Curated Information
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Home > Curated Information Page > PubMed Id: 10652300
Yam CH, Siu WY, Lau A, Poon RY (2000) Degradation of cyclin A does not require its phosphorylation by CDC2 and cyclin-dependent kinase 2. J Biol Chem 275, 3158-67 10652300
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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S154-p - CCNA2 (human)
Modsite: PMDGSFEsPHTMDMS SwissProt Entrez-Gene
Orthologous residues
CCNA2 (human): S154‑p, CCNA2 (mouse): S145‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis
Relevant cell lines - cell types - tissues:  HeLa (cervical)
Cellular systems studied:  cell lines
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) phosphoaminoacid analysis, co-immunoprecipitation, modification site within consensus motif

T395-p - CCNE1 (human)
Modsite: PLPSGLLtPPQsGKK SwissProt Entrez-Gene
Orthologous residues
CCNE1 (human): T395‑p, CCNE1 (mouse): T393‑p, CCNE1 (rat): T396‑p
Characterization
Methods used to characterize site in vivo mutation of modification site
Relevant cell lines - cell types - tissues:  HeLa (cervical)
Cellular systems studied:  cell lines
Species studied:  human
Downstream Regulation
Effect of modification (function):  protein degradation