4r30 - Revision history

OCA at 17:43, 20 September 2023

OCA — Wed, 20 Sep 2023 17:43:22 GMT

←Older revision		Revision as of 17:43, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4r30]] 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=4R30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R30 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r30]] 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=4R30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R30 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.3Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [https://pdbe.org/4r30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [https://www.ebi.ac.uk/pdbsum/4r30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r30 ProSAT]</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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [https://pdbe.org/4r30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [https://www.ebi.ac.uk/pdbsum/4r30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r30 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 14:09, 22 February 2023

OCA — Wed, 22 Feb 2023 14:09:51 GMT

←Older revision		Revision as of 14:09, 22 February 2023
Line 3:		Line 3:
	<StructureSection load='4r30' size='340' side='right'caption='[[4r30]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4r30' size='340' side='right'caption='[[4r30]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r30]] 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=4R30 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4R30 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r30]] 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=4R30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R30 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPM2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [https://pdbe.org/4r30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [https://www.ebi.ac.uk/pdbsum/4r30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r30 ProSAT]</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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [~~http~~://pdbe.org/4r30 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4r30 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4r30 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN]] Lafora disease. The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN] Lafora disease. The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN]] Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.<ref>PMID:11001928</ref> <ref>PMID:11220751</ref> <ref>PMID:16901901</ref> <ref>PMID:18070875</ref> <ref>PMID:18617530</ref> <ref>PMID:19036738</ref> <ref>PMID:20453062</ref> <ref>PMID:23624058</ref>	+	[https://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN] Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.<ref>PMID:11001928</ref> <ref>PMID:11220751</ref> <ref>PMID:16901901</ref> <ref>PMID:18070875</ref> <ref>PMID:18617530</ref> <ref>PMID:19036738</ref> <ref>PMID:20453062</ref> <ref>PMID:23624058</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cingolani, G]]	+	[[Category: Cingolani G]]
-	[[Category: Koksal~~, A C~~]]	+	[[Category: Koksal AC]]
-	[[Category: Sankhala~~, R S]]~~	+	[[Category: Sankhala RS]]
-	~~[[Category: Dual specificity phosphatase]]~~	+
-	~~[[Category: Glucan phosphatase]]~~	+
-	~~[[Category: Glycogen]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Malin~~]]	+

OCA at 09:44, 1 May 2019

OCA — Wed, 01 May 2019 09:44:00 GMT

←Older revision		Revision as of 09:44, 1 May 2019
Line 1:		Line 1:

	==Structure of human laforin dual specificity phosphatase domain==		==Structure of human laforin dual specificity phosphatase domain==
-	<StructureSection load='4r30' size='340' side='right' caption='[[4r30]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='4r30' size='340' side='right'caption='[[4r30]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r30]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R30 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r30]] 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=4R30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R30 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">EPM2A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [http://pdbe.org/4r30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [http://www.ebi.ac.uk/pdbsum/4r30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r30 ProSAT]</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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [http://pdbe.org/4r30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [http://www.ebi.ac.uk/pdbsum/4r30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r30 ProSAT]</span></td></tr>
	</table>		</table>
Line 24:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Cingolani, G]]		[[Category: Cingolani, G]]
	[[Category: Koksal, A C]]		[[Category: Koksal, A C]]

OCA at 17:21, 18 January 2017

OCA — Wed, 18 Jan 2017 17:21:23 GMT

←Older revision		Revision as of 17:21, 18 January 2017
Line 1:		Line 1:
		+
	==Structure of human laforin dual specificity phosphatase domain==		==Structure of human laforin dual specificity phosphatase domain==
	<StructureSection load='4r30' size='340' side='right' caption='[[4r30]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='4r30' size='340' side='right' caption='[[4r30]], [[Resolution\|resolution]] 2.30Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4r30]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R30 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r30]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R30 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [http://www.ebi.ac.uk/pdbsum/4r30 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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [http://pdbe.org/4r30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [http://www.ebi.ac.uk/pdbsum/4r30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r30 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		Line 19:
	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 4r30" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:09, 7 January 2015

