Curated Information
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Home > Curated Information Page > PubMed Id: 11010809
Nori A, et al. (2000) Site-directed mutagenesis and deletion of three phosphorylation sites of calsequestrin of skeletal muscle sarcoplasmic reticulum. Effects on intracellular targeting. Exp Cell Res 260, 40-9 11010809
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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T217-p - calsequestrin 1 (rabbit)
Modsite: SKVAKKLtLKLNEID SwissProt Entrez-Gene
Orthologous residues
calsequestrin 1 (human): T223‑p, calsequestrin 1 (mouse): T223‑p, calsequestrin 1 (rat): T223‑p, calsequestrin 1 (rabbit): T217‑p

T257-p - calsequestrin 1 (rabbit)
Modsite: VEEHRRStLRKLKPE SwissProt Entrez-Gene
Orthologous residues
calsequestrin 1 (human): T263‑p, calsequestrin 1 (mouse): T263‑p, calsequestrin 1 (rat): T263‑p, calsequestrin 1 (rabbit): T257‑p

T381-p - calsequestrin 1 (rabbit)
Modsite: VLEGEINtEDDDDED SwissProt Entrez-Gene
Orthologous residues
calsequestrin 1 (human): T387‑p, calsequestrin 1 (mouse): T387‑p, calsequestrin 1 (rat): T387‑p, calsequestrin 1 (rabbit): T381‑p