About Help Definitions Submit Search Analyse Browse Home


Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:O75928 (2 hits) x


x  Coloured by switch type.
  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

x  Index
E3 SUMO-protein ligase PIAS2


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

E3 SUMO-protein ligase PIAS2 - PIAS2 -  Homo sapiens
LIG_SUMO_SBM_1467471BinaryPhysicochemical compatibilityAcetylation of K33 in Small ubiquitin-related modifier 2 (SUMO2) inhibits binding to E3 SUMO-protein ligase PIAS2 (PIAS2). The acetylation counters SUMO-SIM-dependent transcriptional repression processes. An additional interaction is also possible upon acetylation with the Bromodomain of p300 shown to bind the acetylated version of SUMO2. This does not occur with acetylated SUMO1. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
details
LIG_SUMO_SBM_1467471BinaryPhysicochemical compatibilityAcetylation of K37 in Small ubiquitin-related modifier 1 (SUMO1) inhibits binding to E3 SUMO-protein ligase PIAS2 (PIAS2). The acetylation counters SUMO-SIM-dependent transcriptional repression processes. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
details
           
Please send any suggestions/comments to: switches@elm.eu.org