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Information on EC 2.7.1.48 - uridine/cytidine kinase and Organism(s) Homo sapiens and UniProt Accession Q9HA47
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2.7.1.48 uridine/cytidine kinaseIUBMB Comments
The enzyme, found in prokaryotes and eukaryotes, phosphorylates both uridine and cytidine to their monophosphate forms. The enzyme from Escherichia coli prefers GTP to ATP. The human enzyme also catalyses the phosphorylation of several cytotoxic ribonucleoside analogs. cf. EC 2.7.1.213, cytidine kinase.
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Word Map
- 2.7.1.48
- thymidine
-
salvage
- uracil
-
phosphoribosyltransferase
- phosphorylase
- orotate
- ump
- 5-fluorouracil
- 5-fluorouridine
- deoxycytidine
- 5-azacytidine
- 6-azauridine
- 3-deazauridine
- orotidine
- pyrazofurin
- medicine
- 5-fluoro-2'-deoxyuridine
-
3huridine
- dihydrouracil
- drug development
- diagnostics
- biotechnology
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
uridine kinase, uridine-cytidine kinase, uridine/cytidine kinase, uridine-cytidine kinase 2, uckl1, uridine/cytidine kinase 2, uridine cytidine kinase 2, uridine phosphokinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
UCK1
ATP:uridine 5'-phosphotransferase
-
-
-
-
kinase, uridine (phosphorylating)
-
-
-
-
pyrimidine ribonucleoside kinase
-
-
-
-
UCK2
uridine kinase
-
-
-
-
uridine phosphokinase
-
-
-
-
uridine-cytidine kinase 2
-
additional information
UCK2
-
additional information
-
two different enzymes termed UCK1 and UCK2 with 68.8% identity in the deduced amino acid sequence, increased expression of both forms in many tumor cells
additional information
two different enzymes termed UCK1 and UCK2 with 69% sequence identity, expression of UCK 2 but not UCK1 was shown to be enhanced in cancer cells
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:uridine/cytidine 5'-phosphotransferase
The enzyme, found in prokaryotes and eukaryotes, phosphorylates both uridine and cytidine to their monophosphate forms. The enzyme from Escherichia coli prefers GTP to ATP. The human enzyme also catalyses the phosphorylation of several cytotoxic ribonucleoside analogs. cf. EC 2.7.1.213, cytidine kinase.
CAS REGISTRY NUMBER
COMMENTARY
9026-39-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-thiocytidine
ADP + 2-thiocytidine 5'-monophosphate
recombinant uridine kinase 1, 20% of activity with uridine
-
?
ATP + 3,4,5,6-tetrahydrouridine
ADP + 3,4,5,6-tetrahydrouridine 5'-monophosphate
recombinant uridine kinase 1, 13% of activity with uridine
-
?
ATP + 4-thiouridine
ADP + 4-thiouridine 5'-monophosphate
recombinant uridine kinase 1, 122% of activity with uridine
-
?
ATP + 5-bromouridine
ADP + 5-bromouridine 5'-monophosphate
recombinant uridine kinase 1, 50% of activity with uridine
-
?
ATP + 5-fluorocytidine
ADP + 5-fluorocytidine 5'-monophosphate
recombinant uridine kinase 1, 37% of activity with uridine
-
?
ATP + 5-hydroxyuridine
ADP + 5-hydroxyuridine 5'-monophosphate
recombinant uridine kinase 1, 14% of activity with uridine
-
?
ATP + 5-methoxyuridine
ADP + 5-methoxyuridine 5'-monophosphate
recombinant uridine kinase 1, 122% of activity with uridine
-
?
ATP + 5-methylcytidine
ADP + 5-methylcytidine 5'-monophosphate
recombinant uridine kinase 1, 9% of activity with uridine
-
?
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
recombinant uridine kinase 1, 38% of activity with uridine, recombinant uridine kinase 2, 148% of activity with uridine
-
?
ATP + N4-acetylcytidine
ADP + N4-acetylcytidine 5'-monophosphate
recombinant uridine kinase 1, 142% of activity with uridine
-
?
ATP + N4-aminocytidine
ADP + N4-aminocytidine 5'-monophosphate
recombinant uridine kinase 1, 20% of activity with uridine
-
?
ATP + N4-anisoylcytidine
ADP + N4-anisoylcytidine 5'-monophosphate
recombinant uridine kinase 1, 20% of activity with uridine
-
?
ATP + N4-benzoylcytidine
ADP + N4-benzoylcytidine 5'-monophosphate
recombinant uridine kinase 1, 68% of activity with uridine
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine 5'-phosphate
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 3'-ethynylcytidine 5'-monophosphate
-
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine 5'-phosphate
ATP + 2-thiocytidine
ADP + 2-thiocytidine 5'-monophosphate
recombinant uridine kinase 2, 86% of activity with uridine
-
?
ATP + 3'-deoxy-3'-ethynylcytidine
ADP + 3'-deoxy-3'-ethynylcytidine 5'-monophosphate
-
recombinant uridine kinase, 20% of activity with uridine
-
?
ATP + 3'-deoxy-3'-ethynyluridine
ADP + 3'-deoxy-3'-ethynyluridine 5'-monophosphate
-
recombinant uridine kinase, 20% of activity with uridine
-
?
