5sxp - Revision history

OCA at 12:50, 4 October 2023

2023-10-04T12:50:21Z

←Older revision		Revision as of 12:50, 4 October 2023
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	<StructureSection load='5sxp' size='340' side='right'caption='[[5sxp]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='5sxp' size='340' side='right'caption='[[5sxp]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5sxp]] is a 6 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=5SXP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5SXP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5sxp]] is a 6 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=5SXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SXP FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~ARHGEF7~~, ~~COOL1, KIAA0142, P85SPR, PAK3BP, PIXB, Nbla10314 (~~[~~http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN~~]~~), ITCH ([http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</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]] 1.65Å</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=5sxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sxp OCA], [~~http~~://pdbe.org/5sxp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5sxp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5sxp PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5sxp 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=5sxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sxp OCA], [https://pdbe.org/5sxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5sxp RCSB], [https://www.ebi.ac.uk/pdbsum/5sxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5sxp ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[http://www.uniprot.org/uniprot/ITCH_HUMAN ITCH_HUMAN]] Defects in ITCH are the cause of syndromic multisystem autoimmune disease (SMAD) [MIM:[http://omim.org/entry/613385 613385]]. SMAD is characterized by organomegaly, failure to thrive, developmental delay, dysmorphic features and autoimmune inflammatory cell infiltration of the lungs, liver and gut.<ref>PMID:20170897</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/ARHG7_HUMAN ARHG7_HUMAN]] Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons.<ref>PMID:19041750</ref> <ref>PMID:18716323</ref> <ref>PMID:18184567</ref> [[http://www.uniprot.org/uniprot/ITCH_HUMAN ITCH_HUMAN]] Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination.<ref>PMID:14602072</ref> <ref>PMID:17028573</ref> <ref>PMID:16387660</ref> <ref>PMID:18718448</ref> <ref>PMID:18718449</ref> <ref>PMID:18628966</ref> <ref>PMID:19592251</ref> <ref>PMID:19131965</ref> <ref>PMID:19881509</ref> <ref>PMID:20392206</ref> <ref>PMID:20068034</ref>	+	[https://www.uniprot.org/uniprot/ARHG7_HUMAN ARHG7_HUMAN] Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons.<ref>PMID:19041750</ref> <ref>PMID:18716323</ref> <ref>PMID:18184567</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 5sxp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5sxp" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Rho guanine nucleotide exchange factor 3D structures\|Rho guanine nucleotide exchange factor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Angers, A]]	+	[[Category: Angers A]]
-	[[Category: Cappadocia, L]]	+	[[Category: Cappadocia L]]
-	[[Category: Desrochers, G]]	+	[[Category: Desrochers G]]
-	[[Category: Lussier-Price, M]]	+	[[Category: Lussier-Price M]]
-	[[Category: Omichinski~~, J G]]~~	+	[[Category: Omichinski JG]]
-	~~[[Category: Ligase]]~~	+
-	~~[[Category: Sh3 domain peptide ligand complex]]~~	+
-	~~[[Category: Signaling protein-ligase complex~~]]	+

OCA at 08:14, 8 January 2020

2020-01-08T08:14:03Z

←Older revision		Revision as of 08:14, 8 January 2020
Line 1:		Line 1:

	==STRUCTURAL BASIS FOR THE INTERACTION BETWEEN ITCH PRR AND BETA-PIX==		==STRUCTURAL BASIS FOR THE INTERACTION BETWEEN ITCH PRR AND BETA-PIX==
-	<StructureSection load='5sxp' size='340' side='right' caption='[[5sxp]], [[Resolution\|resolution]] 1.65Å' scene=''>	+	<StructureSection load='5sxp' size='340' side='right'caption='[[5sxp]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5sxp]] is a 6 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=5SXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SXP FirstGlance]. <br>		<table><tr><td colspan='2'>[[5sxp]] is a 6 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=5SXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SXP FirstGlance]. <br>
Line 20:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 5sxp" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5sxp" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Rho guanine nucleotide exchange factor 3D structures\|Rho guanine nucleotide exchange factor 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 25:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Angers, A]]		[[Category: Angers, A]]
	[[Category: Cappadocia, L]]		[[Category: Cappadocia, L]]

