Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.5.9.3
Powered by Cell Signaling Technology
Home > Curated Information Page > PubMed Id: 10702263
Van Linden AA, Cottin V, Leu C, Riches DW (2000) Phosphorylation of the membrane proximal region of tumor necrosis factor receptor CD120a (p55) at ERK consensus sites. J Biol Chem 275, 6996-7003 10702263
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
Download

T265-p - TNF-R1 (mouse)
Modsite: EKAGKPLtPAPsPAF SwissProt Entrez-Gene
Orthologous residues
TNF‑R1 (human): K265‑p, TNF‑R1 (mouse): T265‑p, TNF‑R1 (rat): K265‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site, phosphoamino acid analysis
Relevant cell lines - cell types - tissues:  COS (fibroblast), macrophage-bone marrow
Cellular systems studied:  cell lines, primary cultured cells
Species studied:  green monkey, mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (mouse)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) mutation in upstream enzyme recognition motif, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase

S269-p - TNF-R1 (mouse)
Modsite: KPLtPAPsPAFsPTS SwissProt Entrez-Gene
Orthologous residues
TNF‑R1 (human): N270‑p, TNF‑R1 (mouse): S269‑p, TNF‑R1 (rat): A270‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site, phosphoamino acid analysis
Relevant cell lines - cell types - tissues:  COS (fibroblast), macrophage-bone marrow
Cellular systems studied:  cell lines, primary cultured cells
Species studied:  green monkey, mouse
Comments:  Primary phosphorylation at T265 and S299 allowed the subsequent phosphorylation of S269 and S273, at lower levels.
Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (mouse)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) mutation in upstream enzyme recognition motif, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase

S273-p - TNF-R1 (mouse)
Modsite: PAPsPAFsPTSGFNP SwissProt Entrez-Gene
Orthologous residues
TNF‑R1 (human): S274‑p, TNF‑R1 (mouse): S273‑p, TNF‑R1 (rat): S276‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site, phosphoamino acid analysis
Relevant cell lines - cell types - tissues:  COS (fibroblast), macrophage-bone marrow
Cellular systems studied:  cell lines, primary cultured cells
Species studied:  green monkey, mouse
Comments:  Primary phosphorylation at T265 and S299 allowed the subsequent phosphorylation of S269 and S273, at lower levels.
Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (mouse)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) mutation in upstream enzyme recognition motif, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase

S299-p - TNF-R1 (mouse)
Modsite: PVSStPIsPIFGPSN SwissProt Entrez-Gene
Orthologous residues
TNF‑R1 (human): T300‑p, TNF‑R1 (mouse): S299‑p, TNF‑R1 (rat): S303‑p
Characterization
Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site, phosphoamino acid analysis
Relevant cell lines - cell types - tissues:  COS (fibroblast), macrophage-bone marrow
Cellular systems studied:  cell lines, primary cultured cells
Species studied:  green monkey, mouse
Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (mouse)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK2 (mouse) mutation in upstream enzyme recognition motif, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase