| General Information |
| MoonProt ID | 108 |
| First appeared in release | 4.0 |
| Name(s) | Ribonucleoside-diphosphate reductase large subunit |
| UniProt ID | P23921 |
| GO terms | GO:0036175 ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016491 oxidoreductase activity
GO:0017076 purine nucleotide binding
GO:0042802 identical protein binding
GO:0061731 ribonucleoside-diphosphate reductase activity
GO:0097718 disordered domain specific binding
GO:0000731 DNA synthesis involved in DNA repair
GO:0006264 mitochondrial DNA replication
GO:0006281 DNA repair
GO:0009185 ribonucleoside diphosphate metabolic process
GO:0009263 deoxyribonucleotide biosynthetic process
GO:0009265 2'-deoxyribonucleotide biosynthetic process
GO:0010971 positive regulation of G2/M transition of mitotic cell cycle
GO:0051290 protein heterotetramerization
GO:0070318 positive regulation of G0 to G1 transition
GO:1900087 positive regulation of G1/S transition of mitotic cell cycle
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0005971 ribonucleoside-diphosphate reductase complex |
| Organisms for which functions have been demonstrated | Homo sapiens |
| Sequence length | 792 |
| FASTA sequence | >sp|P23921|RIR1_HUMAN Ribonucleoside-diphosphate reductase large subunit OS=Homo sapiens OX=9606 GN=RRM1 PE=1 SV=1
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS |
| Structure Information |
| PDB ID | 3HNC |
| Quaternary structure | NA |
| SCOP | NA |
| CATH | 3.20.70.20 |
| TM Helix Prediction | |
| DisProt Annotation | |
| Predicted Disorder Regions | |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | enzyme, Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides |
| References for function | Fu Y, Long MJC, Wisitpitthaya S, Inayat H, Pierpont TM, Elsaid IM, Bloom JC, Ortega J, Weiss RS, Aye Y. Nuclear RNR-alpha antagonizes cell proliferation by directly inhibiting ZRANB3. Nat Chem Biol. 2018 Oct;14(10):943-954. doi: 10.1038/s41589-018-0113-5. Epub 2018 Aug 27. PMID: 30150681; PMCID: PMC6171530. |
| E.C. number | 1.17.4.1 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | binds to ZRANB3 (zinc-finger-RAN-binding-domain-containing-3) and promotes DNA synthesis |
| References for function | Fu Y, Long MJC, Wisitpitthaya S, Inayat H, Pierpont TM, Elsaid IM, Bloom JC, Ortega J, Weiss RS, Aye Y. Nuclear RNR-alpha antagonizes cell proliferation by directly inhibiting ZRANB3. Nat Chem Biol. 2018 Oct;14(10):943-954. doi: 10.1038/s41589-018-0113-5. Epub 2018 Aug 27. PMID: 30150681; PMCID: PMC6171530. |
| E.C. number | |
| Location of functional site(s) | |
| Cellular location of function | nucleus |
| Comments | |