ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
ferric iron binding
protein homodimerization activity
Cellular component
cytoplasm
cytosol
ribonucleoside-diphosphate reductase complex
Biological process
regulation of transcription involved in G1/S transition of mitotic cell cycle
deoxyribonucleotide biosynthetic process
DNA replication
negative regulation of G0 to G1 transition
deoxyribonucleotide metabolic process
protein complex oligomerization
protein heterotetramerization
nucleobase-containing small molecule interconversion
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
6241
20135
Ensembl
ENSG00000171848
ENSMUSG00000020649
UniProt
P31350
P11157
RefSeq (mRNA)
NM_001165931 NM_001034
NM_009104
RefSeq (protein)
NP_001025 NP_001159403
NP_033130
Location (UCSC)
Chr 2: 10.12 – 10.21 Mb
Chr 12: 24.76 – 24.76 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Ribonucleoside-diphosphate reductase subunit M2, also known as ribonucleotide reductase small subunit, is an enzyme that in humans is encoded by the RRM2 gene.[5][6]
^ abcGRCh38: Ensembl release 89: ENSG00000171848 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000020649 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Entrez Gene: ribonucleotide reductase M2".
^Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM (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.
ribonucleotide reductase small subunit, is an enzyme that in humans is encoded by the RRM2 gene. This gene encodes one of two non-identical subunits for ribonucleotide...
through RRM2 and CP110 control centrosome duplication and reduce the frequency of genomic mutations. So far, mutations in CCNF and increased RRM2 expression...
deaminase, and NT5C) and that express its other intracellular targets (RRM1, RRM2, and RRM2B) lead to variations in response to the drug. Research has also...
RRM1 gene while there are two isoforms of the beta subunit, encoded by the RRM2 and RRM2B genes: Each Class I alpha monomer consists of three domains: one...
and disposed of on Cygnus NG-16. ) (RRM3 was installed in 2018 to replace RRM2. Payload malfunctioned in 2019 and its payload of methane and ammonia was...
binding affinity to the Py tract on its adjacent 3’ splice site. The RRM1 and RRM2 are sufficient for specific RNA/protein binding, while RRM3 is responsible...
conserved. GBP2 gene can interact with the RNA via the domain RRM1 and RRM2. The RRM2 domain can recognize the core motif GGUC present in the RNA. Besides...
increases when DNA is damaged. The human counterparts of RNR2, or homologs, are RRM2 and RRM2B. Over the next decade, he continued the search for genes and proteins...
domain while the cleft between RRMs 1 and 2 including the beta-sheet face of RRM2 is a sequence-specific RNA binding site. The C-terminal motif is required...
PABPC1 contains four RNA-recognition motifs (RRMs). The first two, RRM1 and RRM2, bind both α-importin and the poly(A) tail of processed mRNA. This feature...
Polypyrimidine Tract Binding Protein Isoform 1 (PTB1) 1sjr: NMR Structure of RRM2 from Human Polypyrimidine Tract Binding Protein Isoform 1 (PTB1) 2ad9: Solution...
ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits". Cancer Research. 63 (5): 980–6. PMID 12615712. Zhou B, Liu X,...
called RNA recognition motifs (RRMs). RBM10 contains two RRMs (RRM1 and RRM2) and other domains such as two zinc fingers (ZnFs), an octamer repeat (OCRE)...
mutation affecting both RNA binding domains is lethal, and a mutation in RRM2 leads to female infertility or developmental arrest in offspring. These two...
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...
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