Curated Information
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Curated Information Page
PubMed Id: 9372912 
Deed RW, et al. (1997) Regulation of Id3 cell cycle function by Cdk-2-dependent phosphorylation. Mol Cell Biol 17, 6815-21 9372912
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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S5-p - ID3 (human)
Orthologous residues
ID3 (human): S5‑p, ID3 (mouse): S5‑p, ID3 (rat): S5‑p
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  B lymphocyte-spleen
 Cellular systems studied:  primary cells
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CDK2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CDK2 (human) pharmacological inhibitor of upstream enzyme
Downstream Regulation
 Effect of modification (process):  cell cycle regulation, transcription, altered
 Comments:  Cdk-dependent phosphorylation inactivates the G1-to-S cell cycle regulatory function of Id3 protein.

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