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Serine/threonine-protein kinase VRK2 (EC 2.7.11.1) (Vaccinia-related kinase 2)

 VRK2_MOUSE              Reviewed;         503 AA.
Q8BN21; Q3U415; Q5F1Z5; Q5SP88; Q8BPU8; Q8CJ46; Q91WS1; Q9CZF9;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
10-OCT-2003, sequence version 2.
20-JUN-2018, entry version 142.
RecName: Full=Serine/threonine-protein kinase VRK2;
EC=2.7.11.1;
AltName: Full=Vaccinia-related kinase 2;
Name=Vrk2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=12417526; DOI=10.1093/hmg/11.24.3047;
Agoulnik A.I., Lu B., Zhu Q., Truong C., Ty M.T., Arango N.,
Chada K.K., Bishop C.E.;
"A novel gene, Pog, is necessary for primordial germ cell
proliferation in the mouse and underlies the germ cell deficient
mutation, gcd.";
Hum. Mol. Genet. 11:3047-3053(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
STRAIN=C57BL/6J, and NOD;
TISSUE=Dendritic cell, Embryo, Eye, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12782311; DOI=10.1016/S0014-5793(03)00501-5;
Vega F.M., Gonzalo P., Gaspar M.L., Lazo P.A.;
"Expression of the VRK (vaccinia-related kinase) gene family of p53
regulators in murine hematopoietic development.";
FEBS Lett. 544:176-180(2003).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND AUTOPHOSPHORYLATION.
PubMed=14645249; DOI=10.1074/jbc.M310813200;
Nichols R.J., Traktman P.;
"Characterization of three paralogous members of the Mammalian
vaccinia related kinase family.";
J. Biol. Chem. 279:7934-7946(2004).
-!- FUNCTION: 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 histone H3. Phosphorylates 'Thr-18'
of p53/TP53, and thereby increases its stability and activity.
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. May also phosphorylate MAPK8IP1. 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, ECO:0000269|PubMed:14645249}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Interacts with MAP3K7, MAP2K7, MAP2K1, KSR1, RAN and
MAPK8IP1. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14645249}.
Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type IV
membrane protein {ECO:0000305}. Mitochondrion membrane
{ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8BN21-1; Sequence=Displayed;
Name=2;
IsoId=Q8BN21-2; Sequence=VSP_008543;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8BN21-3; Sequence=VSP_008541, VSP_008542;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in liver, kidney and muscle. Weakly
expressed in thymus, bone marrow and spleen.
{ECO:0000269|PubMed:12782311}.
-!- DEVELOPMENTAL STAGE: Weakly expressed in embryo compared to VRK1
and VRK3. Expressed from E10.5 to E14 in developing liver and then
decreases. It increases again from E17.5 and remains thereafter.
Highly expressed in hematopoietic embryonic tissues from E10.5 to
E14.5. Weakly expressed in the yolk-sac.
{ECO:0000269|PubMed:12782311}.
-!- PTM: Autophosphorylated.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
protein kinase family. VRK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF513620; AAN64922.1; -; mRNA.
EMBL; AK012664; BAB28393.1; -; mRNA.
EMBL; AK053297; BAC35335.1; -; mRNA.
EMBL; AK154485; BAE32620.1; -; mRNA.
EMBL; AL929272; CAI52021.1; -; Genomic_DNA.
EMBL; AC083815; CAI52021.1; JOINED; Genomic_DNA.
EMBL; BC013520; AAH13520.1; -; mRNA.
CCDS; CCDS24486.1; -. [Q8BN21-1]
RefSeq; NP_001239376.1; NM_001252447.1. [Q8BN21-2]
RefSeq; NP_081536.2; NM_027260.3. [Q8BN21-1]
RefSeq; XP_006514864.1; XM_006514801.3. [Q8BN21-1]
UniGene; Mm.285351; -.
ProteinModelPortal; Q8BN21; -.
SMR; Q8BN21; -.
BioGrid; 213758; 2.
STRING; 10090.ENSMUSP00000077471; -.
iPTMnet; Q8BN21; -.
PhosphoSitePlus; Q8BN21; -.