OCA — Wed, 07 Jan 2015 11:09:14 GMT

←Older revision		Revision as of 11:09, 7 January 2015
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN]] Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.<ref>PMID:11001928</ref> <ref>PMID:11220751</ref> <ref>PMID:16901901</ref> <ref>PMID:18070875</ref> <ref>PMID:18617530</ref> <ref>PMID:19036738</ref> <ref>PMID:20453062</ref> <ref>PMID:23624058</ref>		[[http://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN]] Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.<ref>PMID:11001928</ref> <ref>PMID:11220751</ref> <ref>PMID:16901901</ref> <ref>PMID:18070875</ref> <ref>PMID:18617530</ref> <ref>PMID:19036738</ref> <ref>PMID:20453062</ref> <ref>PMID:23624058</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The phosphatase laforin removes phosphate groups from glycogen during biosynthetic activity. Loss of function mutations in the gene encoding laforin is the predominant cause of Lafora disease (LD), a fatal form of progressive myoclonic epilepsy. Here, we used hybrid structural methods to determine the molecular architecture of human laforin. We found that laforin adopts a dimeric quaternary structure, topologically similar to the prototypical dual specificity phosphatase (DSP) VH1. The interface between laforin carbohydrate-binding module (CBM) and DSP domain generates an intimate substrate-binding crevice that allows for recognition and dephosphorylation of phosphomonoesters of glucose. We identify novel molecular determinants in laforin active site that help decipher the mechanism of glucan phosphatase activity.
		+
		+	Dimeric quaternary structure of human laforin.,Sankhala RS, Koksal AC, Ho L, Nitschke F, Minassian BA, Cingolani G J Biol Chem. 2014 Dec 23. pii: jbc.M114.627406. PMID:25538239<ref>PMID:25538239</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:52, 31 December 2014

OCA — Wed, 31 Dec 2014 14:52:48 GMT

←Older revision		Revision as of 14:52, 31 December 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Structure of human laforin dual specificity phosphatase domain==
-		+	<StructureSection load='4r30' size='340' side='right' caption='[[4r30]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~The entry~~ 4r30 is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4r30]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R30 FirstGlance]. <br>
-	~~Authors~~: ~~Sankhala, R~~.S.~~, Koksal, A~~.C.~~, Cingolani, G~~.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4r30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r30 RCSB], [http://www.ebi.ac.uk/pdbsum/4r30 PDBsum]</span></td></tr>
-	~~Description~~: ~~Structure of human laforin dual specificity phosphatase domain~~	+	</table>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	== Disease ==
-	[[~~Category~~: ~~Koksal, A~~.C]]	+	[[http://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN]] Lafora disease. The disease is caused by mutations affecting the gene represented in this entry.
-	[[~~Category~~: ~~Sankhala, R~~.S]]	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/EPM2A_HUMAN EPM2A_HUMAN]] Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.<ref>PMID:11001928</ref> <ref>PMID:11220751</ref> <ref>PMID:16901901</ref> <ref>PMID:18070875</ref> <ref>PMID:18617530</ref> <ref>PMID:19036738</ref> <ref>PMID:20453062</ref> <ref>PMID:23624058</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Cingolani, G]]		[[Category: Cingolani, G]]
		+	[[Category: Koksal, A C]]
		+	[[Category: Sankhala, R S]]
		+	[[Category: Dual specificity phosphatase]]
		+	[[Category: Glucan phosphatase]]
		+	[[Category: Glycogen]]
		+	[[Category: Hydrolase]]
		+	[[Category: Malin]]

OCA at 16:25, 24 December 2014

OCA — Wed, 24 Dec 2014 16:25:08 GMT

←Older revision		Revision as of 16:25, 24 December 2014
Line 6:		Line 6:

	Description: Structure of human laforin dual specificity phosphatase domain		Description: Structure of human laforin dual specificity phosphatase domain
		+	[[Category: Unreleased Structures]]
		+	[[Category: Koksal, A.C]]
		+	[[Category: Sankhala, R.S]]
		+	[[Category: Cingolani, G]]

OCA at 08:21, 24 September 2014

OCA — Wed, 24 Sep 2014 08:21:17 GMT

←Older revision		Revision as of 08:21, 24 September 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4r30 is ON HOLD	+	The entry 4r30 is ON HOLD until Paper Publication

	Authors: Sankhala, R.S., Koksal, A.C., Cingolani, G.		Authors: Sankhala, R.S., Koksal, A.C., Cingolani, G.

	Description: Structure of human laforin dual specificity phosphatase domain		Description: Structure of human laforin dual specificity phosphatase domain

OCA: Protected "4r30" [edit=sysop:move=sysop]

OCA — Wed, 20 Aug 2014 14:47:48 GMT

Protected "4r30" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:47, 20 August 2014

OCA: New page: '''Unreleased structure''' The entry 4r30 is ON HOLD Authors: Sankhala, R.S., Koksal, A.C., Cingolani, G. Description: Structure of human laforin dual specificity phosphatase domain

OCA — Wed, 20 Aug 2014 14:47:46 GMT

New page: '''Unreleased structure''' The entry 4r30 is ON HOLD Authors: Sankhala, R.S., Koksal, A.C., Cingolani, G. Description: Structure of human laforin dual specificity phosphatase domain

New page

'''Unreleased structure'''

The entry 4r30 is ON HOLD

Authors: Sankhala, R.S., Koksal, A.C., Cingolani, G.

Description: Structure of human laforin dual specificity phosphatase domain