RRM2B

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0009263 deoxyribonucleotide biosynthetic process	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) annotation to deoxyribonucleotide biosynthesis, the canonical process for ribonucleotide reductase small subunits. RRM2B/RRM1 RNR supplies dNTPs via de novo NDP->dNDP reduction. Reason: Core process for RNR small subunits; consistent with direct experimental evidence in this gene and with the IEA/IDA process annotations. Supporting Evidence: PMID:16376858 RR is responsible for the de novo
GO:0005829 cytosol	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) annotation placing RNR activity in the cytosol. Ribonucleotide reduction is a cytosolic process in mammalian cells; the dNTPs produced diffuse to the nucleus or are imported into mitochondria. Reason: Cytosol is the principal, well-supported site of RNR activity for RRM2B (IBA, IDA-HPA, TAS-Reactome all agree). This is the core cellular location. Supporting Evidence: PMID:18997010 find in all cases that ribonucleotide reductase resides in the cytosol
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) annotation to the ribonucleoside-diphosphate reductase molecular function. This is the defining catalytic activity of RRM2B as the radical-generating small subunit of the RRM1/RRM2B RNR holoenzyme (EC 1.17.4.1). Reason: Core molecular function, redundantly supported by direct IDA evidence in this gene (PMID:16376858, PMID:12615712), ISS, and IEA (RHEA:23252/EC:1.17.4.1). Supporting Evidence: PMID:16376858 conversion of ribonucleoside diphosphates to deoxyribonucleoside diphosphates,
GO:0000731 DNA synthesis involved in DNA repair	IDA PMID:11719458 p53R2-dependent pathway for DNA synthesis in a p53-regulated...	ACCEPT	Summary: Direct evidence that p53R2-dependent RNR provides dNTPs for DNA synthesis during repair of damaged DNA in the p53 checkpoint. Inhibition of p53R2 reduced RR activity, DNA repair and survival after genotoxins. Reason: Well-supported specific process for RRM2B's DNA-damage-associated role (supplies dNTPs consumed during repair synthesis). Consistent with the DNA repair BP annotation. Supporting Evidence: PMID:11719458 p53R2-dependent DNA synthesis plays a pivotal role in cell survival by
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	ISS GO_REF:0000024	ACCEPT	Summary: Sequence-similarity transfer of the ribonucleoside-diphosphate reductase function from the mouse ortholog Rrm2b (UniProtKB:Q6PEE3). Same core catalytic activity as the IDA/IBA/IEA annotations. Reason: Duplicate of the core molecular function, transferred by curator from an experimentally characterized ortholog; consistent with direct human evidence. Supporting Evidence: PMID:16376858 conversion of ribonucleoside diphosphates to deoxyribonucleoside diphosphates,
GO:0005634 nucleus	IDA PMID:11719458 p53R2-dependent pathway for DNA synthesis in a p53-regulated...	ACCEPT	Summary: p53R2 protein accumulated in nuclei after gamma-irradiation. UniProt records nuclear localization with translocation from cytoplasm to nucleus in response to DNA damage. Reason: Directly observed localization. Nucleus is a genuine, DNA-damage-associated location for RRM2B, though later work (PMID:18997010) argues the enzyme is predominantly cytosolic; kept as an observed non-core location. Supporting Evidence: PMID:11719458 The p53R2 product accumulated in nuclei
GO:0005737 cytoplasm	IDA PMID:11719458 p53R2-dependent pathway for DNA synthesis in a p53-regulated...	ACCEPT	Summary: Cytoplasmic localization of p53R2, consistent with the cytosolic site of ribonucleotide reduction and with UniProt (Cytoplasm; Nucleus). Reason: Directly observed location; the more specific cytosol term (GO:0005829) is the core location and is also annotated. Supporting Evidence: PMID:18997010 find in all cases that ribonucleotide reductase resides in the cytosol
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IEA GO_REF:0000120	ACCEPT	Summary: Electronic annotation of the ribonucleoside-diphosphate reductase activity mapped from RHEA:23252 / EC:1.17.4.1, matching the UniProt catalytic activity. Reason: Duplicate of the experimentally supported core molecular function; the EC/RHEA mapping is correct for RRM2B. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt EC=1.17.4.1;