ATP + 3'-ethynylcytidine
ADP + 3'-ethynylcytidine 5'-monophosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
?
ATP + 3'-ethynylcytidine 5'-diphosphate
ADP + 3'-ethynylcytidine 5'-triphosphate
-
-
-
?
ATP + 3'-ethynylcytidine 5'-monophosphate
ADP + 3'-ethynylcytidine 5'-diphosphate
-
-
-
?
ATP + 3'-ethynyluridine
ADP + 3'-ethynyluridine 5'-monophosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-ethynyluridine 5'-diphosphate
ADP + 3'-ethynyluridine 5'-triphosphate
-
-
-
?
ATP + 3'-ethynyluridine 5'-monophosphate
ADP + 3'-ethynyluridine 5'-diphosphate
-
-
-
?
ATP + 3,4,5,6-tetrahydrouridine
ADP + 3,4,5,6-tetrahydrouridine 5'-monophosphate
recombinant uridine kinase 2, 81% of activity with uridine
-
?
ATP + 3-deazauridine
ADP + 3-deazauridine 5'-monophosphate
recombinant uridine kinase 2, 49% of activity with uridine
-
?
ATP + 3-methyluridine
ADP + 3-methyluridine 5'-monophosphate
recombinant uridine kinase 2, 18% of activity with uridine
-
?
ATP + 4-amino-1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxy-3-(hydroxymethyl)cyclopent-2-en-1-yl]pyrimidin-2(1H)-one
ADP + [(3S,4S,5R)-3-(4-amino-2-oxopyrimidin-1(2H)-yl)-2-fluoro-4,5-dihydroxycyclopent-1-en-1-yl]methyl phosphate
-
-
-
ir
ATP + 4-thiouridine
ADP + 4-thiouridine 5'-monophosphate
recombinant uridine kinase 2, 125% of activity with uridine
-
?
ATP + 5-bromouridine
ADP + 5-bromouridine 5'-monophosphate
recombinant uridine kinase 2,6% of activity with uridine
-
?
ATP + 5-fluorocytidine
ADP + 5-fluorocytidine 5'-monophosphate
recombinant uridine kinase 2, 184% of activity with uridine
-
?
ATP + 5-hydroxyuridine
ADP + 5-hydroxyuridine 5'-monophosphate
recombinant uridine kinase 2, 12% of activity with uridine
-
?
ATP + 5-methoxyuridine
ADP + 5-methoxyuridine 5'-monophosphate
recombinant uridine kinase 2, 92% of activity with uridine
-
?
ATP + 5-methylcytidine
ADP + 5-methylcytidine 5'-monophosphate
recombinant uridine kinase 2, 30% of activity with uridine
-
?
ATP + 6-azacytidine
ADP + 6-azacytidine 5'-monophosphate
recombinant uridine kinase 2, 75% of activity with uridine
-
?
ATP + 6-azauridine
ADP + 6-azauridine 5'-monophosphate
recombinant uridine kinase 1, 38% of activity with uridine, recombinant uridine kinase 2, 148% of activity with uridine
-
?
ATP + cyclopentenyl-cytosine
ADP + cyclopentenylcytosine 5'-monophosphate
-
-
-
?
ATP + cyclopentenylcytosine
ADP + cyclopentenylcytosine 5'-monophosphate
-
recombinant uridine kinase, 12% of activity with uridine
-
?
ATP + fluorocyclopentenylcytosine
?
an orally available cytidine analogue, RX-3117
-
-
?
ATP + N4-acetylcytidine
ADP + N4-acetylcytidine 5'-monophosphate
recombinant uridine kinase 2, 84% of activity with uridine
-
?
ATP + N4-anisoylcytidine
ADP + N4-anisoylcytidine 5'-monophosphate
recombinant uridine kinase 2, 12% of activity with uridine
-
?
ATP + N4-benzoylcytidine
ADP + N4-benzoylcytidine 5'-monophosphate
recombinant uridine kinase 2, 51% of activity with uridine
-
?
ATP + ribavirin
ADP + ribavirin monophosphate
-
13% of substrate phosphorylated, within 2 h incubation
-
-
?
ATP + uridine
ADP + UMP
no activity with adenosine, guanosine and deoxyribonucleotides, no activity with CTP and UTP
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine 5'-phosphate
-
-
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine 5'-phosphate
-
UCK2 enzyme activity required to produce the antitumoral active metabolite
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine 5'-phosphate
-
-
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine 5'-phosphate
-
UCK2 enzyme activity required to produce the antitumoral active metabolite
-
-
?
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
ir
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
-
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
ir
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
-
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
-
-
-
-
?
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
-
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
-
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
-
-
-
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
-
recombinant uridine kinase
-
?
ATP + 5-fluorouridine
ADP + 5-fluorouridine 5'-monophosphate
recombinant uridine kinase 2, 89% of activity with uridine
-
?
ATP + cytidine
ADP + CMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway, essential for cell proliferation, UCK 2 involved in tumor formation
-
-
?
ATP + cytidine
ADP + CMP
-
89% of substrate phosphorylated, within 2 h incubation
-
-
?
ATP + cytidine
ADP + CMP
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
-
-
?
ATP + uridine
ADP + UMP
no activity with adenosine, guanosine and deoxyribonucleotides, no activity with CTP and UTP
-
?
