5isg - Revision history

OCA at 14:07, 30 August 2023

OCA — Wed, 30 Aug 2023 14:07:54 GMT

←Older revision		Revision as of 14:07, 30 August 2023
Line 3:		Line 3:
	<StructureSection load='5isg' size='340' side='right'caption='[[5isg]], [[Resolution\|resolution]] 2.42Å' scene=''>		<StructureSection load='5isg' size='340' side='right'caption='[[5isg]], [[Resolution\|resolution]] 2.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5isg]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5ISG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5isg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ISG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6D6:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](3-AMINOPROPYL)AMINO}-5-DEOXYADENOSINE'>6D6</scene>, <scene name='pdbligand=DXE:1,2-DIMETHOXYETHANE'>DXE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.418Å</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Carm1, Prmt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6D6:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](3-AMINOPROPYL)AMINO}-5-DEOXYADENOSINE'>6D6</scene>, <scene name='pdbligand=DXE:1,2-DIMETHOXYETHANE'>DXE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_I_protein_arginine_methyltransferase Type I protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.319 2.1.1.319] </span></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=5isg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isg OCA], [https://pdbe.org/5isg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5isg RCSB], [https://www.ebi.ac.uk/pdbsum/5isg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5isg ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5isg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isg OCA], [~~http~~://pdbe.org/5isg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5isg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5isg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5isg ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CARM1_MOUSE CARM1_MOUSE]] Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.<ref>PMID:10381882</ref> <ref>PMID:11341840</ref> <ref>PMID:11701890</ref> <ref>PMID:11713257</ref> <ref>PMID:11983685</ref> <ref>PMID:11997499</ref> <ref>PMID:12756295</ref> <ref>PMID:14966289</ref> <ref>PMID:15186775</ref> <ref>PMID:15616592</ref> <ref>PMID:16322096</ref> <ref>PMID:17218272</ref> <ref>PMID:17882261</ref> <ref>PMID:18188184</ref> <ref>PMID:19843527</ref> <ref>PMID:19897492</ref> <ref>PMID:21138967</ref>	+	[https://www.uniprot.org/uniprot/CARM1_MOUSE CARM1_MOUSE] Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.<ref>PMID:10381882</ref> <ref>PMID:11341840</ref> <ref>PMID:11701890</ref> <ref>PMID:11713257</ref> <ref>PMID:11983685</ref> <ref>PMID:11997499</ref> <ref>PMID:12756295</ref> <ref>PMID:14966289</ref> <ref>PMID:15186775</ref> <ref>PMID:15616592</ref> <ref>PMID:16322096</ref> <ref>PMID:17218272</ref> <ref>PMID:17882261</ref> <ref>PMID:18188184</ref> <ref>PMID:19843527</ref> <ref>PMID:19897492</ref> <ref>PMID:21138967</ref>

	==See Also==		==See Also==
Line 19:		Line 18:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice]]~~	+	[[Category: Mus musculus]]
-	~~[[Category: Type I protein arginine methyltransferase~~]]	+	[[Category: Bonnefond L]]
-	[[Category: Bonnefond, L]]	+	[[Category: Cavarelli J]]
-	[[Category: Cavarelli, J]]	+	[[Category: Cura V]]
-	[[Category: Cura, V]]	+	[[Category: Hassenboehler P]]
-	[[Category: Hassenboehler, P]]	+	[[Category: Mailliot J]]
-	[[Category: Mailliot, J]]	+	[[Category: Marechal N]]
-	[[Category: Marechal, N]]	+	[[Category: Troffer-Charlier N]]
-	[[Category: Troffer-Charlier, N]]	+	[[Category: Wurtz JM]]
-	[[Category: Wurtz~~, J M]]~~	+
-	~~[[Category: Catalytic domain]]~~	+
-	~~[[Category: Chromatin regulator]]~~	+
-	~~[[Category: Mrna processing]]~~	+
-	~~[[Category: Mrna splicing]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Protein arginine methyltransferase]]~~	+
-	~~[[Category: S-adenosyl-l-methionine]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Transcription regulation]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 07:29, 3 June 2020

OCA — Wed, 03 Jun 2020 07:29:51 GMT

←Older revision		Revision as of 07:29, 3 June 2020
Line 1:		Line 1:

	==Crystal structure of mouse CARM1 in complex with inhibitor SA0707==		==Crystal structure of mouse CARM1 in complex with inhibitor SA0707==
-	<StructureSection load='5isg' size='340' side='right' caption='[[5isg]], [[Resolution\|resolution]] 2.42Å' scene=''>	+	<StructureSection load='5isg' size='340' side='right'caption='[[5isg]], [[Resolution\|resolution]] 2.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5isg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISG OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ISG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5isg]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ISG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6D6:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](3-AMINOPROPYL)AMINO}-5-DEOXYADENOSINE'>6D6</scene>, <scene name='pdbligand=DXE:1,2-DIMETHOXYETHANE'>DXE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6D6:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](3-AMINOPROPYL)AMINO}-5-DEOXYADENOSINE'>6D6</scene>, <scene name='pdbligand=DXE:1,2-DIMETHOXYETHANE'>DXE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Carm1, Prmt4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_I_protein_arginine_methyltransferase Type I protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.319 2.1.1.319] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_I_protein_arginine_methyltransferase Type I protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.319 2.1.1.319] </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=5isg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isg OCA], [http://pdbe.org/5isg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isg RCSB], [http://www.ebi.ac.uk/pdbsum/5isg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isg ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5isg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isg OCA], [http://pdbe.org/5isg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isg RCSB], [http://www.ebi.ac.uk/pdbsum/5isg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CARM1_MOUSE CARM1_MOUSE]] Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.<ref>PMID:10381882</ref> <ref>PMID:11341840</ref> <ref>PMID:11701890</ref> <ref>PMID:11713257</ref> <ref>PMID:11983685</ref> <ref>PMID:11997499</ref> <ref>PMID:12756295</ref> <ref>PMID:14966289</ref> <ref>PMID:15186775</ref> <ref>PMID:15616592</ref> <ref>PMID:16322096</ref> <ref>PMID:17218272</ref> <ref>PMID:17882261</ref> <ref>PMID:18188184</ref> <ref>PMID:19843527</ref> <ref>PMID:19897492</ref> <ref>PMID:21138967</ref>		[[http://www.uniprot.org/uniprot/CARM1_MOUSE CARM1_MOUSE]] Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.<ref>PMID:10381882</ref> <ref>PMID:11341840</ref> <ref>PMID:11701890</ref> <ref>PMID:11713257</ref> <ref>PMID:11983685</ref> <ref>PMID:11997499</ref> <ref>PMID:12756295</ref> <ref>PMID:14966289</ref> <ref>PMID:15186775</ref> <ref>PMID:15616592</ref> <ref>PMID:16322096</ref> <ref>PMID:17218272</ref> <ref>PMID:17882261</ref> <ref>PMID:18188184</ref> <ref>PMID:19843527</ref> <ref>PMID:19897492</ref> <ref>PMID:21138967</ref>
		+
		+	==See Also==
		+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Lk3 transgenic mice]]
	[[Category: Type I protein arginine methyltransferase]]		[[Category: Type I protein arginine methyltransferase]]
	[[Category: Bonnefond, L]]		[[Category: Bonnefond, L]]

