ID  Q8BN21;
PN  Serine/threonine-protein kinase VRK2;
GN  Vrk2;
OS  10090;
SL  Nucleus Position: SL-0178;
SL  Comments: Cytoplasm {ECO:0000269|PubMed:14645249}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:31142202}; Single- pass type IV membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q86Y07}; Single-pass type IV membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:31142202}.
DR  UNIPROT: Q8BN21;
DR  UNIPROT: Q3U415;
DR  UNIPROT: Q5F1Z5;
DR  UNIPROT: Q5SP88;
DR  UNIPROT: Q8BPU8;
DR  UNIPROT: Q8CJ46;
DR  UNIPROT: Q91WS1;
DR  UNIPROT: Q9CZF9;
DR  Pfam: PF00069;
DR  PROSITE: PS50011;
DR  PROSITE: PS00108;
DE  Function: Serine/threonine kinase that regulates several signal transduction pathways (PubMed:14645249). 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 (By similarity). Inhibition of signal transmission mediated by the assembly of MAPK8IP1-MAPK complexes reduces JNK phosphorylation and JUN-dependent transcription (By similarity). Phosphorylates histone H3 (By similarity). Phosphorylates 'Thr-18' of p53/TP53, and thereby increases its stability and activity (By similarity). Phosphorylates BANF1 and disrupts its ability to bind DNA and reduces its binding to LEM domain- containing proteins (By similarity). Down-regulates the transactivation of transcription induced by ERBB2, HRAS, BRAF, and MEK1 (By similarity). Blocks the phosphorylation of ERK in response to ERBB2 and HRAS (By similarity). May also phosphorylate MAPK8IP1 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q86Y07, ECO:0000269|PubMed:14645249}.
DE  Reference Proteome: Yes;
GO  GO:0005737;
GO  GO:0005783;
GO  GO:0005789;
GO  GO:0016021;
GO  GO:0016020;
GO  GO:0031966;
GO  GO:0005635;
GO  GO:0005634;
GO  GO:0032991;
GO  GO:0005524;
GO  GO:0019904;
GO  GO:0019901;
GO  GO:0106310;
GO  GO:0004674;
GO  GO:0034599;
GO  GO:0018105;
GO  GO:0046777;
GO  GO:0006468;
GO  GO:2000659;
GO  GO:0043408;
GO  GO:0007165;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MAPRRKEKYKLPVPLPEGKILDDMEGNRWALGKMIGSGGFGLIYLAFPTNKPNKDARHVIKLEYQENGPLFSELKFYQRA
SQ  AKRECIQKWIQQRKLDYLGIPVFYGFGLTDFKGRSYRFMVMERLGIDLQKLLDQNGGFKKLTVLQLGIRMLDVLEYIHEN
SQ  EYVHGDIKAANLLLDFTNPDRVYLADYGLSYRYCPNGNHKQYQEDPRKGHNGTIEFTSLDAHKGVAPSRRSDVEILGYCM
SQ  LHWLFGKLPWEAKLDDPVAVQTAKTNLLDELPESVLKWAPSGSSCSELVKYLMYVHNLAYDDKPDYQKLKKILNPDGVPL
SQ  GPLEFSTKVQSVHVRTPAQQKVDSPKATRKPANEFPAKFPKKVHRETRARQREEQEDSQPTMLQSRPAAPENSRTRKIHE
SQ  YSDIFSEMQSLQQTPSYMSFQGSYCKPYLDCTRRDPIRKPRSLPRYRHTPTGNLGVTDLESSPRFWPAIFQLTLSEETKA
SQ  DVYYYGITIFCLLIFVFLALYFL
//