ATP + uridine
ADP + UMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway, essential for cell proliferation, UCK 2 involved in tumor formation
-
-
?
ATP + uridine
ADP + UMP
-
56% of substrate phosphorylated, within 2 h incubation
-
-
?
ATP + uridine
ADP + UMP
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
-
-
?
additional information
?
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
additional information
?
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
additional information
?
-
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
additional information
?
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
additional information
?
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
additional information
?
-
-
uridine-cytidine kinase (UCK) catalyzes the phosphorylation of uridine, cytidine, and several pyrimidine ribonucleoside analogues
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine 5'-phosphate
-
UCK2 enzyme activity required to produce the antitumoral active metabolite
-
-
?
ATP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
ADP + 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine 5'-phosphate
-
UCK2 enzyme activity required to produce the antitumoral active metabolite
-
-
?
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
ir
ATP + 3'-C-ethynylcytidine
ADP + 3'-C-ethynylcytidine 5'-phosphate
-
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine
-
-
ir
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-diphosphate
ADP + 3'-C-ethynylcytidine 5'-triphosphate
-
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
-
-
-
?
ATP + 3'-C-ethynylcytidine 5'-phosphate
ADP + 3'-C-ethynylcytidine 5'-diphosphate
-
-
-
-
?
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-C-ethynyluridine
ADP + 3'-C-ethynyluridine 5'-phosphate
-
i.e. 1-(3-C-ethynyl-beta-D-ribopentofuranosyl)uridine
-
-
?
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-diphosphate
ADP + 3'-C-ethynyluridine 5'-triphosphate
-
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
-
-
-
?
ATP + 3'-C-ethynyluridine 5'-phosphate
ADP + 3'-C-ethynyluridine 5'-diphosphate
-
-
-
-
?
ATP + cytidine
ADP + CMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + cytidine
ADP + CMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway, essential for cell proliferation, UCK 2 involved in tumor formation
-
-
?
ATP + cytidine
ADP + CMP
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
-
-
?
ATP + uridine
ADP + UMP
-
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway
-
-
?
ATP + uridine
ADP + UMP
rate limiting enzyme of the pyrimidine-nucleotide salvage pathway, essential for cell proliferation, UCK 2 involved in tumor formation
-
-
?
ATP + uridine
ADP + UMP
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1E)-[[4-(4-tert-butylphenyl)-5-cyano-6-hydroxypyrimidin-2-yl]sulfanyl]-N-(2-methoxyphenyl)ethanimidic acid
-
(1Z)-[([5-[(4-fluorophenyl)methyl]-7-oxo-6,7-dihydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]-N-(2-methylphenyl)ethanimidic acid
-
2-[(5-cyano-4-hydroxy-6-phenylpyrimidin-2-yl)sulfanyl]-N-(4-ethylphenyl)acetamide
-
2-[[1-(4-fluorophenyl)-4-oxo-5H-pyrazolo[3,4-d]pyrimidin-6-yl]sulfanyl]-N-[2-(trifluoromethyl)phenyl]acetamide
-
2-[[4-(4-tert-butylphenyl)-5-cyano-6-hydroxypyrimidin-2-yl]sulfanyl]-N-(4-chlorophenyl)acetamide
-
3-(2-[[9-methoxy-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]acetamido)benzoic acid
-
3-(2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]acetamido)benzoic acid
-
3-[[2-[[2-(4-fluorophenyl)-5H-chromeno[2,3-d]pyrimidin-4-yl]sulfanyl]acetyl]amino]benzoic acid
-
4-(2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]acetamido)benzoic acid
-
4-[[2-[[2-(4-methoxyphenyl)-5H-chromeno[2,3-d]pyrimidin-4-yl]sulfanyl]acetyl]amino]benzoic acid
-
bhutkesoside A
isolated from Ligusticopsis wallichiana (Apiaceae). Hydrophobic interactions are predicted for bhutkesoside A with Phe83
bhutkesoside B
isolated from Ligusticopsis wallichiana (Apiaceae). Bhutkesoside B is estimated to inhibit UCK2 protein by binding to the catalytic active site of ATP, thus inhibiting ATP from binding to its active site in the UCK2 protein. Hydrophobic interactions are predicted for bhutkesoside B with Ala30
N-(3,5-dimethylphenyl)-2-[([5-[(4-fluorophenyl)methyl]-7-oxo-2,5,6,7-tetrahydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]acetamide
N-(4-bromophenyl)-2-[[1-(4-fluorophenyl)-4-hydroxy-1H-pyrazolo[3,4-d]pyrimidin-6-yl]sulfanyl]acetamide
-
N-(3,5-dimethylphenyl)-2-[([5-[(4-fluorophenyl)methyl]-7-oxo-2,5,6,7-tetrahydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]acetamide
-
N-(3,5-dimethylphenyl)-2-[([5-[(4-fluorophenyl)methyl]-7-oxo-2,5,6,7-tetrahydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]acetamide
inhibits 3'-ethynylcytidine 5'-triphosphate (5-EU) salvage by about 40% at 0.05 mM
additional information
discovery of two diacetylene glycosides as human uridine-cytidine kinase 2 inhibitors, in an in silico approach. Molecular ligand-protein docking, using uridine-cytidine kinase 2 structure PDB ID 1UDW. Druggability likeliness property of Bhutkesoside A and Bhutkesoside B as GPCR ligands, ion channel modulators (ICM), kinase inhibitors (KI), nuclear receptor ligands (NRL), protease inhibitors (PI) and enzyme inhibitors (EI) are studied, and results are retrieved as bioactivity scores, overview
