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P11157

- RIR2_MOUSE

UniProt

P11157 - RIR2_MOUSE

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
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. 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.

    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 – 1771PROSITE-ProRule annotation
    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. deoxyribonucleoside diphosphate metabolic process Source: InterPro
    2. deoxyribonucleotide biosynthetic process Source: UniProtKB
    3. deoxyribonucleotide metabolic process Source: MGI
    4. DNA replication Source: UniProtKB-UniPathway
    5. protein heterotetramerization Source: UniProtKB
    6. protein oligomerization Source: MGI

    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

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 390390Ribonucleoside-diphosphate reductase subunit M2PRO_0000190450Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201Phosphoserine2 Publications
    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

    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

    1
    390
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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: October 1, 2014
    This is version 150 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