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Q86Y07

- VRK2_HUMAN

UniProt

Q86Y07 - VRK2_HUMAN

Protein

Serine/threonine-protein kinase VRK2

Gene

VRK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    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.
    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.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    RAN inhibits its autophosphorylation and its ability to phosphorylate histone H3.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei61 – 611ATPPROSITE-ProRule annotation
    Active sitei166 – 1661Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi35 – 439ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to oxidative stress Source: UniProtKB
    2. protein autophosphorylation Source: UniProtKB
    3. protein phosphorylation Source: ProtInc
    4. regulation of interleukin-1-mediated signaling pathway Source: UniProtKB
    5. regulation of MAPK cascade Source: UniProtKB
    6. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Host-virus interaction

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    SignaLinkiQ86Y07.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase VRK2 (EC:2.7.11.1)
    Alternative name(s):
    Vaccinia-related kinase 2
    Gene namesi
    Name:VRK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12719. VRK2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. endoplasmic reticulum Source: HPA
    3. endoplasmic reticulum membrane Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. mitochondrial membrane Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37331.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 508508Serine/threonine-protein kinase VRK2PRO_0000086806Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei336 – 3361Phosphothreonine1 Publication

    Post-translational modificationi

    Isoform 1 and isoform 2 are autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86Y07.
    PaxDbiQ86Y07.
    PRIDEiQ86Y07.

    PTM databases

    PhosphoSiteiQ86Y07.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Gene expression databases

    ArrayExpressiQ86Y07.
    BgeeiQ86Y07.
    GenevestigatoriQ86Y07.

    Organism-specific databases

    HPAiCAB046459.
    HPA047503.

    Interactioni

    Subunit structurei

    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.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCL2L1Q07817-12EBI-1207633,EBI-287195
    BHRF1P031827EBI-1207615,EBI-1207659From a different organism.
    KSR1Q8IVT54EBI-1207615,EBI-486984
    Ksr1Q610978EBI-1207633,EBI-1536336From a different organism.
    MAP2K1Q027502EBI-1207615,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.

    Protein-protein interaction databases

    BioGridi113283. 15 interactions.
    IntActiQ86Y07. 19 interactions.
    MINTiMINT-6597566.

    Structurei

    Secondary structure

    1
    508
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 223
    Beta strandi28 – 347
    Beta strandi43 – 519
    Helixi53 – 553
    Beta strandi58 – 647
    Helixi69 – 8012
    Helixi83 – 9311
    Beta strandi103 – 11311
    Beta strandi115 – 1228
    Beta strandi124 – 1274
    Helixi128 – 1314
    Helixi134 – 1363
    Helixi140 – 15920
    Helixi169 – 1713
    Beta strandi172 – 1787
    Beta strandi181 – 1844
    Beta strandi191 – 1944
    Helixi195 – 1973
    Helixi206 – 2083
    Turni214 – 2163
    Helixi219 – 2235
    Helixi229 – 24517
    Helixi251 – 2533
    Helixi257 – 26913
    Turni270 – 2723
    Helixi273 – 2786
    Helixi286 – 29611
    Helixi306 – 3138

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V62X-ray1.70A/B14-335[»]
    ProteinModelPortaliQ86Y07.
    SMRiQ86Y07. Positions 15-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86Y07.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei487 – 50721Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 319291Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni397 – 508112Interaction with MAP3K7Add
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG007532.
    InParanoidiQ86Y07.
    KOiK08816.
    OMAiHQDFTSP.
    OrthoDBiEOG7KSX83.
    PhylomeDBiQ86Y07.
    TreeFamiTF106473.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86Y07-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPPKRNEKYK LPIPFPEGKV LDDMEGNQWV LGKKIGSGGF GLIYLAFPTN    50
    KPEKDARHVV KVEYQENGPL FSELKFYQRV AKKDCIKKWI ERKQLDYLGI 100
    PLFYGSGLTE FKGRSYRFMV MERLGIDLQK ISGQNGTFKK STVLQLGIRM 150
    LDVLEYIHEN EYVHGDIKAA NLLLGYKNPD QVYLADYGLS YRYCPNGNHK 200
    QYQENPRKGH NGTIEFTSLD AHKGVALSRR SDVEILGYCM LRWLCGKLPW 250
    EQNLKDPVAV QTAKTNLLDE LPQSVLKWAP SGSSCCEIAQ FLVCAHSLAY 300
    DEKPNYQALK KILNPHGIPL GPLDFSTKGQ SINVHTPNSQ KVDSQKAATK 350
    QVNKAHNRLI EKKVHSERSA ESCATWKVQK EEKLIGLMNN EAAQESTRRR 400
    QKYQESQEPL NEVNSFPQKI SYTQFPNSFY EPHQDFTSPD IFKKSRSPSW 450
    YKYTSTVSTG ITDLESSTGL WPTISQFTLS EETNADVYYY RIIIPVLLML 500
    VFLALFFL 508
    Length:508
    Mass (Da):58,141
    Last modified:March 7, 2006 - v3
    Checksum:i9F3F6FCC9280568F
    GO
    Isoform 2 (identifier: Q86Y07-2) [UniParc]FASTAAdd to Basket

    Also known as: VRK2B

    The sequence of this isoform differs from the canonical sequence as follows:
         395-397: EST → VEA
         398-508: Missing.

