Serine/threonine-protein kinase VRK2 is an enzyme that in humans is encoded by the VRK2 gene.[5]
This gene encodes a member of the vaccinia-related kinase (VRK) family of serine/threonine protein kinases. This gene is widely expressed in human tissues and has increased expression in actively dividing cells, such as those in testis, leukocytes, fetal liver, and carcinomas. Its protein localizes to the endoplasmic reticulum and has been shown to phosphorylate casein and undergo autophosphorylation.
While several transcript variants may exist for this gene, the full-length nature of only one has been biologically validated to date.[5]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000028116 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000064090 – Ensembl, May 2017
- ^ “Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ “Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b “Entrez Gene: VRK2 vaccinia related kinase 2”.
Further reading
- Blanco S, Santos C, Lazo PA (2008). “Vaccinia-related kinase 2 modulates the stress response to hypoxia mediated by TAK1”. Mol. Cell. Biol. 27 (20): 7273–83. doi:10.1128/MCB.00025-07. PMC 2168905. PMID 17709393.
- Li LY, Liu MY, Shih HM, et al. (2006). “Human cellular protein VRK2 interacts specifically with Epstein-Barr virus BHRF1, a homologue of Bcl-2, and enhances cell survival”. J. Gen. Virol. 87 (Pt 10): 2869–78. doi:10.1099/vir.0.81953-0. PMID 16963744.
- Blanco S, Klimcakova L, Vega FM, Lazo PA (2006). “The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines”. FEBS J. 273 (11): 2487–504. doi:10.1111/j.1742-4658.2006.05256.x. hdl:10261/7155. PMID 16704422. S2CID 6110354.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Nichols RJ, Traktman P (2004). “Characterization of three paralogous members of the Mammalian vaccinia related kinase family”. J. Biol. Chem. 279 (9): 7934–46. doi:10.1074/jbc.M310813200. PMID 14645249.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS…9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). “Construction and characterization of a full length-enriched and a 5′-end-enriched cDNA library”. Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Nezu J, Oku A, Jones MH, Shimane M (1998). “Identification of two novel human putative serine/threonine kinases, VRK1 and VRK2, with structural similarity to vaccinia virus B1R kinase”. Genomics. 45 (2): 327–31. doi:10.1006/geno.1997.4938. PMID 9344656.
- Maruyama K, Sugano S (1994). “Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides”. Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.