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http://purl.uniprot.org/citations/8910496http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8910496http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8910496http://www.w3.org/2000/01/rdf-schema#comment"The steady state distribution of membrane forms of peptidylglycine alpha-amidating monooxygenase (PAM) in the secretory pathway of neurons and endocrine cells depends on signals in its cytosolic COOH-terminal domain (CD). Mutagenesis studies yielded catalytically active PAM proteins that are not properly localized or internalized. Employing the yeast two-hybrid system, we isolated two distinct cDNAs whose protein products showed a strong interaction with the CD of PAM. The interaction of these novel PAM COOH-terminal interactor proteins (P-CIPs) did not occur with a misrouted CD mutant as bait in the yeast system. Both proteins, P-CIP2 and P-CIP10, were expressed as fusion proteins that interacted in vitro with solubilized integral membrane PAM. P-CIP2 was homologous to several serine/threonine and dual specificity protein kinases, while P-CIP10 contained spectrin-like repeats. Endogenous P-CIP2 was localized to the Golgi region of AtT-20 corticotrope tumor cells, and expression of integral membrane PAM disrupted the distribution of endogenous P-CIP2. Both P-CIP2 and P-CIP10 mRNAs were found to be expressed in rat brain neurons also expressing PAM proteins. P-CIP2 and P-CIP10 may be members of a family of cytosolic proteins involved in the routing of membrane proteins that function in the regulated secretory pathway."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.45.28636"xsd:string
http://purl.uniprot.org/citations/8910496http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.45.28636"xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Johnson R.C."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Johnson R.C."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Caldwell B.D."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Caldwell B.D."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Darlington D.N."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Darlington D.N."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Eipper B.A."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Eipper B.A."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Mains R.E."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Mains R.E."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Alam M.R."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/author"Alam M.R."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/pages"28636-28640"xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/pages"28636-28640"xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/title"Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme."xsd:string
http://purl.uniprot.org/citations/8910496http://purl.uniprot.org/core/title"Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme."xsd:string