VRK1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2KTY, 2KUL, 2LAV, 2RSV, 3OP5

Identifiers

Aliases

VRK1, PCH1, PCH1A, vaccinia related kinase 1

External IDs

MGI: 1261847 HomoloGene: 2541 GeneCards: VRK1

Gene ontology
Molecular function	• transferase activity • nucleotide binding • protein kinase activity • kinase activity • nucleosomal histone binding • protein serine/threonine kinase activity • protein binding • histone kinase activity (H3-T3 specific) • histone kinase activity (H3-S10 specific) • ATP binding • protein kinase binding
Cellular component	• cytoplasm • cytosol • spindle • nucleoplasm • nucleolus • Golgi stack • cytoskeleton • nucleus
Biological process	• mitotic nuclear division • phosphorylation • histone H3-S10 phosphorylation • histone H3-T3 phosphorylation • cell division • protein phosphorylation • mitotic nuclear envelope disassembly • protein autophosphorylation • cell cycle • mitotic nuclear envelope reassembly • Golgi disassembly • regulation of cell shape
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


7443


22367

Ensembl


ENSG00000100749


ENSMUSG00000021115

UniProt


Q99986


Q80X41

RefSeq (mRNA)


NM_003384


NM_001029843 NM_001029844 NM_011705

RefSeq (protein)


NP_003375.1


NP_001025014.1 NP_001025015.1 NP_035835.1

Location (UCSC)

Chr 14: 96.8 – 96.93 Mb

Chr 12: 106.01 – 106.08 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein kinase VRK1 is an enzyme that in humans is encoded by the VRK1 gene.^[3]^[4]

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.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: VRK1 vaccinia related kinase 1".

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.
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.
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.
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.
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.
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) kinase (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

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

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 CDK12 CDC2L5 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

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VRK1

References

Further reading