HDAC10

The protein encoded by this gene belongs to the histone deacetylase family, members of which deacetylate lysine residues on the N-terminal part of the core histones. Histone deacetylation modulates chromatin structure, and plays an important role in transcriptional regulation, cell cycle progression, and developmental events. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.

HDAC10

Polyamine deacetylase (PDAC), which acts preferentially on N8-acetylspermidine, and also on acetylcadaverine and acetylputrescine (PubMed:28516954).

Exhibits attenuated catalytic activity toward N1,N8-diacetylspermidine and very low activity, if any, toward N1-acetylspermidine (PubMed:28516954).

Histone deacetylase activity has been observed in vitro (PubMed:11861901, PubMed:11726666, PubMed:11677242, PubMed:11739383).

Has also been shown to be involved in MSH2 deacetylation (PubMed:26221039).

The physiological relevance of protein/histone deacetylase activity is unclear and could be very weak (PubMed:28516954).

May play a role in the promotion of late stages of autophagy, possibly autophagosome-lysosome fusion and/or lysosomal exocytosis in neuroblastoma cells (PubMed:23801752, PubMed:29968769).

May play a role in homologous recombination (PubMed:21247901).

May promote DNA mismatch repair (PubMed:26221039).

Chromatin organization Source: UniProtKB
DNA repair Source: UniProtKB-KW
Histone deacetylation Source: UniProtKB
Homologous recombination Source: UniProtKB
Macroautophagy Source: UniProtKB
Negative regulation of transcription, DNA-templated Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Peptidyl-lysine deacetylation Source: UniProtKB
Polyamine deacetylation Source: UniProtKB
Positive regulation of mismatch repair Source: UniProtKB
Protein deacetylation Source: UniProtKB
Regulation of transcription, DNA-templated Source: UniProtKB
Spermidine deacetylation Source: UniProtKB

Cytoplasm; Nucleus. Excluded from nucleoli.

In neuroblastoma cells, may promote autophagy in response to chemotherapy-induced DNA damage and efflux of chemotherapeutics via lysosomal exocytosis, hence protecting cells from cytotoxic agents (PubMed:23801752, PubMed:29968769). Expression levels may correlate with survival in neuroblastoma patients, with low levels in the tumor correlating with long-term patient survival and high expression with poor prognosis (PubMed:23801752). Therefore has been proposed as a biomarker to predict neuroblastoma chemoresistance and treatment outcome (PubMed:23801752).