-
additional information
establishment and miniaturization of an in vitro assay for UCK2 activity and high-throughput screen against an about 40,000-compound library to generate drug-like leads. Analysis of the structures, activities, and modes of inhibition of the most promising hits, overview. Non-competitive UCK2 inhibitors are identified which are able to suppress nucleoside salvage in cells both in the presence and absence of dihydroorotate dehydrogenase (DHODH) inhibitors. No inhibition by 2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]-N-phenylacetamide, and (1Z)-N-(4-fluorophenyl)[([5-[(4-fluorophenyl)methyl]-7-oxo-6,7-dihydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]ethanimidic acid
-
additional information
-
establishment and miniaturization of an in vitro assay for UCK2 activity and high-throughput screen against an about 40,000-compound library to generate drug-like leads. Analysis of the structures, activities, and modes of inhibition of the most promising hits, overview. Non-competitive UCK2 inhibitors are identified which are able to suppress nucleoside salvage in cells both in the presence and absence of dihydroorotate dehydrogenase (DHODH) inhibitors. No inhibition by 2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]-N-phenylacetamide, and (1Z)-N-(4-fluorophenyl)[([5-[(4-fluorophenyl)methyl]-7-oxo-6,7-dihydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]ethanimidic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-bromo-1-(methanesulfonyl) uracil
-
significantly increased activity at 0.001 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics in a coupled assay with lactate dehydrogenase and pyruvate kinase
-
additional information
additional information
-
Michaelis-Menten kinetics in a coupled assay with lactate dehydrogenase and pyruvate kinase
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1372
(1Z)-[([5-[(4-fluorophenyl)methyl]-7-oxo-6,7-dihydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]-N-(2-methylphenyl)ethanimidic acid
pH 8.5, temperature not specified in the publication
0.0038
4-(2-[[9-methyl-2-(4-methylphenyl)-5H-[1]benzopyrano[2,3-d]pyrimidin-4-yl]sulfanyl]acetamido)benzoic acid
pH 8.5, temperature not specified in the publication
0.012 - 0.031
ATP
dependent on the assay method, pH 8.5, temperature not specified in the publication
0.013 - 0.05
uridine
dependent on the assay method, pH 8.5, temperature not specified in the publication
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0189 - 0.048
N-(3,5-dimethylphenyl)-2-[([5-[(4-fluorophenyl)methyl]-7-oxo-2,5,6,7-tetrahydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]acetamide
0.0092 - 0.0166
N-(4-bromophenyl)-2-[[1-(4-fluorophenyl)-4-hydroxy-1H-pyrazolo[3,4-d]pyrimidin-6-yl]sulfanyl]acetamide
0.0189 - 0.048
N-(3,5-dimethylphenyl)-2-[([5-[(4-fluorophenyl)methyl]-7-oxo-2,5,6,7-tetrahydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]acetamide
Homo sapiens
22°C, 20 mM HEPES (pH 7.2), 100 mM KCl, 2 mM MgCl2, 6-300 microM ATP, 6-300 microM uridine, 1-10 nanoM enzyme UCK2
0.048
N-(3,5-dimethylphenyl)-2-[([5-[(4-fluorophenyl)methyl]-7-oxo-2,5,6,7-tetrahydro-3H-[1,2,3]triazolo[4,5-d]pyrimidin-3-yl]methyl)sulfanyl]acetamide
Homo sapiens
pH 8.5, temperature not specified in the publication
0.0092 - 0.0166
N-(4-bromophenyl)-2-[[1-(4-fluorophenyl)-4-hydroxy-1H-pyrazolo[3,4-d]pyrimidin-6-yl]sulfanyl]acetamide
Homo sapiens
22°C, 20 mM HEPES (pH 7.2), 100 mM KCl, 2 mM MgCl2, 6-300 microM ATP, 6-300 microM uridine, 1-10 nanoM enzyme UCK2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
5-13fold increase of uridine kinase activity in ovarian carcinomas over the activity in normal ovaries
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
SW480 colorectal cells, uridine kinases mRNA expression is higher than in normal tissue
analysis of the correlation between UCK2 gene expression and breast cancer survival, overview
-
A549 lung carcinoma cells, uridine kinases mRNA expression is higher than in normal tissue
-
Raji and Daud Burkitt's lymphoma cells, uridine kinases mRNA expression is higher than in normal tissue
-
gastric carcinoma cell line highly resistant to 3-ethynyl nucleosides
additional information
generation of a specific antibody against UCK1 and analysis of expression of both UCK isoforms 1 and 2 in a panel of neuroblastoma cell lines, overview. No differences are observed for UCK1 and UCK2 expression between MYCN-single copy cell lines and MYCN-amplified neuroblastoma cell lines
UCK2 is differentially expressed in many cancer tissues and in cells subjected to viral infection
UCK2 is significantly upregulated in hepatocellular carcinoma tissues compared to adjacent normal tissues
UCKL1 is significantly upregulated in hepatocellular carcinoma tissues compared to adjacent normal tissues
-
fibrosarcoma cell line highly resistant to 3-ethynyl nucleosides
-
leukemia cells Hl-60, K562 and Molt-4, uridine kinases mRNA expression is higher than in normal tissue
generation of a specific antibody against UCK1 and analysis of expression of both UCK isoforms 1 and 2 in a panel of neuroblastoma cell lines, overview. No differences are observed for UCK1 and UCK2 expression between MYCN-single copy cell lines and MYCN-amplified neuroblastoma cell lines
