VRK1_DANRE
ID VRK1_DANRE Reviewed; 425 AA.
AC Q7ZUS1;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Serine/threonine-protein kinase VRK1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q99986};
DE AltName: Full=Vaccinia-related kinase 1;
GN Name=vrk1; ORFNames=zgc:56266;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) 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 p53/TP53 and may thereby prevent the interaction between p53/TP53 and
CC MDM2. Phosphorylates KAT5 in response to DNA damage, promoting KAT5
CC association with chromatin and histone acetyltransferase activity.
CC Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its
CC binding to LEM domain-containing proteins and causes its relocalization
CC from the nucleus to the cytoplasm. Phosphorylates ATF2 which activates
CC its transcriptional activity. {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99986}. Cytoplasm
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; BC047853; AAH47853.1; -; mRNA.
DR RefSeq; NP_998550.1; NM_213385.1.
DR AlphaFoldDB; Q7ZUS1; -.
DR SMR; Q7ZUS1; -.
DR STRING; 7955.ENSDARP00000045990; -.
DR PaxDb; Q7ZUS1; -.
DR GeneID; 406694; -.
DR KEGG; dre:406694; -.
DR CTD; 7443; -.
DR ZFIN; ZDB-GENE-040426-2709; vrk1.
DR eggNOG; KOG1164; Eukaryota.
DR InParanoid; Q7ZUS1; -.
DR OrthoDB; 866200at2759; -.
DR PhylomeDB; Q7ZUS1; -.
DR Reactome; R-DRE-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR PRO; PR:Q7ZUS1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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; Kinase; Mitosis;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..425
FT /note="Serine/threonine-protein kinase VRK1"
FT /id="PRO_0000086805"
FT DOMAIN 38..329
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 343..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 44..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 425 AA; 47771 MW; 6D6BB030D3D34A86 CRC64;
MPPKKADGVK KARAPAKRKL AEEFPSGEVL TDNAKKKWKL GSAVGQGGFG LLYLANEDSS
GPVTADAPYV IKVEPSDNGP LFSELKFYMR AAKPDLIGAW MKSKKMEYLG VPKYWGSGFH
EKNGKRYRFM VMDRFGTDLQ KLFEGNGKKF SRKLVLQLGL RLLDILEYIH DHEYVHADIK
ASNLLLSYTN PNQVFLVDYG LAYRYAPEGV PKEYKEDPKR CHDGTIEFTS IDAHKGVSPS
RRADLEIMGY CMIQWLCSRL PWEDKLQDPL YVRDSKLRCR DNIDEFLKSC FASGNIPAEM
GKFMQEVKVL GYTDRPDYDK LRGILQQGLK SIGSTDDKKL DFGVATNSTS LPSVKTPKRK
KAEEKGQSAD ETDSTPAKKR RAPQKKEVNG AKKTASPAKR PVKKETQASS EPAVKKSRGR
PKKNS
