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Protein

Ribonucleoside-diphosphate reductase subunit M2

Gene

Rrm2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling (By similarity).By similarity

Catalytic activityi

2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.PROSITE-ProRule annotation

Cofactori

Fe cationNote: Binds 2 iron ions per subunit.

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
Metal bindingi139Iron 11
Metal bindingi170Iron 11
Metal bindingi170Iron 21
Metal bindingi173Iron 11
Active sitei177PROSITE-ProRule annotation1
Metal bindingi233Iron 21
Metal bindingi267Iron 11
Metal bindingi267Iron 21
Metal bindingi270Iron 21

GO - Molecular functioni

GO - Biological processi

  • deoxyribonucleotide biosynthetic process Source: UniProtKB
  • deoxyribonucleotide metabolic process Source: MGI
  • DNA replication Source: UniProtKB-UniPathway
  • protein heterotetramerization Source: UniProtKB
  • protein oligomerization Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.17.4.1. 3474.
ReactomeiR-MMU-113510. E2F mediated regulation of DNA replication.
R-MMU-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-MMU-69205. G1/S-Specific Transcription.
UniPathwayiUPA00326.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase subunit M2 (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase small chain
Ribonucleotide reductase small subunit
Gene namesi
Name:Rrm2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:98181. Rrm2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3527.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001904501 – 390Ribonucleoside-diphosphate reductase subunit M2Add BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei20PhosphoserineCombined sources1
Modified residuei33PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt signaling.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP11157.
MaxQBiP11157.
PaxDbiP11157.
PeptideAtlasiP11157.
PRIDEiP11157.

PTM databases

iPTMnetiP11157.
PhosphoSitePlusiP11157.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020649.
CleanExiMM_RRM2.
ExpressionAtlasiP11157. baseline and differential.
GenevisibleiP11157. MM.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Protein-protein interaction databases

BioGridi203023. 4 interactors.
IntActiP11157. 1 interactor.
MINTiMINT-1605522.
STRINGi10090.ENSMUSP00000020980.

Structurei

Secondary structure

1390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi68 – 70Combined sources3
Turni72 – 74Combined sources3
Helixi78 – 81Combined sources4
Beta strandi83 – 85Combined sources3
Helixi89 – 100Combined sources12
Helixi105 – 107Combined sources3
Helixi113 – 119Combined sources7
Helixi122 – 148Combined sources27
Helixi150 – 153Combined sources4
Helixi157 – 184Combined sources28
Helixi188 – 195Combined sources8
Helixi197 – 200Combined sources4
Helixi202 – 216Combined sources15
Beta strandi218 – 220Combined sources3
Helixi222 – 249Combined sources28
Helixi254 – 279Combined sources26
Helixi287 – 306Combined sources20
Helixi311 – 314Combined sources4
Helixi318 – 335Combined sources18
Helixi349 – 351Combined sources3
Turni386 – 388Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AFTNMR-A384-390[»]
1H0NX-ray2.40A1-390[»]
1H0OX-ray2.20A1-390[»]
1W68X-ray2.20A1-390[»]
1W69X-ray2.20A1-390[»]
1XSMX-ray2.30A1-390[»]
DisProtiDP00462.
ProteinModelPortaliP11157.
SMRiP11157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11157.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1567. Eukaryota.
COG0208. LUCA.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiP11157.
KOiK10808.
OMAiNEVQYSE.
OrthoDBiEOG091G0AZQ.
PhylomeDBiP11157.
TreeFamiTF300465.

