This entry represents the PHD domain of ING2.
","llm":false,"checked":false,"updated":false},{"text":"Members of the ING (inhibitor of growth protein) family of tumour suppressors regulate cell cycle progression, senescence, apoptosis, and DNA repair as important cofactors of p53. Inhibitor of growth protein 2 (ING2) seems to be involved in p53/TP53 activation and p53/TP53-dependent apoptotic pathways, probably by enhancing acetylation of p53/TP53 [[cite:PUB00069013]]. It is also a component of a chromatin-modifying complex containing the transcriptional co-repressor SIN3A and HDAC1 (histone deacetylase 1), which is involved in deacetylation of nucleosomal histones [[cite:PUB00069007], [cite:PUB00054915]]. The stability of ING2 is regulated by nuclear phosphatidylinositol-5-phosphate at discrete chromatin targets in response to DNA damage [[cite:PUB00069014], [cite:PUB00069015]].
","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00069015":{"PMID":23823870,"ISBN":null,"volume":"3","issue":null,"year":2013,"title":"Nuclear phosphatidylinositol-5-phosphate regulates ING2 stability at discrete chromatin targets in response to DNA damage.","URL":null,"raw_pages":"2137","medline_journal":"Sci Rep","ISO_journal":"Sci Rep","authors":["Bua DJ","Martin GM","Binda O","Gozani O."],"DOI_URL":"http://dx.doi.org/10.1038/srep02137"},"PUB00069013":{"PMID":11481424,"ISBN":null,"volume":"98","issue":"17","year":2001,"title":"DNA damage-inducible gene p33ING2 negatively regulates cell proliferation through acetylation of p53.","URL":null,"raw_pages":"9671-6","medline_journal":"Proc Natl Acad Sci U S A","ISO_journal":"Proc. Natl. Acad. Sci. U.S.A.","authors":["Nagashima M","Shiseki M","Miura K","Hagiwara K","Linke SP","Pedeux R","Wang XW","Yokota J","Riabowol K","Harris CC."],"DOI_URL":"http://dx.doi.org/10.1073/pnas.161151798"},"PUB00069014":{"PMID":12859901,"ISBN":null,"volume":"114","issue":"1","year":2003,"title":"The PHD finger of the chromatin-associated protein ING2 functions as a nuclear phosphoinositide receptor.","URL":null,"raw_pages":"99-111","medline_journal":"Cell","ISO_journal":"Cell","authors":["Gozani O","Karuman P","Jones DR","Ivanov D","Cha J","Lugovskoy AA","Baird CL","Zhu H","Field SJ","Lessnick SL","Villasenor J","Mehrotra B","Chen J","Rao VR","Brugge JS","Ferguson CG","Payrastre B","Myszka DG","Cantley LC","Wagner G","Divecha N","Prestwich GD","Yuan J."],"DOI_URL":"http://dx.doi.org/10.1016/S0092-8674(03)00480-X"},"PUB00054915":{"PMID":20676127,"ISBN":null,"volume":"29","issue":"44","year":2010,"title":"Sumoylation of ING2 regulates the transcription mediated by Sin3A.","URL":null,"raw_pages":"5946-56","medline_journal":"Oncogene","ISO_journal":"Oncogene","authors":["Ythier D","Larrieu D","Binet R","Binda O","Brambilla C","Gazzeri S","Pedeux R."],"DOI_URL":"http://dx.doi.org/10.1038/onc.2010.325"},"PUB00069007":{"PMID":16387653,"ISBN":null,"volume":"21","issue":"1","year":2006,"title":"ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation.","URL":null,"raw_pages":"51-64","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Doyon Y","Cayrou C","Ullah M","Landry AJ","Cote V","Selleck W","Lane WS","Tan S","Yang XJ","Cote J."],"DOI_URL":"http://dx.doi.org/10.1016/j.molcel.2005.12.007"}},"set_info":null,"overlaps_with":[{"accession":"IPR011011","name":"Zinc finger, FYVE/PHD-type","type":"homologous_superfamily"},{"accession":"IPR013083","name":"Zinc finger, RING/FYVE/PHD-type","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":681,"pathways":4,"proteins":681,"proteomes":590,"sets":0,"structural_models":{"alphafold":646,"bfvd":0},"structures":1,"taxa":1804},"entry_annotations":{},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}