Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.5.8
Powered by Cell Signaling Technology
Home > Curated Information Page > PubMed Id: 16738310
Deng X, et al. (2006) Bcl2's flexible loop domain regulates p53 binding and survival. Mol Cell Biol 26, 4421-34 16738310
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.
Information from this record has been curated, but not yet edited in PhosphoSitePlus® and may be incomplete.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
Download

T69-p - Bcl-2 (human)
Modsite: SRDPVARtsPLQtPA SwissProt Entrez-Gene
Orthologous residues
Bcl‑2 (human): T69‑p, Bcl‑2 (mouse): T69‑p, Bcl‑2 (rat): T69‑p
Characterization
Methods used to characterize site in vivo mutation of modification site
Disease tissue studied:  leukemia, lung cancer, non-small cell lung cancer
Relevant cell lines - cell types - tissues:  NCI-H1299 (pulmonary), NSF/N1.H7 (myeloid)
Cellular systems studied:  cell lines
Species studied:  human, mouse
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
cisplatin decrease
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  apoptosis, inhibited
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
BAX (mouse) Induces co-immunoprecipitation
p53 (mouse) Disrupts sequence-specific competitor, co-immunoprecipitation

S70-p - Bcl-2 (human)
Modsite: RDPVARtsPLQtPAA SwissProt Entrez-Gene
Orthologous residues
Bcl‑2 (human): S70‑p, Bcl‑2 (mouse): S70‑p, Bcl‑2 (rat): S70‑p
Characterization
Methods used to characterize site in vivo mutation of modification site
Disease tissue studied:  leukemia, lung cancer, non-small cell lung cancer
Relevant cell lines - cell types - tissues:  NCI-H1299 (pulmonary), NSF/N1.H7 (myeloid)
Cellular systems studied:  cell lines
Species studied:  human, mouse
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
cisplatin decrease
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  apoptosis, inhibited
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
p53 (mouse) Disrupts sequence-specific competitor, co-immunoprecipitation
BAX (mouse) Induces co-immunoprecipitation

S87-p - Bcl-2 (human)
Modsite: AAAGPALsPVPPVVH SwissProt Entrez-Gene
Orthologous residues
Bcl‑2 (human): S87‑p, Bcl‑2 (mouse): S84‑p, Bcl‑2 (rat): S84‑p
Characterization
Methods used to characterize site in vivo mutation of modification site
Disease tissue studied:  leukemia, lung cancer, non-small cell lung cancer
Relevant cell lines - cell types - tissues:  NCI-H1299 (pulmonary), NSF/N1.H7 (myeloid)
Cellular systems studied:  cell lines
Species studied:  human, mouse
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
cisplatin decrease
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Effect of modification (process):  apoptosis, inhibited
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
BAX (mouse) Induces co-immunoprecipitation
p53 (mouse) Disrupts sequence-specific competitor, co-immunoprecipitation