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Q6PEE3

- RIR2B_MOUSE

UniProt

Q6PEE3 - RIR2B_MOUSE

Protein

Ribonucleoside-diphosphate reductase subunit M2 B

Gene

Rrm2b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage.2 Publications

    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 bindingi100 – 1001Iron 1PROSITE-ProRule annotation
    Metal bindingi131 – 1311Iron 1PROSITE-ProRule annotation
    Metal bindingi131 – 1311Iron 2By similarity
    Metal bindingi134 – 1341Iron 1PROSITE-ProRule annotation
    Active sitei138 – 1381PROSITE-ProRule annotation
    Metal bindingi194 – 1941Iron 2By similarity
    Metal bindingi228 – 2281Iron 2By similarity
    Metal bindingi231 – 2311Iron 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
    2. deoxyribonucleoside triphosphate metabolic process Source: MGI
    3. deoxyribonucleotide biosynthetic process Source: MGI
    4. DNA repair Source: MGI
    5. kidney development Source: MGI
    6. mitochondrial DNA replication Source: MGI
    7. negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
    8. renal system process Source: MGI
    9. response to oxidative stress Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase subunit M2 B (EC:1.17.4.1)
    Alternative name(s):
    TP53-inducible ribonucleotide reductase M2 B
    p53-inducible ribonucleotide reductase small subunit 2-like protein
    Short name:
    p53R2
    Gene namesi
    Name:Rrm2b
    Synonyms:P53r2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:2155865. Rrm2b.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Translocates from cytoplasm to nucleus in response to DNA damage.By similarity

    GO - Cellular componenti

    1. mitochondrion Source: MGI
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice develop normally until they are weaned but from then on exhibit growth retardation and early mortality. Pathological examination indicates that multiple organs fail and that they die from severe renal failure by the age of 14 weeks.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 351351Ribonucleoside-diphosphate reductase subunit M2 BPRO_0000228152Add
    BLAST

    Proteomic databases

    PaxDbiQ6PEE3.
    PRIDEiQ6PEE3.

    PTM databases

    PhosphoSiteiQ6PEE3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6PEE3.
    BgeeiQ6PEE3.
    CleanExiMM_RRM2B.
    GenevestigatoriQ6PEE3.

    Interactioni

    Subunit structurei

    Heterotetramer with large (RRM1) subunit. Interacts with p53/TP53. Interacts with RRM1 in response to DNA damage By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000022901.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PEE3.
    SMRiQ6PEE3. Positions 28-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0208.
    GeneTreeiENSGT00390000013305.
    HOGENOMiHOG000255975.
    HOVERGENiHBG001647.
    InParanoidiQ6PEE3.
    KOiK10808.
    OMAiCLMFHYL.
    OrthoDBiEOG7VMP5N.
    PhylomeDBiQ6PEE3.
    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.

    Q6PEE3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDPERPEAA RPEKGEQLCS ETEENVVRSN EEPLLRKSSR RFVIFPIQYP    50
    DIWRMYKQAQ ASFWTAEEVD LSKDLPHWNK LKSDEKYFIS HILAFFAASD 100
    GIVNENLVER FSQEVQVPEA RCFYGFQILI ENVHSEMYSL LIDTYIRDPK 150
    KREFLFNAIE TMPYVKKKAD WALRWIADRK STFGERVVAF AAVEGIFFSG 200
    SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ YLVNKPSEDR 250
    VREIIADAVQ IEQEFLTEAL PVGLIGMNCV LMKQYIEFVA DRLLGELGFS 300
    KIFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD 350
    F 351
    Length:351
    Mass (Da):40,804
    Last modified:July 5, 2004 - v1
    Checksum:i4E1259233C9CC8A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK138731 mRNA. Translation: BAE23760.1.
    BC058103 mRNA. Translation: AAH58103.1.
    CCDSiCCDS27437.1.
    RefSeqiNP_955770.1. NM_199476.1.
    UniGeneiMm.24738.

    Genome annotation databases

    EnsembliENSMUST00000022901; ENSMUSP00000022901; ENSMUSG00000022292.
    GeneIDi382985.
    KEGGimmu:382985.
    UCSCiuc007vnl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK138731 mRNA. Translation: BAE23760.1 .
    BC058103 mRNA. Translation: AAH58103.1 .
    CCDSi CCDS27437.1.
    RefSeqi NP_955770.1. NM_199476.1.
    UniGenei Mm.24738.

    3D structure databases

    ProteinModelPortali Q6PEE3.
    SMRi Q6PEE3. Positions 28-314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000022901.

    PTM databases

    PhosphoSitei Q6PEE3.

    Proteomic databases

    PaxDbi Q6PEE3.
    PRIDEi Q6PEE3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022901 ; ENSMUSP00000022901 ; ENSMUSG00000022292 .
    GeneIDi 382985.
    KEGGi mmu:382985.
    UCSCi uc007vnl.1. mouse.

    Organism-specific databases

    CTDi 50484.
    MGIi MGI:2155865. Rrm2b.

    Phylogenomic databases

    eggNOGi COG0208.
    GeneTreei ENSGT00390000013305.
    HOGENOMi HOG000255975.
    HOVERGENi HBG001647.
    InParanoidi Q6PEE3.
    KOi K10808.
    OMAi CLMFHYL.
    OrthoDBi EOG7VMP5N.
    PhylomeDBi Q6PEE3.
    TreeFami TF300465.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Miscellaneous databases

    NextBioi 403612.
    PROi Q6PEE3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PEE3.
    Bgeei Q6PEE3.
    CleanExi MM_RRM2B.
    Genevestigatori Q6PEE3.

    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 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.
      Tissue: Thymus.
    2. "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.
    3. "Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells."
      Guittet O., Haakansson P., Voevodskaya N., Fridd S., Graeslund A., Arakawa H., Nakamura Y., Thelander L.
      J. Biol. Chem. 276:40647-40651(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT.
    4. "Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools."
      Kimura T., Takeda S., Sagiya Y., Gotoh M., Nakamura Y., Arakawa H.
      Nat. Genet. 34:440-445(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiRIR2B_MOUSE
    AccessioniPrimary (citable) accession number: Q6PEE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3