UCKL1_MOUSE
ID UCKL1_MOUSE Reviewed; 548 AA.
AC Q91YL3;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Uridine-cytidine kinase-like 1;
DE EC=2.7.1.48;
GN Name=Uckl1; Synonyms=Urkl1;
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 [LARGE SCALE MRNA].
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC 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: May contribute to UTP accumulation needed for blast
CC transformation and proliferation. {ECO:0000250}.
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 -!- 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 -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC UMP from uridine: step 1/1.
CC -!- SUBUNIT: Interacts with RNF19B. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RNF19B; which induces proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the uridine kinase family. {ECO:0000305}.
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DR EMBL; BC016535; AAH16535.1; -; mRNA.
DR CCDS; CCDS17216.1; -.
DR RefSeq; NP_081041.2; NM_026765.3.
DR AlphaFoldDB; Q91YL3; -.
DR SMR; Q91YL3; -.
DR BioGRID; 212925; 13.
DR STRING; 10090.ENSMUSP00000050398; -.
DR iPTMnet; Q91YL3; -.
DR PhosphoSitePlus; Q91YL3; -.
DR EPD; Q91YL3; -.
DR MaxQB; Q91YL3; -.
DR PaxDb; Q91YL3; -.
DR PeptideAtlas; Q91YL3; -.
DR PRIDE; Q91YL3; -.
DR ProteomicsDB; 297799; -.
DR Antibodypedia; 1482; 141 antibodies from 27 providers.
DR DNASU; 68556; -.
DR Ensembl; ENSMUST00000057816; ENSMUSP00000050398; ENSMUSG00000089917.
DR GeneID; 68556; -.
DR KEGG; mmu:68556; -.
DR UCSC; uc008oms.2; mouse.
DR CTD; 54963; -.
DR MGI; MGI:1915806; Uckl1.
DR VEuPathDB; HostDB:ENSMUSG00000089917; -.
DR eggNOG; KOG4203; Eukaryota.
DR GeneTree; ENSGT01020000230412; -.
DR HOGENOM; CLU_021278_0_1_1; -.
DR InParanoid; Q91YL3; -.
DR OMA; RTKTMYG; -.
DR OrthoDB; 929897at2759; -.
DR PhylomeDB; Q91YL3; -.
DR TreeFam; TF105902; -.
DR Reactome; R-MMU-73614; Pyrimidine salvage.
DR UniPathway; UPA00574; UER00637.
DR BioGRID-ORCS; 68556; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Uckl1; mouse.
DR PRO; PR:Q91YL3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91YL3; protein.
DR Bgee; ENSMUSG00000089917; Expressed in retinal neural layer and 241 other tissues.
DR ExpressionAtlas; Q91YL3; baseline and differential.
DR Genevisible; Q91YL3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004849; F:uridine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR CDD; cd06223; PRTases_typeI; 1.
DR CDD; cd02023; UMPK; 1.
DR Gene3D; 3.40.50.2020; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR006083; PRK/URK.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR029933; UCKL1.
DR InterPro; IPR000764; Uridine_kinase-like.
DR PANTHER; PTHR10285:SF68; PTHR10285:SF68; 1.
DR Pfam; PF00485; PRK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR00235; udk; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..548
FT /note="Uridine-cytidine kinase-like 1"
FT /id="PRO_0000164461"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWZ5"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 539
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWZ5"
SQ SEQUENCE 548 AA; 60842 MW; 99A5CA23E9BD8525 CRC64;
MAAPPASMSA APSPLQSAVA PDVPGRQAEQ NETACEDRSN AGTLDRLLPP VGTGRSPRKR
TTSQCKSEPP LLRTSKRTIY TAGRPPWYNE HGTQSKEAFA IGLGGGSASG KTTVARMIIE
ALDVPWVVLL SMDSFYKVLT QQQQEQAACN NFNFDHPDAF DFDLIISTLK KLKQGRSVQV
PIYDFTTHSR KKDWKTLYGA NVIIFEGIMA FADKTLLELL DMKIFVDTDS DIRLVRRLRR
DISERGRDIE GVIKQYNKFV KPAFDQYIQP TMRLADIVVP RGSGNTVAID LIVQHVHSQL
EERELSVRAA LASAHQCHPL PQTLSVLKST PQVRGMHTII RDKETSRDEF IFYSKRLMRL
LIEHALSFLP FQDCTVQTPQ GQDYVGKCYA GKQITGVSIL RAGETMEPAL RAVCKDVRIG
TILIQTNQLT GEPELHYLRL PKDISDDHVI LMDCTVSTGA AAMMAVRVLL DHDVPEDKIF
LLSLLMAEMG VHSVAYAFPR VRIITTAVDK RVNDLFRIIP GIGNFGDRYF GTDAVPDGSD
DDEAATVG
