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Q86Y07 (VRK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase VRK2

EC=2.7.11.1
Alternative name(s):
Vaccinia-related kinase 2
Gene names
Name:VRK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine kinase that regulates several signal transduction pathways. Isoform 1 modulates the stress response to hypoxia and cytokines, such as interleukin-1 beta (IL1B) and this is dependent on its interaction with MAPK8IP1, which assembles mitogen-activated protein kinase (MAPK) complexes. Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription. Phosphorylates 'Thr-18' of p53/TP53, histone H3, and may also phosphorylate MAPK8IP1. Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain-containing proteins. Downregulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1. Blocks the phosphorylation of ERK in response to ERBB2 and HRAS. Can also phosphorylate the following substrates that are commonly used to establish in vitro kinase activity: casein, MBP and histone H2B, but it is not sure that this is physiologically relevant. Ref.2 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17

Isoform 2 phosphorylates 'Thr-18' of p53/TP53, as well as histone H3. Reduces p53/TP53 ubiquitination by MDM2, promotes p53/TP53 acetylation by EP300 and thereby increases p53/TP53 stability and activity. Ref.2 Ref.9 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

RAN inhibits its autophosphorylation and its ability to phosphorylate histone H3. Ref.14

Subunit structure

Isoform 1 interacts with MAP3K7, MAP2K7, MAP2K1 and KSR1. Isoform 1 and isoform 2 interact with RAN and MAPK8IP1. Isoform 1 interacts with Epstein-Barr virus BHRF1; this interaction is involved in protecting cells from apoptosis. Ref.10 Ref.12 Ref.14 Ref.15 Ref.17

Subcellular location

Isoform 1: Cytoplasm. Endoplasmic reticulum membrane; Single-pass type IV membrane protein Potential. Mitochondrion membrane; Single-pass type IV membrane protein Potential Ref.2 Ref.9 Ref.14 Ref.15 Ref.17.

Isoform 2: Cytoplasm. Nucleus Ref.2 Ref.9 Ref.14 Ref.15 Ref.17.

Tissue specificity

Isoform 1 and isoform 2 are expressed in various tumor cell lines. Expression of isoform 1 inversely correlates with ERBB2 in breast carcinomas (at protein level). Widely expressed. Highly expressed in fetal liver, skeletal muscle, pancreas, heart, peripheral blood leukocytes and testis. Ref.1 Ref.2 Ref.17

Post-translational modification

Isoform 1 and isoform 2 are autophosphorylated. Ref.2 Ref.9

Sequence similarities

Belongs to the protein kinase superfamily. CK1 Ser/Thr protein kinase family. VRK subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence CAD54446.2 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to oxidative stress

Inferred from mutant phenotype Ref.12. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.9Ref.2. Source: UniProtKB

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of MAPK cascade

Inferred from mutant phenotype Ref.17. Source: UniProtKB

regulation of interleukin-1-mediated signaling pathway

Inferred from mutant phenotype Ref.15. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay. Source: HPA

endoplasmic reticulum membrane

Inferred from direct assay Ref.15. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial membrane

Inferred from direct assay Ref.15. Source: UniProtKB

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay Ref.9Ref.11Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCL2L1Q07817-12EBI-1207633,EBI-287195
BHRF1P031827EBI-1207615,EBI-1207659From a different organism.
KSR1Q8IVT54EBI-1207615,EBI-486984
Ksr1Q610978EBI-1207633,EBI-1536336From a different organism.
MAP2K1Q027502EBI-1207633,EBI-492564
Map3k7Q620733EBI-1207633,EBI-1775345From a different organism.
Mapk8ip1Q9WVI9-22EBI-1207636,EBI-288464From a different organism.
NFATC2Q134694EBI-1207636,EBI-716258
Nfatc2Q605912EBI-1207633,EBI-643104From a different organism.
RANP628262EBI-1207649,EBI-286642
Tab1Q8CF892EBI-1207633,EBI-1778503From a different organism.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86Y07-1)

Also known as: VRK2A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q86Y07-2)

Also known as: VRK2B;

The sequence of this isoform differs from the canonical sequence as follows:
     395-397: EST → VEA
     398-508: Missing.
Isoform 3 (identifier: Q86Y07-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q86Y07-4)

Also known as: 5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-118: Missing.
Isoform 5 (identifier: Q86Y07-5)

Also known as: 6;

The sequence of this isoform differs from the canonical sequence as follows:
     395-396: ES → FR
     397-508: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Serine/threonine-protein kinase VRK2
PRO_0000086806

Regions

Transmembrane487 – 50721Helical; Anchor for type IV membrane protein; Potential
Domain29 – 319291Protein kinase
Nucleotide binding35 – 439ATP By similarity
Region397 – 508112Interaction with MAP3K7

