BATF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BATF_HUMAN
• UniProt AC: Q16520
• Protein Name: Basic leucine zipper transcriptional factor ATF-like
• Gene Name: BATF
• Organism: Homo sapiens (Human).
• 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 (By similarity)..
• Protein Sequence: MPHSSDSSDSSFSRSPPPGKQDSSDDVRRVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLNSHEPLCSVLAASTPSPPEVVYSAHAFHQPHVSSPRFQP

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
35	Acetylation	RRVQRREKNRIAAQK HHHHHHHHHHHHHHH	50.11	25825284
43	Phosphorylation	NRIAAQKSRQRQTQK HHHHHHHHHHHHHHH	22.89	12809553
48	Phosphorylation	QKSRQRQTQKADTLH HHHHHHHHHHHHHCC	33.94	12809553
76	Phosphorylation	RKEIKQLTEELKYFT HHHHHHHHHHHHHHH	25.56	-
99	Phosphorylation	LCSVLAASTPSPPEV CHHHHHHCCCCCCCC	34.93	28348404
100	Phosphorylation	CSVLAASTPSPPEVV HHHHHHCCCCCCCCE	24.06	28348404
102	Phosphorylation	VLAASTPSPPEVVYS HHHHCCCCCCCCEEE	53.85	28348404
108	Phosphorylation	PSPPEVVYSAHAFHQ CCCCCCEEECCCCCC	12.81	28348404
109	Phosphorylation	SPPEVVYSAHAFHQP CCCCCEEECCCCCCC	11.28	28348404
119	Phosphorylation	AFHQPHVSSPRFQP- CCCCCCCCCCCCCC-	31.43	28348404
120	Phosphorylation	FHQPHVSSPRFQP-- CCCCCCCCCCCCC--	21.00	28348404

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

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

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 (By similarity).	-

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IN35_HUMAN	IFI35	physical	8954125
BATF3_HUMAN	BATF3	physical	23661758
BATF_HUMAN	BATF	physical	23661758
ATF3_HUMAN	ATF3	physical	23661758
ATF4_HUMAN	ATF4	physical	23661758
JUNB_HUMAN	JUNB	physical	23661758
DBP_HUMAN	DBP	physical	23661758
ATF2_HUMAN	ATF2	physical	23661758
CEBPE_HUMAN	CEBPE	physical	23661758
CEBPA_HUMAN	CEBPA	physical	23661758
CEBPG_HUMAN	CEBPG	physical	23661758
DDIT3_HUMAN	DDIT3	physical	23661758
KDM1A_HUMAN	KDM1A	physical	23455924
GOPC_HUMAN	GOPC	physical	25416956
JUNB_HUMAN	JUNB	physical	21516116

Drug and Disease Associations

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