P07742 · RIR1_MOUSE

  • Protein
    Ribonucleoside-diphosphate reductase large subunit
  • Gene
    Rrm1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.

Miscellaneous

Two 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.
The level of the enzyme activity is closely correlated with the growth rate of a cell and appears to vary with the cell cycle.

Catalytic activity

Activity regulation

Under 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 (By similarity).

Features

Showing features for binding site, site, active site.

TypeIDPosition(s)Description
Binding site5-6ATP (UniProtKB | ChEBI); allosteric activator
Binding site11-17ATP (UniProtKB | ChEBI); allosteric activator
Binding site53ATP (UniProtKB | ChEBI); allosteric activator
Binding site57ATP (UniProtKB | ChEBI); allosteric activator
Binding site202GDP (UniProtKB | ChEBI)
Binding site217GDP (UniProtKB | ChEBI)
Site218Important for hydrogen atom transfer
Binding site226-228dTTP (UniProtKB | ChEBI); allosteric effector that controls substrate specificity
Binding site243dTTP (UniProtKB | ChEBI); allosteric effector that controls substrate specificity
Binding site256dTTP (UniProtKB | ChEBI); allosteric effector that controls substrate specificity
Binding site263-264dTTP (UniProtKB | ChEBI); allosteric effector that controls substrate specificity
Active site427Proton acceptor
Binding site427GDP (UniProtKB | ChEBI)
Active site429Cysteine radical intermediate
Active site431Proton acceptor
Binding site431GDP (UniProtKB | ChEBI)
Site444Important for hydrogen atom transfer
Binding site604-607GDP (UniProtKB | ChEBI)
Site737Important for electron transfer
Site738Important for electron transfer
Site787Interacts with thioredoxin/glutaredoxin
Site790Interacts with thioredoxin/glutaredoxin

GO annotations

AspectTerm
Cellular Componentcell projection
Cellular Componentcytosol
Cellular Componentmitochondrion
Cellular Componentneuronal cell body
Cellular Componentnuclear envelope
Cellular Componentribonucleoside-diphosphate reductase complex
Molecular FunctionATP binding
Molecular Functiondisordered domain specific binding
Molecular Functionidentical protein binding
Molecular Functionpurine nucleotide binding
Molecular Functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
Biological Process2'-deoxyribonucleotide biosynthetic process
Biological Processcell proliferation in forebrain
Biological Processdeoxyribonucleotide biosynthetic process
Biological ProcessDNA repair
Biological ProcessDNA synthesis involved in DNA repair
Biological Processmale gonad development
Biological Processmitochondrial DNA replication
Biological Processpositive regulation of G0 to G1 transition
Biological Processpositive regulation of G1/S transition of mitotic cell cycle
Biological Processpositive regulation of G2/M transition of mitotic cell cycle
Biological Processprotein heterotetramerization
Biological Processpyrimidine nucleobase metabolic process
Biological Processresponse to ionizing radiation
Biological Processretina development in camera-type eye
Biological Processribonucleoside diphosphate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribonucleoside-diphosphate reductase large subunit
  • EC number
  • Alternative names
    • Ribonucleoside-diphosphate reductase subunit M1
    • Ribonucleotide reductase large subunit

Gene names

    • Name
      Rrm1

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • NOD
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P07742
  • Secondary accessions
    • Q91YM8

Proteomes

Organism-specific databases

Phenotypes & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 39 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain, modified residue, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00001871911-792Ribonucleoside-diphosphate reductase large subunit
Modified residue17N6-acetyllysine
Disulfide bond218↔444Redox-active
Modified residue376N6-acetyllysine
Modified residue751Phosphothreonine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Heterodimer of a large and a small subunit. Interacts with RRM2B. Interacts with AHCYL1 which inhibits its activity (By similarity).
View interactors in UniProtKB
View CPX-370 in Complex Portal

Protein-protein interaction databases

Chemistry

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-92ATP-cone

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    792
  • Mass (Da)
    90,210
  • Last updated
    2011-07-27 v2
  • Checksum
    051C6CE407D24C69
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGRHSPMVASSTLDIVMANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSEKWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYESYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTPEHTYDFEKLAEVTKVIVRNLNKIIDINYYPIPEAHLSNKRHRPIGIGVQGLADAFILMRYPFESPEAQLLNKQIFETIYYGALEASCELAKEYGPYETYEGSPVSKGILQYDMWNVAPTDLWDWKPLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWNEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKALKEEEEKERNTAAMVCSLENREECLMCGS

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1B0GSB1A0A1B0GSB1_MOUSERrm165
A0A1B0GRW5A0A1B0GRW5_MOUSERrm136

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict202in Ref. 1; AAA40061

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
K02927
EMBL· GenBank· DDBJ
AAA40061.1
EMBL· GenBank· DDBJ
mRNA
AK088043
EMBL· GenBank· DDBJ
BAC40112.1
EMBL· GenBank· DDBJ
mRNA
AK137075
EMBL· GenBank· DDBJ
BAE23230.1
EMBL· GenBank· DDBJ
mRNA
AK168586
EMBL· GenBank· DDBJ
BAE40455.1
EMBL· GenBank· DDBJ
mRNA
CH466531
EMBL· GenBank· DDBJ
EDL16602.1
EMBL· GenBank· DDBJ
Genomic DNA
BC016450
EMBL· GenBank· DDBJ
AAH16450.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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