Curated Information
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Home > Curated Information Page > PubMed Id: 29348869
Chan JV, et al. (2017) Role of the N-terminal lid in regulating the interaction of phosphorylated MDMX with p53. Oncotarget 8, 112825-112840 29348869
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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Y55-p - MDM4 (human)
Modsite: TVKEVMHyLGQYIMV SwissProt Entrez-Gene
Orthologous residues
MDM4 (human): Y55‑p, MDM4 iso5 (human): Y55‑p, MDM4 (mouse): Y55‑p, MDM4 (rat): Y56‑p
Downstream Regulation
Effect of modification (function):  molecular association, regulation, protein conformation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
53BP1 (human) Induces

Y99-p - MDM4 (human)
Modsite: VkDPsPLyDMLRKNL SwissProt Entrez-Gene
Orthologous residues
MDM4 (human): Y99‑p, MDM4 iso5 (human): Y99‑p, MDM4 (mouse): Y99‑p, MDM4 (rat): Y100‑p
Downstream Regulation
Effect of modification (function):  molecular association, regulation, protein conformation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
53BP1 (human) Disrupts NMR spectroscopy