EKS-HOS-00042
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00042
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
CK1/VRK421.36.8E-12629292264
StatusReviewed
Ensembl ProteinENSP00000402375
UniProt AccessionQ86Y07; B4DKL0; D6W5D4; D6W5D6; Q49AK9; Q53EU9; Q53S39; Q53S77; Q53TU1; Q86Y08; Q86Y09; Q86Y10; Q86Y11; Q86Y12; Q8IXI5; Q99987;
Protein NameSerine/threonine-protein kinase VRK2
Protein Synonyms/Alias Vaccinia-related kinase 2;
Gene NameVRK2
Gene Synonyms/Alias VRK2;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000028116ENSP00000404961ENST00000428021
ENSG00000028116ENSP00000404156ENST00000412104
ENSG00000028116ENSP00000402375ENST00000417641
ENSG00000028116ENSP00000400006ENST00000432057
ENSG00000028116ENSP00000398323ENST00000440705
ENSG00000028116ENSP00000342381ENST00000340157
ENSG00000028116ENSP00000408002ENST00000435505
OrganismHomo sapiens
Functional DescriptionSerine/threonine kinase that regulates several signaltransduction 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 wellas histone H3. Reduces p53/TP53 ubiquitination by MDM2, promotes p53/TP53 acetylation by EP300 and thereby increases p53/TP53 stability and activity.
Protein Length396
Protein Sequence
(FASTA)
MPPKRNEKYK LPIPFPEGKV LDDMEGNQWV LGKKIGSGGF GLIYLAFPTN KPEKDARHVV 60
KVEYQENGPL FSELKFYQRV AKKDCIKKWI ERKQLDYLGI PLFYGSGLTE FKGRSYRFMV 120
MERLGIDLQK ISGQNGTFKK STVLQLGIRM LDVLEYIHEN EYVHGDIKAA NLLLGYKNPD 180
QVYLADYGLS YRYCPNGNHK QYQENPRKGH NGTIEFTSLD AHKGVALSRR SDVEILGYCM 240
LRWLCGKLPW EQNLKDPVAV QTAKTNLLDE LPQSVLKWAP SGSSCCEIAQ FLVCAHSLAY 300
DEKPNYQALK KILNPHGIPL GPLDFSTKGQ SINVHTPNSQ KVDSQKAATK QVNKAHNRLI 360
EKKVHSERSA ESCATWKVQK EEKLIGLMNN EAAQFR 396
Nucleotide Sequence
(FASTA)
ATGCCACCAA AAAGAAATGA AAAATACAAA CTTCCTATTC CATTTCCAGA AGGCAAGGTT 60
CTGGATGATA TGGAAGGCAA TCAGTGGGTA CTGGGCAAGA AGATTGGCTC TGGAGGATTT 120
GGATTGATAT ATTTAGCTTT CCCCACAAAT AAACCAGAGA AAGATGCAAG ACATGTAGTA 180
AAAGTGGAAT ATCAAGAAAA TGGCCCGTTA TTTTCAGAAC TTAAATTTTA TCAGAGAGTT 240
GCAAAAAAAG ACTGTATCAA AAAGTGGATA GAACGCAAAC AACTTGATTA TTTAGGAATT 300
CCTCTGTTTT ATGGATCTGG TCTGACTGAA TTCAAGGGAA GAAGTTACAG ATTTATGGTA 360
ATGGAAAGAC TAGGAATAGA TTTACAGAAG ATCTCAGGCC AGAATGGTAC CTTTAAAAAG 420
TCAACTGTCC TGCAATTAGG TATCCGAATG TTGGATGTAC TGGAATATAT ACATGAAAAT 480
GAATATGTTC ATGGTGATAT AAAAGCAGCA AATCTACTTT TGGGTTACAA AAATCCAGAC 540
CAGGTTTATC TTGCAGATTA TGGACTTTCC TACAGATATT GTCCCAATGG GAACCACAAA 600
CAGTATCAGG AAAATCCTAG AAAAGGCCAT AATGGGACAA TAGAGTTTAC CAGCTTGGAT 660
GCCCACAAGG GAGTAGCCTT GTCCAGACGA AGTGACGTTG AGATCCTCGG CTACTGCATG 720
CTGCGGTGGT TGTGTGGGAA ACTTCCCTGG GAACAGAACC TGAAGGACCC TGTGGCTGTG 780
CAGACTGCTA AAACAAATCT GTTGGACGAG CTCCCCCAGT CAGTGCTTAA ATGGGCTCCT 840
TCTGGAAGCA GTTGCTGTGA AATAGCCCAA TTTTTGGTAT GTGCTCATAG TTTAGCATAT 900
GATGAAAAGC CAAACTATCA AGCCCTCAAG AAAATTTTGA ACCCTCATGG AATACCTTTA 960
GGACCACTGG ACTTTTCCAC AAAAGGACAG AGTATAAATG TCCATACTCC AAACAGTCAA 1020
AAAGTTGATT CACAAAAGGC TGCAACAAAG CAAGTCAACA AGGCACACAA TAGGTTAATC 1080
GAAAAAAAAG TCCACAGTGA GAGAAGCGCT GAGTCCTGTG CAACATGGAA AGTGCAGAAA 1140
GAGGAGAAAC TGATTGGATT GATGAACAAT GAAGCAGCTC AGTTTAGGTA G 1191
Domain Profile
S: 1     wklgkkigkggfGeiylaltckkeekdaklvvkvepkenGpLfvelkfyqraakkeqikk  60
         w lgkkig+ggfG iyla++++k+ekda++vvkve++enGpLf+elkfyqr+akk++ikk
Q: 29    WVLGKKIGSGGFGLIYLAFPTNKPEKDARHVVKVEYQENGPLFSELKFYQRVAKKDCIKK  88
         99**********************************************************
S: 61    wkkkkklkllgiPtliasGlhefegekyRflvlprlgrdLqklleqngkrlsektvlqla  120
