4gyw - Revision history

OCA at 07:27, 26 October 2022

OCA — Wed, 26 Oct 2022 07:27:42 GMT

←Older revision		Revision as of 07:27, 26 October 2022
Line 1:		Line 1:

	==Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide==		==Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide==
-	<StructureSection load='4gyw' size='340' side='right' caption='[[4gyw]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='4gyw' size='340' side='right'caption='[[4gyw]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gyw]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4GYW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gyw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GYW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gyy\|4gyy]], [[4gz3\|4gz3]], [[4gz5\|4gz5]], [[4gz6\|4gz6]]</td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyw OCA], [https://pdbe.org/4gyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gyw RCSB], [https://www.ebi.ac.uk/pdbsum/4gyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyw ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">OGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase Protein O-GlcNAc transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.255 2.4.1.255] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4gyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyw OCA], [~~http~~://pdbe.org/4gyw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4gyw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4gyw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyw ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/OGT1_HUMAN OGT1_HUMAN]] Regulation of OGT activity and altered O-GlcNAcylations are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of AKT1 affects insulin signaling and, possibly diabetes. Reduced O-GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are observed in Alzheimer disease (AD) brain cerebrum.	+	[https://www.uniprot.org/uniprot/OGT1_HUMAN OGT1_HUMAN] Regulation of OGT activity and altered O-GlcNAcylations are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of AKT1 affects insulin signaling and, possibly diabetes. Reduced O-GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are observed in Alzheimer disease (AD) brain cerebrum.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/OGT1_HUMAN OGT1_HUMAN]] Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues.<ref>PMID:12150998</ref> <ref>PMID:18288188</ref> <ref>PMID:19451179</ref> <ref>PMID:19377461</ref> <ref>PMID:20018852</ref> <ref>PMID:20018868</ref> <ref>PMID:20200153</ref> <ref>PMID:20824293</ref> <ref>PMID:21285374</ref> <ref>PMID:22121020</ref> <ref>PMID:22923583</ref> <ref>PMID:23353889</ref> <ref>PMID:23222540</ref> <ref>PMID:15361863</ref> <ref>PMID:21240259</ref> Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.<ref>PMID:12150998</ref> <ref>PMID:18288188</ref> <ref>PMID:19451179</ref> <ref>PMID:19377461</ref> <ref>PMID:20018852</ref> <ref>PMID:20018868</ref> <ref>PMID:20200153</ref> <ref>PMID:20824293</ref> <ref>PMID:21285374</ref> <ref>PMID:22121020</ref> <ref>PMID:22923583</ref> <ref>PMID:23353889</ref> <ref>PMID:23222540</ref> <ref>PMID:15361863</ref> <ref>PMID:21240259</ref> [[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>	+	[https://www.uniprot.org/uniprot/OGT1_HUMAN OGT1_HUMAN] Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues.<ref>PMID:12150998</ref> <ref>PMID:18288188</ref> <ref>PMID:19451179</ref> <ref>PMID:19377461</ref> <ref>PMID:20018852</ref> <ref>PMID:20018868</ref> <ref>PMID:20200153</ref> <ref>PMID:20824293</ref> <ref>PMID:21285374</ref> <ref>PMID:22121020</ref> <ref>PMID:22923583</ref> <ref>PMID:23353889</ref> <ref>PMID:23222540</ref> <ref>PMID:15361863</ref> <ref>PMID:21240259</ref> Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.<ref>PMID:12150998</ref> <ref>PMID:18288188</ref> <ref>PMID:19451179</ref> <ref>PMID:19377461</ref> <ref>PMID:20018852</ref> <ref>PMID:20018868</ref> <ref>PMID:20200153</ref> <ref>PMID:20824293</ref> <ref>PMID:21285374</ref> <ref>PMID:22121020</ref> <ref>PMID:22923583</ref> <ref>PMID:23353889</ref> <ref>PMID:23222540</ref> <ref>PMID:15361863</ref> <ref>PMID:21240259</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 22:

	==See Also==		==See Also==
-	*[[O-GlcNAc transferase\|O-GlcNAc transferase]]	+	*[[O-GlcNAc transferase 3D structures\|O-GlcNAc transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Protein O-GlcNAc transferase~~]]	+	[[Category: Large Structures]]
-	[[Category: Gloster~~, T M~~]]	+	[[Category: Gloster TM]]
-	[[Category: Jiang, J]]	+	[[Category: Jiang J]]
-	[[Category: Lazarus~~, M B~~]]	+	[[Category: Lazarus MB]]
-	[[Category: Vocadlo~~, D J~~]]	+	[[Category: Vocadlo DJ]]
-	[[Category: Walker, S]]	+	[[Category: Walker S]]
-	[[Category: Zandberg~~, W F]]~~	+	[[Category: Zandberg WF]]
-	~~[[Category: Glcnacylation]]~~	+
-	~~[[Category: Glycosyltransferase]]~~	+
-	~~[[Category: Gt-b]]~~	+
-	~~[[Category: Transferase-peptide complex~~]]	+

