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P11157

- RIR2_MOUSE

UniProt

P11157 - RIR2_MOUSE

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Protein
Ribonucleoside-diphosphate reductase subunit M2
Gene
Rrm2
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Binds 2 iron ions per subunit.

Pathwayi

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. DNA replication Source: UniProtKB-UniPathway
  2. deoxyribonucleoside diphosphate metabolic process Source: InterPro
  3. deoxyribonucleotide biosynthetic process Source: UniProtKB
  4. deoxyribonucleotide metabolic process Source: MGI
  5. protein heterotetramerization Source: UniProtKB
  6. 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.
ReactomeiREACT_198608. G1/S-Specific Transcription.
REACT_206830. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:98181. Rrm2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Ribonucleoside-diphosphate reductase subunit M2
PRO_0000190450Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201Phosphoserine2 Publications
Modified residuei33 – 331Phosphothreonine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP11157.
PaxDbiP11157.
PRIDEiP11157.

PTM databases

PhosphoSiteiP11157.

Expressioni

Gene expression databases

ArrayExpressiP11157.
BgeeiP11157.
CleanExiMM_RRM2.
GenevestigatoriP11157.

Interactioni

Subunit structurei

Heterodimer of a large and a small subunit.

Protein-protein interaction databases

BioGridi203023. 4 interactions.
IntActiP11157. 1 interaction.
MINTiMINT-1605522.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi68 – 703
Turni72 – 743
Helixi78 – 814
Beta strandi83 – 853
Helixi89 – 10012
Helixi105 – 1073
Helixi113 – 1197
Helixi122 – 14827
Helixi150 – 1534
Helixi157 – 18428
Helixi188 – 1958
Helixi197 – 2004
Helixi202 – 21615
Beta strandi218 – 2203
Helixi222 – 24928
Helixi254 – 27926
Helixi287 – 30620
Helixi311 – 3144
Helixi318 – 33518
Helixi349 – 3513
Turni386 – 3883

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 8-353.

Miscellaneous databases

EvolutionaryTraceiP11157.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0208.
GeneTreeiENSGT00390000013305.
HOGENOMiHOG000255975.
HOVERGENiHBG001647.
InParanoidiP11157.
KOiK10808.
OMAiGVMNSTK.
OrthoDBiEOG7VMP5N.
PhylomeDBiP11157.
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.

P11157-1 [UniParc]FASTAAdd to Basket

« Hide

MLSVRTPLAT IADQQQLQLS PLKRLTLADK ENTPPTLSST RVLASKAARR    50
IFQDSAELES KAPTNPSVED EPLLRENPRR FVVFPIEYHD IWQMYKKAEA 100
SFWTAEEVDL SKDIQHWEAL KPDERHFISH VLAFFAASDG IVNENLVERF 150
SQEVQVTEAR CFYGFQIAME NIHSEMYSLL IDTYIKDPKE REYLFNAIET 200
MPCVKKKADW ALRWIGDKEA TYGERVVAFA AVEGIFFSGS FASIFWLKKR 250
GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPAEQRV REIITNAVRI 300
EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFRVENPFDF 350
MENISLEGKT NFFEKRVGEY QRMGVMSNST ENSFTLDADF 390
Length:390
Mass (Da):45,096
Last modified:July 1, 1989 - v1
Checksum:iAC7ACC4FAF8A4A2F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25844.1.
PIRi S06735.
RefSeqi NP_033130.1. NM_009104.2.
UniGenei Mm.471826.
Mm.99.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AFT NMR - A 384-390 [» ]
1H0N X-ray 2.40 A 1-390 [» ]
1H0O X-ray 2.20 A 1-390 [» ]
1W68 X-ray 2.20 A 1-390 [» ]
1W69 X-ray 2.20 A 1-390 [» ]
1XSM X-ray 2.30 A 1-390 [» ]
DisProti DP00462.
ProteinModelPortali P11157.
SMRi P11157. Positions 8-353.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203023. 4 interactions.
IntActi P11157. 1 interaction.
MINTi MINT-1605522.

Chemistry

BindingDBi P11157.
ChEMBLi CHEMBL3527.

PTM databases

PhosphoSitei P11157.

Proteomic databases

MaxQBi P11157.
PaxDbi P11157.
PRIDEi P11157.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020980 ; ENSMUSP00000020980 ; ENSMUSG00000020649 .
GeneIDi 20135.
KEGGi mmu:20135.
UCSCi uc007ner.2. mouse.

Organism-specific databases

CTDi 6241.
MGIi MGI:98181. Rrm2.

Phylogenomic databases

eggNOGi COG0208.
GeneTreei ENSGT00390000013305.
HOGENOMi HOG000255975.
HOVERGENi HBG001647.
InParanoidi P11157.
KOi K10808.
OMAi GVMNSTK.
OrthoDBi EOG7VMP5N.
PhylomeDBi P11157.
TreeFami TF300465.

Enzyme and pathway databases

UniPathwayi UPA00326 .
BRENDAi 1.17.4.1. 3474.
Reactomei REACT_198608. G1/S-Specific Transcription.
REACT_206830. E2F mediated regulation of DNA replication.

Miscellaneous databases

ChiTaRSi RRM2. mouse.
EvolutionaryTracei P11157.
NextBioi 297647.
PROi P11157.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11157.
Bgeei P11157.
CleanExi MM_RRM2.
Genevestigatori P11157.

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

« Hide 'large scale' publications
  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.
    , 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. 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.

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: September 3, 2014
This is version 149 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

External Data

Dasty 3

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