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| | <StructureSection load='2vrr' size='340' side='right'caption='[[2vrr]], [[Resolution|resolution]] 2.22Å' scene=''> | | <StructureSection load='2vrr' size='340' side='right'caption='[[2vrr]], [[Resolution|resolution]] 2.22Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2vrr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2vrr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VRR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.22Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a5r|1a5r]], [[2asq|2asq]], [[2uyz|2uyz]], [[2bf8|2bf8]], [[1u9a|1u9a]], [[2iy1|2iy1]], [[1tgz|1tgz]], [[1z5s|1z5s]], [[2iy0|2iy0]], [[1wyw|1wyw]], [[1u9b|1u9b]], [[2io2|2io2]], [[1y8r|1y8r]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </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=2vrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrr OCA], [https://pdbe.org/2vrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrr RCSB], [https://www.ebi.ac.uk/pdbsum/2vrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrr 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=2vrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vrr OCA], [https://pdbe.org/2vrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vrr RCSB], [https://www.ebi.ac.uk/pdbsum/2vrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vrr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/UBC9_MOUSE UBC9_MOUSE]] Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).<ref>PMID:16326389</ref> <ref>PMID:17187077</ref>
| + | [https://www.uniprot.org/uniprot/UBC9_MOUSE UBC9_MOUSE] Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).<ref>PMID:16326389</ref> <ref>PMID:17187077</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Ubiquitin--protein ligase]]
| + | [[Category: Fish A]] |
| - | [[Category: Dijk, W J.van]]
| + | [[Category: Flotho A]] |
| - | [[Category: Fish, A]] | + | [[Category: Johnson ES]] |
| - | [[Category: Flotho, A]] | + | [[Category: Klug H]] |
| - | [[Category: Johnson, E S]] | + | [[Category: Knipscheer P]] |
| - | [[Category: Klug, H]] | + | [[Category: Mann M]] |
| - | [[Category: Knipscheer, P]] | + | [[Category: Olsen JV]] |
| - | [[Category: Mann, M]] | + | [[Category: Pichler A]] |
| - | [[Category: Olsen, J V]] | + | [[Category: Sixma TK]] |
| - | [[Category: Pichler, A]] | + | [[Category: Van Dijk WJ]] |
| - | [[Category: Sixma, T K]] | + | |
| - | [[Category: Cell cycle]] | + | |
| - | [[Category: Cell cycle-ligase complex]]
| + | |
| - | [[Category: Cell cycle/ligase]]
| + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Chromosome partition]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Developmental protein]]
| + | |
| - | [[Category: E2]]
| + | |
| - | [[Category: Host-virus interaction]]
| + | |
| - | [[Category: Isopeptide bond]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Mitosis]]
| + | |
| - | [[Category: Modification]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Posttranslational modification]]
| + | |
| - | [[Category: Sumo]]
| + | |
| - | [[Category: Ubc9]]
| + | |
| - | [[Category: Ubiquitin like molecule]]
| + | |
| - | [[Category: Ubl conjugation pathway]]
| + | |
| Structural highlights
Function
UBC9_MOUSE Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2 or CBX4. Can catalyze the formation of poly-SUMO chains. Essential for nuclear architecture, chromosome segregation and embryonic viability. Necessary for sumoylation of FOXL2 and KAT5 (By similarity).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Posttranslational modification with small ubiquitin-related modifier, SUMO, is a widespread mechanism for rapid and reversible changes in protein function. Considering the large number of known targets, the number of enzymes involved in modification seems surprisingly low: a single E1, a single E2, and a few distinct E3 ligases. Here we show that autosumoylation of the mammalian E2-conjugating enzyme Ubc9 at Lys14 regulates target discrimination. While not altering its activity toward HDAC4, E2-25K, PML, or TDG, sumoylation of Ubc9 impairs its activity on RanGAP1 and strongly activates sumoylation of the transcriptional regulator Sp100. Enhancement depends on a SUMO-interacting motif (SIM) in Sp100 that creates an additional interface with the SUMO conjugated to the E2, a mechanism distinct from Ubc9 approximately SUMO thioester recruitment. The crystal structure of sumoylated Ubc9 demonstrates how the newly created binding interface can provide a gain in affinity otherwise provided by E3 ligases.
Ubc9 sumoylation regulates SUMO target discrimination.,Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK, Pichler A Mol Cell. 2008 Aug 8;31(3):371-82. PMID:18691969[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Nacerddine K, Lehembre F, Bhaumik M, Artus J, Cohen-Tannoudji M, Babinet C, Pandolfi PP, Dejean A. The SUMO pathway is essential for nuclear integrity and chromosome segregation in mice. Dev Cell. 2005 Dec;9(6):769-79. PMID:16326389 doi:S1534-5807(05)00389-8
- ↑ Park SW, Hu X, Gupta P, Lin YP, Ha SG, Wei LN. SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells. Nat Struct Mol Biol. 2007 Jan;14(1):68-75. Epub 2006 Dec 24. PMID:17187077 doi:10.1038/nsmb1185
- ↑ Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK, Pichler A. Ubc9 sumoylation regulates SUMO target discrimination. Mol Cell. 2008 Aug 8;31(3):371-82. PMID:18691969 doi:10.1016/j.molcel.2008.05.022
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