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Q86Y07

- VRK2_HUMAN

UniProt

Q86Y07 - VRK2_HUMAN

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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

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.7 Publications
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.7 Publications

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 – 611ATP By similarity
Active sitei166 – 1661Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi35 – 439ATP By similarity

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
Complete GO annotation...

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

Isoform 1 : Cytoplasm. Endoplasmic reticulum membrane; Single-pass type IV membrane protein Reviewed prediction. Mitochondrion membrane; Single-pass type IV membrane protein Reviewed prediction 5 Publications
Isoform 2 : Cytoplasm. Nucleus 5 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei487 – 50721Helical; Anchor for type IV membrane protein; Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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.2 Publications

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-1207633,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.

Miscellaneous databases

EvolutionaryTraceiQ86Y07.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 319291Protein kinaseAdd
BLAST

Region

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

Sequence similaritiesi

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.

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. VSP_008534Add
BLAST
Alternative sequencei1 – 2323Missing in isoform 3. VSP_008533Add
BLAST
Alternative sequencei395 – 3973EST → VEA in isoform 2. VSP_008537
Alternative sequencei395 – 3962ES → FR in isoform 5. VSP_008535
Alternative sequencei397 – 508112Missing in isoform 5. VSP_008536Add
BLAST
Alternative sequencei398 – 508111Missing in isoform 2. VSP_008538Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 130 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

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