OCA at 22:53, 5 August 2016

OCA — Fri, 05 Aug 2016 22:53:07 GMT

←Older revision		Revision as of 22:53, 5 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide==		==Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide==
	<StructureSection load='4gyw' size='340' side='right' caption='[[4gyw]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4gyw' size='340' side='right' caption='[[4gyw]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4gyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GYW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4gyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GYW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gyy\|4gyy]], [[4gz3\|4gz3]], [[4gz5\|4gz5]], [[4gz6\|4gz6]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gyy\|4gyy]], [[4gz3\|4gz3]], [[4gz5\|4gz5]], [[4gz6\|4gz6]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">OGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">OGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase Protein O-GlcNAc transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.255 2.4.1.255] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase Protein O-GlcNAc transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.255 2.4.1.255] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gyw RCSB], [http://www.ebi.ac.uk/pdbsum/4gyw PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyw OCA], [http://pdbe.org/4gyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gyw RCSB], [http://www.ebi.ac.uk/pdbsum/4gyw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gyw ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4gyw" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 28:		Line 30:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Protein O-GlcNAc transferase]]		[[Category: Protein O-GlcNAc transferase]]
	[[Category: Gloster, T M]]		[[Category: Gloster, T M]]

OCA at 22:38, 25 December 2014

OCA — Thu, 25 Dec 2014 22:38:06 GMT

←Older revision		Revision as of 22:38, 25 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4gyw.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide==
		+	<StructureSection load='4gyw' size='340' side='right' caption='[[4gyw]], [[Resolution\|resolution]] 1.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4gyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GYW FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4gyy\|4gyy]], [[4gz3\|4gz3]], [[4gz5\|4gz5]], [[4gz6\|4gz6]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">OGT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase Protein O-GlcNAc transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.255 2.4.1.255] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4gyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gyw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gyw RCSB], [http://www.ebi.ac.uk/pdbsum/4gyw PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/OGT1_HUMAN OGT1_HUMAN]] Regulation of OGT activity and altered O-GlcNAcylations are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of AKT1 affects insulin signaling and, possibly diabetes. Reduced O-GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are observed in Alzheimer disease (AD) brain cerebrum.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/OGT1_HUMAN OGT1_HUMAN]] Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues.<ref>PMID:12150998</ref> <ref>PMID:18288188</ref> <ref>PMID:19451179</ref> <ref>PMID:19377461</ref> <ref>PMID:20018852</ref> <ref>PMID:20018868</ref> <ref>PMID:20200153</ref> <ref>PMID:20824293</ref> <ref>PMID:21285374</ref> <ref>PMID:22121020</ref> <ref>PMID:22923583</ref> <ref>PMID:23353889</ref> <ref>PMID:23222540</ref> <ref>PMID:15361863</ref> <ref>PMID:21240259</ref> Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.<ref>PMID:12150998</ref> <ref>PMID:18288188</ref> <ref>PMID:19451179</ref> <ref>PMID:19377461</ref> <ref>PMID:20018852</ref> <ref>PMID:20018868</ref> <ref>PMID:20200153</ref> <ref>PMID:20824293</ref> <ref>PMID:21285374</ref> <ref>PMID:22121020</ref> <ref>PMID:22923583</ref> <ref>PMID:23353889</ref> <ref>PMID:23222540</ref> <ref>PMID:15361863</ref> <ref>PMID:21240259</ref> [[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Visualization of the reaction coordinate undertaken by glycosyltransferases has remained elusive but is critical for understanding this important class of enzyme. Using substrates and substrate mimics, we describe structural snapshots of all species along the kinetic pathway for human O-linked beta-N-acetylglucosamine transferase (O-GlcNAc transferase), an intracellular enzyme that catalyzes installation of a dynamic post-translational modification. The structures reveal key features of the mechanism and show that substrate participation is important during catalysis.

