1u9a

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[[Image:1u9a.gif|left|200px]]
 
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==HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9==
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The line below this paragraph, containing "STRUCTURE_1u9a", creates the "Structure Box" on the page.
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<StructureSection load='1u9a' size='340' side='right'caption='[[1u9a]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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&#8491;</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=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>
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{{STRUCTURE_1u9a| PDB=1u9a | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/u9/1u9a_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1u9a ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9'''
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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<ref>PMID:9261152</ref>
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==Overview==
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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.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1U9A is a [[Single protein]] structure of sequence from [http://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].
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</div>
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<div class="pdbe-citations 1u9a" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9261152 9261152]
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*[[SUMO conjugating enzyme Ubc9|SUMO conjugating enzyme Ubc9]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Bernards R]]
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[[Category: Ubiquitin--protein ligase]]
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[[Category: Hateboer G]]
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[[Category: Bernards, R.]]
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[[Category: Perrakis A]]
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[[Category: Hateboer, G.]]
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[[Category: Sixma TK]]
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[[Category: Perrakis, A.]]
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[[Category: Tong H]]
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[[Category: Sixma, T K.]]
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[[Category: Tong, H.]]
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[[Category: Cell cycle control]]
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[[Category: Ligase]]
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[[Category: Ubiquitin-conjugating enzyme]]
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[[Category: Ubiquitin-directed proteolysis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:55:31 2008''
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Current revision

HUMAN UBIQUITIN-CONJUGATING ENZYME UBC9

PDB ID 1u9a

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