Vaccinia Related Kinase 1 (VRK1)

Serine/threonine-protein kinase VRK1

SPN	U251
HGNC	12718
MGI	1261847
PubMed	16547155
RGD	1306069
UniProt	Q99986
Wiki	VRK1

Serine/threonine-protein kinase VRK1 is 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, thymus, fetal liver, and carcinomas.

Its protein localizes to the nucleus and has been shown to promote the stability and nuclear accumulation of a transcriptionally active p53 molecule and, in vitro, to phosphorylate Thr18 of p53 and reduce p53 ubiquitination. This gene, therefore, may regulate cell proliferation. This protein also phosphorylates histone, casein, and the transcription factors ATF2 (activating transcription factor 2) and c-JUN.

Reference

"Identification of two novel human putative serine/threonine kinases, VRK1 and VRK2, with structural similarity to Vaccinia virus B1R kinase."
Genomics 45:327-331(1997) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein."
Oncogene 19:3656-3664(2000) [PubMed] [Europe PMC] [Abstract]

"Kinetic properties of p53 phosphorylation by the human vaccinia-related kinase 1."
Arch. Biochem. Biophys. 399:1-5(2002) [PubMed] [Europe PMC] [Abstract]

"Characterization of three paralogous members of the Mammalian vaccinia related kinase family."
J. Biol. Chem. 279:7934-7946(2004) [PubMed] [Europe PMC] [Abstract]

"Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK."
J. Biol. Chem. 279:27458-27465(2004) [PubMed] [Europe PMC] [Abstract]

"The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines."
FEBS J. 273:2487-2504(2006) [PubMed] [Europe PMC] [Abstract]

"The vaccinia-related kinases phosphorylate the N' terminus of BAF, regulating its interaction with DNA and its retention in the nucleus."
Mol. Biol. Cell 17:2451-2464(2006) [PubMed] [Europe PMC] [Abstract]

"Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities."
Mol. Cell. Proteomics 7:2199-2214(2008) [PubMed] [Europe PMC] [Abstract]

"Spinal muscular atrophy with pontocerebellar hypoplasia is caused by a mutation in the VRK1 gene."
Am. J. Hum. Genet. 85:281-289(2009) [PubMed] [Europe PMC] [Abstract]

"Plk3 interacts with and specifically phosphorylates VRK1 in Ser342, a downstream target in a pathway that induces Golgi fragmentation."
Mol. Cell. Biol. 29:1189-1201(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]

"Human vaccinia-related kinase 1."
Submitted (SEP-2010) to the PDB data bank

"NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity."
J. Biol. Chem. 286:22131-22138(2011) [PubMed] [Europe PMC] [Abstract]