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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:O75925 (3 hits) x


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  Domain hiding  Altered binding specificity  Motif hiding  Composite binding site formation
  Uncategorised  Rheostatic  Allostery  Avidity-sensing
  Physicochemical compatibility  Pre-translational  Competition

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E3 SUMO-protein ligase PIAS1


MotifStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

E3 SUMO-protein ligase PIAS1 - PIAS1 -  Homo sapiens
LIG_SUMO_SBM_1457461BinaryPhysicochemical compatibilityPhosphorylation of S466 and S467 and S468 in the SUMO-binding motif of E3 SUMO-protein ligase PIAS1 (PIAS1) by CK2 subfamily and CK2 subfamily and CK2 subfamily increases the strength of its interaction with Small ubiquitin-related modifier 1 (SUMO1).
details
LIG_SUMO_SBM_1457461BinaryPhysicochemical compatibilityAcetylation of K33 in Small ubiquitin-related modifier 2 (SUMO2) inhibits binding to E3 SUMO-protein ligase PIAS1 (PIAS1). 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_1457461BinaryPhysicochemical compatibilityAcetylation of K37 in Small ubiquitin-related modifier 1 (SUMO1) inhibits binding to E3 SUMO-protein ligase PIAS1 (PIAS1). The acetylation counters SUMO-SIM-dependent transcriptional repression processes. Acetylation is countered by Histone deacetylase family, HD type 1 subfamily.
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