Family and domain databases

CDDicd01049. RNRR2. 1 hit.
Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR033909. RNR_small.
IPR030475. RNR_small_AS.
IPR000358. RNR_small_fam.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSVRTPLAT IADQQQLQLS PLKRLTLADK ENTPPTLSST RVLASKAARR
60 70 80 90 100
IFQDSAELES KAPTNPSVED EPLLRENPRR FVVFPIEYHD IWQMYKKAEA
110 120 130 140 150
SFWTAEEVDL SKDIQHWEAL KPDERHFISH VLAFFAASDG IVNENLVERF
160 170 180 190 200
SQEVQVTEAR CFYGFQIAME NIHSEMYSLL IDTYIKDPKE REYLFNAIET
210 220 230 240 250
MPCVKKKADW ALRWIGDKEA TYGERVVAFA AVEGIFFSGS FASIFWLKKR
260 270 280 290 300
GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPAEQRV REIITNAVRI
310 320 330 340 350
EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFRVENPFDF
360 370 380 390
MENISLEGKT NFFEKRVGEY QRMGVMSNST ENSFTLDADF
Length:390
Mass (Da):45,096
Last modified:July 1, 1989 - v1
Checksum:iAC7ACC4FAF8A4A2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14223 mRNA. Translation: AAA40062.1.
X15666 Genomic DNA. Translation: CAA33707.1.
AK088907 mRNA. Translation: BAC40647.1.
AK142027 mRNA. Translation: BAE24918.1.
AK147111 mRNA. Translation: BAE27683.1.
AK161643 mRNA. Translation: BAE36508.1.
AK167078 mRNA. Translation: BAE39238.1.
AK167204 mRNA. Translation: BAE39331.1.
AK168205 mRNA. Translation: BAE40165.1.
AK168994 mRNA. Translation: BAE40793.1.
BC085136 mRNA. Translation: AAH85136.1.
CCDSiCCDS25844.1.
PIRiS06735.
RefSeqiNP_033130.1. NM_009104.2.
UniGeneiMm.471826.
Mm.99.

Genome annotation databases

EnsembliENSMUST00000020980; ENSMUSP00000020980; ENSMUSG00000020649.
GeneIDi20135.
KEGGimmu:20135.
UCSCiuc007ner.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14223 mRNA. Translation: AAA40062.1.
X15666 Genomic DNA. Translation: CAA33707.1.
AK088907 mRNA. Translation: BAC40647.1.
AK142027 mRNA. Translation: BAE24918.1.
AK147111 mRNA. Translation: BAE27683.1.
AK161643 mRNA. Translation: BAE36508.1.
AK167078 mRNA. Translation: BAE39238.1.
AK167204 mRNA. Translation: BAE39331.1.
AK168205 mRNA. Translation: BAE40165.1.
AK168994 mRNA. Translation: BAE40793.1.
BC085136 mRNA. Translation: AAH85136.1.
CCDSiCCDS25844.1.
PIRiS06735.
RefSeqiNP_033130.1. NM_009104.2.
UniGeneiMm.471826.
Mm.99.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AFTNMR-A384-390[»]
1H0NX-ray2.40A1-390[»]
1H0OX-ray2.20A1-390[»]
1W68X-ray2.20A1-390[»]
1W69X-ray2.20A1-390[»]
1XSMX-ray2.30A1-390[»]
DisProtiDP00462.
ProteinModelPortaliP11157.
SMRiP11157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203023. 4 interactors.
IntActiP11157. 1 interactor.
MINTiMINT-1605522.
STRINGi10090.ENSMUSP00000020980.

Chemistry databases

ChEMBLiCHEMBL3527.

PTM databases

iPTMnetiP11157.
PhosphoSitePlusiP11157.

Proteomic databases

EPDiP11157.
MaxQBiP11157.
PaxDbiP11157.
PeptideAtlasiP11157.
PRIDEiP11157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020980; ENSMUSP00000020980; ENSMUSG00000020649.
GeneIDi20135.
KEGGimmu:20135.
UCSCiuc007ner.2. mouse.

Organism-specific databases

CTDi6241.
MGIiMGI:98181. Rrm2.

Phylogenomic databases

eggNOGiKOG1567. Eukaryota.
COG0208. LUCA.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiP11157.
KOiK10808.
OMAiNEVQYSE.
OrthoDBiEOG091G0AZQ.
PhylomeDBiP11157.
TreeFamiTF300465.

Enzyme and pathway databases

UniPathwayiUPA00326.
BRENDAi1.17.4.1. 3474.
ReactomeiR-MMU-113510. E2F mediated regulation of DNA replication.
R-MMU-499943. Synthesis and interconversion of nucleotide di- and triphosphates.
R-MMU-69205. G1/S-Specific Transcription.

Miscellaneous databases

EvolutionaryTraceiP11157.
PROiP11157.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020649.
CleanExiMM_RRM2.
ExpressionAtlasiP11157. baseline and differential.
GenevisibleiP11157. MM.

Family and domain databases

CDDicd01049. RNRR2. 1 hit.
Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR033909. RNR_small.
IPR030475. RNR_small_AS.
IPR000358. RNR_small_fam.
[Graphical view]
PANTHERiPTHR23409. PTHR23409. 1 hit.
PfamiPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMiSSF47240. SSF47240. 1 hit.
PROSITEiPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRIR2_MOUSE
AccessioniPrimary (citable) accession number: P11157
Secondary accession number(s): Q3UI23, Q542E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.