RGD Reference Report - The alpha and beta subunits of phosphorylase kinase are homologous: cDNA cloning and primary structure of the beta subunit. - Rat Genome Database

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The alpha and beta subunits of phosphorylase kinase are homologous: cDNA cloning and primary structure of the beta subunit.

Authors: Kilimann, MW  Zander, NF  Kuhn, CC  Crabb, JW  Meyer, HE  Heilmeyer LM, JR 
Citation: Kilimann MW, etal., Proc Natl Acad Sci U S A 1988 Dec;85(24):9381-5.
RGD ID: 633585
Pubmed: PMID:3200826   (View Abstract at PubMed)
PMCID: PMC282756   (View Article at PubMed Central)

We have cloned cDNA molecules encoding the beta subunit of phosphorylase kinase (ATP:phosphorylase-b phosphotransferase; EC 2.7.1.38) from rabbit fast-twitch skeletal muscle and have determined the complete primary structure of the polypeptide by a combination of peptide and DNA sequencing. In the mature beta subunit, the initial methionine is replaced by an acetyl group. The subunit is composed of 1092 amino acids and has a calculated molecular mass of 125,205 Da. Alignment of its sequence with the alpha subunit of phosphorylase kinase reveals extensive regions of homology, but each molecule also possesses unique sequences. Two of the three phosphorylation sites known for the beta subunit and all seven phosphorylation sites known for the alpha subunit are located in these unique domains.



Objects referenced in this article
Gene Phkb phosphorylase kinase regulatory subunit beta Rattus norvegicus

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