HDAC7 Recombinant Rabbit Monoclonal Antibody [SD082-4]

Function

In the intact cell, DNA closely associates with histones and other nuclear proteins to form chromatin. The remodeling of chromatin is believed to be a critical component of transcriptional regulation and a major source of this remodeling is brought about by the acetylation of nucleosomal histones. Acetylation of lysine residues in the amino terminal tail domain of histone results in an allosteric change in the nucleosomal conformation and an increased accessibility to transcription factors by DNA. Conversely, the deacetylation of histones is associated with transcriptional silencing. Several mammalian proteins have been identified as nuclear histone acetylases, including GCN5, PCAF (p300/CBP-associated factor), p300/CBP, HAT1, and the TFIID subunit TAF II p250. Mammalian HDAC7 is a histone deacetylase that interacts with the adaptor mSin3A. The interaction of HDAC7 with mSin3A suggests the association of multiple repression complexes of transcription factors.

Background References

1. Galán M et al. Induction of histone deacetylases (HDACs) in human abdominal aortic aneurysm: therapeutic potential of HDAC inhibitors. Dis Model Mech 9:541-52 (2016).

2. Shen W et al. Epigenetic modification of the leptin promoter in diet-induced obese mice and the effects of N-3 polyunsaturated Fatty acids. Sci Rep 4:5282 (2014).

Sequence Similarity

Belongs to the histone deacetylase family. HD type 2 subfamily.

Post-translational Modification

May be phosphorylated by CaMK1. Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear import. Phosphorylation at Ser-155 by MARK2, MARK3 and PRKD1 promotes interaction with 14-3-3 proteins and export from the nucleus. Phosphorylation at Ser-155 is a prerequisite for phosphorylation at Ser-181.

Subcellular Location

Nucleus, Cytoplasm.

UNIPROT

SwissProt: Q8WUI4 Human

SwissProt: Q8C2B3 Mouse

SwissProt: Q99P96 Rat

Synonyms