    Show »
    Length:397
    Mass (Da):45,030
    Checksum:i0308378DD02D85EC
    GO
    Isoform 3 (identifier: Q86Y07-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:485
    Mass (Da):55,446
    Checksum:i425363D6092A57FC
    GO
    Isoform 4 (identifier: Q86Y07-4) [UniParc]FASTAAdd to Basket

    Also known as: 5

    The sequence of this isoform differs from the canonical sequence as follows:
         1-118: Missing.

    Show »
    Length:390
    Mass (Da):44,411
    Checksum:i9F320B446A872E5D
    GO
    Isoform 5 (identifier: Q86Y07-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:396
    Mass (Da):45,034
    Checksum:i773C8DD02D85EC43
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti419 – 4191K → E in AAO73048. 1 PublicationCurated
    Sequence conflicti419 – 4191K → E in AAO73049. 1 PublicationCurated
    Sequence conflicti419 – 4191K → E in AAO73051. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501N → D.1 Publication
    Corresponds to variant rs34130684 [ dbSNP | Ensembl ].
    VAR_041293
    Natural varianti157 – 1571I → M.1 Publication
    Corresponds to variant rs35966666 [ dbSNP | Ensembl ].
    VAR_041294
    Natural varianti167 – 1671I → V.4 Publications
    Corresponds to variant rs1051061 [ dbSNP | Ensembl ].
    VAR_017095
    Natural varianti211 – 2111N → S.
    Corresponds to variant rs36081172 [ dbSNP | Ensembl ].
    VAR_051681

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 118118Missing in isoform 4. 2 PublicationsVSP_008534Add
    BLAST
    Alternative sequencei1 – 2323Missing in isoform 3. 1 PublicationVSP_008533Add
    BLAST
    Alternative sequencei395 – 3973EST → VEA in isoform 2. 1 PublicationVSP_008537
    Alternative sequencei395 – 3962ES → FR in isoform 5. 1 PublicationVSP_008535
    Alternative sequencei397 – 508112Missing in isoform 5. 1 PublicationVSP_008536Add
    BLAST
    Alternative sequencei398 – 508111Missing in isoform 2. 1 PublicationVSP_008538Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1859.1. [Q86Y07-1]
    CCDS46291.1. [Q86Y07-5]
    CCDS46292.1. [Q86Y07-3]
    RefSeqiNP_001123952.1. NM_001130480.2. [Q86Y07-1]
    NP_001123953.1. NM_001130481.2. [Q86Y07-1]
    NP_001123954.1. NM_001130482.2. [Q86Y07-3]
    NP_001123955.1. NM_001130483.2. [Q86Y07-5]
    NP_001275765.1. NM_001288836.1. [Q86Y07-4]
    NP_001275766.1. NM_001288837.1. [Q86Y07-1]
    NP_001275767.1. NM_001288838.1. [Q86Y07-5]
    NP_001275768.1. NM_001288839.1. [Q86Y07-4]
    NP_006287.2. NM_006296.6. [Q86Y07-1]
    XP_005264597.1. XM_005264540.2. [Q86Y07-1]
    XP_005264598.1. XM_005264541.1. [Q86Y07-4]
    XP_006712153.1. XM_006712090.1. [Q86Y07-2]
    XP_006712154.1. XM_006712091.1. [Q86Y07-5]
    XP_006712155.1. XM_006712092.1. [Q86Y07-4]
    XP_006712156.1. XM_006712093.1. [Q86Y07-4]
    UniGeneiHs.715298.
    Hs.744058.

    Genome annotation databases

    EnsembliENST00000340157; ENSP00000342381; ENSG00000028116. [Q86Y07-1]
    ENST00000412104; ENSP00000404156; ENSG00000028116. [Q86Y07-5]
    ENST00000417641; ENSP00000402375; ENSG00000028116. [Q86Y07-5]
    ENST00000435505; ENSP00000408002; ENSG00000028116. [Q86Y07-1]
    ENST00000440705; ENSP00000398323; ENSG00000028116. [Q86Y07-3]
    GeneIDi7444.
    KEGGihsa:7444.
    UCSCiuc002rzo.2. human. [Q86Y07-1]
    uc002rzs.3. human. [Q86Y07-5]
    uc002rzu.3. human. [Q86Y07-2]

    Polymorphism databases

    DMDMi90116515.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1859.1. [Q86Y07-1 ]
    CCDS46291.1. [Q86Y07-5 ]
    CCDS46292.1. [Q86Y07-3 ]
    RefSeqi NP_001123952.1. NM_001130480.2. [Q86Y07-1 ]
    NP_001123953.1. NM_001130481.2. [Q86Y07-1 ]
    NP_001123954.1. NM_001130482.2. [Q86Y07-3 ]
    NP_001123955.1. NM_001130483.2. [Q86Y07-5 ]
    NP_001275765.1. NM_001288836.1. [Q86Y07-4 ]
    NP_001275766.1. NM_001288837.1. [Q86Y07-1 ]
    NP_001275767.1. NM_001288838.1. [Q86Y07-5 ]
    NP_001275768.1. NM_001288839.1. [Q86Y07-4 ]
    NP_006287.2. NM_006296.6. [Q86Y07-1 ]
    XP_005264597.1. XM_005264540.2. [Q86Y07-1 ]
    XP_005264598.1. XM_005264541.1. [Q86Y07-4 ]
    XP_006712153.1. XM_006712090.1. [Q86Y07-2 ]
    XP_006712154.1. XM_006712091.1. [Q86Y07-5 ]
    XP_006712155.1. XM_006712092.1. [Q86Y07-4 ]
    XP_006712156.1. XM_006712093.1. [Q86Y07-4 ]
    UniGenei Hs.715298.
    Hs.744058.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V62 X-ray 1.70 A/B 14-335 [» ]
    ProteinModelPortali Q86Y07.
    SMRi Q86Y07. Positions 15-330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113283. 15 interactions.
    IntActi Q86Y07. 19 interactions.
    MINTi MINT-6597566.

    Chemistry

    BindingDBi Q86Y07.
    ChEMBLi CHEMBL1649059.
    GuidetoPHARMACOLOGYi 2276.

    PTM databases

    PhosphoSitei Q86Y07.

    Polymorphism databases

    DMDMi 90116515.

    Proteomic databases

    MaxQBi Q86Y07.
    PaxDbi Q86Y07.
    PRIDEi Q86Y07.

    Protocols and materials databases

    DNASUi 7444.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000340157 ; ENSP00000342381 ; ENSG00000028116 . [Q86Y07-1 ]
    ENST00000412104 ; ENSP00000404156 ; ENSG00000028116 . [Q86Y07-5 ]
    ENST00000417641 ; ENSP00000402375 ; ENSG00000028116 . [Q86Y07-5 ]
    ENST00000435505 ; ENSP00000408002 ; ENSG00000028116 . [Q86Y07-1 ]
    ENST00000440705 ; ENSP00000398323 ; ENSG00000028116 . [Q86Y07-3 ]
    GeneIDi 7444.
    KEGGi hsa:7444.
    UCSCi uc002rzo.2. human. [Q86Y07-1 ]
    uc002rzs.3. human. [Q86Y07-5 ]
    uc002rzu.3. human. [Q86Y07-2 ]

    Organism-specific databases

    CTDi 7444.
    GeneCardsi GC02P058185.
    H-InvDB HIX0002070.
    HGNCi HGNC:12719. VRK2.
    HPAi CAB046459.
    HPA047503.
    MIMi 602169. gene.
    neXtProti NX_Q86Y07.
    PharmGKBi PA37331.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG007532.
    InParanoidi Q86Y07.
    KOi K08816.
    OMAi HQDFTSP.
    OrthoDBi EOG7KSX83.
    PhylomeDBi Q86Y07.
    TreeFami TF106473.

    Enzyme and pathway databases

    Reactomei REACT_160242. Initiation of Nuclear Envelope Reformation.
    REACT_160251. Clearance of Nuclear Envelope Membranes from Chromatin.
    SignaLinki Q86Y07.

    Miscellaneous databases

    ChiTaRSi VRK2. human.
    EvolutionaryTracei Q86Y07.
    GeneWikii VRK2.
    GenomeRNAii 7444.
    NextBioi 29154.
    PROi Q86Y07.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86Y07.
    Bgeei Q86Y07.
    Genevestigatori Q86Y07.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiVRK2_HUMAN
    AccessioniPrimary (citable) accession number: Q86Y07
    Secondary accession number(s): B4DKL0
    , D6W5D4, D6W5D6, Q49AK9, Q53EU9, Q53S39, Q53S77, Q53TU1, Q86Y08, Q86Y09, Q86Y10, Q86Y11, Q86Y12, Q8IXI5, Q99987
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3