Sites

Active site1661Proton acceptor By similarity
Binding site611ATP By similarity

Amino acid modifications

Modified residue3361Phosphothreonine Ref.13

Natural variations

Alternative sequence1 – 118118Missing in isoform 4.
VSP_008534
Alternative sequence1 – 2323Missing in isoform 3.
VSP_008533
Alternative sequence395 – 3973EST → VEA in isoform 2.
VSP_008537
Alternative sequence395 – 3962ES → FR in isoform 5.
VSP_008535
Alternative sequence397 – 508112Missing in isoform 5.
VSP_008536
Alternative sequence398 – 508111Missing in isoform 2.
VSP_008538
Natural variant501N → D. Ref.20
Corresponds to variant rs34130684 [ dbSNP | Ensembl ].
VAR_041293
Natural variant1571I → M. Ref.20
Corresponds to variant rs35966666 [ dbSNP | Ensembl ].
VAR_041294
Natural variant1671I → V. Ref.1 Ref.2 Ref.8 Ref.20
Corresponds to variant rs1051061 [ dbSNP | Ensembl ].
VAR_017095
Natural variant2111N → S.
Corresponds to variant rs36081172 [ dbSNP | Ensembl ].
VAR_051681

Experimental info

Sequence conflict4191K → E in AAO73048. Ref.3
Sequence conflict4191K → E in AAO73049. Ref.3
Sequence conflict4191K → E in AAO73051. Ref.3

Secondary structure

.................................................... 508
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (VRK2A) [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: 9F3F6FCC9280568F

FASTA50858,141
        10         20         30         40         50         60 
MPPKRNEKYK LPIPFPEGKV LDDMEGNQWV LGKKIGSGGF GLIYLAFPTN KPEKDARHVV 

        70         80         90        100        110        120 
KVEYQENGPL FSELKFYQRV AKKDCIKKWI ERKQLDYLGI PLFYGSGLTE FKGRSYRFMV 

       130        140        150        160        170        180 
MERLGIDLQK ISGQNGTFKK STVLQLGIRM LDVLEYIHEN EYVHGDIKAA NLLLGYKNPD 

       190        200        210        220        230        240 
QVYLADYGLS YRYCPNGNHK QYQENPRKGH NGTIEFTSLD AHKGVALSRR SDVEILGYCM 

       250        260        270        280        290        300 
LRWLCGKLPW EQNLKDPVAV QTAKTNLLDE LPQSVLKWAP SGSSCCEIAQ FLVCAHSLAY 

       310        320        330        340        350        360 
DEKPNYQALK KILNPHGIPL GPLDFSTKGQ SINVHTPNSQ KVDSQKAATK QVNKAHNRLI 

       370        380        390        400        410        420 
EKKVHSERSA ESCATWKVQK EEKLIGLMNN EAAQESTRRR QKYQESQEPL NEVNSFPQKI 

       430        440        450        460        470        480 
SYTQFPNSFY EPHQDFTSPD IFKKSRSPSW YKYTSTVSTG ITDLESSTGL WPTISQFTLS 

       490        500 
EETNADVYYY RIIIPVLLML VFLALFFL 

« Hide

Isoform 2 (VRK2B) [UniParc].

Checksum: 0308378DD02D85EC
Show »

FASTA39745,030
Isoform 3 [UniParc].

Checksum: 425363D6092A57FC
Show »

FASTA48555,446
Isoform 4 (5) [UniParc].

Checksum: 9F320B446A872E5D
Show »

FASTA39044,411
Isoform 5 (6) [UniParc].

Checksum: 773C8DD02D85EC43
Show »

