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5ghc
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5ghc is ON HOLD until Jun 19 2018 Authors: Naik, M.T., Naik, N., Shih, H., Huang, T. Description: SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==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]] | ||
Current revision
SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2
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Categories: Homo sapiens | Large Structures | Huang T | Naik MT | Naik N | Shih H