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: Electronic annotation to nucleus from the UniProt Subcellular Location vocabulary. Redundant with the IDA nucleus annotation. Reason: Consistent with UniProt-documented nuclear localization (post-DNA-damage translocation); observed non-core location. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt Cytoplasm. Nucleus. Note=Translocates from
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: Electronic annotation to cytoplasm from the UniProt Subcellular Location vocabulary. Redundant with the IDA cytoplasm annotation. Reason: Consistent with UniProt and with cytosolic ribonucleotide reduction; the more specific cytosol term is the core location. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt Cytoplasm. Nucleus. Note=Translocates from
GO:0005739 mitochondrion	IEA GO_REF:0000108	MARK AS OVER ANNOTATED	Summary: Electronic annotation to mitochondrion, logically inferred from the mitochondrial DNA replication process term (GO:0006264). RRM2B is not documented as a mitochondrial-matrix protein; the enzyme is cytosolic and supplies dNTPs that are imported into mitochondria. Reason: This is an inter-ontology logical inference from the mtDNA-replication process, not physical mitochondrial localization. Direct localization studies place RNR in the cytosol (PMID:18997010); p53R2 supports mtDNA synthesis by supplying cytosolic dNTPs rather than by residing in mitochondria. Supporting Evidence: PMID:18997010 find in all cases that ribonucleotide reductase resides in the cytosol
GO:0006281 DNA repair	IEA GO_REF:0000117	ACCEPT	Summary: ARBA machine-learning electronic annotation to DNA repair. RRM2B supplies dNTPs for DNA repair synthesis in the p53 checkpoint. Reason: Consistent with direct experimental evidence (IDA PMID:11719458) and the p53R2 DNA-damage literature; redundant but correct. Supporting Evidence: PMID:11719458 p53R2-dependent DNA synthesis plays a pivotal role in cell survival by
GO:0009185 ribonucleoside diphosphate metabolic process	IEA GO_REF:0000117	ACCEPT	Summary: ARBA electronic annotation to ribonucleoside diphosphate metabolism, the substrate side of the RNR reaction (NDP -> dNDP). Reason: Correct and consistent with the catalytic activity and with the IDA annotation of the same term (PMID:16376858). Somewhat general but not wrong. Supporting Evidence: PMID:16376858 conversion of ribonucleoside diphosphates to deoxyribonucleoside diphosphates,
GO:0009263 deoxyribonucleotide biosynthetic process	IEA GO_REF:0000002	ACCEPT	Summary: InterPro2GO electronic annotation to deoxyribonucleotide biosynthesis from the RNR small-subunit domain signatures. Reason: Duplicate of the core IBA process annotation; the InterPro RNR small-chain family mapping is appropriate for RRM2B. Supporting Evidence: PMID:16376858 RR is responsible for the de novo
GO:0009265 2'-deoxyribonucleotide biosynthetic process	IEA GO_REF:0000117	ACCEPT	Summary: ARBA electronic annotation to 2'-deoxyribonucleotide biosynthesis, the product side of the RNR reaction. Reason: Correct and supported by direct IDA evidence for the same term (PMID:16376858). Supporting Evidence: PMID:16376858 conversion of ribonucleoside diphosphates to deoxyribonucleoside diphosphates,
GO:0016491 oxidoreductase activity	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: InterPro2GO electronic annotation to the broad parent term oxidoreductase activity from a general RNR-like domain signature (IPR012348). Reason: Correct but uninformatively general given that the specific child term GO:0004748 (ribonucleoside-diphosphate reductase activity) is already annotated with direct evidence. The specific term should be used. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt EC=1.17.4.1;
