6jxx
From Proteopedia
(Difference between revisions)
m (Protected "6jxx" [edit=sysop:move=sysop]) |
|||
Line 1: | Line 1: | ||
- | '''Unreleased structure''' | ||
- | + | ==SUMO2 bound to phosphorylated SLS4-SIM peptide from ICP0== | |
- | + | <StructureSection load='6jxx' size='340' side='right'caption='[[6jxx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6jxx]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JXX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JXX FirstGlance]. <br> | |
- | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | |
- | [[Category: | + | <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=6jxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jxx OCA], [http://pdbe.org/6jxx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jxx RCSB], [http://www.ebi.ac.uk/pdbsum/6jxx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jxx 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: Large Structures]] | ||
+ | [[Category: Das, R]] | ||
+ | [[Category: Hembram, D S.S]] | ||
+ | [[Category: Negi, H]] | ||
[[Category: Shet, D]] | [[Category: Shet, D]] | ||
- | [[Category: | + | [[Category: Phosphorylation]] |
- | [[Category: | + | [[Category: Protein binding-peptide complex]] |
- | [[Category: | + | [[Category: Protein-binding-peptide complex]] |
+ | [[Category: Sumoylation]] |
Revision as of 07:59, 5 February 2020
SUMO2 bound to phosphorylated SLS4-SIM peptide from ICP0
|