritic cell differentiation via interaction with IRF4 and IRF8 to mediate cooperative gene activation. Regulates effector CD8(+) T-cell differentiation by regulating expression of SIRT1. Following DNA damage, part of a differentiation checkpoint that limits self-renewal of hematopoietic stem cells (HSCs): up-regulated by STAT3, leading to differentiation of HSCs, thereby restricting self-renewal of HSCs. {ECO:0000269|PubMed:11466704, ECO:0000269|PubMed:12594265, ECO:0000269|PubMed:19578362, ECO:0000269|PubMed:20421391, ECO:0000269|PubMed:21572431, ECO:0000269|PubMed:22001828, ECO:0000269|PubMed:22385964, ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992523, ECO:0000269|PubMed:22992524, ECO:0000269|PubMed:23021777}.
uniprot
proteins
mass_dalton
14065
uniprot
proteins
mutagenesis
MUTAGEN 43; /note="S->A: Decreased phosphorylation; when associated with A-48."; /evidence="ECO:0000269|PubMed:12809553"; MUTAGEN 43; /note="S->D: Retains the ability to dimerize with JUNB and localization in the nucleus but abolishes DNA-binding."; /evidence="ECO:0000269|PubMed:12809553"; MUTAGEN 48; /note="T->A: Decreased phosphorylation; when associated with A-43."; /evidence="ECO:0000269|PubMed:12809553"; MUTAGEN 55; /note="H->Q: Impairs interaction with IRF4 and the recruitment of IRF4 to AICE motifs, leading to defects in mediate differentiation of Th17 cells. Loss of function; when associated with A-56; D-63 and K-77."; /evidence="ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992524"; MUTAGEN 56; /note="L->A: Loss of function; when associated with Q-55; D-63 and K-77."; /evidence="ECO:0000269|PubMed:22992524"; MUTAGEN 63; /note="K->D: Retains 50% of activity; when associated with 69-Q-T-70 and K-77. Loss of function; when associated with Q-55; A-56 and K-77."; /evidence="ECO:0000269|PubMed:22992524"; MUTAGEN 69..70; /note="RK->QT: Retains 50% of activity; when associated with D-63 and K-77."; /evidence="ECO:0000269|PubMed:22992524"; MUTAGEN 77; /note="E->K: Does not affect interaction with IRF4 and ability to mediate differentiation of Th17 cells. Retains 50% of activity; when associated with D63 and 69-Q-T-70. Loss of function; when associated with Q-55; A-56 and D-63."; /evidence="ECO:0000269|PubMed:22983707, ECO:0000269|PubMed:22992524
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription. {ECO:0000269|PubMed:12809553}.
uniprot
proteins
protein_family
BZIP family
uniprot
proteins
pubmed
11466704
uniprot
proteins
pubmed
12444555
uniprot
proteins
pubmed
12594265
uniprot
proteins
pubmed
12809553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19578362
uniprot
proteins
pubmed
20421391
uniprot
proteins
pubmed
21572431
uniprot
proteins
pubmed
21873234
uniprot
proteins
pubmed
22001828
uniprot
proteins
pubmed
22318729
uniprot
proteins
pubmed
22385964
uniprot
proteins
pubmed
22983707
uniprot
proteins
pubmed
22992523
uniprot
proteins
pubmed
22992524
uniprot
proteins
pubmed
23021777
uniprot
proteins
sequence_length
125
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells.
uniprot
proteins