PaxDb; Q8BN21; -.
PeptideAtlas; Q8BN21; -.
PRIDE; Q8BN21; -.
Ensembl; ENSMUST00000078362; ENSMUSP00000077471; ENSMUSG00000064090. [Q8BN21-1]
Ensembl; ENSMUST00000109504; ENSMUSP00000105130; ENSMUSG00000064090. [Q8BN21-1]
GeneID; 69922; -.
KEGG; mmu:69922; -.
UCSC; uc007igf.2; mouse. [Q8BN21-1]
UCSC; uc007igg.2; mouse. [Q8BN21-3]
UCSC; uc011xsk.2; mouse. [Q8BN21-2]
CTD; 7444; -.
MGI; MGI:1917172; Vrk2.
eggNOG; KOG1164; Eukaryota.
eggNOG; ENOG410XPGP; LUCA.
GeneTree; ENSGT00920000148988; -.
HOVERGEN; HBG007532; -.
InParanoid; Q8BN21; -.
KO; K08816; -.
OMA; SSCCEIA; -.
OrthoDB; EOG091G05V5; -.
PhylomeDB; Q8BN21; -.
TreeFam; TF106473; -.
Reactome; R-MMU-2995383; Initiation of Nuclear Envelope Reformation.
PRO; PR:Q8BN21; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000064090; -.
CleanEx; MM_VRK2; -.
ExpressionAtlas; Q8BN21; baseline and differential.
Genevisible; Q8BN21; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
GO; GO:2000659; P:regulation of interleukin-1-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; ISS:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Kinase; Membrane; Mitochondrion;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 503 Serine/threonine-protein kinase VRK2.
/FTId=PRO_0000086807.
TRANSMEM 482 502 Helical; Anchor for type IV membrane
protein. {ECO:0000255}.
DOMAIN 29 313 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 35 43 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 392 503 Interaction with MAP3K7. {ECO:0000250}.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 61 61 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 336 336 Phosphothreonine.
{ECO:0000250|UniProtKB:Q86Y07}.
VAR_SEQ 151 163 LDVLEYIHENEYV -> VSLRDLTGDLLDI (in
isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008541.
VAR_SEQ 164 503 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008542.
VAR_SEQ 342 390 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_008543.
CONFLICT 33 33 K -> R (in Ref. 1; AAN64922).
{ECO:0000305}.
CONFLICT 226 226 A -> P (in Ref. 2; BAB28393).
{ECO:0000305}.
CONFLICT 319 319 P -> L (in Ref. 2; BAE32620 and 4;
AAH13520). {ECO:0000305}.
CONFLICT 333 333 H -> R (in Ref. 2; BAE32620 and 4;
AAH13520). {ECO:0000305}.
SEQUENCE 503 AA; 58119 MW; 6F29E3E412ECB221 CRC64;
MAPRRKEKYK LPVPLPEGKI LDDMEGNRWA LGKMIGSGGF GLIYLAFPTN KPNKDARHVI
KLEYQENGPL FSELKFYQRA AKRECIQKWI QQRKLDYLGI PVFYGFGLTD FKGRSYRFMV
MERLGIDLQK LLDQNGGFKK LTVLQLGIRM LDVLEYIHEN EYVHGDIKAA NLLLDFTNPD
RVYLADYGLS YRYCPNGNHK QYQEDPRKGH NGTIEFTSLD AHKGVAPSRR SDVEILGYCM
LHWLFGKLPW EAKLDDPVAV QTAKTNLLDE LPESVLKWAP SGSSCSELVK YLMYVHNLAY
DDKPDYQKLK KILNPDGVPL GPLEFSTKVQ SVHVRTPAQQ KVDSPKATRK PANEFPAKFP
KKVHRETRAR QREEQEDSQP TMLQSRPAAP ENSRTRKIHE YSDIFSEMQS LQQTPSYMSF
QGSYCKPYLD CTRRDPIRKP RSLPRYRHTP TGNLGVTDLE SSPRFWPAIF QLTLSEETKA
DVYYYGITIF CLLIFVFLAL YFL


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