Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

Rrm1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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 activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.1 Publication

Activity regulationi

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).By similarity

Pathwayi: DNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei5Allosteric activatorBy similarity1
Binding sitei53Allosteric activatorBy similarity1
Binding sitei88Allosteric activatorBy similarity1
Sitei218Important for hydrogen atom transferBy similarity1
Sitei226Allosteric effector binding, determines substrate specificityBy similarity1
Binding sitei247Substrate; via amide nitrogenBy similarity1
Sitei256Allosteric effector binding, determines substrate specificityBy similarity1
Active sitei427Proton acceptorBy similarity1
Active sitei429Cysteine radical intermediateBy similarity1
Active sitei431Proton acceptorBy similarity1
Sitei444Important for hydrogen atom transferBy similarity1
Sitei737Important for electron transferBy similarity1
Sitei738Important for electron transferBy similarity1
Sitei787Interacts with thioredoxin/glutaredoxinBy similarity1
Sitei790Interacts with thioredoxin/glutaredoxinBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Oxidoreductase
Biological processDNA replication
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-499943 Interconversion of nucleotide di- and triphosphates
UniPathwayi
UPA00326

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
Alternative name(s):
Ribonucleoside-diphosphate reductase subunit M1
Ribonucleotide reductase large subunit
Gene namesi
Name:Rrm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:98180 Rrm1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3739

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001871911 – 792Ribonucleoside-diphosphate reductase large subunitAdd BLAST792

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17N6-acetyllysineBy similarity1
Disulfide bondi218 ↔ 444Redox-activeBy similarity
Modified residuei376N6-acetyllysineBy similarity1
Modified residuei751PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP07742
MaxQBiP07742
PaxDbiP07742
PeptideAtlasiP07742
PRIDEiP07742

PTM databases

iPTMnetiP07742
PhosphoSitePlusiP07742

Expressioni

Gene expression databases

BgeeiENSMUSG00000030978 Expressed in 328 organ(s), highest expression level in fetal liver hematopoietic progenitor cell
CleanExiMM_RRM1
ExpressionAtlasiP07742 baseline and differential
GenevisibleiP07742 MM

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit. Interacts with RRM2B. Interacts with AHCYL1 which inhibits its activity (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203022, 5 interactors
ComplexPortaliCPX-370 Ribonucleoside-diphosphate reductase RR1 complex, RRM2 variant
CPX-371 Ribonucleoside-diphosphate reductase RR1 complex, RRM2B variant
IntActiP07742, 2 interactors
MINTiP07742
STRINGi10090.ENSMUSP00000033283

Chemistry databases

BindingDBiP07742

Structurei

3D structure databases

ProteinModelPortaliP07742
SMRiP07742
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 92ATP-conePROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni11 – 17Allosteric activator bindingBy similarity7
Regioni217 – 218Substrate bindingBy similarity2
Regioni285 – 288Allosteric effector binding, determines substrate specificityBy similarity4
Regioni427 – 431Substrate bindingBy similarity5
Regioni603 – 607Substrate bindingBy similarity5

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1112 Eukaryota
COG0209 LUCA
GeneTreeiENSGT00910000144246
HOGENOMiHOG000057035
HOVERGENiHBG003447
InParanoidiP07742
KOiK10807
OMAiGEFIVVN
OrthoDBiEOG091G01XV
TreeFamiTF300578

Family and domain databases

InterProiView protein in InterPro
IPR005144 ATP-cone_dom
IPR013346 NrdE_NrdA
IPR000788 RNR_lg_C
IPR013509 RNR_lsu_N
IPR008926 RNR_R1-su_N
IPR039718 Rrm1
PANTHERiPTHR11573 PTHR11573, 1 hit
PfamiView protein in Pfam
PF03477 ATP-cone, 1 hit
PF02867 Ribonuc_red_lgC, 1 hit
PF00317 Ribonuc_red_lgN, 1 hit
PRINTSiPR01183 RIBORDTASEM1
SUPFAMiSSF48168 SSF48168, 1 hit
TIGRFAMsiTIGR02506 NrdE_NrdA, 1 hit
PROSITEiView protein in PROSITE
PS51161 ATP_CONE, 1 hit
PS00089 RIBORED_LARGE, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P07742-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG
60 70 80 90 100
VTTVELDTLA AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED
110 120 130 140 150
LYNYINPHNG RHSPMVASST LDIVMANKDR LNSAIIYDRD FSYNYFGFKT
160 170 180 190 200
LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIDAAIETY NLLSEKWFTH
210 220 230 240 250
ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL ISKSAGGIGV
260 270 280 290 300
AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY
310 320 330 340 350
LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL
360 370 380 390 400
MCPNECPGLD EVWGEEFEKL YESYEKQGRV RKVVKAQQLW YAIIESQTET
410 420 430 440 450
GTPYMLYKDS CNRKSNQQNL GTIKCSNLCT EIVEYTSKDE VAVCNLASLA
460 470 480 490 500
LNMYVTPEHT YDFEKLAEVT KVIVRNLNKI IDINYYPIPE AHLSNKRHRP
510 520 530 540 550
IGIGVQGLAD AFILMRYPFE SPEAQLLNKQ IFETIYYGAL EASCELAKEY
560 570 580 590 600
GPYETYEGSP VSKGILQYDM WNVAPTDLWD WKPLKEKIAK YGIRNSLLIA
610 620 630 640 650
PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL
660 670 680 690 700
WNEEMKNQII ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA
710 720 730 740 750
FIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF
760 770 780 790
TLNKEKLKDK EKALKEEEEK ERNTAAMVCS LENREECLMC GS
Length:792
Mass (Da):90,210
Last modified:July 27, 2011 - v2
Checksum:i051C6CE407D24C69
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1B0GSB1A0A1B0GSB1_MOUSE
Ribonucleoside-diphosphate reductas...
Rrm1
65Annotation score:
A0A1B0GRW5A0A1B0GRW5_MOUSE
Ribonucleoside-diphosphate reductas...
Rrm1
36Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti202S → P in AAA40061 (PubMed:2581962).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02927 mRNA Translation: AAA40061.1
AK088043 mRNA Translation: BAC40112.1
AK137075 mRNA Translation: BAE23230.1
AK168586 mRNA Translation: BAE40455.1
CH466531 Genomic DNA Translation: EDL16602.1
BC016450 mRNA Translation: AAH16450.1
CCDSiCCDS40049.1
PIRiA24050
RefSeqiNP_033129.2, NM_009103.3
UniGeneiMm.197486
Mm.415177