-	~~{{STRUCTURE_4gyw\| PDB=4gyw \| SCENE= }}~~	+	Structural snapshots of the reaction coordinate for O-GlcNAc transferase.,Lazarus MB, Jiang J, Gloster TM, Zandberg WF, Whitworth GE, Vocadlo DJ, Walker S Nat Chem Biol. 2012 Dec;8(12):966-8. doi: 10.1038/nchembio.1109. Epub 2012 Oct, 28. PMID:23103939<ref>PMID:23103939</ref>

-	~~===Crystal structure of human O-GlcNAc Transferase in complex with UDP and~~ a ~~glycopeptide===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_23103939}}~~	+	==See Also==
-		+	*[[O-GlcNAc transferase\|O-GlcNAc transferase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~4gyw~~]] ~~is a 4 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYW OCA].~~	+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Protein O-GlcNAc transferase]]		[[Category: Protein O-GlcNAc transferase]]
-	[[Category: Gloster, T M.]]	+	[[Category: Gloster, T M]]
-	[[Category: Jiang, J.]]	+	[[Category: Jiang, J]]
-	[[Category: Lazarus, M B.]]	+	[[Category: Lazarus, M B]]
-	[[Category: Vocadlo, D J.]]	+	[[Category: Vocadlo, D J]]
-	[[Category: Walker, S.]]	+	[[Category: Walker, S]]
-	[[Category: Zandberg, W F.]]	+	[[Category: Zandberg, W F]]
	[[Category: Glcnacylation]]		[[Category: Glcnacylation]]
	[[Category: Glycosyltransferase]]		[[Category: Glycosyltransferase]]
	[[Category: Gt-b]]		[[Category: Gt-b]]
	[[Category: Transferase-peptide complex]]		[[Category: Transferase-peptide complex]]

OCA at 21:06, 12 December 2012

OCA — Wed, 12 Dec 2012 21:06:43 GMT

←Older revision		Revision as of 21:06, 12 December 2012
Line 1:		Line 1:
-	[[Image:4gyw.~~jpg~~\|left\|200px]]	+	[[Image:4gyw.png\|left\|200px]]

	{{STRUCTURE_4gyw\| PDB=4gyw \| SCENE= }}		{{STRUCTURE_4gyw\| PDB=4gyw \| SCENE= }}
Line 5:		Line 5:
	===Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide===		===Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide===

		+	{{ABSTRACT_PUBMED_23103939}}

	==About this Structure==		==About this Structure==

OCA at 09:25, 31 October 2012

OCA — Wed, 31 Oct 2012 09:25:49 GMT

←Older revision		Revision as of 09:25, 31 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4gyw.jpg\|left\|200px]]

-	~~The entry~~ 4gyw ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4gyw\| PDB=4gyw \| SCENE= }}

-	~~Authors: Lazarus, M.B., Jiang, J., Gloster, T.M., Zandberg, W.F., Vocadlo, D.J., Walker, S.~~	+	===Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide===

-	~~Description: Crystal~~ structure ~~of human~~ O-GlcNAc Transferase in complex ~~with UDP and a glycopeptide~~	+
		+	==About this Structure==
		+	[[4gyw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GYW OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Protein O-GlcNAc transferase]]
		+	[[Category: Gloster, T M.]]
		+	[[Category: Jiang, J.]]
		+	[[Category: Lazarus, M B.]]
		+	[[Category: Vocadlo, D J.]]
		+	[[Category: Walker, S.]]
		+	[[Category: Zandberg, W F.]]
		+	[[Category: Glcnacylation]]
		+	[[Category: Glycosyltransferase]]
		+	[[Category: Gt-b]]
		+	[[Category: Transferase-peptide complex]]

OCA at 20:09, 26 September 2012

OCA — Wed, 26 Sep 2012 20:09:56 GMT

←Older revision		Revision as of 20:09, 26 September 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4gyw is ON HOLD	+	The entry 4gyw is ON HOLD until Paper Publication

	Authors: Lazarus, M.B., Jiang, J., Gloster, T.M., Zandberg, W.F., Vocadlo, D.J., Walker, S.		Authors: Lazarus, M.B., Jiang, J., Gloster, T.M., Zandberg, W.F., Vocadlo, D.J., Walker, S.

	Description: Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide		Description: Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide

OCA: Protected "4gyw" [edit=sysop:move=sysop]

OCA — Wed, 12 Sep 2012 04:57:04 GMT

Protected "4gyw" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:57, 12 September 2012

OCA: New page: '''Unreleased structure''' The entry 4gyw is ON HOLD Authors: Lazarus, M.B., Jiang, J., Gloster, T.M., Zandberg, W.F., Vocadlo, D.J., Walker, S. Description: Crystal structure of human...

OCA — Wed, 12 Sep 2012 04:57:03 GMT

New page: '''Unreleased structure''' The entry 4gyw is ON HOLD Authors: Lazarus, M.B., Jiang, J., Gloster, T.M., Zandberg, W.F., Vocadlo, D.J., Walker, S. Description: Crystal structure of human...

New page

'''Unreleased structure'''

The entry 4gyw is ON HOLD

Authors: Lazarus, M.B., Jiang, J., Gloster, T.M., Zandberg, W.F., Vocadlo, D.J., Walker, S.

Description: Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide