VRK1_BOVIN
ID VRK1_BOVIN Reviewed; 396 AA.
AC Q32PI1; F1ML67;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Serine/threonine-protein kinase VRK1;
DE EC=2.7.11.1;
DE AltName: Full=Vaccinia-related kinase 1;
GN Name=VRK1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serine/threonine kinase involved in cell cycle, nuclear
CC condensation and transcription regulation. Involved in Golgi
CC disassembly during the cell cycle: following phosphorylation by PLK3
CC during mitosis, required to induce Golgi fragmentation. Phosphorylates
CC 'Thr-18' of p53/TP53 and may thereby prevent the interaction between
CC p53/TP53 and MDM2. Phosphorylates KAT5 in response to DNA damage,
CC promoting KAT5 association with chromatin and histone acetyltransferase
CC activity. Phosphorylates BANF1: disrupts its ability to bind DNA,
CC reduces its binding to LEM domain-containing proteins and causes its
CC relocalization from the nucleus to the cytoplasm. Phosphorylates ATF2
CC which activates its transcriptional activity.
CC {ECO:0000250|UniProtKB:Q99986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q99986};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q99986};
CC -!- ACTIVITY REGULATION: Active in presence of Mn(2+), Mg(2+) and Zn(2+),
CC but is not functional with Ca(2+) or Cu(2+). Has a higher affinity for
CC Mn(2+) than for Mg(2+). RAN inhibits its autophosphorylation and its
CC ability to phosphorylate histone H3 (By similarity).
CC {ECO:0000250|UniProtKB:Q99986}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99986}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99986}. Note=Dispersed throughout the cell but
CC not located on mitotic spindle or chromatids during mitosis.
CC {ECO:0000250|UniProtKB:Q99986}.
CC -!- PTM: Autophosphorylated at various serine and threonine residues.
CC Autophosphorylation does not impair its ability to phosphorylate
CC p53/TP53. Phosphorylation by PLK3 leads to induction of Golgi
CC fragmentation during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q99986}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC protein kinase family. VRK subfamily. {ECO:0000305}.
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DR EMBL; DAAA02053166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02053167; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108107; AAI08108.1; -; mRNA.
DR RefSeq; NP_001033313.1; NM_001038224.2.
DR AlphaFoldDB; Q32PI1; -.
DR SMR; Q32PI1; -.
DR STRING; 9913.ENSBTAP00000018916; -.
DR PRIDE; Q32PI1; -.
DR Ensembl; ENSBTAT00000018916; ENSBTAP00000018916; ENSBTAG00000014230.
DR Ensembl; ENSBTAT00000078182; ENSBTAP00000074019; ENSBTAG00000014230.
DR GeneID; 618880; -.
DR KEGG; bta:618880; -.
DR CTD; 7443; -.
DR VEuPathDB; HostDB:ENSBTAG00000014230; -.
DR VGNC; VGNC:36834; VRK1.
DR eggNOG; KOG1164; Eukaryota.
DR GeneTree; ENSGT00940000155554; -.
DR InParanoid; Q32PI1; -.
DR OrthoDB; 866200at2759; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000014230; Expressed in oocyte and 106 other tissues.
DR ExpressionAtlas; Q32PI1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0090166; P:Golgi disassembly; ISS:UniProtKB.
DR GO; GO:0016572; P:histone phosphorylation; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0120187; P:positive regulation of protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:AgBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:AgBase.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Isopeptide bond; Kinase;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..396
FT /note="Serine/threonine-protein kinase VRK1"
FT /id="PRO_0000271432"
FT DOMAIN 37..317
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 352..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99986"
FT CROSSLNK 71
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99986"
SQ SEQUENCE 396 AA; 45358 MW; A30A8F0A7BEC7684 CRC64;
MPRVKAAQAG RQGPAKRRLA EHFAAGEIIT DMNKKEWKLG SPIGQGGFGC IYLADMNSSK
SVGNDAPCVV KVEPSDNGPL FTELKFYQRA AKPEQIQKWI RTHKLKYLGV PKYWGSGLHD
KNGKSYRFMI IDRFGSDLQK IYEANAKRFS RKTVLQLSLR ILDILEYIHE HEYVHGDIKA
SNLLLSYKNP DQVYLVDYGL AYRYCPEGTH KEYKEDPKRC HDGTVEFTSI DAHNGVAPSR
RGDLEILGYC MIQWLSGHLP WEDNLKDPNY VRDSKIRYRE NIASLMDKCF PEKNKPDEIA
KYMETVKLLD YVEKPLYQKL RDILLQGLKA IGSKDDGKLD LTVVENGSLK AKPVAKKRKK
EAEESVESSV EDMECSDKQT EEATQTRSKT RKRVQK
