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New page: left|200px<br /> <applet load="2awt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2awt" /> '''Solution Structure of Human Small Ubiquitin... |
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== | ==Solution Structure of Human Small Ubiquitin-Like Modifier Protein Isoform 2 (SUMO-2)== | ||
<StructureSection load='2awt' size='340' side='right'caption='[[2awt]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2awt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AWT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2awt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2awt OCA], [https://pdbe.org/2awt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2awt RCSB], [https://www.ebi.ac.uk/pdbsum/2awt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2awt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SUMO2_HUMAN SUMO2_HUMAN] Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.<ref>PMID:9556629</ref> <ref>PMID:18538659</ref> <ref>PMID:18408734</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/2awt_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=2awt ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[SUMO 3D Structures|SUMO 3D Structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chang | [[Category: Chang CF]] | ||
[[Category: Chang | [[Category: Chang CK]] | ||
[[Category: Chung | [[Category: Chung TL]] | ||
[[Category: Huang | [[Category: Huang TH]] | ||
[[Category: Li | [[Category: Li SSL]] | ||
[[Category: Wang | [[Category: Wang YH]] | ||
Latest revision as of 14:18, 22 May 2024
Solution Structure of Human Small Ubiquitin-Like Modifier Protein Isoform 2 (SUMO-2)Solution Structure of Human Small Ubiquitin-Like Modifier Protein Isoform 2 (SUMO-2)
Structural highlights
FunctionSUMO2_HUMAN Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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