additional information
analysis of the differential expression of UCK2 gene in breast cancer tissues, overview
additional information
-
analysis of the differential expression of UCK2 gene in breast cancer tissues, overview
additional information
enzyme activity in two panels of tumor cell lines and xenograft cells correlated only with UCK2-mRNA expression, but not with UCK1-mRNA. Moreover, accumulation of RX-3117 nucleotides correlates with UCK2 expression
additional information
-
enzyme activity in two panels of tumor cell lines and xenograft cells correlated only with UCK2-mRNA expression, but not with UCK1-mRNA. Moreover, accumulation of RX-3117 nucleotides correlates with UCK2 expression
additional information
isoenzyme UCK2 (but not UCK1) is most abundantly overexpressed in numerous tumour cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
metabolism
physiological function
additional information
drug target
1-(3-C-ethynyl-beta-D-ribopentofuranosyl)cytosine (ECyd) is a potent inhibitor of RNA polymerase I and shows anticancer activity to various human solid tumors. ECyd is phosphorylated to 3'-ethynylcytidine 5'-monophosphate by uridine/cytidine kinase 2 (UCK2) and subsequently further to diphosphate and triphosphate (3'-ethyntlcytidine 5'-diphosphate, 3'-ethyntlcytidine 5'-triphosphate). 3'-Ethyntlcytidine 5'-triphosphate is an active metabolite that can inhibit RNA polymerase I competitively. IVS5 + 5 G > A mutation would affect the expression level of the UCK2 transcript and result in decreased sensitivity to ECyd. The UCK2 is a key drug-response predictive marker for innate or acquired resistance to uridine/cytidine-type nucleoside analogs
drug target
inhibition of enzyme (UCK2) induces nucleolar stress, probably by depleting nucleotide biosynthesis, thereby destabilising ribosomal biogenesis and subsequently causing cancer cell arrest and apoptotic cell death induction
malfunction
mutation H117Y of UCK2 results in a loss of uridine phosphorylation activity of the enzyme
malfunction
overexpression of uridine-cytidine kinase 2 correlates with breast cancer progression and poor prognosis. UCK2, along with other genes involved in the 5-FU anabolic pathway, produces a phenotype of cell sensitivity to 5-FU folxadlowing knockdown
malfunction
probable ribosomal stress condition during inhibition of the UCK2 enzyme, overview. The released and subsequent activation of p53 leads towards apoptosis induction
malfunction
role of a uridine/cytidine kinase 2 mutation in cellular sensitiveness toward 3'-ethynylcytidine (ECyd) treatment of human cancer cells. The splice-site mutation of the UCK2 gene resulting in the IVS5+5 G>A variant affects the expression level of the UCK2 transcript, causing decreased sensitivity to ECyd. The IVS5+5 G>A variant generates an aberrant mRNA transcript, namely, truncated mRNA is produced and normal mRNA levels are markedly decreased in the ECyd-resistant cancer cell line HT1080. Relationship of UCK2 mutations and drug sensitivity with ECyd in several cancer cell lines, overview. Detection of the aberrant mRNA transcript in the ECyd/EUrd-resistant cancer cells with the IVS5 +5 A/A genotype
metabolism
UCK2 is feedback inhibited by UTP and CTP to adjust cellular needs and prevent overproduction of the nucleotides. In the course of cancer cell proliferation, these nucleotides are continuously synthesized to sustain protein synthesis. During gene degradation, some NMPs are released and recycled via the salvage pathway by the action of UCK2, thereby facilitating the prevention of energy loss and the waste of valuable precursors. Molecular crosstalks between UCK2 and cell death, the role of ribosomal proteins, MDM2 and p53 in regulation of cell death, and the role of UCK2 in regulation of cell death
metabolism
the enzyme is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis
physiological function
a nucleosidic medicine, 1-(3-C-ethynyl-beta-D-ribopentofuranosyl) cytosine [3'-ethynylcytidine (ECyd)], is a potent inhibitor of RNA polymerase I and shows anticancer activity to various human solid tumors in vitro and in vivo. ECyd is phosphorylated to 3'-ethynylcytidine 5'-monophosphate by uridine/cytidine kinase 2 (UCK2) and subsequently further to diphosphate and triphosphate (3'-ethynylcytidine 5'-diphosphate, 3'-ethynylcytidine 5'-triphosphate). 3'-ethynylcytidine 5'-triphosphate is an active metabolite that can inhibit RNA polymerase I competitively, causing cancer cell death
physiological function
enzyme activity in two panels of tumor cell lines and xenograft cells correlated only with UCK2-mRNA expression, but not with UCK1-mRNA. Moreover, accumulation of RX-3117 nucleotides correlates with UCK2 expression
physiological function
the pyrimidine salvage enzyme uridine-cytidine kinase 2 (UCK2) is necessary for uridine salvage. Biological significance of UCK2 in the uridine salvage is measured by incorporating exogenous 5-ethynyl-uridine (5-EU) specifically into cellular RNA
physiological function
