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2eqg

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==Solution structure of the first A20-type zinc finger domain from human tumor necrosis factor, alpha-induced protein3==
==Solution structure of the first A20-type zinc finger domain from human tumor necrosis factor, alpha-induced protein3==
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<StructureSection load='2eqg' size='340' side='right' caption='[[2eqg]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2eqg' size='340' side='right'caption='[[2eqg]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2eqg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EQG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2eqg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EQG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TNFAIP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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=2eqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eqg OCA], [http://pdbe.org/2eqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eqg RCSB], [http://www.ebi.ac.uk/pdbsum/2eqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eqg ProSAT], [http://www.topsan.org/Proteins/RSGI/2eqg TOPSAN]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eqg OCA], [https://pdbe.org/2eqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eqg RCSB], [https://www.ebi.ac.uk/pdbsum/2eqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eqg ProSAT], [https://www.topsan.org/Proteins/RSGI/2eqg TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TNAP3_HUMAN TNAP3_HUMAN]] Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, 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 NF-kappa-B. Deubiquinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system.<ref>PMID:8692885</ref> <ref>PMID:9299557</ref> <ref>PMID:9882303</ref> <ref>PMID:14748687</ref> <ref>PMID:15258597</ref> <ref>PMID:16684768</ref> <ref>PMID:18952128</ref> <ref>PMID:19494296</ref> <ref>PMID:22099304</ref> <ref>PMID:17961127</ref> <ref>PMID:18164316</ref>
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[https://www.uniprot.org/uniprot/TNAP3_HUMAN TNAP3_HUMAN] Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, 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 NF-kappa-B. Deubiquinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system.<ref>PMID:8692885</ref> <ref>PMID:9299557</ref> <ref>PMID:9882303</ref> <ref>PMID:14748687</ref> <ref>PMID:15258597</ref> <ref>PMID:16684768</ref> <ref>PMID:18952128</ref> <ref>PMID:19494296</ref> <ref>PMID:22099304</ref> <ref>PMID:17961127</ref> <ref>PMID:18164316</ref>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Hayahsi, F]]
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[[Category: Large Structures]]
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[[Category: Structural genomic]]
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[[Category: Hayahsi F]]
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[[Category: Yokoyama, S]]
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[[Category: Yokoyama S]]
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[[Category: Zhang, H P]]
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[[Category: Zhang HP]]
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[[Category: Alpha-induced protein 3]]
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[[Category: Hydrolase]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Putative dna-binding protein a20]]
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[[Category: Rsgi]]
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[[Category: Tumor necrosis factor]]
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[[Category: Zf-a20 domain]]
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[[Category: Zinc finger protein a20]]
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Current revision

Solution structure of the first A20-type zinc finger domain from human tumor necrosis factor, alpha-induced protein3

PDB ID 2eqg

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