GO:1901992 positive regulation of mitotic cell cycle phase transition	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: ARBA electronic annotation to positive regulation of a mitotic cell cycle phase transition. RRM2B is a metabolic enzyme; any cell-cycle effect is indirect (dNTP supply / p53 checkpoint) rather than a direct regulatory role. Reason: RRM2B does not directly regulate cell-cycle phase transitions; if anything, p53R2 induction promotes a DNA-damage checkpoint arrest (PMID:10716435), not a positive transition. This ARBA-inferred regulatory term over-interprets the enzyme's metabolic role. Supporting Evidence: PMID:10716435 caused G2/M arrest and prevented cells
GO:0005515 protein binding	IPI PMID:19015526 ATM-mediated serine 72 phosphorylation stabilizes ribonucleo...	MARK AS OVER ANNOTATED	Summary: IntAct-curated protein-binding evidence. In this study p53R2 interacts with ATM and with the ubiquitin ligase MDM2; ATM phosphorylates p53R2 at Ser72 to stabilize it against MDM2-mediated turnover after genotoxic stress. Reason: The bare 'protein binding' term is uninformative and does not capture a molecular function. The underlying interactions (ATM/MDM2) are real and regulatory but are better represented as regulation of protein stability; per curation policy the IPI is retained rather than removed. Supporting Evidence: PMID:19015526 MDM2, a ubiquitin ligase for p53, interacts and
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MARK AS OVER ANNOTATED	Summary: Protein-binding evidence from a proteome-scale high-throughput yeast two-hybrid interactome map (partner ORC4). Not a specific molecular function. Reason: Bare 'protein binding' from a systematic interactome screen is uninformative about molecular function and is not corroborated by a focused functional study; retained per policy rather than removed. Supporting Evidence: PMID:25416956 we describe a systematic map of ?14,000 high-quality human
GO:0005515 protein binding	IPI PMID:25910212 Widespread macromolecular interaction perturbations in human...	MARK AS OVER ANNOTATED	Summary: Protein-binding evidence from a large-scale interaction-perturbation study (partner RNF41). Not a specific molecular function. Reason: Bare 'protein binding' from a high-throughput screen; uninformative for molecular function. Retained per policy. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt Q7LG56; Q9H4P4: RNF41
GO:0042802 identical protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MARK AS OVER ANNOTATED	Summary: Self-interaction (homotypic) evidence from a proteome-scale interactome map. RNR small subunits adopt a ferritin-like fold and can homodimerize; UniProt lists a Q7LG56-Q7LG56 self-interaction. Reason: Homodimerization is a structural property rather than an informative molecular function for RRM2B (the functional unit is the RRM1/RRM2B heteromeric RNR). Retained per policy. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt Q7LG56; Q7LG56: RRM2B
GO:0042802 identical protein binding	IPI PMID:25502805 A massively parallel pipeline to clone DNA variants and exam...	MARK AS OVER ANNOTATED	Summary: Self-interaction evidence from a large-scale ORF-clone / variant interaction pipeline. Reason: Homodimerization is a structural feature, not an informative molecular function; retained per policy rather than removed. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt Q7LG56; Q7LG56: RRM2B
GO:0042802 identical protein binding	IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari...	MARK AS OVER ANNOTATED	Summary: Self-interaction evidence from a large-scale study of interaction perturbation by genetic variants. Reason: Homodimerization is structural and uninformative as a molecular function; retained per policy. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt Q7LG56; Q7LG56: RRM2B
GO:0006264 mitochondrial DNA replication	IEA GO_REF:0000107	ACCEPT	Summary: Ensembl-Compara electronic transfer from the mouse ortholog (Rrm2b, Q6PEE3) of the mitochondrial DNA replication process. p53R2 supplies dNTPs required for mtDNA synthesis in quiescent/post-mitotic cells. Reason: Consistent with the human IMP annotation (PMID:17486094) and with MTDPS8 disease biology; RRM2B provides the deoxyribonucleotide precursors for mtDNA replication. Supporting Evidence: PMID:17486094 in dNTP supply for mtDNA synthesis.