UCK2 is responsible for the phosphorylation of uridine and cytidine to their corresponding monophosphate in a salvage pathway of pyrimidine nucleotides biosynthesis. Uridine-cytidine kinase 2 (UCK2) is linked to cell apoptosis induction. Molecular crosstalk involving UCK2 protein and cancer cell death through cell cycle arrest and triggering of apoptosis involving proteins, MDM2 and the subsequent activation of p53. UCK2 is also involved in the phosphorylation of ribonucleoside analogues, 5-azacytidine, cyclopentenyl cytosine/uracil, 5-fluorocytidine, 6-azauridine, 3-deazauridine, 5-fluorouridine as well as ethynyl cytidine and uridine. These cytotoxic drugs depends on the action of the UCK2 enzyme to sequentially transformed into nucleoside 5'-triphosphate, thereby interfering with gene synthesis vital for metabolic processes required for cancer cell growth and maintenance
physiological function
uridine-cytidine kinase (UCK) 2 is a rate-limiting enzyme involved in the salvage pathway of pyrimidine-nucleotide biosynxadthesis. Isozyme UCK2 is overexpressed in many types of cancer and may play a crucial role in activating antitumor prodrugs in human cancer cells. The isozyme catalyzes the phosphorylation of urixaddine and cytidine to form uridine monophosphate (UMP) and cytidine monophosphate (CMP) with efficiency 15 to 20fold higher than that of ubiquitously expressed isozyme UCK1
physiological function
uridine-cytidine kinase (UCK) is one of the enzymes in the nucleoside salvage pathway. UCK generally converts both cytidine and uridine to nucleoside monophosphate using ATP as the phosphate donor
additional information
uridine phosphorylation activity commonly depends on a single residue in the UCK family. Structure comparison of Thermus thermophilus enzyme ttCK and human enzyme hsUCK2
additional information
-
uridine phosphorylation activity commonly depends on a single residue in the UCK family. Structure comparison of Thermus thermophilus enzyme ttCK and human enzyme hsUCK2
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UCK1_HUMAN
277
0
31435
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
tetramer
two asymmetric dimers form a tetramer, crystal structure analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of uridine kinase 2 and in complex with CTP, UTP, cytidine, ATPgammaS and with both cytidine and ATP, the latter complex diffracted to 1.8 A resolution
in complex with Mg2+, ADP, and CMP by sitting drop vapor diffusion method
truncated form of UCK2 (1-250) in complex with substrates or feedback inhibitors UTP and CTP
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H117Y
site-directed mutagenesis, the mutation results in a loss of uridine phosphorylation activity of the enzyme
additional information
additional information
enzyme silencing by transfection of A549 and SW1573 cell lines with UCK-siRNAs. Transfection of UCK1-siRNA efficiently downregulates UCK1-mRNA, but not UCK2-mRNA expression, and does not affect sensitivity to RX-3117. Transfection of UCK2-siRNA completely downregulates UCK2-mRNA and protein and protects both A549 and SW1573 against RX-3117
additional information
-
enzyme silencing by transfection of A549 and SW1573 cell lines with UCK-siRNAs. Transfection of UCK1-siRNA efficiently downregulates UCK1-mRNA, but not UCK2-mRNA expression, and does not affect sensitivity to RX-3117. Transfection of UCK2-siRNA completely downregulates UCK2-mRNA and protein and protects both A549 and SW1573 against RX-3117
additional information
several functional point mutations, including the splice-site mutation of the UCK2 gene IVS5+5 G>A, are identified in the UCK2 enzyme protein. The IVS5+5 G>A variant generates an aberrant mRNA transcript, namely, truncated mRNA is produced and normal mRNA levels are markedly decreased in the ECyd-resistant cancer cell line HT1080. Effect of the IVS5+5G>A variation on pre-mRNA splicing. The IVS5+ 5 A/A genotype that is 98 bp shorter than a normal PCR product is detected. This variant-type UCK2 mRNA in HT1080/EUrd generates an aberrant stop codon and it produces an UCK2 protein without the C-terminal region. The wild-type UCK2 protein consists of 261 amino acid residues. In contrast, although the variant-type UCK2 mRNA conserves 166 amino acids in part of the N-terminus of UCK2, codons 167-171 are substituted by other amino acids by the frameshift mutation and parts of the C-terminal, codons 172-261, are missing (truncated). This missing region has been considered the substrate recognition site (LID domain) as well as the tetramer stabilization site. In addition, the mRNA with premature translation termination codon and coding nonfunctional protein is known to be eliminated by nonsense-mediated mRNA decay. It is possible that deletion of this region causes loss of stabilization and specific substrate recognition in UCK2 functions
additional information
-
several functional point mutations, including the splice-site mutation of the UCK2 gene IVS5+5 G>A, are identified in the UCK2 enzyme protein. The IVS5+5 G>A variant generates an aberrant mRNA transcript, namely, truncated mRNA is produced and normal mRNA levels are markedly decreased in the ECyd-resistant cancer cell line HT1080. Effect of the IVS5+5G>A variation on pre-mRNA splicing. The IVS5+ 5 A/A genotype that is 98 bp shorter than a normal PCR product is detected. This variant-type UCK2 mRNA in HT1080/EUrd generates an aberrant stop codon and it produces an UCK2 protein without the C-terminal region. The wild-type UCK2 protein consists of 261 amino acid residues. In contrast, although the variant-type UCK2 mRNA conserves 166 amino acids in part of the N-terminus of UCK2, codons 167-171 are substituted by other amino acids by the frameshift mutation and parts of the C-terminal, codons 172-261, are missing (truncated). This missing region has been considered the substrate recognition site (LID domain) as well as the tetramer stabilization site. In addition, the mRNA with premature translation termination codon and coding nonfunctional protein is known to be eliminated by nonsense-mediated mRNA decay. It is possible that deletion of this region causes loss of stabilization and specific substrate recognition in UCK2 functions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography and Sephadex G25 gel filtration
recombinant N-terminally His-tagged isozyme UCK1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Ni-NTA agarose column chromatography and Sephadex G25 gel filtration
recombinant C-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography followed by ion-exchange chromatography
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography
recombinant N-terminally His-tagged isozyme UCK2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene UCK1, recombinant expression of N-terminally His-tagged isozyme in Escherichia coli strain BL21(DE3)
gene UCK2, located on chromosome 1q22-23.2, i.e. human testis-specific gene TSA903, enzyme expression analysis
gene UCK2, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli
gene UCK2, recombinant expression of GST-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene UCK2, recombinant expression of N-terminally His-tagged isozyme in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme (UCK2) is significantly upregulated in hepatocellular carcinoma tissues compared to adjacent normal tissues
the enzyme (UCK2) is significantly upregulated in the deceased group and the recurrence group, compared to the control groups
UCKL1 is significantly upregulated in hepatocellular carcinoma tissues compared to adjacent normal tissues
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
drug development
RX-3117, an orally available cytidine analogue, is activated by UCK2 which may be used to select patients potentially sensitive to RX-3117
medicine
diagnostics
prognostic significance of UCK2 gene in patients with breast cancer. UCK2 is required for chexadmosensitivity
diagnostics
increased UCK2 expression is an independent prognostic indicator of shorter overall survival and recurrence-free survival. UCK2 upregulation might serve as an indicator of unfavorable prognosis of hepatocellular carcinoma
medicine
-
liver-specific targeting of ribavirin by conjugation with asialoglycoprotein to enhance its antiviral activity. Conjugation reaction starts with ribavirin phosphorylation by uridine kinase followed by direct conjugation to asioloosomucoid
medicine
role of UCK2-dependant nucleoside analogues in cancer therapy, overview. Nucleoside antimetabolites are amongst the most important chemotherapeutic agents currently used or under clinical trials against several cancers. This included the important clinically used nucleoside analogue, 5-fluorouracil. UCK2 is also involved in the phosphorylation of ribonucleoside analogues, 5-azacytidine, cyclopentenyl cytosine/uracil, 5-fluorocytidine, 6-azauridine, 3-deazauridine, 5-fluorouridine as well as ethynyl cytidine and uridine. To exert their pharmacological actions, these cytotoxic drugs depend on the action of the UCK2 enzyme to sequentially transform them into nucleoside 5'-triphosphate, thereby interfering with gene synthesis vital for metabolic processes required for cancer cell growth and maintenance
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Drake, J.C.; Stoller, R.G.; Chabner, B.A.
Characteristics of the enzyme uridine-cytidine kinase isolated from a cultured human cell line
Biochem. Pharmacol.
26
64-66
1977
Homo sapiens
Shen, F.; Look, K.Y.; Yeh, Y.A.; Weber, G.
Increased uridine kinase (ATP: uridine 5'-phosphotransferase; EC 2.7.1.48) activity in human and rat tumors
Cancer Biochem. Biophys.
16
1-15
1998
Homo sapiens, Rattus norvegicus
Koizumi, K.; Shimamoto, Y.; Azuma, A.; Wataya, Y.; Matsuda, A.; Sasaki, T.; Fukushima, M.
Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells
Int. J. Mol. Med.
8
273-278
2001
Escherichia coli, Homo sapiens, Mus musculus, Saccharomyces cerevisiae
Van Rompay, A.R.; Norda, A.; Linden, K.; Johansson, M.; Karlsson, A.
Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases
Mol. Pharmacol.
59
1181-1186
2001
Homo sapiens (Q9BZX2), Homo sapiens (Q9HA47)
Suzuki, N.N.; Koizumi, K.; Fukushima, M.; Matsuda, A.; Inagaki, F.
Crystallization and preliminary X-ray analysis of human uridine-cytidine kinase 2
Acta Crystallogr. Sect. D
59
1477-1478
2003
Homo sapiens (Q9BZX2), Homo sapiens
Appleby, T.C.; Larson, G.; Cheney, I.W.; Walker, H.; Wu, J.Z.; Zhong, W.; Hong, Z.; Yao, N.
Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative
Acta Crystallogr. Sect. D
61
278-284
2005
Homo sapiens (Q9BZX2), Homo sapiens
Murata, D.; Endo, Y.; Obata, T.; Sakamoto, K.; Syouji, Y.; Kadohira, M.; Matsuda, A.; Sasaki, T.
