Curated Information
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Home > Curated Information Page > PubMed Id: 16376875
Tarapore P, et al. (2006) Thr199 phosphorylation targets nucleophosmin to nuclear speckles and represses pre-mRNA processing. FEBS Lett 580, 399-409 16376875
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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T198-p - NPM1 (mouse)
Modsite: VKKsVRdtPAKNAQK SwissProt Entrez-Gene
Orthologous residues
NPM1 (human): T199‑p, NPM1 iso2 (human): , NPM1 iso3 (human): T199‑p, NPM1 (mouse): T198‑p, NPM1 (rat): T198‑p, NPM1 iso2 (rat): T198‑p
Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
Relevant cell lines - cell types - tissues:  fibroblast-skin
Cellular systems studied:  primary cultured cells
Species studied:  mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE CDK2 (human)
Comments:  CDK2/Cyclin E. Not phosphorylated by CK2 in vitro.
Downstream Regulation
Effect of modification (function):  intracellular localization
Effect of modification (process):  RNA splicing, altered
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Comments:  T198A no longer localizes to nuclear speckles (instead more across the nucleus and nucleolus). Phosphorylated NPM binds more RNA and represses pre-mRNA splicing in vitro.