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| | <StructureSection load='1u9a' size='340' side='right'caption='[[1u9a]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1u9a' size='340' side='right'caption='[[1u9a]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1u9a]] is a 1 chain structure with sequence from [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=1U9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U9A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1u9a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U9A FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=1u9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9a OCA], [https://pdbe.org/1u9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u9a RCSB], [https://www.ebi.ac.uk/pdbsum/1u9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9a 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=1u9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9a OCA], [https://pdbe.org/1u9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u9a RCSB], [https://www.ebi.ac.uk/pdbsum/1u9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9a 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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Ubiquitin--protein ligase]]
| + | [[Category: Bernards R]] |
| - | [[Category: Bernards, R]] | + | [[Category: Hateboer G]] |
| - | [[Category: Hateboer, G]] | + | [[Category: Perrakis A]] |
| - | [[Category: Perrakis, A]] | + | [[Category: Sixma TK]] |
| - | [[Category: Sixma, T K]] | + | [[Category: Tong H]] |
| - | [[Category: Tong, H]] | + | |
| - | [[Category: Cell cycle control]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Ubiquitin-conjugating enzyme]]
| + | |
| - | [[Category: Ubiquitin-directed proteolysis]]
| + | |
| 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
Murine/human ubiquitin-conjugating enzyme Ubc9 is a functional homolog of Saccharomyces cerevisiae Ubc9 that is essential for the viability of yeast cells with a specific role in the G2-M transition of the cell cycle. The structure of recombinant mammalian Ubc9 has been determined from two crystal forms at 2.0 A resolution. Like Arabidopsis thaliana Ubc1 and S. cerevisiae Ubc4, murine/human Ubc9 was crystallized as a monomer, suggesting that previously reported hetero- and homo-interactions among Ubcs may be relatively weak or indirect. Compared with the known crystal structures of Ubc1 and Ubc4, which regulate different cellular processes, Ubc9 has a 5-residue insertion that forms a very exposed tight beta-hairpin and a 2-residue insertion that forms a bulge in a loop close to the active site. Mammalian Ubc9 also possesses a distinct electrostatic potential distribution that may provide possible clues to its remarkable ability to interact with other proteins. The 2-residue insertion and other sequence and structural heterogeneity observed at the catalytic site suggest that different Ubcs may utilize catalytic mechanisms of varying efficiency and substrate specificity.
Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system.,Tong H, Hateboer G, Perrakis A, Bernards R, Sixma TK J Biol Chem. 1997 Aug 22;272(34):21381-7. PMID:9261152[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
- ↑ Tong H, Hateboer G, Perrakis A, Bernards R, Sixma TK. Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system. J Biol Chem. 1997 Aug 22;272(34):21381-7. PMID:9261152
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