Skip Header

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

Q60561

- RIR2_MESAU

UniProt

Q60561 - RIR2_MESAU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ribonucleoside-diphosphate reductase subunit M2

Gene

RRM2

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Cofactori

Binds 2 iron ions per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Iron 1PROSITE-ProRule annotation
Metal bindingi170 – 1701Iron 1PROSITE-ProRule annotation
Metal bindingi170 – 1701Iron 2By similarity
Metal bindingi173 – 1731Iron 1PROSITE-ProRule annotation
Active sitei177 – 1771PROSITE-ProRule annotation
Metal bindingi233 – 2331Iron 2By similarity
Metal bindingi267 – 2671Iron 2By similarity
Metal bindingi270 – 2701Iron 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

GO - Biological processi

  1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  2. deoxyribonucleotide biosynthetic process Source: UniProtKB
  3. DNA replication Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

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
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Ribonucleoside-diphosphate reductase subunit M2PRO_0000190449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei33 – 331PhosphothreonineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Structurei

3D structure databases

ProteinModelPortaliQ60561.
SMRiQ60561. Positions 7-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG001647.

Family and domain databases

Gene3Di1.10.620.20. 1 hit.
InterProiIPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[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.

Q60561 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFSVRVPLAT ITDQQQLQVS PLKALSLADK ENTPPSLSAT PVLASKVARR
60 70 80 90 100
ILQDVAEPES KVSTNPSVED EPLLRENPRR FVVFPIEYHD IWKMYKKAEA
110 120 130 140 150
SFWTAEEVDL SKDIQHWEAL KPDERHFISH VLAFFAASDG IVNENLVERF
160 170 180 190 200
SQEVQVTEAR CFYGFQIAME NIHSEMYSLL IDTYIKDSKE REYLFNAIET
210 220 230 240 250
MPCVKKKADW ALRWIGDKEA TYGERVVAFA AVEGIFFSGS FASIFWLKKR
260 270 280 290 300
GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPSEQRV QEIITNAVRI
310 320 330 340 350
EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFKVENPFDF
360 370 380
MENISLEGKT NFFEKRVGEY QRMGVMSNSF TLDADF
Length:386
Mass (Da):44,482
Last modified:November 1, 1997 - v1
Checksum:i8B057993D859F9A6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68127 mRNA. Translation: CAA48232.1.
PIRiS27153.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68127 mRNA. Translation: CAA48232.1 .
PIRi S27153.

3D structure databases

ProteinModelPortali Q60561.
SMRi Q60561. Positions 7-353.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG001647.

Enzyme and pathway databases

UniPathwayi UPA00326 .

Family and domain databases

Gene3Di 1.10.620.20. 1 hit.
InterProi IPR009078. Ferritin-like_SF.
IPR012348. RNR-rel.
IPR000358. RNR_small.
[Graphical view ]
PANTHERi PTHR23409. PTHR23409. 1 hit.
Pfami PF00268. Ribonuc_red_sm. 1 hit.
[Graphical view ]
SUPFAMi SSF47240. SSF47240. 1 hit.
PROSITEi PS00368. RIBORED_SMALL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiRIR2_MESAU
AccessioniPrimary (citable) accession number: Q60561
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 85 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.

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3