RRM1

RRM1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2WGH, 3HNC, 3HND, 3HNE, 3HNF, 5D1Y, 4X3V
Identifiers
Aliases	RRM1, R1, RIR1, RR1, ribonucleotide reductase catalytic subunit M1
External IDs	OMIM: 180410 MGI: 98180 HomoloGene: 806 GeneCards: RRM1
Gene location (Human) Chr. Chromosome 11 (human) Band 11p15.4 Start 4,094,707 bp End 4,138,932 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 E3|7 54.72 cM Start 102,090,902 bp End 102,118,978 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ganglionic eminence human penis nipple spongy bone vulva Achilles tendon hair follicle stromal cell of endometrium superior surface of tongue oral cavity Top expressed in maxillary prominence primitive streak spermatocyte dermis abdominal wall ureter spermatid somite hair follicle endocardial cushion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding catalytic activity oxidoreductase activity ATP binding protein binding ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor identical protein binding purine nucleotide binding disordered domain specific binding Cellular component cytoplasm cytosol nuclear envelope ribonucleoside-diphosphate reductase complex cell projection neuronal cell body Biological process DNA replication metabolism mitotic cell cycle pyrimidine nucleobase metabolic process male gonad development deoxyribonucleotide biosynthetic process response to ionizing radiation cell proliferation in forebrain protein complex oligomerization protein heterotetramerization retina development in camera-type eye nucleobase-containing small molecule interconversion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6240 20133 Ensembl ENSG00000167325 ENSMUSG00000030978 UniProt P23921 P07742 RefSeq (mRNA) NM_001033 NM_001318064 NM_001318065 NM_001330193 NM_009103 RefSeq (protein) NP_001024 NP_001304993 NP_001304994 NP_001317122 NP_033129 Location (UCSC) Chr 11: 4.09 – 4.14 Mb Chr 7: 102.09 – 102.12 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Ribonucleoside-diphosphate reductase large subunit is an enzyme that in humans is encoded by the RRM1 gene.

This gene encodes one of two non-identical subunits which constitute ribonucleoside-diphosphate reductase, an enzyme essential for the production of deoxyribonucleotides prior to DNA synthesis in S phase of dividing cells. It is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocortical carcinoma, and lung, ovarian, and breast cancer. This gene may play a role in malignancies and disease that involve this region. This gene is oriented in a head-to-tail configuration with the stromal interaction molecule 1 gene (STIM1), with the 3' end of STIM1 situated 1.6 kb from the 5' end of this gene.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.

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|alt=Fluorouracil (5-FU) Activity edit]]

Fluorouracil (5-FU) Activity edit

See also

• Ribonucleotide reductase

Further reading

• Pavloff N, Rivard D, Masson S, et al. (1992). "Sequence analysis of the large and small subunits of human ribonucleotide reductase". DNA Seq. 2 (4): 227–34. doi:10.3109/10425179209020807. PMID 1627826.
• Byrne J, Smith P (1991). "Human polymorphic probe pE1.8 detects SacI polymorphism in the ribonucleotide reductase M1 subunit gene". Hum. Genet. 87 (3): 376. doi:10.1007/BF00200924. PMID 1677928. S2CID 9398850.
• Parker NJ, Begley CG, Fox RM (1991). "Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes". Nucleic Acids Res. 19 (13): 3741. doi:10.1093/nar/19.13.3741. PMC 328406. PMID 1840662.
• Mann GJ, Musgrove EA, Fox RM, Thelander L (1988). "Ribonucleotide reductase M1 subunit in cellular proliferation, quiescence, and differentiation". Cancer Res. 48 (18): 5151–6. PMID 3044582.
• Brissenden JE, Caras I, Thelander L, Francke U (1988). "The structural gene for the M1 subunit of ribonucleotide reductase maps to chromosome 11, band p15, in human and to chromosome 7 in mouse". Exp. Cell Res. 174 (1): 302–8. doi:10.1016/0014-4827(88)90165-6. PMID 3275546.
• Engström Y, Francke U (1985). "Assignment of the structural gene for subunit M1 of human ribonucleotide reductase to the short arm of chromosome 11". Exp. Cell Res. 158 (2): 477–83. doi:10.1016/0014-4827(85)90470-7. PMID 3891388.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Parker NJ, Begley CG, Fox RM (1994). "Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene". Genomics. 19 (1): 91–6. doi:10.1006/geno.1994.1017. PMID 8188248.
• Byrne JA, Smith PJ (1993). "The 11p15.5 ribonucleotide reductase M1 subunit locus is not imprinted in Wilms' tumour and hepatoblastoma". Hum. Genet. 91 (3): 275–7. doi:10.1007/BF00218271. PMID 8386696. S2CID 22372180.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Bepler G, O'briant KC, Kim YC, et al. (1999). "A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region". Genomics. 55 (2): 164–75. doi:10.1006/geno.1998.5659. PMID 9933563.
• Pitterle DM, Kim YC, Jolicoeur EM, et al. (1999). "Lung cancer and the human gene for ribonucleotide reductase subunit M1 (RRM1)". Mamm. Genome. 10 (9): 916–22. doi:10.1007/s003359901114. PMID 10441745. S2CID 22700595.
• Guittet O, Håkansson P, Voevodskaya N, et al. (2001). "Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells" (PDF). J. Biol. Chem. 276 (44): 40647–51. doi:10.1074/jbc.M106088200. PMID 11517226. S2CID 25065915.
• Kashlan OB, Scott CP, Lear JD, Cooperman BS (2002). "A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP- and dATP-induced oligomerization of the large subunit". Biochemistry. 41 (2): 462–74. doi:10.1021/bi011653a. PMID 11781084.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Kashlan OB, Cooperman BS (2003). "Comprehensive model for allosteric regulation of mammalian ribonucleotide reductase: refinements and consequences". Biochemistry. 42 (6): 1696–706. doi:10.1021/bi020634d. PMID 12578384.
• Xue L, Zhou B, Liu X, et al. (2003). "Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits". Cancer Res. 63 (5): 980–6. PMID 12615712.
• Gautam A, Li ZR, Bepler G (2003). "RRM1-induced metastasis suppression through PTEN-regulated pathways". Oncogene. 22 (14): 2135–42. doi:10.1038/sj.onc.1206232. PMID 12687015.
• Rosell R, Scagliotti G, Danenberg KD, et al. (2003). "Transcripts in pretreatment biopsies from a three-arm randomized trial in metastatic non-small-cell lung cancer". Oncogene. 22 (23): 3548–53. doi:10.1038/sj.onc.1206419. PMID 12789263.