Genome annotation databases

EnsembliENSMUST00000033283; ENSMUSP00000033283; ENSMUSG00000030978
GeneIDi20133
KEGGimmu:20133
UCSCiuc009irp.2 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02927 mRNA Translation: AAA40061.1
AK088043 mRNA Translation: BAC40112.1
AK137075 mRNA Translation: BAE23230.1
AK168586 mRNA Translation: BAE40455.1
CH466531 Genomic DNA Translation: EDL16602.1
BC016450 mRNA Translation: AAH16450.1
CCDSiCCDS40049.1
PIRiA24050
RefSeqiNP_033129.2, NM_009103.3
UniGeneiMm.197486
Mm.415177

3D structure databases

ProteinModelPortaliP07742
SMRiP07742
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203022, 5 interactors
ComplexPortaliCPX-370 Ribonucleoside-diphosphate reductase RR1 complex, RRM2 variant
CPX-371 Ribonucleoside-diphosphate reductase RR1 complex, RRM2B variant
IntActiP07742, 2 interactors
MINTiP07742
STRINGi10090.ENSMUSP00000033283

Chemistry databases

BindingDBiP07742
ChEMBLiCHEMBL3739

PTM databases

iPTMnetiP07742
PhosphoSitePlusiP07742

Proteomic databases

EPDiP07742
MaxQBiP07742
PaxDbiP07742
PeptideAtlasiP07742
PRIDEiP07742

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033283; ENSMUSP00000033283; ENSMUSG00000030978
GeneIDi20133
KEGGimmu:20133
UCSCiuc009irp.2 mouse

Organism-specific databases

CTDi6240
MGIiMGI:98180 Rrm1

Phylogenomic databases

eggNOGiKOG1112 Eukaryota
COG0209 LUCA
GeneTreeiENSGT00910000144246
HOGENOMiHOG000057035
HOVERGENiHBG003447
InParanoidiP07742
KOiK10807
OMAiGEFIVVN
OrthoDBiEOG091G01XV
TreeFamiTF300578

Enzyme and pathway databases

UniPathwayi
UPA00326

ReactomeiR-MMU-499943 Interconversion of nucleotide di- and triphosphates

Miscellaneous databases

PROiPR:P07742
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030978 Expressed in 328 organ(s), highest expression level in fetal liver hematopoietic progenitor cell
CleanExiMM_RRM1
ExpressionAtlasiP07742 baseline and differential
GenevisibleiP07742 MM

Family and domain databases

InterProiView protein in InterPro
IPR005144 ATP-cone_dom
IPR013346 NrdE_NrdA
IPR000788 RNR_lg_C
IPR013509 RNR_lsu_N
IPR008926 RNR_R1-su_N
IPR039718 Rrm1
PANTHERiPTHR11573 PTHR11573, 1 hit
PfamiView protein in Pfam
PF03477 ATP-cone, 1 hit
PF02867 Ribonuc_red_lgC, 1 hit
PF00317 Ribonuc_red_lgN, 1 hit
PRINTSiPR01183 RIBORDTASEM1
SUPFAMiSSF48168 SSF48168, 1 hit
TIGRFAMsiTIGR02506 NrdE_NrdA, 1 hit
PROSITEiView protein in PROSITE
PS51161 ATP_CONE, 1 hit
PS00089 RIBORED_LARGE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRIR1_MOUSE
AccessioniPrimary (citable) accession number: P07742
Secondary accession number(s): Q91YM8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 160 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again