Tag | Content |
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EKPD ID | EKS-HOS-00042 |
Classification | Group/Family | Score | E-Value | Start | End | Domain Length |
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CK1/VRK | 421.3 | 6.8E-126 | 29 | 292 | 264 |
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Status | Reviewed |
Ensembl Protein | ENSP00000402375 |
UniProt Accession | Q86Y07; B4DKL0; D6W5D4; D6W5D6; Q49AK9; Q53EU9; Q53S39; Q53S77; Q53TU1; Q86Y08; Q86Y09; Q86Y10; Q86Y11; Q86Y12; Q8IXI5; Q99987; |
Protein Name | Serine/threonine-protein kinase VRK2 |
Protein Synonyms/Alias | Vaccinia-related kinase 2; |
Gene Name | VRK2 |
Gene Synonyms/Alias | VRK2; |
Ensembl Information | |
Organism | Homo sapiens |
Functional Description | Serine/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 Length | 396 |
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 |
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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 |
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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 |
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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 |
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Keyword | 3D-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 Source | Ensembl |
Orthology | |
Gene Ontology | |
KEGG | |
InterPros | |
Pfam | |
SMARTs | |
Prosites | |
Prints | |
Created Date | 20-Feb-2013 |