domain:The PHD-type zinc finger domain binds to phosphoinositides (PtdInsPs), including phosphatidylinositol 5-phosphate (PtdIns(5)P).,function:Seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53. Component of a mSin3A-like corepressor complex, which is probably involved in deacetylation of nucleosomal histones. ING2 activity seems to be modulated by binding to phosphoinositides (PtdInsPs).,induction:Induced by the DNA-damaging agents etoposide and neocarzinostatin.,similarity:Belongs to the ING family.,similarity:Contains 1 PHD-type zinc finger.,subcellular location:Predominantly nuclear. Localized to chromatin and nuclear matrix. Upon reduced PtdIns(5)P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm.,subunit:Component of a mSin3A-like complex at least consisting of SIN3A, HDAC1, HDAC2, RBBP4/RbAp48, RBBP7/RbAp46, SAP30 and ING2.,tissue specificity:Widely expressed. Higher expressed in colon-cancer tumor than in normal colon tissues.,
Nucleus . Predominantly nuclear. Localized to chromatin and nuclear matrix. Upon reduced PtdIns(5)P levels seems to be released from chromatin and, at least partially, translocated to the cytoplasm.
Widely expressed. Higher expressed in colon-cancer tumor than in normal colon tissues.