Curated Information
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Home > Curated Information Page > PubMed Id: 30962349
Gkotinakou IM, Befani C, Simos G, Liakos P (2019) ERK1/2 phosphorylates HIF-2α and regulates its activity by controlling its CRM1-dependent nuclear shuttling. J Cell Sci 132 30962349
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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S672-p - HIF2A (human)
Modsite: APLGPPVsPPHVSTF SwissProt Entrez-Gene
Orthologous residues
HIF2A (human): S672‑p, HIF2A (mouse): A676‑p, HIF2A (rat): T676‑p
Characterization
Methods used to characterize site in vivo [32P] ATP in vitro, immunoprecipitation, mutation of modification site, western blotting
Disease tissue studied:  liver cancer, hepatocellular carcinoma
Relevant cell lines - cell types - tissues:  E.coli (bacterial), HeLa (cervical), Huh7 (hepatic)
Cellular systems studied:  cell lines
Species studied:  bacteria, human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
KINASE ERK1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK1 (human) pharmacological inhibitor of upstream enzyme
KINASE ERK2 (human) pharmacological inhibitor of upstream enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
U0126 decrease
Downstream Regulation
Effect of modification (function):  intracellular localization, molecular association, regulation
Effect of modification (process):  transcription, induced
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Exportin-1 (human) Disrupts co-immunoprecipitation
Comments:  inhibition of CRM1-dependent nuclear export