GO:0014075 response to amine	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Ensembl-Compara electronic transfer from a rat ortholog (D4ADQ1) of 'response to amine'. This is a peripheral, non-specific phenotype-derived term not connected to RRM2B's characterized function. Reason: Electronic transfer of a vague stimulus-response term from a rodent ortholog; not supported by any human functional evidence and not part of the gene's core biology. Peripheral over-annotation. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt Belongs to the ribonucleoside diphosphate reductase small
GO:0070318 positive regulation of G0 to G1 transition	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Ensembl-Compara electronic transfer from the mouse ortholog of 'positive regulation of G0 to G1 transition'. RRM2B/p53R2 supplies dNTPs in resting (G0/G1) cells, but a direct role in driving the G0->G1 transition is not established. Reason: RRM2B is a metabolic enzyme providing dNTPs; any effect on the G0-to-G1 transition is an indirect consequence of precursor supply, not a direct regulatory function. Over-interpreted regulatory term. Supporting Evidence: PMID:11517226 can supply resting cells with deoxyribonucleotides for DNA repair.
GO:0000731 DNA synthesis involved in DNA repair	IDA PMID:12615712 Wild-type p53 regulates human ribonucleotide reductase by pr...	ACCEPT	Summary: Direct evidence that, after UV irradiation, p53R2 and hRRM1 form an active RR complex in the nucleus to provide dNDPs for DNA repair. Reason: Well-supported specific process; duplicate of the IDA from PMID:11719458. RRM2B supplies dNTP precursors for DNA repair synthesis. Supporting Evidence: PMID:12615712 form an active RR complex to provide dNDPs for DNA
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IDA PMID:12615712 Wild-type p53 regulates human ribonucleotide reductase by pr...	ACCEPT	Summary: Direct evidence for reconstituted, active ribonucleotide reductase activity from a p53R2/hRRM1 complex (in vivo RR activity assay tracking nuclear RR subunit accumulation). Reason: Core molecular function, directly demonstrated; consistent with the reconstitution assays of PMID:16376858. Supporting Evidence: PMID:12615712 form an active RR complex to provide dNDPs for DNA
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor	IDA PMID:16376858 Characterization of enzymatic properties of human ribonucleo...	ACCEPT	Summary: Direct enzymatic characterization of RR holoenzyme reconstituted in vitro from p53R2 + hRRM1; [3H]CDP reduction assay confirmed functional ribonucleotide reductase activity. Reason: Definitive direct evidence for the core catalytic function of RRM2B as the RNR small subunit. Supporting Evidence: PMID:16376858 p53R2 proteins could interact with hRRM1 to form functional RR
GO:0005634 nucleus	IDA PMID:12615712 Wild-type p53 regulates human ribonucleotide reductase by pr...	ACCEPT	Summary: Confocal microscopy showed translocation of p53R2 (with hRRM1 and hRRM2) from cytoplasm to nucleus after UV treatment. Reason: Directly observed nuclear localization after DNA damage; observed non-core location (predominant site of RNR activity is cytosolic, PMID:18997010). Supporting Evidence: PMID:12615712 translocation of hRRM1, p53R2 and hRRM2 from the cytoplasm to the
GO:0005515 protein binding	IPI PMID:12615712 Wild-type p53 regulates human ribonucleotide reductase by pr...	MARK AS OVER ANNOTATED	Summary: Coimmunoprecipitation evidence that p53R2 binds p53/TP53 (UniProtKB:P04637), and that after UV it shifts from binding p53 to binding hRRM1. A functional regulatory interaction, but annotated to the uninformative 'protein binding' term. Reason: The bare 'protein binding' term does not capture a molecular function. The p53R2-TP53 interaction is biologically meaningful (links RNR to the p53 DNA-damage response) but would be better captured as a specific interaction/regulation term; retained per curation policy rather than removed. Supporting Evidence: PMID:12615712 bound to p53 in KB cells, which express wild-type p53.
