Curated Information

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Curated Information Page

PubMed Id: 10066812

This page summarizes selected information from the article 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.

Haug LS, et al. (1999) Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cyclic nucleotide-dependent kinases in vitro and in rat cerebellar slices in situ. J Biol Chem 274, 7467-73 10066812

Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.

S1589-p - IP3R1 (rat)

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Orthologous residues

IP3R1 (human): S1598‑p, IP3R1 iso3 (human): S1589‑p, IP3R1 (mouse): S1588‑p, IP3R1 iso2 (mouse): S1573‑p, IP3R1 (rat): S1589‑p

Characterization

Methods used to characterize site in vivo: [32P] bio-synthetic labeling, back-titration, phosphopeptide mapping

Relevant cell lines - cell types - tissues: 'brain, cerebellum'

Cellular systems studied: tissue

Species studied: rat

Enzymes shown to modify site in vitro:

Type	Enzyme
KINASE	PKACa (human)
KINASE	PKG1 (human)

Upstream Regulation

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Manipulated Protein	Referenced Protein	Effect	Notes
cAMP analog				increase
cGMP analog				increase

S1756-p - IP3R1 (rat)

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