6m2d
From Proteopedia
(Difference between revisions)
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==MUL1-RING domain== | ==MUL1-RING domain== | ||
| - | <StructureSection load='6m2d' size='340' side='right'caption='[[6m2d]]' scene=''> | + | <StructureSection load='6m2d' size='340' side='right'caption='[[6m2d]], [[Resolution|resolution]] 1.79Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M2D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6m2d]] is a 6 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=6M2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M2D FirstGlance]. <br> |
| - | </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=6m2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m2d OCA], [https://pdbe.org/6m2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m2d RCSB], [https://www.ebi.ac.uk/pdbsum/6m2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m2d ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUL1, C1orf166, GIDE, MAPL, MULAN, RNF218 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </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=6m2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m2d OCA], [https://pdbe.org/6m2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m2d RCSB], [https://www.ebi.ac.uk/pdbsum/6m2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m2d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/MUL1_HUMAN MUL1_HUMAN]] Exhibits weak E3 ubiquitin-protein ligase activity (PubMed:18591963, PubMed:19407830, PubMed:22410793). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (PubMed:18591963, PubMed:19407830, PubMed:22410793). Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation (PubMed:22410793). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (PubMed:19407830). Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization (PubMed:19407830, PubMed:18207745, PubMed:18213395). Likely to promote mitochondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway (PubMed:24898855). May also be involved in the sumoylation of the membrane fission protein DNM1L (PubMed:18207745, PubMed:19407830). Inhibits cell growth (PubMed:18591963, PubMed:22410793). When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (PubMed:23399697). Involved in the modulation of innate immune defense against viruses by inhibiting DDX58-dependent antiviral response (PubMed:23399697). Can mediate DDX58 sumoylation and disrupt its polyubiquitination (PubMed:23399697).<ref>PMID:18207745</ref> <ref>PMID:18213395</ref> <ref>PMID:18591963</ref> <ref>PMID:19407830</ref> <ref>PMID:22410793</ref> <ref>PMID:23399697</ref> <ref>PMID:24898855</ref> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chi S | + | [[Category: RING-type E3 ubiquitin transferase]] |
| - | [[Category: Lee | + | [[Category: Chi, S W]] |
| - | [[Category: Ryu | + | [[Category: Lee, S O]] |
| + | [[Category: Ryu, K S]] | ||
| + | [[Category: Mul1]] | ||
| + | [[Category: Structural protein]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:51, 14 April 2021
MUL1-RING domain
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