DCK_MOUSE
ID DCK_MOUSE Reviewed; 260 AA.
AC P43346;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Deoxycytidine kinase;
DE Short=dCK;
DE EC=2.7.1.74 {ECO:0000269|PubMed:7929097};
DE AltName: Full=Deoxyadenosine kinase;
DE EC=2.7.1.76 {ECO:0000269|PubMed:7929097};
DE AltName: Full=Deoxyguanosine kinase;
DE EC=2.7.1.113 {ECO:0000269|PubMed:7929097};
GN Name=Dck;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7929097; DOI=10.1016/s0021-9258(19)51093-6;
RA Karlsson A., Johansson M., Eriksson S.;
RT "Cloning and expression of mouse deoxycytidine kinase. Pure recombinant
RT mouse and human enzymes show differences in substrate specificity.";
RL J. Biol. Chem. 269:24374-24378(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Liver;
RX PubMed=11150511; DOI=10.1016/s0014-5793(00)02347-4;
RA Johansson M., Norda A., Karlsson A.;
RT "Conserved gene structure and transcription factor sites in the human and
RT mouse deoxycytidine kinase genes.";
RL FEBS Lett. 487:209-212(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Phosphorylates the deoxyribonucleosides deoxycytidine,
CC deoxyguanosine and deoxyadenosine. {ECO:0000269|PubMed:7929097}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a
CC ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74;
CC Evidence={ECO:0000269|PubMed:7929097};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+);
CC Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216;
CC EC=2.7.1.76; Evidence={ECO:0000269|PubMed:7929097};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+);
CC Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216;
CC EC=2.7.1.113; Evidence={ECO:0000269|PubMed:7929097};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 uM for deoxycytidine {ECO:0000269|PubMed:7929097};
CC KM=553 uM for deoxyadenosine {ECO:0000269|PubMed:7929097};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27707}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27707}.
CC -!- PTM: Phosphorylated and activated in vitro upon phosphorylation at Ser-
CC 74 by CSNK1D/CK1. {ECO:0000250|UniProtKB:P27707}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; X77731; CAA54787.1; -; mRNA.
DR EMBL; AF260315; AAG53743.1; -; Genomic_DNA.
DR EMBL; BC060062; AAH60062.1; -; mRNA.
DR CCDS; CCDS19405.1; -.
DR PIR; A55122; A55122.
DR RefSeq; NP_031858.1; NM_007832.4.
DR AlphaFoldDB; P43346; -.
DR SMR; P43346; -.
DR BioGRID; 199066; 1.
DR STRING; 10090.ENSMUSP00000031311; -.
DR BindingDB; P43346; -.
DR ChEMBL; CHEMBL2570; -.
DR iPTMnet; P43346; -.
DR PhosphoSitePlus; P43346; -.
DR EPD; P43346; -.
DR jPOST; P43346; -.
DR PaxDb; P43346; -.
DR PeptideAtlas; P43346; -.
DR PRIDE; P43346; -.
DR ProteomicsDB; 279493; -.
DR Antibodypedia; 12905; 616 antibodies from 38 providers.
DR DNASU; 13178; -.
DR Ensembl; ENSMUST00000031311; ENSMUSP00000031311; ENSMUSG00000029366.
DR GeneID; 13178; -.
DR KEGG; mmu:13178; -.
DR UCSC; uc008yah.1; mouse.
DR CTD; 1633; -.
DR MGI; MGI:102726; Dck.
DR VEuPathDB; HostDB:ENSMUSG00000029366; -.
DR eggNOG; KOG4235; Eukaryota.
DR GeneTree; ENSGT00940000157321; -.
DR HOGENOM; CLU_030466_1_1_1; -.
DR InParanoid; P43346; -.
DR OMA; YQDWHEW; -.
DR OrthoDB; 1505356at2759; -.
DR PhylomeDB; P43346; -.
DR TreeFam; TF324413; -.
DR BRENDA; 2.7.1.74; 3474.
DR Reactome; R-MMU-73614; Pyrimidine salvage.
DR Reactome; R-MMU-74217; Purine salvage.
DR SABIO-RK; P43346; -.
DR BioGRID-ORCS; 13178; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Dck; mouse.
DR PRO; PR:P43346; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P43346; protein.
DR Bgee; ENSMUSG00000029366; Expressed in indifferent gonad and 254 other tissues.
DR ExpressionAtlas; P43346; baseline and differential.
DR Genevisible; P43346; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0043771; F:cytidine kinase activity; ISO:MGI.
DR GO; GO:0004136; F:deoxyadenosine kinase activity; IMP:MGI.
DR GO; GO:0004137; F:deoxycytidine kinase activity; ISS:UniProtKB.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; ISO:MGI.
DR GO; GO:0019136; F:deoxynucleoside kinase activity; IBA:GO_Central.
DR GO; GO:0032546; F:deoxyribonucleoside binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0032548; F:pyrimidine deoxyribonucleoside binding; ISO:MGI.
DR GO; GO:0106383; P:dAMP salvage; IMP:MGI.
DR GO; GO:0046092; P:deoxycytidine metabolic process; ISO:MGI.
DR GO; GO:0106384; P:dGMP salvage; TAS:MGI.
DR GO; GO:1901293; P:nucleoside phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0046939; P:nucleotide phosphorylation; ISO:MGI.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; ISS:UniProtKB.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..260
FT /note="Deoxycytidine kinase"
FT /id="PRO_0000175091"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P27707"
FT MOD_RES 15
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P27707"
FT MOD_RES 72
FT /note="Phosphothreonine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P27707"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 260 AA; 30367 MW; 778FDDDD07407BDE CRC64;
MATPPKRFCP SPSTSSEGTR IKKISIEGNI AAGKSTFVNI LKQASEDWEV VPEPVARWCN
VQSTQEEFEE LTTSQKSGGN VLQMMYEKPE RWSFTFQSYA CLSRIRAQLA SLNGKLKDAE
KPVLFFERSV YSDRYIFASN LYESDCMNET EWTIYQDWHD WMNSQFGQSL ELDGIIYLRA
TPEKCLNRIY LRGRNEEQGI PLEYLEKLHY KHESWLLHRT LKTSFDYLQE VPVLTLDVNE
DFKDKHESLV EKVKEFLSTL
