BATF_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BATF_MOUSE
• UniProt AC: O35284
• Protein Name: Basic leucine zipper transcriptional factor ATF-like
• Gene Name: Batf
• Organism: Mus musculus (Mouse).
• Sequence Length: 125
• Subcellular Localization: Nucleus. Cytoplasm. Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells.
• Protein Description: 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..
• Protein Sequence: MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	DSSDSSFSRSPPPGK CCCCCCCCCCCCCCC	33.52	-
15	Phosphorylation	SDSSFSRSPPPGKQD CCCCCCCCCCCCCCC	40.33	-
43	Phosphorylation	NRIAAQKSRQRQTQK HHHHHHHHHHHHHHH	22.89	12809553
48	Phosphorylation	QKSRQRQTQKADTLH HHHHHHHHHHHHHCC	33.94	12809553

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BATF_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
43	S	Phosphorylation	Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription.	12809553

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BATF_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of BATF_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.