5ghc: Difference between revisions
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==SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2== | |||
<StructureSection load='5ghc' size='340' side='right'caption='[[5ghc]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ghc]] 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=5GHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GHC 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></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=5ghc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ghc OCA], [https://pdbe.org/5ghc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ghc RCSB], [https://www.ebi.ac.uk/pdbsum/5ghc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ghc 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> | |||
==See Also== | |||
*[[SUMO 3D Structures|SUMO 3D Structures]] | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: Huang | __TOC__ | ||
[[Category: Naik | </StructureSection> | ||
[[Category: Naik | [[Category: Homo sapiens]] | ||
[[Category: Shih | [[Category: Large Structures]] | ||
[[Category: Huang T]] | |||
[[Category: Naik MT]] | |||
[[Category: Naik N]] | |||
[[Category: Shih H]] | |||
Latest revision as of 14:31, 2 August 2023
SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2
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] See AlsoReferences
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