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P07742

- RIR1_MOUSE

UniProt

P07742 - RIR1_MOUSE

Protein

Ribonucleoside-diphosphate reductase large subunit

Gene

Rrm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin.1 Publication

    Enzyme regulationi

    Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the M1 subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei5 – 51Allosteric activatorBy similarity
    Binding sitei53 – 531Allosteric activatorBy similarity
    Binding sitei88 – 881Allosteric activatorBy similarity
    Sitei218 – 2181Important for hydrogen atom transferBy similarity
    Sitei226 – 2261Allosteric effector binding, determines substrate specificityBy similarity
    Binding sitei247 – 2471Substrate; via amide nitrogenBy similarity
    Sitei256 – 2561Allosteric effector binding, determines substrate specificityBy similarity
    Active sitei427 – 4271Proton acceptorBy similarity
    Active sitei429 – 4291Cysteine radical intermediateBy similarity
    Active sitei431 – 4311Proton acceptorBy similarity
    Sitei444 – 4441Important for hydrogen atom transferBy similarity
    Sitei737 – 7371Important for electron transferBy similarity
    Sitei738 – 7381Important for electron transferBy similarity
    Sitei787 – 7871Interacts with thioredoxin/glutaredoxinBy similarity
    Sitei790 – 7901Interacts with thioredoxin/glutaredoxinBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. purine nucleotide binding Source: MGI
    4. ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: UniProtKB

    GO - Biological processi

    1. cell proliferation in forebrain Source: Ensembl
    2. deoxyribonucleotide biosynthetic process Source: UniProtKB
    3. DNA replication Source: UniProtKB-UniPathway
    4. male gonad development Source: Ensembl
    5. mitotic cell cycle Source: Ensembl
    6. protein heterotetramerization Source: UniProtKB
    7. protein oligomerization Source: MGI
    8. pyrimidine nucleobase metabolic process Source: Ensembl
    9. response to ionizing radiation Source: Ensembl
    10. retina development in camera-type eye Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribonucleoside-diphosphate reductase large subunit (EC:1.17.4.1)
    Alternative name(s):
    Ribonucleoside-diphosphate reductase subunit M1
    Ribonucleotide reductase large subunit
    Gene namesi
    Name:Rrm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:98180. Rrm1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell projection Source: Ensembl
    2. neuronal cell body Source: Ensembl
    3. nuclear envelope Source: Ensembl
    4. ribonucleoside-diphosphate reductase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 792792Ribonucleoside-diphosphate reductase large subunitPRO_0000187191Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171N6-acetyllysineBy similarity
    Disulfide bondi218 ↔ 444Redox-activeBy similarity
    Modified residuei376 – 3761N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP07742.
    PaxDbiP07742.
    PRIDEiP07742.

    PTM databases

    PhosphoSiteiP07742.

    Expressioni

    Gene expression databases

    BgeeiP07742.
    CleanExiMM_RRM1.
    GenevestigatoriP07742.

    Interactioni

    Subunit structurei

    Heterodimer of a large and a small subunit. Interacts with RRM2B By similarity.By similarity

    Protein-protein interaction databases

    BioGridi203022. 4 interactions.
    IntActiP07742. 1 interaction.
    MINTiMINT-4121992.

    Structurei

    3D structure databases

    ProteinModelPortaliP07742.
    SMRiP07742. Positions 14-742.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 9292ATP-conePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni11 – 177Allosteric activator bindingBy similarity
    Regioni217 – 2182Substrate bindingBy similarity
    Regioni285 – 2884Allosteric effector binding, determines substrate specificityBy similarity
    Regioni427 – 4315Substrate bindingBy similarity
    Regioni603 – 6075Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 1 ATP-cone domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0209.
    GeneTreeiENSGT00390000001372.
    HOGENOMiHOG000057035.
    HOVERGENiHBG003447.
    InParanoidiQ91YM8.
    KOiK10807.
    OMAiLLWQMPS.
    OrthoDBiEOG7BGHK2.
    TreeFamiTF300578.

    Family and domain databases

    InterProiIPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view]
    PfamiPF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view]
    PRINTSiPR01183. RIBORDTASEM1.
    SUPFAMiSSF48168. SSF48168. 1 hit.
    TIGRFAMsiTIGR02506. NrdE_NrdA. 1 hit.
    PROSITEiPS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P07742-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHVIKRDGRQ ERVMFDKITS RIQKLCYGLN MDFVDPAQIT MKVIQGLYSG    50
    VTTVELDTLA AETAATLTTK HPDYAILAAR IAVSNLHKET KKVFSDVMED 100
    LYNYINPHNG RHSPMVASST LDIVMANKDR LNSAIIYDRD FSYNYFGFKT 150
    LERSYLLKIN GKVAERPQHM LMRVSVGIHK EDIDAAIETY NLLSEKWFTH 200
    ASPTLFNAGT NRPQLSSCFL LSMKDDSIEG IYDTLKQCAL ISKSAGGIGV 250
    AVSCIRATGS YIAGTNGNSN GLVPMLRVYN NTARYVDQGG NKRPGAFAIY 300
    LEPWHLDIFE FLDLKKNTGK EEQRARDLFF ALWIPDLFMK RVETNQDWSL 350
    MCPNECPGLD EVWGEEFEKL YESYEKQGRV RKVVKAQQLW YAIIESQTET 400
    GTPYMLYKDS CNRKSNQQNL GTIKCSNLCT EIVEYTSKDE VAVCNLASLA 450
    LNMYVTPEHT YDFEKLAEVT KVIVRNLNKI IDINYYPIPE AHLSNKRHRP 500
    IGIGVQGLAD AFILMRYPFE SPEAQLLNKQ IFETIYYGAL EASCELAKEY 550
    GPYETYEGSP VSKGILQYDM WNVAPTDLWD WKPLKEKIAK YGIRNSLLIA 600
    PMPTASTAQI LGNNESIEPY TSNIYTRRVL SGEFQIVNPH LLKDLTERGL 650
    WNEEMKNQII ACNGSIQSIP EIPDDLKQLY KTVWEISQKT VLKMAAERGA 700
    FIDQSQSLNI HIAEPNYGKL TSMHFYGWKQ GLKTGMYYLR TRPAANPIQF 750
    TLNKEKLKDK EKALKEEEEK ERNTAAMVCS LENREECLMC GS 792
    Length:792
    Mass (Da):90,210
    Last modified:July 27, 2011 - v2
    Checksum:i051C6CE407D24C69
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti202 – 2021S → P in AAA40061. (PubMed:2581962)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02927 mRNA. Translation: AAA40061.1.
    AK088043 mRNA. Translation: BAC40112.1.
    AK137075 mRNA. Translation: BAE23230.1.
    AK168586 mRNA. Translation: BAE40455.1.
    CH466531 Genomic DNA. Translation: EDL16602.1.
    BC016450 mRNA. Translation: AAH16450.1.
    CCDSiCCDS40049.1.
    PIRiA24050.
    RefSeqiNP_033129.2. NM_009103.3.
    UniGeneiMm.197486.
    Mm.415177.

