MGP Database

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MGP002730

UniProt Annotations

Entry Information
Gene Nameribonucleotide reductase M1
Protein EntryRIR1_HUMAN
UniProt IDP23921
SpeciesHuman
Comments
Comment typeDescription
Catalytic Activity2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H(2)O = ribonucleoside diphosphate + thioredoxin. {ECO:0000269|PubMed:16376858}.
Enzyme RegulationUnder complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site, the dATP inhibition is mediated by AHCYL1 which stabilizes dATP in the site. {ECO:0000269|PubMed:16376858, ECO:0000269|PubMed:1867633, ECO:0000269|PubMed:25237103}.
FunctionProvides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
InteractionP31350:RRM2; NbExp=3; IntAct=EBI-717006, EBI-2339245;
MiscellaneousThe level of the enzyme activity is closely correlated with the growth rate of a cell and appears to vary with the cell cycle.
MiscellaneousTwo distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on M1, is formed only in the presence of the second subunit M2.
PathwayGenetic information processing; DNA replication.
SimilarityBelongs to the ribonucleoside diphosphate reductase large chain family. {ECO:0000305}.
SimilarityContains 1 ATP-cone domain. {ECO:0000255|PROSITE- ProRule:PRU00492}.
Subcellular LocationCytoplasm.
SubunitHeterodimer of a large and a small subunit. Heterodimer with small subunit RRM2 or RRM2B. The heterodimer with RRM2 has higher catalytic activity than the heterodimer with RRM2B. Interacts with AHCYL1 which inhibits its activity. {ECO:0000269|PubMed:16376858, ECO:0000269|PubMed:21336276, ECO:0000269|PubMed:25237103}.
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/RRM1ID42174ch11p15.html";
Web ResourceName=Wikipedia; Note=Ribonucleotide reductase entry; URL="http://en.wikipedia.org/wiki/Ribonucleotide_reductase";
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