GO:0005737 cytoplasm	IDA PMID:12615712 Wild-type p53 regulates human ribonucleotide reductase by pr...	ACCEPT	Summary: p53R2 localized to the cytoplasm prior to UV-induced nuclear translocation, consistent with cytosolic ribonucleotide reduction. Reason: Directly observed location; the specific cytosol term is the core location and is separately annotated. Supporting Evidence: PMID:12615712 translocation of hRRM1, p53R2 and hRRM2 from the cytoplasm to the
GO:0005654 nucleoplasm	IDA GO_REF:0000052	ACCEPT	Summary: Human Protein Atlas immunofluorescence localization to the nucleoplasm. Reason: Consistent with the documented DNA-damage-associated nuclear pool of RRM2B; observed non-core location relative to the predominant cytosolic activity. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt GO:0005654; C:nucleoplasm; IDA:HPA.
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: Human Protein Atlas immunofluorescence localization to the cytosol, the principal site of ribonucleotide reduction. Reason: Core cellular location, consistent with IBA/TAS and with PMID:18997010. Supporting Evidence: file:human/RRM2B/RRM2B-uniprot.txt GO:0005829; C:cytosol; IDA:HPA.
GO:0000731 DNA synthesis involved in DNA repair	NAS PMID:10716435 A ribonucleotide reductase gene involved in a p53-dependent ...	ACCEPT	Summary: Author statement (from the founding p53R2 paper) that p53R2 encodes a ribonucleotide reductase directly involved in the p53 checkpoint for repair of damaged DNA, supplying nucleotides for DNA repair synthesis. Reason: Consistent with the direct IDA evidence for the same term (PMID:11719458, PMID:12615712); RRM2B provides dNTPs for DNA repair synthesis. Supporting Evidence: PMID:10716435 reductase that is directly involved in the p53 checkpoint for repair of damaged
GO:0005829 cytosol	IDA PMID:18997010 Ribonucleotide reduction is a cytosolic process in mammalian...	ACCEPT	Summary: Three independent localization methods (cytosol/nuclei fractionation, immunofluorescence, fluorescent-tag transfection) showed p53R2 (and R1/R2) reside in the cytosol, arguing against DNA-damage-induced nuclear translocation as a regulatory mechanism. Reason: Strongest direct evidence for the core cytosolic localization of RRM2B/RNR; dNTPs made in the cytosol diffuse to the nucleus or are imported into mitochondria. Supporting Evidence: PMID:18997010 find in all cases that ribonucleotide reductase resides in the cytosol
GO:0006264 mitochondrial DNA replication	IMP PMID:17486094 Mutation of RRM2B, encoding p53-controlled ribonucleotide re...	ACCEPT	Summary: Loss-of-function RRM2B mutations in humans cause severe mtDNA depletion, and the Rrm2b-/- mouse shows severe mtDNA depletion in various tissues, implying p53R2 has a crucial role in dNTP supply for mtDNA synthesis. Reason: Core physiological role established by human mutant phenotype and mouse knockout (MTDPS8). RRM2B does not itself replicate DNA but supplies the deoxyribonucleotide precursors essential for mtDNA replication; this is the disease-defining function. Supporting Evidence: PMID:17486094 in dNTP supply for mtDNA synthesis.