FASTA39645,034

References

« Hide 'large scale' references
[1]"Identification of two novel human putative serine/threonine kinases, VRK1 and VRK2, with structural similarity to Vaccinia virus B1R kinase."
Nezu J., Oku A., Jones M.H., Shimane M.
Genomics 45:327-331(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT VAL-167.
Tissue: Liver.
[2]"The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines."
Blanco S., Klimcakova L., Vega F.M., Lazo P.A.
FEBS J. 273:2487-2504(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, VARIANT VAL-167.
[3]"Identification of 6 different isoforms for Vaccinia-related kinase 2 (VRK2) gene."
Suriyapperuma S.P., Sarfarazi M.
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Colon.
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-167.
[9]"Characterization of three paralogous members of the Mammalian vaccinia related kinase family."
Nichols R.J., Traktman P.
J. Biol. Chem. 279:7934-7946(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION.
[10]"Human cellular protein VRK2 interacts specifically with Epstein-Barr virus BHRF1, a homologue of Bcl-2, and enhances cell survival."
Li L.Y., Liu M.Y., Shih H.M., Tsai C.H., Chen J.Y.
J. Gen. Virol. 87:2869-2878(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS BHRF1.
[11]"The vaccinia-related kinases phosphorylate the N' terminus of BAF, regulating its interaction with DNA and its retention in the nucleus."
Nichols R.J., Wiebe M.S., Traktman P.
Mol. Biol. Cell 17:2451-2464(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Vaccinia-related kinase 2 modulates the stress response to hypoxia mediated by TAK1."
Blanco S., Santos C., Lazo P.A.
Mol. Cell. Biol. 27:7273-7283(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MAP3K7.
[13]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities."
Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A.
Mol. Cell. Proteomics 7:2199-2214(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAN, ENZYME REGULATION.
[15]"Modulation of interleukin-1 transcriptional response by the interaction between VRK2 and the JIP1 scaffold protein."
Blanco S., Sanz-Garcia M., Santos C.R., Lazo P.A.
PLoS ONE 3:E1660-E1660(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAPK8IP1; MAPK3K7 AND MAP2K7.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"VRK2 inhibits mitogen-activated protein kinase signaling and inversely correlates with ErbB2 in human breast cancer."
Fernandez I.F., Blanco S., Lozano J., Lazo P.A.
Mol. Cell. Biol. 30:4687-4697(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MAP2K1 AND KSR1, TISSUE SPECIFICITY.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Structure of the pseudokinase VRK3 reveals a degraded catalytic site, a highly conserved kinase fold, and a putative regulatory binding site."
Scheeff E.D., Eswaran J., Bunkoczi G., Knapp S., Manning G.
Structure 17:128-138(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 14-335.
[20]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-50; MET-157 AND VAL-167.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB000450 mRNA. Translation: BAA19109.1.
AJ512204 mRNA. Translation: CAD54446.2. Sequence problems.
AY228367 mRNA. Translation: AAO73047.1.
AY228368 mRNA. Translation: AAO73048.1.
AY228369 mRNA. Translation: AAO73049.1.
AY228370 mRNA. Translation: AAO73050.1.
AY228371 mRNA. Translation: AAO73051.1.
AY228372 mRNA. Translation: AAO73052.1.
AK296611 mRNA. Translation: BAG59222.1.
AK223540 mRNA. Translation: BAD97260.1.
AC007250 Genomic DNA. Translation: AAY15019.1.
AC068193 Genomic DNA. Translation: AAX93262.1.
AC073215 Genomic DNA. Translation: AAY14648.1.
CH471053 Genomic DNA. Translation: EAX00062.1.
CH471053 Genomic DNA. Translation: EAX00064.1.
CH471053 Genomic DNA. Translation: EAX00066.1.
CH471053 Genomic DNA. Translation: EAX00067.1.
CH471053 Genomic DNA. Translation: EAX00068.1.
BC027854 mRNA. Translation: AAH27854.1.
RefSeqNP_001123952.1. NM_001130480.2.
NP_001123953.1. NM_001130481.2.
NP_001123954.1. NM_001130482.2.
NP_001123955.1. NM_001130483.2.
NP_001275765.1. NM_001288836.1.
NP_001275766.1. NM_001288837.1.
NP_001275767.1. NM_001288838.1.
NP_001275768.1. NM_001288839.1.
NP_006287.2. NM_006296.6.
XP_005264597.1. XM_005264540.2.
XP_005264598.1. XM_005264541.1.
UniGeneHs.715298.
Hs.744058.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V62X-ray1.70A/B14-335[»]
ProteinModelPortalQ86Y07.
SMRQ86Y07. Positions 15-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113283. 11 interactions.
IntActQ86Y07. 19 interactions.
MINTMINT-6597566.

Chemistry

BindingDBQ86Y07.
ChEMBLCHEMBL1649059.
GuidetoPHARMACOLOGY2276.

PTM databases

PhosphoSiteQ86Y07.

Polymorphism databases

DMDM90116515.

Proteomic databases

PaxDbQ86Y07.
PRIDEQ86Y07.

Protocols and materials databases

DNASU7444.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340157; ENSP00000342381; ENSG00000028116. [Q86Y07-1]
ENST00000412104; ENSP00000404156; ENSG00000028116. [Q86Y07-5]
ENST00000417641; ENSP00000402375; ENSG00000028116. [Q86Y07-5]
ENST00000435505; ENSP00000408002; ENSG00000028116. [Q86Y07-1]
ENST00000440705; ENSP00000398323; ENSG00000028116. [Q86Y07-3]
GeneID7444.
KEGGhsa:7444.
UCSCuc002rzo.2. human. [Q86Y07-1]
uc002rzs.3. human. [Q86Y07-5]
uc002rzu.3. human. [Q86Y07-2]

Organism-specific databases

CTD7444.
GeneCardsGC02P058185.
H-InvDBHIX0002070.
HGNCHGNC:12719. VRK2.
HPACAB046459.
HPA047503.
MIM602169. gene.
neXtProtNX_Q86Y07.
PharmGKBPA37331.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG007532.
InParanoidQ86Y07.
KOK08816.
OMAHQDFTSP.
OrthoDBEOG7KSX83.
PhylomeDBQ86Y07.
TreeFamTF106473.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
SignaLinkQ86Y07.

Gene expression databases

ArrayExpressQ86Y07.
BgeeQ86Y07.
GenevestigatorQ86Y07.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVRK2. human.
EvolutionaryTraceQ86Y07.
GeneWikiVRK2.
GenomeRNAi7444.
NextBio29154.
PROQ86Y07.
SOURCESearch...

Entry information

Entry nameVRK2_HUMAN
AccessionPrimary (citable) accession number: Q86Y07
Secondary accession number(s): B4DKL0 expand/collapse secondary AC list , D6W5D4, D6W5D6, Q49AK9, Q53EU9, Q53S39, Q53S77, Q53TU1, Q86Y08, Q86Y09, Q86Y10, Q86Y11, Q86Y12, Q8IXI5, Q99987
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM