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Protein

Serine/threonine-protein kinase VRK2

Gene

VRK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.
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

  • ATP binding Source: UniProtKB-KW
  • protein domain specific binding Source: MGI
  • protein kinase binding Source: MGI
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • cellular response to oxidative stress Source: UniProtKB
  • endocytosis Source: GO_Central
  • peptidyl-serine phosphorylation Source: GO_Central
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: ProtInc
  • regulation of cell shape Source: GO_Central
  • regulation of interleukin-1-mediated signaling pathway Source: UniProtKB
  • regulation of MAPK cascade Source: UniProtKB
  • viral process Source: UniProtKB-KW
  • Wnt signaling pathway Source: GO_Central
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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12719. VRK2.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: HPA
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37331.

Polymorphism and mutation databases

BioMutaiVRK2.
DMDMi90116515.

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.

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

BgeeiQ86Y07.
ExpressionAtlasiQ86Y07. baseline and differential.
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-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-1207633,EBI-286642
Tab1Q8CF892EBI-1207633,EBI-1778503From a different organism.

Protein-protein interaction databases

BioGridi113283. 19 interactions.
IntActiQ86Y07. 20 interactions.
MINTiMINT-6597566.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ86Y07.

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.
GeneTreeiENSGT00760000119040.
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. AlignAdd to basket

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

        10         20         30         40         50
MPPKRNEKYK LPIPFPEGKV LDDMEGNQWV LGKKIGSGGF GLIYLAFPTN
60 70 80 90 100
KPEKDARHVV KVEYQENGPL FSELKFYQRV AKKDCIKKWI ERKQLDYLGI
110 120 130 140 150
PLFYGSGLTE FKGRSYRFMV MERLGIDLQK ISGQNGTFKK STVLQLGIRM
160 170 180 190 200
LDVLEYIHEN EYVHGDIKAA NLLLGYKNPD QVYLADYGLS YRYCPNGNHK
210 220 230 240 250
QYQENPRKGH NGTIEFTSLD AHKGVALSRR SDVEILGYCM LRWLCGKLPW
260 270 280 290 300
EQNLKDPVAV QTAKTNLLDE LPQSVLKWAP SGSSCCEIAQ FLVCAHSLAY
310 320 330 340 350
DEKPNYQALK KILNPHGIPL GPLDFSTKGQ SINVHTPNSQ KVDSQKAATK
360 370 380 390 400
QVNKAHNRLI EKKVHSERSA ESCATWKVQK EEKLIGLMNN EAAQESTRRR
410 420 430 440 450
QKYQESQEPL NEVNSFPQKI SYTQFPNSFY EPHQDFTSPD IFKKSRSPSW
460 470 480 490 500
YKYTSTVSTG ITDLESSTGL WPTISQFTLS EETNADVYYY RIIIPVLLML

VFLALFFL
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.Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti419 – 4191K → E in AAO73048 (Ref. 3) Curated
Sequence conflicti419 – 4191K → E in AAO73049 (Ref. 3) Curated
Sequence conflicti419 – 4191K → E in AAO73051 (Ref. 3) Curated

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:
EMBLi
GenBanki
DDBJi
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_005264540.3. [Q86Y07-1]
XP_005264598.1. XM_005264541.2. [Q86Y07-4]
XP_006712153.1. XM_006712090.2. [Q86Y07-2]
XP_006712154.1. XM_006712091.2. [Q86Y07-5]
XP_006712155.1. XM_006712092.2. [Q86Y07-4]
XP_006712156.1. XM_006712093.2. [Q86Y07-4]
UniGeneiHs.715298.
Hs.744058.

Genome annotation databases

EnsembliENST00000340157; ENSP00000342381; ENSG00000028116. [Q86Y07-1]
ENST00000412104; ENSP00000404156; ENSG00000028116. [Q86Y07-4]
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]

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:
EMBLi
GenBanki
DDBJi
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_005264540.3. [Q86Y07-1]
XP_005264598.1. XM_005264541.2. [Q86Y07-4]
XP_006712153.1. XM_006712090.2. [Q86Y07-2]
XP_006712154.1. XM_006712091.2. [Q86Y07-5]
XP_006712155.1. XM_006712092.2. [Q86Y07-4]
XP_006712156.1. XM_006712093.2. [Q86Y07-4]
UniGeneiHs.715298.
Hs.744058.

3D structure databases

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

Protein-protein interaction databases

BioGridi113283. 19 interactions.
IntActiQ86Y07. 20 interactions.
MINTiMINT-6597566.

Chemistry

BindingDBiQ86Y07.
ChEMBLiCHEMBL1649059.
GuidetoPHARMACOLOGYi2276.

PTM databases

PhosphoSiteiQ86Y07.

Polymorphism and mutation databases

BioMutaiVRK2.
DMDMi90116515.

Proteomic databases

MaxQBiQ86Y07.
PaxDbiQ86Y07.
PRIDEiQ86Y07.

Protocols and materials databases

DNASUi7444.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340157; ENSP00000342381; ENSG00000028116. [Q86Y07-1]
ENST00000412104; ENSP00000404156; ENSG00000028116. [Q86Y07-4]
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]

Organism-specific databases

CTDi7444.
GeneCardsiGC02P058185.
H-InvDBHIX0002070.
HGNCiHGNC:12719. VRK2.
HPAiCAB046459.
HPA047503.
MIMi602169. gene.
neXtProtiNX_Q86Y07.
PharmGKBiPA37331.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119040.
HOVERGENiHBG007532.
InParanoidiQ86Y07.
KOiK08816.
OMAiHQDFTSP.
OrthoDBiEOG7KSX83.
PhylomeDBiQ86Y07.
TreeFamiTF106473.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiVRK2. human.
EvolutionaryTraceiQ86Y07.
GeneWikiiVRK2.
GenomeRNAii7444.
NextBioi29154.
PROiQ86Y07.
SOURCEiSearch...

Gene expression databases

BgeeiQ86Y07.
ExpressionAtlasiQ86Y07. baseline and differential.
GenevestigatoriQ86Y07.

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]
ProtoNetiSearch...

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: May 27, 2015
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.