| http://purl.uniprot.org/citations/9430683 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9430683 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9430683 | http://www.w3.org/2000/01/rdf-schema#comment | "A novel serine/threonine protein phosphatase (PPase) designated PP7 was identified from cDNA produced from human retina RNA. PP7 has a molecular mass of approximately 75 kDa, and the deduced amino acid sequence of PP7 contains a phosphatase catalytic core domain that possesses all of the invariant motifs of the PP1, PP2A, PP2B, PP4, PP5, and PP6 gene family. However, PP7 has unique N- and C-terminal regions and shares < 35% identity with the other known PPases. The unique C-terminal region of PP7 contains multiple Ca2+ binding sites (i.e. EF-hand motifs). This region of PP7 is similar to the Drosophila retinal degeneration C gene product (rdgC), and PP7 and rdgC share 42.1% identity. Unlike the other known PPases, the expression of PP7 is not ubiquitous; PP7 was only detected in retina and retinal-derived Y-79 retinoblastoma cells. Expression of recombinant human PP7 in baculovirus-infected SF21 insect cells produces an active soluble enzyme that is capable of utilizing phosphohistone and p-nitrophenyl phosphate as substrates. The activity of recombinant PP7 is dependent on Mg2+ and is activated by calcium (IC50 approximately equal to 250 microM). PP7 is not affected by calmodulin and is insensitive to inhibition by okadaic acid, microcystin-LR, calyculin A, and cantharidin."xsd:string |
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| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/author | "Huang X."xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/author | "Huang X."xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/author | "Honkanen R.E."xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/author | "Honkanen R.E."xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/pages | "1462-1468"xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/pages | "1462-1468"xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/title | "Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)."xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/title | "Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase, PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)."xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/volume | "273"xsd:string |
| http://purl.uniprot.org/citations/9430683 | http://purl.uniprot.org/core/volume | "273"xsd:string |
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| http://purl.uniprot.org/citations/9430683 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9430683 |
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| http://purl.uniprot.org/uniprot/O14829 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9430683 |
| http://purl.uniprot.org/uniprot/#_kb.O14829_up.isolatedFrom_tissue.865 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/9430683 |