1ca9: Difference between revisions

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<StructureSection load='1ca9' size='340' side='right'caption='[[1ca9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1ca9' size='340' side='right'caption='[[1ca9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ca9]] is a 8 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=1CA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CA9 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ca9]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CA9 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=1ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ca9 OCA], [http://pdbe.org/1ca9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ca9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ca9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ca9 ProSAT]</span></td></tr>
</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=1ca9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ca9 OCA], [https://pdbe.org/1ca9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ca9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ca9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ca9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN]] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref> <ref>PMID:11907583</ref> <ref>PMID:12917689</ref> <ref>PMID:15383523</ref> <ref>PMID:19506082</ref> <ref>PMID:19150425</ref> <ref>PMID:18981220</ref> <ref>PMID:19918265</ref> <ref>PMID:20064526</ref> <ref>PMID:19937093</ref> <ref>PMID:20047764</ref> <ref>PMID:20577214</ref> <ref>PMID:19810754</ref> <ref>PMID:20385093</ref>  [[http://www.uniprot.org/uniprot/TNR1B_HUMAN TNR1B_HUMAN]] Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity.<ref>PMID:14688072</ref> <ref>PMID:12370298</ref>   
[[https://www.uniprot.org/uniprot/TRAF2_HUMAN TRAF2_HUMAN]] Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain.<ref>PMID:10346818</ref> <ref>PMID:11907583</ref> <ref>PMID:12917689</ref> <ref>PMID:15383523</ref> <ref>PMID:19506082</ref> <ref>PMID:19150425</ref> <ref>PMID:18981220</ref> <ref>PMID:19918265</ref> <ref>PMID:20064526</ref> <ref>PMID:19937093</ref> <ref>PMID:20047764</ref> <ref>PMID:20577214</ref> <ref>PMID:19810754</ref> <ref>PMID:20385093</ref>  [[https://www.uniprot.org/uniprot/TNR1B_HUMAN TNR1B_HUMAN]] Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity.<ref>PMID:14688072</ref> <ref>PMID:12370298</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
*[[TNF receptor-associated factor|TNF receptor-associated factor]]
*[[TNF receptor-associated factor 3D structures|TNF receptor-associated factor 3D structures]]
== References ==
== References ==
<references/>
<references/>

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