5ghc
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2== | |
| - | + | <StructureSection load='5ghc' size='340' side='right' caption='[[5ghc]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5ghc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GHC FirstGlance]. <br> | |
| - | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2n1w|2n1w]], [[5b7a|5b7a]], [[5ghd|5ghd]], [[5ghb|5ghb]]</td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SUMO2, SMT3B, SMT3H2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ghc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ghc OCA], [http://pdbe.org/5ghc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ghc RCSB], [http://www.ebi.ac.uk/pdbsum/5ghc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ghc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Huang, T]] | [[Category: Huang, T]] | ||
| - | [[Category: Naik, M | + | [[Category: Naik, M T]] |
[[Category: Naik, N]] | [[Category: Naik, N]] | ||
[[Category: Shih, H]] | [[Category: Shih, H]] | ||
| + | [[Category: Acetylated protein]] | ||
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Ubiquitin-like protein]] | ||
Revision as of 10:39, 16 November 2017
SOLUTION STRUCTURE OF LYS33 ACETYLATED HUMAN SUMO2
| |||||||||||
