FunctionResponsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity.
Tissue specificityWidely expressed; lower levels in brain and lung.
Sequence similaritiesBelongs to the histone deacetylase family. HD type 1 subfamily.
Post-translational modificationsS-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development. In embryonic cortical neurons, S-Nitrosylation regulates dendritic growth and branching.
Ab39669 staining human HDAC2 in human breast carcinoma by immunohistochemistry using paraffin embedded tissue.
Right: Treated with synthesized peptide.
References for Anti-HDAC2 antibody (ab39669)
This product has been referenced in:
Benard A et al. Nuclear expression of histone deacetylases and their histone modifications predicts clinical outcome in colorectal cancer. Histopathology66:270-82 (2015).
Read more (PubMed: 25307864) »
Derr RS et al. High nuclear expression levels of histone-modifying enzymes LSD1, HDAC2 and SIRT1 in tumor cells correlate with decreased survival and increased relapse in breast cancer patients. BMC Cancer14:604 (2014).
Read more (PubMed: 25139823) »