{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Guangrong Yan"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0002291000"],"submitter_email":["jxygr007@yahoo.com"],"submitter_affiliation":["Biomedicine Research Center, The Third Affiliated Hospital of Guangzhou Medical University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"pubmed_abstract":["N6-methyladenosine (m<sup>6</sup>A) modification plays important roles in bioprocesses and diseases. AlkB homolog 5 (ALKBH5) is one of two m<sup>6</sup>A demethylases. Here, we reveal that ALKBH5 is acetylated at lysine 235 (K235) by lysine acetyltransferase 8 and deacetylated by histone deacetylase 7. K235 acetylation strengthens the m<sup>6</sup>A demethylation activity of ALKBH5 by increasing its recognition of m<sup>6</sup>A on mRNA. RNA-binding protein paraspeckle component 1 (PSCP1) is a regulatory subunit of ALKBH5 and preferentially interacts with K235-acetylated ALKBH5 to recruit and facilitate the recognition of m<sup>6</sup>A mRNA by ALKBH5, thereby promoting m<sup>6</sup>A erasure. Mitogenic signals promote ALKBH5 K235 acetylation. K235 acetylation of ALKBH5 is upregulated in cancers and promotes tumorigenesis. Thus, our findings reveal that the m<sup>6</sup>A demethylation activity of ALKBH5 is orchestrated by its K235 acetylation and regulatory subunit PSPC1 and that K235 acetylation is necessary for the m<sup>6</sup>A demethylase activity and oncogenic roles of ALKBH5."],"pubmed_title":["K235 acetylation couples with PSPC1 to regulate the m<sup>6</sup>A demethylation activity of ALKBH5 and tumorigenesis."],"pubmed_authors":["Zhang Xiao-Lan XL, Chen Xin-Hui XH, Xu Binwu B, Chen Min M, Zhu Song S, Meng Nan N, Wang Ji-Zhong JZ, Zhu Huifang H, Chen De, Liu Jin-Bao JB, Yan Guang-Rong GR"],"additional_accession":[]},"is_claimable":false,"name":"Identification of the acetylation sites in ALKBH5","description":"The acetylation modification sites in ALKBH5 was identified by mass spectrometry.","dates":{"publication":"Thu Apr 13 00:00:00 BST 2023"},"accession":"PXD020070","cross_references":{"TAXONOMY":["9606"],"pubmed":["37369679"]}}