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Q60561 (RIR2_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Protein attributes

Sequence length386 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 iron ions per subunit By similarity.

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 – 386386Ribonucleoside-diphosphate reductase subunit M2
PRO_0000190449

Sites

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

Amino acid modifications

Modified residue201Phosphoserine By similarity
Modified residue331Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60561 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 8B057993D859F9A6

FASTA38644,482
        10         20         30         40         50         60 
MFSVRVPLAT ITDQQQLQVS PLKALSLADK ENTPPSLSAT PVLASKVARR ILQDVAEPES 

        70         80         90        100        110        120 
KVSTNPSVED EPLLRENPRR FVVFPIEYHD IWKMYKKAEA SFWTAEEVDL SKDIQHWEAL 

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

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

       250        260        270        280        290        300 
FASIFWLKKR GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPSEQRV QEIITNAVRI 

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

       370        380 
NFFEKRVGEY QRMGVMSNSF TLDADF 

« Hide

References

[1]"cDNA sequence of the small subunit of the hamster ribonucleotide reductase."
Chaudhuri M.M., Tonin P.N., Srinivasan P.R.
Biochim. Biophys. Acta 1171:117-121(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68127 mRNA. Translation: CAA48232.1.
PIRS27153.

3D structure databases

ProteinModelPortalQ60561.
SMRQ60561. Positions 7-353.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG001647.

Enzyme and pathway databases

UniPathwayUPA00326.

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...

Entry information

Entry nameRIR2_MESAU
AccessionPrimary (citable) accession number: Q60561
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 11, 2013
This is version 83 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

PATHWAY comments

Index of metabolic and biosynthesis pathways