http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID212535
Outgoing Links
| Predicate | Object |
|---|---|
| abstract | Histone deacetylase 2 (HDAC2). Histone deacetylase 2 (HDAC2) is a Zn-dependent class I enzyme that catalyzes hydrolysis of N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone (EC 3.5.1.98). Histone acetylation/deacetylation process is important for mediation of transcriptional regulation of many genes. HDAC2 is involved in regulation through association with DNA binding proteins to target specific chromatin regions. It forms transcriptional repressor complexes by associating with several proteins, including the mammalian zinc-finger transcription factor YY1, thus playing an important role in transcriptional regulation, cell cycle progression and developmental events. Additionally, a few non-histone HDAC2 substrates have been found. HDAC2 plays a role in embryonic development and cytokine signaling important for immune response, and is over-expressed in several solid tumors including oral, prostate, ovarian, endometrial and gastric cancer. It participates in DNA-damage response, along with HDAC1; together, they can promote DNA non-homologous end-joining. HDAC2 is considered an important cancer prognostic marker. Inhibitors specifically targeting HDAC2 could be a therapeutic drug option. |
| title | HDAC2 |
| isDiscussedBy | http://rdf.ncbi.nlm.nih.gov/pubchem/reference/33494758 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/19300358 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28187044 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/33597186 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/8456061 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5144573 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/20045299 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/13980442 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23974561 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30899416 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/25147508 http://rdf.ncbi.nlm.nih.gov/pubchem/reference/30221052 |
| type | http://purl.obolibrary.org/obo/SO_0000417 |
Incoming Links
Total number of triples: 20.