    Genome annotation databases

    EnsembliENSMUST00000033283; ENSMUSP00000033283; ENSMUSG00000030978.
    GeneIDi20133.
    KEGGimmu:20133.
    UCSCiuc009irp.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02927 mRNA. Translation: AAA40061.1 .
    AK088043 mRNA. Translation: BAC40112.1 .
    AK137075 mRNA. Translation: BAE23230.1 .
    AK168586 mRNA. Translation: BAE40455.1 .
    CH466531 Genomic DNA. Translation: EDL16602.1 .
    BC016450 mRNA. Translation: AAH16450.1 .
    CCDSi CCDS40049.1.
    PIRi A24050.
    RefSeqi NP_033129.2. NM_009103.3.
    UniGenei Mm.197486.
    Mm.415177.

    3D structure databases

    ProteinModelPortali P07742.
    SMRi P07742. Positions 14-742.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203022. 4 interactions.
    IntActi P07742. 1 interaction.
    MINTi MINT-4121992.

    Chemistry

    BindingDBi P07742.
    ChEMBLi CHEMBL3739.

    PTM databases

    PhosphoSitei P07742.

    Proteomic databases

    MaxQBi P07742.
    PaxDbi P07742.
    PRIDEi P07742.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033283 ; ENSMUSP00000033283 ; ENSMUSG00000030978 .
    GeneIDi 20133.
    KEGGi mmu:20133.
    UCSCi uc009irp.2. mouse.

    Organism-specific databases

    CTDi 6240.
    MGIi MGI:98180. Rrm1.

    Phylogenomic databases

    eggNOGi COG0209.
    GeneTreei ENSGT00390000001372.
    HOGENOMi HOG000057035.
    HOVERGENi HBG003447.
    InParanoidi Q91YM8.
    KOi K10807.
    OMAi LLWQMPS.
    OrthoDBi EOG7BGHK2.
    TreeFami TF300578.

    Enzyme and pathway databases

    UniPathwayi UPA00326 .

    Miscellaneous databases

    NextBioi 297643.
    PROi P07742.
    SOURCEi Search...

    Gene expression databases

    Bgeei P07742.
    CleanExi MM_RRM1.
    Genevestigatori P07742.

    Family and domain databases

    InterProi IPR005144. ATP-cone.
    IPR013346. NrdE_NrdA.
    IPR000788. RNR_lg_C.
    IPR013509. RNR_lsu_N.
    IPR008926. RNR_R1-su_N.
    [Graphical view ]
    Pfami PF03477. ATP-cone. 1 hit.
    PF02867. Ribonuc_red_lgC. 1 hit.
    PF00317. Ribonuc_red_lgN. 1 hit.
    [Graphical view ]
    PRINTSi PR01183. RIBORDTASEM1.
    SUPFAMi SSF48168. SSF48168. 1 hit.
    TIGRFAMsi TIGR02506. NrdE_NrdA. 1 hit.
    PROSITEi PS51161. ATP_CONE. 1 hit.
    PS00089. RIBORED_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloned mouse ribonucleotide reductase subunit M1 cDNA reveals amino acid sequence homology with Escherichia coli and herpesvirus ribonucleotide reductases."
      Caras I.W., Levinson B.B., Fabry M., Williams S.R., Martin D.W. Jr.
      J. Biol. Chem. 260:7015-7022(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Caras I.W.
      Submitted (AUG-1985) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    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 and NOD.
      Tissue: Embryo, Embryonic liver and Thymus.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: FVB/N.
      Tissue: Mammary tumor.
    6. "Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for mammalian S phase ribonucleotide reductase."
      Avval F.Z., Holmgren A.
      J. Biol. Chem. 284:8233-8240(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBUNIT.

    Entry informationi

    Entry nameiRIR1_MOUSE
    AccessioniPrimary (citable) accession number: P07742
    Secondary accession number(s): Q91YM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 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.
    The level of the enzyme activity is closely correlated with the growth rate of a cell and appears to vary with the cell cycle.

    Keywords - Technical termi

    Allosteric enzyme, 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