Skip Header

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

Q4KLN6

- RIR2_RAT

UniProt

Q4KLN6 - RIR2_RAT

(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
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 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

Fe cationBy similarityNote: 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 1PROSITE-ProRule annotation
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
  4. mitotic cell cycle Source: RGD
  5. positive regulation of cell proliferation Source: RGD
  6. pyrimidine nucleobase metabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196414. G1/S-Specific Transcription.
REACT_215006. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_249225. E2F mediated regulation of DNA replication.
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi1598310. Rrm2.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nuclear envelope Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Ribonucleoside-diphosphate reductase subunit M2PRO_0000190451Add
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

Proteomic databases

PRIDEiQ4KLN6.

Expressioni

Gene expression databases

GenevestigatoriQ4KLN6.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000037227.

Structurei

3D structure databases

ProteinModelPortaliQ4KLN6.
SMRiQ4KLN6. Positions 7-353.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0208.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiQ4KLN6.
KOiK10808.
OMAiXFHELIS.
OrthoDBiEOG7VMP5N.
PhylomeDBiQ4KLN6.
TreeFamiTF300465.

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.

Q4KLN6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSVRAPLAT IADQQQLHLS PLKRLSLADK ENTPPTLSSA RVLASKAARR
60 70 80 90 100
IFQDSAELES KAPTKPSIEE EPLLRENPRR FVVFPIEYHD IWQMYKKAEA
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 KEIITNSVRI
310 320 330 340 350
EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFKVENPFDF
360 370 380 390
MENISLEGKT NFFEKRVGEY QRMGVMSNST ENSFTLDADF
Length:390
Mass (Da):45,039
Last modified:August 2, 2005 - v1
Checksum:iA1BD4EABB7920F69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099082 mRNA. Translation: AAH99082.1.
RefSeqiNP_001020911.1. NM_001025740.1.
UniGeneiRn.144946.

Genome annotation databases

EnsembliENSRNOT00000037387; ENSRNOP00000037227; ENSRNOG00000023272.
GeneIDi362720.
KEGGirno:362720.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC099082 mRNA. Translation: AAH99082.1 .
RefSeqi NP_001020911.1. NM_001025740.1.
UniGenei Rn.144946.

3D structure databases

ProteinModelPortali Q4KLN6.
SMRi Q4KLN6. Positions 7-353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000037227.

Proteomic databases

PRIDEi Q4KLN6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000037387 ; ENSRNOP00000037227 ; ENSRNOG00000023272 .
GeneIDi 362720.
KEGGi rno:362720.

Organism-specific databases

CTDi 6241.
RGDi 1598310. Rrm2.

Phylogenomic databases

eggNOGi COG0208.
GeneTreei ENSGT00390000013305.
HOGENOMi HOG000255975.
HOVERGENi HBG001647.
InParanoidi Q4KLN6.
KOi K10808.
OMAi XFHELIS.
OrthoDBi EOG7VMP5N.
PhylomeDBi Q4KLN6.
TreeFami TF300465.

Enzyme and pathway databases

UniPathwayi UPA00326 .
Reactomei REACT_196414. G1/S-Specific Transcription.
REACT_215006. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_249225. E2F mediated regulation of DNA replication.

Miscellaneous databases

NextBioi 680993.

Gene expression databases

Genevestigatori Q4KLN6.

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. "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].
    Tissue: Placenta.

Entry informationi

Entry nameiRIR2_RAT
AccessioniPrimary (citable) accession number: Q4KLN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: August 2, 2005
Last modified: November 26, 2014
This is version 81 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 (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3