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P11157 (RIR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonucleoside-diphosphate reductase subunit M2

EC=1.17.4.1
Alternative name(s):
Ribonucleotide reductase small chain
Ribonucleotide reductase small subunit
Gene names
Name:Rrm2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 iron ions per subunit.

Pathway

Genetic information processing; DNA replication.

Subunit structure

Heterodimer of a large and a small subunit.

Subcellular location

Cytoplasm.

Post-translational modification

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

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.

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Ribonucleoside-diphosphate reductase subunit M2
PRO_0000190450

Sites

Active site1771 By similarity
Metal binding1391Iron 1
Metal binding1701Iron 1
Metal binding1701Iron 2
Metal binding1731Iron 1
Metal binding2331Iron 2
Metal binding2671Iron 1
Metal binding2671Iron 2
Metal binding2701Iron 2

Amino acid modifications

Modified residue201Phosphoserine Ref.5 Ref.6
Modified residue331Phosphothreonine By similarity

Secondary structure

........................................... 390
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11157 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: AC7ACC4FAF8A4A2F

FASTA39045,096
        10         20         30         40         50         60 
MLSVRTPLAT IADQQQLQLS PLKRLTLADK ENTPPTLSST RVLASKAARR IFQDSAELES 

        70         80         90        100        110        120 
KAPTNPSVED EPLLRENPRR FVVFPIEYHD IWQMYKKAEA SFWTAEEVDL SKDIQHWEAL 

       130        140        150        160        170        180 
KPDERHFISH VLAFFAASDG IVNENLVERF SQEVQVTEAR CFYGFQIAME NIHSEMYSLL 

       190        200        210        220        230        240 
IDTYIKDPKE REYLFNAIET MPCVKKKADW ALRWIGDKEA TYGERVVAFA AVEGIFFSGS 

       250        260        270        280        290        300 
FASIFWLKKR GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPAEQRV REIITNAVRI 

       310        320        330        340        350        360 
EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFRVENPFDF MENISLEGKT 

       370        380        390 
NFFEKRVGEY QRMGVMSNST ENSFTLDADF 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of expressible cDNA clones encoding the M1 and M2 subunits of mouse ribonucleotide reductase."
Thelander L., Berg P.
Mol. Cell. Biol. 6:3433-3442(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and expression of the functional gene encoding the M2 subunit of mouse ribonucleotide reductase: a new dominant marker gene."
Thelander M., Thelander L.
EMBO J. 8:2475-2479(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J, DBA/2 and NOD.
Tissue: Eye, Kidney, Liver and Thymus.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2."
Kauppi B., Nielsen B.B., Ramaswamy S., Larsen I.K., Thelander M., Thelander L., Eklund H.
J. Mol. Biol. 262:706-720(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 65-352.
[8]"Cobalt substitution of mouse R2 ribonucleotide reductase as a model for the reactive diferrous state. Spectroscopic and structural evidence for a ferromagnetically coupled dinuclear cobalt cluster."
Strand K.R., Karlsen S., Andersson K.K.
J. Biol. Chem. 277:34229-34238(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 65-352.
[9]"NMR structure of an inhibitory R2 C-terminal peptide bound to mouse ribonucleotide reductase R1 subunit."
Fisher A.L., Laub P.B., Cooperman B.S.
Nat. Struct. Biol. 2:951-955(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 384-390.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS06735.
RefSeqNP_033130.1. NM_009104.2.
UniGeneMm.471826.
Mm.99.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00462.
ProteinModelPortalP11157.
SMRP11157. Positions 8-353.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203023. 4 interactions.
IntActP11157. 1 interaction.
MINTMINT-1605522.

Chemistry

BindingDBP11157.
ChEMBLCHEMBL3527.

PTM databases

PhosphoSiteP11157.

Proteomic databases

PaxDbP11157.
PRIDEP11157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020980; ENSMUSP00000020980; ENSMUSG00000020649.
GeneID20135.
KEGGmmu:20135.
UCSCuc007ner.2. mouse.

Organism-specific databases

CTD6241.
MGIMGI:98181. Rrm2.

Phylogenomic databases

eggNOGCOG0208.
GeneTreeENSGT00390000013305.
HOGENOMHOG000255975.
HOVERGENHBG001647.
InParanoidP11157.
KOK10808.
OMAGMPEIEY.
OrthoDBEOG7VMP5N.
PhylomeDBP11157.
TreeFamTF300465.

Enzyme and pathway databases

BRENDA1.17.4.1. 3474.
UniPathwayUPA00326.

Gene expression databases

ArrayExpressP11157.
BgeeP11157.
CleanExMM_RRM2.
GenevestigatorP11157.

Family and domain databases

Gene3D1.10.620.20. 1 hit.
InterProIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view]
PANTHERPTHR23409. PTHR23409. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
SUPFAMSSF47240. SSF47240. 1 hit.
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRRM2. mouse.
EvolutionaryTraceP11157.
NextBio297647.
PROP11157.
SOURCESearch...

Entry information

Entry nameRIR2_MOUSE
AccessionPrimary (citable) accession number: P11157
Secondary accession number(s): Q3UI23, Q542E2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot