VRK1

Vaccinia related kinase 1

Identifiers

VRK1; MGC117401; MGC138280; MGC142070; PCH1

External IDs

OMIM: 602168 MGI: 1261847 HomoloGene: 2541 GeneCards: VRK1 Gene

2.7.11.1

Gene Ontology
Molecular function	• nucleotide binding • protein serine/threonine kinase activity • protein binding • ATP binding
Cellular component	• nucleus • nucleolus • nucleolus • cytoplasm
Biological process	• protein phosphorylation • protein autophosphorylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 14:
97.26 – 97.35 Mb

Chr 12:
107.25 – 107.32 Mb

PubMed search

[1]

[2]

Serine/threonine-protein kinase VRK1 is an enzyme that in humans is encoded by the VRK1 gene.^[1]^[2]

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, 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.^[2]

References

^ Nezu J, Oku A, Jones MH, Shimane M (Feb 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.
^ ^a ^b "Entrez Gene: VRK1 vaccinia related kinase 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7443.

Sugimoto J, Yamauchi T, Hatakeyama T, Isobe M (1999). "Isolation and mapping of a polymorphic CA repeat sequence at the human VRK1 locus.". J. Hum. Genet. 44 (2): 133–4. doi:10.1007/s100380050127. PMID 10083742.
Sayed M, Kim SO, Salh BS, et al. (2000). "Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase.". J. Biol. Chem. 275 (22): 16569–73. doi:10.1074/jbc.M000312200. PMID 10747897.
Lopez-Borges S, Lazo PA (2000). "The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein.". Oncogene 19 (32): 3656–64. doi:10.1038/sj.onc.1203709. PMID 10951572.
Latonen L, Taya Y, Laiho M (2001). "UV-radiation induces dose-dependent regulation of p53 response and modulates p53-HDM2 interaction in human fibroblasts.". Oncogene 20 (46): 6784–93. doi:10.1038/sj.onc.1204883. PMID 11709713.
Barcia R, López-Borges S, Vega FM, Lazo PA (2002). "Kinetic properties of p53 phosphorylation by the human vaccinia-related kinase 1.". Arch. Biochem. Biophys. 399 (1): 1–5. doi:10.1006/abbi.2001.2746. PMID 11883897.
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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.
Boyle KA, Traktman P (2004). "Members of a novel family of mammalian protein kinases complement the DNA-negative phenotype of a vaccinia virus ts mutant defective in the B1 kinase.". J. Virol. 78 (4): 1992–2005. doi:10.1128/JVI.78.4.1992-2005.2004. PMC 369515. PMID 14747564. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=369515.
Sevilla A, Santos CR, Vega FM, Lazo PA (2004). "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 (26): 27458–65. doi:10.1074/jbc.M401009200. PMID 15105425.
Sevilla A, Santos CR, Barcia R, et al. (2004). "c-Jun phosphorylation by the human vaccinia-related kinase 1 (VRK1) and its cooperation with the N-terminal kinase of c-Jun (JNK).". Oncogene 23 (55): 8950–8. doi:10.1038/sj.onc.1208015. PMID 15378002.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Vega FM, Sevilla A, Lazo PA (2005). "p53 Stabilization and accumulation induced by human vaccinia-related kinase 1.". Mol. Cell. Biol. 24 (23): 10366–80. doi:10.1128/MCB.24.23.10366-10380.2004. PMC 529057. PMID 15542844. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=529057.
Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
Santos CR, Rodríguez-Pinilla M, Vega FM, et al. (2006). "VRK1 signaling pathway in the context of the proliferation phenotype in head and neck squamous cell carcinoma.". Mol. Cancer Res. 4 (3): 177–85. doi:10.1158/1541-7786.MCR-05-0212. PMID 16547155.
Valbuena A, Vega FM, Blanco S, Lazo PA (2006). "p53 downregulates its activating vaccinia-related kinase 1, forming a new autoregulatory loop.". Mol. Cell. Biol. 26 (13): 4782–93. doi:10.1128/MCB.00069-06. PMC 1489172. PMID 16782868. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1489172.
Valbuena A, López-Sánchez I, Vega FM, et al. (2007). "Identification of a dominant epitope in human vaccinia-related kinase 1 (VRK1) and detection of different intracellular subpopulations.". Arch. Biochem. Biophys. 465 (1): 219–26. doi:10.1016/j.abb.2007.06.005. PMID 17617371.

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1, LATS2, MAST1, MAST2, STK38, STK38L, CIT, ROCK1, SGK, SGK2, SGK3, Protein kinase B (AKT1, AKT2, AKT3), Ataxia telangiectasia mutated, Mammalian target of rapamycin, EIF-2 kinases (PKR, HRI, EIF2AK3, EIF2AK4), Wee1 (WEE1)

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1, PDK2, PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α (PRKAA1, PRKAA2) · β (PRKAB1, PRKAB2) · γ (PRKAG1, PRKAG2, PRKAG3)

(3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)) (EC 2.7.11.4)	BCKDK, BCKDHA, BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2, IDH3A, IDH3B, IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase (Aurora A kinase, Aurora B kinase)

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK, STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK, IKK2, TBK1, IKBKE, IKBKG, IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A, PRKACG, PRKACB, PRKACA, PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G, PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C, Protein kinase Cζ, PKC alpha, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, PRKCQ, Protein kinase N1, PKN2, PKN3,

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase, Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4, GRK5, GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2, CAMK1, CAMK2A, CAMK2B, CAMK2D, CAMK2G, CAMK4, MLCK, CASK, CHEK1, CHEK2, DAPK1, DAPK2, DAPK3, STK11, MAPKAPK2, MAPKAPK3, MAPKAPK5, MARK1, MARK2, MARK3, MARK4, MELK, MKNK1, MKNK2, NUAK1, NUAK2, OBSCN, PASK, PHKG1, PHKG2, PIM1, PIM2, PKD1, PRKD2, PRKD3, PSKH1, SNF1LK2, KIAA0999, STK40, SNF1LK, SNRK, SPEG, TSSK2, Kalirin, TRIB1, TRIB2, TRIB3, TRIO, Titin, DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK, MYLK2, MYLK3, MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1, PHKA2, PHKB, PHKG1, PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K, STK19

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1, PLK2, PLK3, PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1, CDK2, CDKL2, CDK3, CDK4, CDK5, CDKL5, CDK6, CDK7, CDK8, CDK9, CDK10, CDC2L5, CRKRS, PCTK1, PCTK2, PCTK3, PFTK1, CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5, RPS6KA4, P70S6 kinase, P70-S6 Kinase 1, RPS6KB2, RPS6KA2, RPS6KA3, RPS6KA1, RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated (MAPK1, MAPK3, MAPK4, MAPK6, MAPK7, MAPK12, MAPK15), C-Jun N-terminal (MAPK8, MAPK9, MAPK10), P38 mitogen-activated protein (MAPK11, MAPK13, MAPK14)

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases (MAP3K1, MAP3K2, MAP3K3, MAP3K4, MAP3K5, MAP3K6, MAP3K7, MAP3K8) RAFs (ARAF, BRAF, KSR1, KSR2), MLKs (MAP3K12, MAP3K13, MAP3K9, MAP3K10, MAP3K11, MAP3K7, ZAK), CDC7, MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1, TTK, GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors (BMPR1, BMPR1A, BMPR1B, BMPR2), ACVR1, ACVR1B, ACVR1C, ACVR2A, ACVR2B, ACVRL1, Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1, MAP2K2, MAP2K3, MAP2K4, MAP2K5, MAP2K6, MAP2K7

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

VRK1

References

Further reading