http://purl.uniprot.org/citations/6501302 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/6501302 | http://www.w3.org/2000/01/rdf-schema#comment | "DARPP-32 (dopamine- and cyclic AMP-regulated phosphoprotein, Mr = 32,000) is a major endogenous cytosolic substrate for dopamine- and cyclic AMP-stimulated protein phosphorylation in neurons of the basal ganglia of mammalian brain. It shares many properties with phosphatase inhibitor 1, a substrate for cyclic AMP-dependent protein kinase, and with G-substrate, a substrate for cyclic GMP-dependent protein kinase. We have, therefore, undertaken an analysis of the amino acid sequence around the site at which purified DARPP-32 is phosphorylated by the catalytic subunit of cyclic AMP-dependent protein kinase. The results indicate that DARPP-32 is phosphorylated at a single threonine residue contained in the sequence Arg-Arg-Arg-Pro-Thr(P)-Pro-Ala-Met-Leu-Phe-Arg. This sequence was obtained by automated solid phase sequencing of two overlapping tryptic phosphopeptides and one overlapping chymotryptic phosphopeptide which were purified by reverse-phase high-performance liquid chromatography. A 9-amino acid sequence containing the phosphorylatable threonine residue in DARPP-32 shares 8 identical residues with a sequence containing the phosphorylatable threonine residue in phosphatase inhibitor 1, and shares 5 identical residues with the two identical sequences surrounding the 2 phosphorylatable threonine residues in G-substrate. These observations support the view that DARPP-32, inhibitor 1, and G-substrate are members of a family of regulatory proteins which are involved in the control of protein phosphatase activity by both cyclic AMP and cyclic GMP, but which differ in their cellular and tissue distributions."xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(17)42625-1"xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/author | "Konigsberg W.H."xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/author | "Williams K.R."xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/author | "Greengard P."xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/author | "Hemmings H.C. Jr."xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/date | "1984"xsd:gYear |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/pages | "14486-14490"xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/title | "DARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated neuronal phosphoprotein. I. Amino acid sequence around the phosphorylated threonine."xsd:string |
http://purl.uniprot.org/citations/6501302 | http://purl.uniprot.org/core/volume | "259"xsd:string |
http://purl.uniprot.org/citations/6501302 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/6501302 |
http://purl.uniprot.org/citations/6501302 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/6501302 |
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