         w+++k+l++lgiP +++sGl+ef+g++yRf+v++rlg+dLqk+  qng+ ++++tvlql+
Q: 89    WIERKQLDYLGIPLFYGSGLTEFKGRSYRFMVMERLGIDLQKISGQNGT-FKKSTVLQLG  147
         ************************************************5.**********
S: 121   vrlldvleylHeneYvHgdikAanllleeeeasqvyLvdyGlayrycpegkhkeykedkr  180
         +r+ldvley+HeneYvHgdikAanlll++++++qvyL+dyGl+yrycp+g+hk+y+e++r
Q: 148   IRMLDVLEYIHENEYVHGDIKAANLLLGYKNPDQVYLADYGLSYRYCPNGNHKQYQENPR  207
         ************************************************************
S: 181   raHdGtleftslDaHkGvapsrRsDleiLgYcllkWltgkLPWeallkdpekvqkakekf  240
         + H+Gt+eftslDaHkGva srRsD+eiLgYc+l+Wl+gkLPWe++lkdp +vq+ak+++
Q: 208   KGHNGTIEFTSLDAHKGVALSRRSDVEILGYCMLRWLCGKLPWEQNLKDPVAVQTAKTNL  267
         ************************************************************
S: 241   ldelpellkkllkkkssseelakyl  265
         ldelp+++ k+++++ss++e+a++l
Q: 268   LDELPQSVLKWAPSGSSCCEIAQFL  292
         ***********************97
Domain Sequence
(FASTA)
WVLGKKIGSG GFGLIYLAFP TNKPEKDARH VVKVEYQENG PLFSELKFYQ RVAKKDCIKK 60
WIERKQLDYL GIPLFYGSGL TEFKGRSYRF MVMERLGIDL QKISGQNGTF KKSTVLQLGI 120
RMLDVLEYIH ENEYVHGDIK AANLLLGYKN PDQVYLADYG LSYRYCPNGN HKQYQENPRK 180
GHNGTIEFTS LDAHKGVALS RRSDVEILGY CMLRWLCGKL PWEQNLKDPV AVQTAKTNLL 240
DELPQSVLKW APSGSSCCEI AQFL 264
Keyword3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Endoplasmic reticulum; Host-virus interaction; Kinase; Membrane; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Transmembrane; Transmembrane helix.
Sequence SourceEnsembl
Orthology
Ortholog group
Ailuropoda melanoleuca"; ?>Bos taurus"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Choloepus hoffmanni"; ?>Danio rerio"; ?>Dipodomys ordii"; ?>Equus caballus"; ?>Felis catus"; ?>Gadus morhua"; ?>Gallus gallus"; ?>Gasterosteus aculeatus"; ?>Gorilla gorilla"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Monodelphis domestica"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Oreochromis niloticus"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Oryzias latipes"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Sorex araneus"; ?>Sus scrofa"; ?>Taeniopygia guttata"; ?>Takifugu rubripes"; ?>Tetraodon nigroviridis"; ?>Xenopus tropicalis"; ?>Xiphophorus maculatus"; ?>
EKS-AIM-00037
EKS-BOT-00042
EKS-CAJ-00041
EKS-CAF-00042
EKS-CAP-00042
EKS-CHH-00021
EKS-DAR-00053
EKS-DIO-00026
EKS-EQC-00039
EKS-FEC-00038
EKS-GAM-00018
EKS-GAG-00033
EKS-GAA-00057
EKS-GOG-00040
EKS-ICT-00037
EKS-LAC-00043
EKS-LOA-00041
EKS-MAM-00040
EKS-MOD-00041
EKS-MUM-00043
EKS-MUP-00043
EKS-MYL-00044
EKS-NOL-00040
EKS-ORN-00057
EKS-ORA-00036
EKS-ORC-00040
EKS-ORL-00054
EKS-OTG-00043
EKS-PAT-00039
EKS-PES-00037
EKS-POA-00039
EKS-PTV-00045
EKS-RAN-00044
EKS-SAH-00040
EKS-SOA-00028
EKS-SUS-00033
EKS-TAG-00037
EKS-TAR-00058
EKS-TEN-00061
EKS-XET-00041
EKS-XIM-00055
Gene Ontology
GO:0005789; C:endoplasmic reticulum membrane
GO:0016021; C:integral to membrane
GO:0031966; C:mitochondrial membrane
GO:0005634; C:nucleus
GO:0005524; F:ATP binding
GO:0004674; F:protein serine/threonine kinase activity
GO:0034599; P:cellular response to oxidative stress
GO:0046777; P:protein autophosphorylation
GO:2000659; P:regulation of interleukin-1-mediated signaling pathway
GO:0043408; P:regulation of MAPK cascade
GO:0019048; P:virus-host interaction
KEGG
hsa:7444;
InterPros
IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
IPR008271; Ser/Thr_kinase_AS.
Pfam
PF00069; Pkinase; 1.
SMARTs
Prosites
PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
Prints
Created Date20-Feb-2013