OCA at 21:19, 15 March 2017

OCA — Wed, 15 Mar 2017 21:19:25 GMT

←Older revision		Revision as of 21:19, 15 March 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5isg is ~~ON HOLD until Paper Publication~~	+	==Crystal structure of mouse CARM1 in complex with inhibitor SA0707==
-		+	<StructureSection load='5isg' size='340' side='right' caption='[[5isg]], [[Resolution\|resolution]] 2.42Å' scene=''>
-	~~Authors~~: ~~Cura~~, V., ~~Marechal~~, N., ~~Mailliot~~, J., ~~Troffer~~-~~Charlier~~, N., ~~Hassenboehler~~, P., ~~Wurtz~~, J.M., ~~Bonnefond~~, L., ~~Cavarelli~~, J.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5isg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ISG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ISG FirstGlance]. <br>
-	~~Description~~: ~~Crystal structure of mouse CARM1 in complex with inhibitor SA0707~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6D6:5-{[(3S)-3-AMINO-3-CARBOXYPROPYL](3-AMINOPROPYL)AMINO}-5-DEOXYADENOSINE'>6D6</scene>, <scene name='pdbligand=DXE:1,2-DIMETHOXYETHANE'>DXE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_I_protein_arginine_methyltransferase Type I protein arginine methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.319 2.1.1.319] </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=5isg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5isg OCA], [http://pdbe.org/5isg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5isg RCSB], [http://www.ebi.ac.uk/pdbsum/5isg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5isg ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CARM1_MOUSE CARM1_MOUSE]] Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.<ref>PMID:10381882</ref> <ref>PMID:11341840</ref> <ref>PMID:11701890</ref> <ref>PMID:11713257</ref> <ref>PMID:11983685</ref> <ref>PMID:11997499</ref> <ref>PMID:12756295</ref> <ref>PMID:14966289</ref> <ref>PMID:15186775</ref> <ref>PMID:15616592</ref> <ref>PMID:16322096</ref> <ref>PMID:17218272</ref> <ref>PMID:17882261</ref> <ref>PMID:18188184</ref> <ref>PMID:19843527</ref> <ref>PMID:19897492</ref> <ref>PMID:21138967</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Type I protein arginine methyltransferase]]
		+	[[Category: Bonnefond, L]]
		+	[[Category: Cavarelli, J]]
		+	[[Category: Cura, V]]
		+	[[Category: Hassenboehler, P]]
	[[Category: Mailliot, J]]		[[Category: Mailliot, J]]
-	[[Category: ~~Cavarelli~~, J]]	+	[[Category: Marechal, N]]
	[[Category: Troffer-Charlier, N]]		[[Category: Troffer-Charlier, N]]
-	[[Category: ~~Bonnefond~~, L]]	+	[[Category: Wurtz, J M]]
-	[[Category: ~~Marechal, N~~]]	+	[[Category: Catalytic domain]]
-	[[Category: ~~Wurtz, J.M~~]]	+	[[Category: Chromatin regulator]]
-	[[Category: ~~Hassenboehler, P~~]]	+	[[Category: Mrna processing]]
-	[[Category: ~~Cura, V~~]]	+	[[Category: Mrna splicing]]
		+	[[Category: Nucleus]]
		+	[[Category: Protein arginine methyltransferase]]
		+	[[Category: S-adenosyl-l-methionine]]
		+	[[Category: Transcription]]
		+	[[Category: Transcription regulation]]
		+	[[Category: Transferase]]

OCA at 09:40, 9 March 2017

OCA — Thu, 09 Mar 2017 09:40:01 GMT

←Older revision		Revision as of 09:40, 9 March 2017
Line 9:		Line 9:
	[[Category: Mailliot, J]]		[[Category: Mailliot, J]]
	[[Category: Cavarelli, J]]		[[Category: Cavarelli, J]]
		+	[[Category: Troffer-Charlier, N]]
	[[Category: Bonnefond, L]]		[[Category: Bonnefond, L]]
	[[Category: Marechal, N]]		[[Category: Marechal, N]]
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	[[Category: Hassenboehler, P]]		[[Category: Hassenboehler, P]]
	[[Category: Cura, V]]		[[Category: Cura, V]]
-	[[Category: Troffer-Charlier, N]]

OCA: Protected "5isg" [edit=sysop:move=sysop]

OCA — Wed, 11 May 2016 00:51:43 GMT

Protected "5isg" [edit=sysop:move=sysop]

←Older revision

Revision as of 00:51, 11 May 2016

OCA: New page: '''Unreleased structure''' The entry 5isg is ON HOLD until Paper Publication Authors: Cura, V., Marechal, N., Mailliot, J., Troffer-Charlier, N., Hassenboehler, P., Wurtz, J.M., Bonnefo...

OCA — Wed, 11 May 2016 00:51:42 GMT

New page: '''Unreleased structure''' The entry 5isg is ON HOLD until Paper Publication Authors: Cura, V., Marechal, N., Mailliot, J., Troffer-Charlier, N., Hassenboehler, P., Wurtz, J.M., Bonnefo...

New page

'''Unreleased structure'''

The entry 5isg is ON HOLD until Paper Publication

Authors: Cura, V., Marechal, N., Mailliot, J., Troffer-Charlier, N., Hassenboehler, P., Wurtz, J.M., Bonnefond, L., Cavarelli, J.

Description: Crystal structure of mouse CARM1 in complex with inhibitor SA0707
[[Category: Unreleased Structures]]
[[Category: Mailliot, J]]
[[Category: Cavarelli, J]]
[[Category: Bonnefond, L]]
[[Category: Marechal, N]]
[[Category: Wurtz, J.M]]
[[Category: Hassenboehler, P]]
[[Category: Cura, V]]
[[Category: Troffer-Charlier, N]]