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Identification
HMDB Protein ID HMDBP00111
Secondary Accession Numbers
  • 5343
  • HMDBP03563
Name Ribonucleoside-diphosphate reductase subunit M2
Synonyms
  1. Ribonucleotide reductase small chain
  2. Ribonucleotide reductase small subunit
Gene Name RRM2
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling.
Pathways
  • Adenine phosphoribosyltransferase deficiency (APRT)
  • Adenosine Deaminase Deficiency
  • Adenylosuccinate Lyase Deficiency
  • AICA-Ribosiduria
  • Azathioprine Action Pathway
  • Beta Ureidopropionase Deficiency
  • Dihydropyrimidinase Deficiency
  • DNA replication
  • Gemcitabine Action Pathway
  • Gemcitabine Metabolism Pathway
  • Glutathione metabolism
  • Gout or Kelley-Seegmiller Syndrome
  • Lesch-Nyhan Syndrome (LNS)
  • Mercaptopurine Action Pathway
  • Mitochondrial DNA depletion syndrome
  • MNGIE (Mitochondrial Neurogastrointestinal Encephalopathy)
  • Molybdenum Cofactor Deficiency
  • Myoadenylate deaminase deficiency
  • p53 signaling pathway
  • Purine metabolism
  • Purine metabolism
  • Purine Nucleoside Phosphorylase Deficiency
  • Pyrimidine metabolism
  • Pyrimidine metabolism
  • Thioguanine Action Pathway
  • UMP Synthase Deficiency (Orotic Aciduria)
  • Xanthine Dehydrogenase Deficiency (Xanthinuria)
  • Xanthinuria type I
  • Xanthinuria type II
Reactions
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + Water → ribonucleoside diphosphate + thioredoxin details
dADP + Thioredoxin disulfide + Water → Thioredoxin + ADP details
dGDP + Thioredoxin disulfide + Water → Guanosine diphosphate + Thioredoxin details
dCDP + Thioredoxin disulfide + Water → Thioredoxin + CDP details
2'-Deoxyribonucleoside diphosphate + Tryparedoxin disulfide + Water → Ribonucleoside diphosphate + Tryparedoxin details
2'-Deoxyribonucleoside diphosphate + Trypanothione disulfide + Water → Ribonucleoside diphosphate + Trypanothione details
GO Classification
Biological Process
protein heterotetramerization
nucleobase-containing small molecule interconversion
DNA replication
regulation of transcription involved in G1/S phase of mitotic cell cycle
deoxyribonucleotide biosynthetic process
deoxyribonucleoside diphosphate metabolic process
Cellular Component
cytosol
nucleoplasm
ribonucleoside-diphosphate reductase complex
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
oxidoreductase activity, acting on ch or ch2 groups
oxidoreductase activity, acting on ch or ch2 groups, disulfide as acceptor
ribonucleoside-diphosphate reductase activity
oxidoreductase activity
Molecular Function
transition metal ion binding
ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
Process
metabolic process
nitrogen compound metabolic process
cellular nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
nucleoside diphosphate metabolic process
deoxyribonucleoside diphosphate metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 2
Locus 2p25-p24
SNPs RRM2
Gene Sequence
>1170 bp
ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA
Protein Properties
Number of Residues 389
Molecular Weight 44877.25
Theoretical pI 5.38
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ribonucleoside-diphosphate reductase subunit M2
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
GenBank ID Protein 36155
UniProtKB/Swiss-Prot ID P31350
UniProtKB/Swiss-Prot Entry Name RIR2_HUMAN
PDB IDs
GenBank Gene ID X59618
GeneCard ID RRM2
GenAtlas ID RRM2
HGNC ID HGNC:10452
References
General References
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  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  8. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
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  12. Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [PubMed:11978970 ]
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