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Group by :Switch typeMotif classProteinEnzymePathway            Group Index    Colouring Info              Filtered: UNIPROT:Q00987 (4 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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DEG_MDM2_1TRG_NES_CRM1_2TRG_NLS_MonoExtC_3


ProteinStartEndSwitch TypeSwitch SubtypeSwitch DescriptionInformation

DEG_MDM2_1 - Motif found in p53 family members which confers binding to the N-terminal domain of MDM2.
P53_HUMAN1926BinaryPhysicochemical compatibilityPhosphorylation of Cellular tumor antigen p53 (TP53) on T18 (in vitro by Casein kinase I subfamily, requiring prior phosphorylation of S15) inhibits its binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). In vivo, T18 is phosphorylated in response to DNA damage.
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P53_HUMAN1926BinaryPre‑translationalAlternative promoter usage and alternative splicing removes the E3 ubiquitin ligase MDM2-binding motif of Cellular tumor antigen p53 (TP53), abrogating binding to E3 ubiquitin-protein ligase Mdm2 (MDM2). The splice variant without this motif is resistant to MDM2-mediated degradation, leading to a longer half-life.
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TRG_NES_CRM1_2 -
MDM2_HUMAN190202BinaryPre‑translationalAlternative splicing removes the nuclear export signal (NES) of E3 ubiquitin-protein ligase Mdm2 (MDM2), abrogating binding to Exportin-1 (XPO1).
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TRG_NLS_MonoExtC_3 - Monopartite variant of the classical basically charged NLS. C-extended version.
MDM2_HUMAN181187BinaryPre‑translationalAlternative splicing removes the nuclear localisation signal (NLS) of E3 ubiquitin-protein ligase Mdm2 (MDM2), abrogating binding to Importin subunit alpha-1 (KPNA1). The exclusion from the nucleus is not complete however, as another NLS (466-473) is speculated to target splice variants to the nucleus, however, to the annotator it seems more likely that splice variants can dimerise with full-length MDM2 and be simultaneously transported into nucleus.
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