| First Author | Zelko I | Year | 1998 |
| Journal | Arch Biochem Biophys | Volume | 352 |
| Issue | 1 | Pages | 31-6 |
| PubMed ID | 9521809 | Mgi Jnum | J:46795 |
| Mgi Id | MGI:1202089 | Doi | 10.1006/abbi.1998.0582 |
| Citation | Zelko I, et al. (1998) Molecular cloning and characterization of a novel nuclear protein kinase in mice. Arch Biochem Biophys 352(1):31-6 |
| abstractText | We cloned cDNAs which encode a mouse liver nuclear protein with an apparent molecular mass of 51 kDa, using sequences derived from a purified protein as the basis for designing specific primers. The deduced amino acid sequences revealed that the 51-kDa protein contains characteristic subdomain structures of a protein kinase. The bacterially expressed recombinant 51-kDa protein catalyzed phosphorylation of general substrates such as casein and was autophosphorylated at serine residue(s). This 51-kDa protein kinase, designated 51PK, is 40% identical to the 34-kDa protein kinase encoded by the vaccinia virus B1 gene and 25% identical to the casein kinase I isoforms, including yeast HRR25. The 51PK mRNA was expressed as two splice variants and the 51PK protein was exclusively localized in nuclei. Northern hybridization showed that 51PK mRNA was expressed in various tissues, with highest levels in testis, spleen, lung, and liver. These results, therefore, indicate that 51PK is a nuclear serine/threonine kinase and a novel distinct member of the protein kinase superfamily. Copyright 1998 Academic Press. |