A crucial role of uridine/cytidine kinase 2 in antitumor activity of 3'-ethynyl nucleosides
Drug Metab. Dispos.
32
1178-1182
2004
Homo sapiens
Suzuki, N.N.; Koizumi, K.; Fukushima, M.; Matsuda, A.; Inagaki, F.
Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase
Structure
12
751-764
2004
Homo sapiens (Q9BZX2), Homo sapiens
Glavas-Obrovac, L.; Karner, I.; Stefanic, M.; Kasnar-Samprec, J.; Zinic, B.
Metabolic effects of novel N-1-sulfonylpyrimidine derivatives on human colon carcinoma cells
Farmaco
60
479-483
2005
Homo sapiens
Niemeyer, T.; Dietz, C.; Fairbanks, L.; Schroeder-Printzen, I.; Henkel, R.; Loeeffler, M.
Evaluation of uridine metabolism in human and animal spermatozoa
Nucleosides Nucleotides Nucleic Acids
25
1215-1219
2006
Homo sapiens
Jukic, L.V.; Duvnjak, M.; Wu, C.H.; Wu, G.Y.
Human uridine-cytidine kinase phosphorylation of ribavirin: a convenient method for activation of ribavirin for conjugation to proteins
J. Biomed. Sci.
15
205-213
2008
Homo sapiens
Smith, A.J.; Li, Y.; Houk, K.N.
Quantum mechanics/molecular mechanics investigation of the mechanism of phosphate transfer in human uridine-cytidine kinase 2
Org. Biomol. Chem.
7
2716-2724
2009
Homo sapiens (Q9BZX2), Homo sapiens
van Kuilenburg, A.B.; Meinsma, R.
The pivotal role of uridine-cytidine kinases in pyrimidine metabolism and activation of cytotoxic nucleoside analogues in neuroblastoma
Biochim. Biophys. Acta
1862
1504-1512
2016
Homo sapiens (Q9BZX2), Homo sapiens (Q9HA47)
Malami, I.; Abdul, A.B.; Abdullah, R.; Bt Kassim, N.K.; Waziri, P.; Christopher Etti, I.
In silico discovery of potential uridine-cytidine kinase 2 inhibitors from the rhizome of Alpinia mutica
Molecules
21
417
2016
Homo sapiens (Q9BZX2)
Sato, A.; Takano, T.; Hiramoto, A.; Naito, T.; Matsuda, A.; Fukushima, M.; Wataya, Y.; Kim, H.S.
Role of the uridine/cytidine kinase 2 mutation in cellular sensitiveness toward 3-ethynylcytidine treatment of human cancer cells
Anticancer Drugs
28
781-786
2017
Homo sapiens (Q9BZX2), Homo sapiens
Tomoike, F.; Nakagawa, N.; Fukui, K.; Yano, T.; Kuramitsu, S.; Masui, R.
Indispensable residue for uridine binding in the uridine-cytidine kinase family
Biochem. Biophys. Rep.
11
93-98
2017
Thermus thermophilus (Q5SKR5), Homo sapiens (Q9BZX2), Homo sapiens, Thermus thermophilus DSM 579 (Q5SKR5), Thermus thermophilus ATCC 27634 (Q5SKR5)
Malami, I.; Abdul, A.B.
Involvement of the uridine cytidine kinase 2 enzyme in cancer cell death a molecular crosstalk between the enzyme and cellular apoptosis induction
Biomed. Pharmacother.
109
1506-1510
2019
Homo sapiens (Q9BZX2)
Okesli-Armlovich, A.; Gupta, A.; Jimenez, M.; Auld, D.; Liu, Q.; Bassik, M.C.; Khosla, C.
Discovery of small molecule inhibitors of human uridine-cytidine kinase 2 by high-throughput screening
Bioorg. Med. Chem. Lett.
29
2559-2564
2019
Homo sapiens (Q9BZX2), Homo sapiens
Mohamed, M.; Dirar, A.; Hamdoun, S.
Discovery of two diacetylene glycosides as human uridine-cytidine kinase 2 inhibitors An in silico approach
J. Appl. Pharm. Sci.
6
034-039
2016
Homo sapiens (Q9BZX2)
-
Shen, G.; He, P.; Mao, Y.; Li, P.; Luh, F.; Ding, G.; Liu, X.; Yen, Y.
Overexpression of uridine-cytidine kinase 2 correlates with breast cancer progression and poor prognosis
J. Breast Cancer
20
132-141
2017
Homo sapiens (Q9BZX2), Homo sapiens
Meinsma, R.; van Kuilenburg, A.B.
Purification, activity, and expression levels of two uridine-cytidine kinase isoforms in neuroblastoma cell lines
Nucleosides Nucleotides Nucleic Acids
35
613-618
2016
Homo sapiens (Q9BZX2), Homo sapiens (Q9HA47), Homo sapiens
Sarkisjan, D.; Julsing, J.R.; Smid, K.; de Klerk, D.; van Kuilenburg, A.B.; Meinsma, R.; Lee, Y.B.; Kim, D.J.; Peters, G.J.
The cytidine analog fluorocyclopentenylcytosine (RX-3117) is activated by uridine-cytidine kinase 2
PLoS ONE
11
e0162901
2016
Homo sapiens (Q9BZX2), Homo sapiens
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