OCA at 14:18, 6 November 2017

2017-11-06T14:18:50Z

←Older revision		Revision as of 14:18, 6 November 2017
Line 3:		Line 3:
	<StructureSection load='5sxp' size='340' side='right' caption='[[5sxp]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='5sxp' size='340' side='right' caption='[[5sxp]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5sxp]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SXP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5sxp]] is a 6 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=5SXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SXP FirstGlance]. <br>
-	</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=5sxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sxp OCA], [http://pdbe.org/5sxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sxp RCSB], [http://www.ebi.ac.uk/pdbsum/5sxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sxp ProSAT]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ARHGEF7, COOL1, KIAA0142, P85SPR, PAK3BP, PIXB, Nbla10314 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ITCH ([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=5sxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sxp OCA], [http://pdbe.org/5sxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sxp RCSB], [http://www.ebi.ac.uk/pdbsum/5sxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sxp ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Angers, A]]		[[Category: Angers, A]]
	[[Category: Cappadocia, L]]		[[Category: Cappadocia, L]]

OCA at 13:38, 15 March 2017

2017-03-15T13:38:09Z

←Older revision		Revision as of 13:38, 15 March 2017
Line 10:		Line 10:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/ARHG7_HUMAN ARHG7_HUMAN]] Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons.<ref>PMID:19041750</ref> <ref>PMID:18716323</ref> <ref>PMID:18184567</ref> [[http://www.uniprot.org/uniprot/ITCH_HUMAN ITCH_HUMAN]] Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination.<ref>PMID:14602072</ref> <ref>PMID:17028573</ref> <ref>PMID:16387660</ref> <ref>PMID:18718448</ref> <ref>PMID:18718449</ref> <ref>PMID:18628966</ref> <ref>PMID:19592251</ref> <ref>PMID:19131965</ref> <ref>PMID:19881509</ref> <ref>PMID:20392206</ref> <ref>PMID:20068034</ref>		[[http://www.uniprot.org/uniprot/ARHG7_HUMAN ARHG7_HUMAN]] Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons.<ref>PMID:19041750</ref> <ref>PMID:18716323</ref> <ref>PMID:18184567</ref> [[http://www.uniprot.org/uniprot/ITCH_HUMAN ITCH_HUMAN]] Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination.<ref>PMID:14602072</ref> <ref>PMID:17028573</ref> <ref>PMID:16387660</ref> <ref>PMID:18718448</ref> <ref>PMID:18718449</ref> <ref>PMID:18628966</ref> <ref>PMID:19592251</ref> <ref>PMID:19131965</ref> <ref>PMID:19881509</ref> <ref>PMID:20392206</ref> <ref>PMID:20068034</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The ligase Itch plays major roles in signalling pathways by inducing ubiquitylation-dependent degradation of several substrates. Substrate recognition and binding is critical for the regulation of this reaction. Like closely related ligases, Itch can interact with proteins containing a PPxY motif via its WW domains. In addition to these WW domains, Itch possesses a proline-rich region (PRR) that has been shown to interact with several Src Homology 3 (SH3) domain-containing proteins. We have previously established that despite the apparent surface uniformity and conserved fold of SH3 domains, they display different binding mechanisms and affinities for their interaction with the PRR of Itch. Here, we attempt to determine the molecular bases underlying the wide range of binding properties of the Itch PRR. Using pull-down assays combined with mass spectrometry analysis, we show that the Itch PRR preferentially forms complexes with Endophilins, Amphyphisins and Pacsins, but can also target a variety of other SH3 domain-containing proteins. In addition, we map the binding sites of these proteins using a combination of PRR sub-sequences and mutants. We find that different SH3 domains target distinct proline-rich sequences overlapping significantly. We also structurally analyze these protein complexes using crystallography and molecular modelling. These structures depict the position of Itch PRR engaged in a 1:2 protein complex with beta-PIX and a 1:1 complex with the other SH3 domain-containing proteins. Taken together, these results reveal the binding preferences of the Itch PRR towards its most common SH3 domain-containing partners, and demonstrate that the PRR region is sufficient for binding.
		+
		+	Molecular Basis of Interactions Between SH3 Domain-Containing Proteins and the Proline-Rich Region of the Ubiquitin Ligase Itch.,Desrochers G, Cappadocia L, Lussier-Price M, Ton AT, Ayoubi R, Serohijos A, Omichinski JG, Angers A J Biol Chem. 2017 Feb 24. pii: jbc.M116.754440. doi: 10.1074/jbc.M116.754440. PMID:28235806<ref>PMID:28235806</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5sxp" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:39, 11 March 2017

