Curated Information
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Home > Curated Information Page > PubMed Id: 10617621
Kharbanda S, et al. (2000) Translocation of SAPK/JNK to mitochondria and interaction with Bcl-x(L) in response to DNA damage. J Biol Chem 275, 322-7 10617621
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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T47-p - Bcl-xL (human)
Modsite: GTESEMEtPsAINGN SwissProt Entrez-Gene
Orthologous residues
Bcl‑xL (human): T47‑p, Bcl‑xL (mouse): T47‑p, Bcl‑xL (rat): T47‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis, phosphopeptide mapping
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), U-937 (myeloid)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE JNK2 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE JNK1 (human) transfection of inactive enzyme, transfection of wild-type enzyme, co-immunoprecipitation

T115-p - Bcl-xL (human)
Modsite: LTSQLHItPGTAYQS SwissProt Entrez-Gene
Orthologous residues
Bcl‑xL (human): T115‑p, Bcl‑xL (mouse): T115‑p, Bcl‑xL (rat): T115‑p
Characterization
Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phosphoamino acid analysis, phosphopeptide mapping
Relevant cell lines - cell types - tissues:  HEK293T (epithelial), U-937 (myeloid)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE JNK2 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE JNK1 (human) transfection of inactive enzyme, transfection of wild-type enzyme, co-immunoprecipitation