UCK2_MOUSE
ID UCK2_MOUSE Reviewed; 261 AA.
AC Q99PM9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Uridine-cytidine kinase 2;
DE Short=UCK 2;
DE EC=2.7.1.48 {ECO:0000250|UniProtKB:Q9BZX2};
DE AltName: Full=Cytidine monophosphokinase 2;
DE AltName: Full=Uridine monophosphokinase 2;
GN Name=Uck2; Synonyms=Umpk;
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].
RX PubMed=11306702; DOI=10.1124/mol.59.5.1181;
RA Van Rompay A.R., Norda A., Linden K., Johansson M., Karlsson A.;
RT "Phosphorylation of uridine and cytidine nucleoside analogs by two human
RT uridine-cytidine kinases.";
RL Mol. Pharmacol. 59:1181-1186(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 uridine and cytidine to uridine monophosphate
CC and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides
CC or purine ribonucleosides. Can use ATP or GTP as a phosphate donor.
CC {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + uridine = ADP + H(+) + UMP; Xref=Rhea:RHEA:16825,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16704, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q9BZX2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cytidine = ADP + CMP + H(+); Xref=Rhea:RHEA:24674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17562, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q9BZX2};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via salvage pathway;
CC CTP from cytidine: step 1/3. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9BZX2}.
CC -!- INTERACTION:
CC Q99PM9; Q60631: Grb2; NbExp=3; IntAct=EBI-644712, EBI-1688;
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; AF236636; AAK14052.1; -; mRNA.
DR EMBL; BC023789; AAH23789.1; -; mRNA.
DR CCDS; CCDS15455.1; -.
DR RefSeq; NP_109649.1; NM_030724.3.
DR AlphaFoldDB; Q99PM9; -.
DR SMR; Q99PM9; -.
DR BioGRID; 219851; 2.
DR IntAct; Q99PM9; 3.
DR STRING; 10090.ENSMUSP00000027839; -.
DR iPTMnet; Q99PM9; -.
DR PhosphoSitePlus; Q99PM9; -.
DR EPD; Q99PM9; -.
DR MaxQB; Q99PM9; -.
DR PaxDb; Q99PM9; -.
DR PRIDE; Q99PM9; -.
DR ProteomicsDB; 299636; -.
DR Antibodypedia; 34333; 200 antibodies from 27 providers.
DR DNASU; 80914; -.
DR Ensembl; ENSMUST00000053686; ENSMUSP00000060202; ENSMUSG00000026558.
DR GeneID; 80914; -.
DR KEGG; mmu:80914; -.
DR UCSC; uc007dku.2; mouse.
DR CTD; 7371; -.
DR MGI; MGI:1931744; Uck2.
DR VEuPathDB; HostDB:ENSMUSG00000026558; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_021278_1_1_1; -.
DR InParanoid; Q99PM9; -.
DR OMA; WGEISNN; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q99PM9; -.
DR TreeFam; TF316686; -.
DR Reactome; R-MMU-73614; Pyrimidine salvage.
DR UniPathway; UPA00574; UER00637.
DR UniPathway; UPA00579; UER00640.
DR BioGRID-ORCS; 80914; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Uck2; mouse.
DR PRO; PR:Q99PM9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q99PM9; protein.
DR Bgee; ENSMUSG00000026558; Expressed in ectoderm and 265 other tissues.
DR ExpressionAtlas; Q99PM9; baseline and differential.
DR Genevisible; Q99PM9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043771; F:cytidine kinase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004849; F:uridine kinase activity; ISS:UniProtKB.
DR GO; GO:0044211; P:CTP salvage; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; ISS:UniProtKB.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029925; UCK-2.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF131; PTHR10285:SF131; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT CHAIN 2..261
FT /note="Uridine-cytidine kinase 2"
FT /id="PRO_0000164456"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZX2"
SQ SEQUENCE 261 AA; 29404 MW; 780AA3CFF5CA8153 CRC64;
MAGDSEQTLQ NHQQPNGGEP FLIGVSGGTA SGKSSVCAKI VQLLGQNEVD YHQKQVVILS
QDSFYRVLTS EQKAKALKGQ FNFDHPDAFD NELIFKTLKE ITEGKTVQIP VYDFVSHSRK
EETVTIYPAD VVLFEGILAF YSQEVRDLFQ MKLFVDTDAD TRLSRRVLRD ISERGRDLEQ
ILSQYITFVK PAFEEFCLPT KKYADVIIPR GADNLVAINL IVQHIQDILN GGLSKRQTNG
YLNGYTPSRK RQASESSSRP H