GO:0006281 DNA repair	IDA PMID:11719458 p53R2-dependent pathway for DNA synthesis in a p53-regulated...	ACCEPT	Summary: Inhibition of endogenous p53R2 reduced ribonucleotide reductase activity, DNA repair, and cell survival after exposure to genotoxins, establishing a role in DNA repair. Reason: Directly supported role; RRM2B supplies the dNTP precursors required for DNA repair synthesis in the p53-dependent checkpoint. Supporting Evidence: PMID:11719458 p53R2-dependent DNA synthesis plays a pivotal role in cell survival by
GO:0009185 ribonucleoside diphosphate metabolic process	IDA PMID:16376858 Characterization of enzymatic properties of human ribonucleo...	ACCEPT	Summary: Reconstituted p53R2/hRRM1 RNR catalyzes reduction of ribonucleoside diphosphates, the substrate side of the RNR reaction. Reason: Directly demonstrated; general metabolic-process framing of the RNR reaction, consistent with the more specific biosynthetic terms. Supporting Evidence: PMID:16376858 conversion of ribonucleoside diphosphates to deoxyribonucleoside diphosphates,
GO:0009265 2'-deoxyribonucleotide biosynthetic process	IDA PMID:16376858 Characterization of enzymatic properties of human ribonucleo...	ACCEPT	Summary: Reconstituted p53R2/hRRM1 RNR produces deoxyribonucleoside diphosphates, the biosynthetic (product) side of the RNR reaction, essential for DNA synthesis and repair. Reason: Directly demonstrated core biosynthetic process for RRM2B; supported by in vitro reconstitution ([3H]CDP reduction). Supporting Evidence: PMID:16376858 which are essential for DNA synthesis and repair.
GO:0010971 positive regulation of G2/M transition of mitotic cell cycle	IDA PMID:10716435 A ribonucleotide reductase gene involved in a p53-dependent ...	MARK AS OVER ANNOTATED	Summary: In the founding paper, induction of p53R2 in p53-deficient cells caused G2/M arrest (a checkpoint), not a positive drive through the G2/M transition. RRM2B is a metabolic enzyme; any cell-cycle effect is indirect. Reason: The cited evidence describes G2/M arrest, which is the opposite direction from 'positive regulation of G2/M transition'. RRM2B does not directly regulate the G2/M transition; this term over-interprets an indirect checkpoint effect. Supporting Evidence: PMID:10716435 caused G2/M arrest and prevented cells
GO:0070318 positive regulation of G0 to G1 transition	IDA PMID:11517226 Mammalian p53R2 protein forms an active ribonucleotide reduc...	MARK AS OVER ANNOTATED	Summary: The cited paper shows an R1-p53R2 complex can supply resting (G0/G1) cells with deoxyribonucleotides for DNA repair; it does not demonstrate that RRM2B positively regulates the G0-to-G1 transition. Reason: RRM2B provides dNTPs in resting cells but a direct role in driving the G0->G1 transition is not established by this evidence; the regulatory term over-interprets the enzyme's metabolic function. Supporting Evidence: PMID:11517226 can supply resting cells with deoxyribonucleotides for DNA repair.
GO:0005829 cytosol	TAS Reactome:R-HSA-111804	ACCEPT	Summary: Reactome traceable-author-statement placing the RNR (M1M2B) NDP->dNDP reaction (thioredoxin) in the cytosol. Reason: Consistent with the core cytosolic localization of RNR (IBA/IDA); redundant but correct. Supporting Evidence: PMID:18997010 find in all cases that ribonucleotide reductase resides in the cytosol
GO:0005829 cytosol	TAS Reactome:R-HSA-5632892	ACCEPT	Summary: Reactome traceable-author-statement (TP53 stimulates transcription of RRM2B) placing RRM2B in the cytosol. Reason: Consistent with the core cytosolic localization; redundant but correct. Supporting Evidence: PMID:18997010 find in all cases that ribonucleotide reductase resides in the cytosol
GO:0005829 cytosol	TAS Reactome:R-HSA-8866405	ACCEPT	Summary: Reactome traceable-author-statement placing the RNR (M1M2B) NDP->dNDP reaction (glutaredoxin) in the cytosol. Reason: Consistent with the core cytosolic localization of RNR; redundant but correct. Supporting Evidence: PMID:18997010 find in all cases that ribonucleotide reductase resides in the cytosol

Gene Description

Existing Annotations Review

Core Functions

p53/TP53-inducible provider of deoxyribonucleotide precursors for mitochondrial DNA synthesis. In quiescent and post-mitotic cells that lack RRM2, the RRM1/RRM2B complex supplies the dNTPs required for mtDNA replication; loss of RRM2B causes mitochondrial DNA depletion (MTDPS8).

References

📚 Additional Documentation

Notes

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