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翻訳と辞書　辞書検索 [ 開発暫定版 ] スポンサード リンク Protein O-GlcNAc transferase ： ウィキペディア英語版 Protein O-GlcNAc transferase O-GlcNAc transferase (, ''O-GlcNAc transferase'', ''OGTase'', ''O-linked N-acetylglucosaminyltransferase'', ''uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase'', ''protein O-linked beta-N-acetylglucosamine transferase'') is an enzyme with system name ''UDP-N-acetyl-D-glucosamine:protein-O-beta-N-acetyl-D-glucosaminyl transferase''. In humans the enzyme is encoded by the ''OGT'' gene.〔〔(【引用サイトリンク】 url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8473 )〕 == Function == O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues of intracellular proteins. Since both phosphorylation and O-GlcNAcylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. Two transcript variants encoding cytoplasmic and mitochondrial isoforms have been found for this gene.〔 OGT glycosylates many proteins including: Histone H2B, AKT1, PFKL,〔(【引用サイトリンク】url=http://www.uniprot.org/uniprot/O15294#ref11 )〕 KMT2E/MLL5,〔 MAPT/TAU, Host cell factor C1, and SIN3A. O-GlcNAc transferase is a part of a host of biological functions within the human body. OGT is involved in the resistance of insulin in muscle cells and adipocytes by inhibiting the Threonine 308 phosphorylation of AKT1, increasing the rate of IRS1 phosphorylation (at Serine 307 and Serine 632/635), reducing insulin signaling, and glycosylating components of insulin signals. Additionally, O-GlcNAc transferase catalyzes intracellular glycosylation of serine and threonine residues with the addition of N-acetylglucosamine. Studies show that OGT alleles are vital for embryogenesis, and that OGT is necessary for intracellular glycosylation and embryonic stem cell vitality. O-GlcNAc transferase also catalyzes the posttranslational modification that modifies transcription factors and RNA polymerase II, however the specific function of this modification is mostly unknown. OGT cleaves Host Cell Factor C1, at one of the 6 repeat sequences. The TPR repeat domain of OGT binds to the carboxyl terminal portion of an HCF1 proteolytic repeat so that the cleavage region is in the glycosyltransferase active site above uridine-diphosphate-GlcNAc 〔 The large proportion of OGT complexed with HCF1 is necessary for HCF1 cleavage, and HCFC1 is required for OGT stabilization in the nucleus. HCF1 regulates OGT stability using a post-transcriptional mechanism, however the mechanism of the interaction with HCFC1 is still unknown. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Protein O-GlcNAc transferase」の詳細全文を読む スポンサード リンク 翻訳と辞書 : 翻訳のためのインターネットリソース Copyright(C) kotoba.ne.jp 1997-2016. All Rights Reserved.