RRM1
entrez
6240
canonical
uniprot
P23921
canonical
ensembl
ENSG00000167325
resolver
ensp
ENSP00000300738
resolver
ensp
ENSP00000431464
resolver
enst
ENST00000300738
resolver
enst
ENST00000534285
resolver
genesymbol
RRM1
resolver
genesymbol_syn
RR1
resolver
hgnc
HGNC:10451
resolver
uniprot
B4DXD1
resolver
uniprot
B4E0I8
resolver
uniprot
E9PL69
resolver
uniprot
Q9UNN2
resolver
uniprot_entry
B4DXD1_HUMAN
resolver
uniprot_entry
B4E0I8_HUMAN
resolver
uniprot_entry
E9PL69_HUMAN
resolver
uniprot_entry
RIR1_HUMAN
resolver
uniprot_sec
Q9UNN2
resolver
activity_regulation
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. {ECO:0000269|PubMed:16376858, ECO:0000269|PubMed:1867633, ECO:0000269|PubMed:25237103}.
uniprot
proteins
amino_acid_sequence
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS
uniprot
proteins
disease_involvement
DISEASE: Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal recessive 6 (PEOB6) [MIM:620647]: A form of progressive external ophthalmoplegia, a mitochondrial myopathy characterized by progressive paralysis of the levator palpebrae, orbicularis oculi, and extraocular muscles. Ragged red fibers are seen on muscle biopsy. {ECO:0000269|PubMed:35617047}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.17.4.1
uniprot
proteins
function
FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
uniprot
proteins
mass_dalton
90070
uniprot
proteins
mutagenesis
MUTAGEN 57; /note="D->N: Severely decreases interaction with AHCYL1 in the presence of dATP."; /evidence="ECO:0000269|PubMed:25237103
uniprot
proteins
protein_family
Ribonucleoside diphosphate reductase large chain family
uniprot
proteins
pubmed
12615712
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1627826
uniprot
proteins
pubmed
16376858
uniprot
proteins
pubmed
1840662
uniprot
proteins
pubmed
1867633
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21336276
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25237103
uniprot
proteins
pubmed
35617047
uniprot
proteins
pubmed
8188248
uniprot
proteins
pubmed
9933563
uniprot
proteins
sequence_length
792
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm.
uniprot
proteins