Curated Information
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Home > Curated Information Page > PubMed Id: 21215369
Leonard TA, et al. (2011) Crystal structure and allosteric activation of protein kinase C βII. Cell 144, 55-66 21215369
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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T500-p - PKCB (rat)
Modsite: WDGVTTktFCGtPDy SwissProt Entrez-Gene
Orthologous residues
PKCB (human): T500‑p, PKCB iso2 (human): T500‑p, PKCB (mouse): T500‑p, PKCB iso2 (mouse): T500‑p, PKCB (rat): T500‑p, PKCB iso2 (rat): T500‑p, PKCB (cow): T500‑p
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced

T642-p - PKCB (rat)
Modsite: tRQPVELtPTDKLFI SwissProt Entrez-Gene
Orthologous residues
PKCB (human): T642‑p, PKCB iso2 (human): , PKCB (mouse): T642‑p, PKCB iso2 (mouse): , PKCB (rat): T642‑p, PKCB iso2 (rat): , PKCB (cow):
Downstream Regulation
Effect of modification (function):  protein conformation

S661-p - PKCB (rat)
Modsite: QNEFAGFsYTNPEFV SwissProt Entrez-Gene
Orthologous residues
PKCB (human): S661‑p, PKCB iso2 (human): , PKCB (mouse): S661‑p, PKCB iso2 (mouse): , PKCB (rat): S661‑p, PKCB iso2 (rat): , PKCB (cow):
Downstream Regulation
Effect of modification (function):  protein conformation