2017-03-11T09:39:32Z

←Older revision		Revision as of 09:39, 11 March 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5sxp is ~~ON HOLD~~ ~~until Paper Publication~~	+	==STRUCTURAL BASIS FOR THE INTERACTION BETWEEN ITCH PRR AND BETA-PIX==
-		+	<StructureSection load='5sxp' size='340' side='right' caption='[[5sxp]], [[Resolution\|resolution]] 1.65Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5sxp]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SXP FirstGlance]. <br>
-	~~Description~~:	+	</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=5sxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5sxp OCA], [http://pdbe.org/5sxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5sxp RCSB], [http://www.ebi.ac.uk/pdbsum/5sxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5sxp ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/ITCH_HUMAN ITCH_HUMAN]] Defects in ITCH are the cause of syndromic multisystem autoimmune disease (SMAD) [MIM:[http://omim.org/entry/613385 613385]]. SMAD is characterized by organomegaly, failure to thrive, developmental delay, dysmorphic features and autoimmune inflammatory cell infiltration of the lungs, liver and gut.<ref>PMID:20170897</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ARHG7_HUMAN ARHG7_HUMAN]] Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions (By similarity). May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade, promotes the formation of spines and synapses in hippocampal neurons.<ref>PMID:19041750</ref> <ref>PMID:18716323</ref> <ref>PMID:18184567</ref> [[http://www.uniprot.org/uniprot/ITCH_HUMAN ITCH_HUMAN]] Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation. It is involved in the control of inflammatory signaling pathways. Is an essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, TAX1BP1 and RNF11, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of the complex after TNF stimulation. Once the complex is formed, TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NFKB1. Ubiquitinates RIPK2 by 'Lys-63'-linked conjugation and influences NOD2-dependent signal transduction pathways. Regulates the transcriptional activity of several transcription factors, and probably plays an important role in the regulation of immune response. Ubiquitinates NFE2 by 'Lys-63' linkages and is implicated in the control of the development of hematopoietic lineages. Critical regulator of T-helper (TH2) cytokine development through its ability to induce JUNB ubiquitination and degradation (By similarity). Ubiquitinates SNX9. Ubiquitinates CXCR4 and HGS/HRS and regulates sorting of CXCR4 to the degradative pathway. It is involved in the negative regulation of MAVS-dependent cellular antiviral responses. Ubiquitinates MAVS through 'Lys-48'-linked conjugation resulting in MAVS proteasomal degradation. Involved in the regulation of apoptosis and reactive oxygen species levels through the ubiquitination and proteasomal degradation of TXNIP. Mediates the antiapoptotic activity of epidermal growth factor through the ubiquitination and proteasomal degradation of p15 BID. Targets DTX1 for lysosomal degradation and controls NOTCH1 degradation, in the absence of ligand, through 'Lys-29'-linked polyubiquitination.<ref>PMID:14602072</ref> <ref>PMID:17028573</ref> <ref>PMID:16387660</ref> <ref>PMID:18718448</ref> <ref>PMID:18718449</ref> <ref>PMID:18628966</ref> <ref>PMID:19592251</ref> <ref>PMID:19131965</ref> <ref>PMID:19881509</ref> <ref>PMID:20392206</ref> <ref>PMID:20068034</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Angers, A]]
		+	[[Category: Cappadocia, L]]
		+	[[Category: Desrochers, G]]
		+	[[Category: Lussier-Price, M]]
		+	[[Category: Omichinski, J G]]
		+	[[Category: Ligase]]
		+	[[Category: Sh3 domain peptide ligand complex]]
		+	[[Category: Signaling protein-ligase complex]]

OCA at 13:49, 14 September 2016

2016-09-14T13:49:05Z

←Older revision		Revision as of 13:49, 14 September 2016
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5sxp is ON HOLD	+	The entry 5sxp is ON HOLD until Paper Publication

	Authors:		Authors:

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

2016-09-09T15:23:42Z

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

←Older revision

Revision as of 15:23, 9 September 2016

OCA: New page: '''Unreleased structure''' The entry 5sxp is ON HOLD Authors: Description: Category: Unreleased Structures

2016-09-09T15:23:41Z

New page: '''Unreleased structure''' The entry 5sxp is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5sxp is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]