Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P09938

- RIR2_YEAST

UniProt

P09938 - RIR2_YEAST

Protein

Ribonucleoside-diphosphate reductase small chain 1

Gene

RNR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR2 provides the diiron-tyrosyl radical center.1 Publication

    Catalytic activityi

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

    Cofactori

    Binds 2 iron ions per subunit.

    Kineticsi

      Vmax=2250 nmol/min/mg enzyme for cytidine 5'-diphosphate1 Publication

      Temperature dependencei

      Optimum temperature is 30 degrees Celsius.1 Publication

      Pathwayi

      Sites

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Metal bindingi145 – 1451Iron 1
      Metal bindingi176 – 1761Iron 1
      Metal bindingi176 – 1761Iron 2
      Metal bindingi179 – 1791Iron 1
      Active sitei183 – 1831
      Metal bindingi239 – 2391Iron 2
      Metal bindingi273 – 2731Iron 2
      Metal bindingi276 – 2761Iron 2

      GO - Molecular functioni

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

      GO - Biological processi

      1. deoxyribonucleoside diphosphate metabolic process Source: InterPro
      2. deoxyribonucleotide biosynthetic process Source: SGD
      3. DNA replication Source: UniProtKB-UniPathway

      Keywords - Molecular functioni

      Oxidoreductase

      Keywords - Biological processi

      DNA replication

      Keywords - Ligandi

      Iron, Metal-binding

      Enzyme and pathway databases

      BioCyciMetaCyc:YJL026W-MONOMER.
      YEAST:YJL026W-MONOMER.
      ReactomeiREACT_189247. G1/S-Specific Transcription.
      UniPathwayiUPA00326.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Ribonucleoside-diphosphate reductase small chain 1 (EC:1.17.4.1)
      Alternative name(s):
      Ribonucleotide reductase R2 subunit 1
      Ribonucleotide reductase small subunit 1
      Gene namesi
      Name:RNR2
      Synonyms:CRT6
      Ordered Locus Names:YJL026W
      ORF Names:J1271
      OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
      Taxonomic identifieri559292 [NCBI]
      Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
      ProteomesiUP000002311: Chromosome X

      Organism-specific databases

      CYGDiYJL026w.
      SGDiS000003563. RNR2.

      Subcellular locationi

      Nucleus 2 Publications
      Note: Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner. Nuclear localization is mediated by DIF1.

      GO - Cellular componenti

      1. cytoplasm Source: SGD
      2. nucleus Source: SGD
      3. ribonucleoside-diphosphate reductase complex Source: SGD

      Keywords - Cellular componenti

      Nucleus

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 399399Ribonucleoside-diphosphate reductase small chain 1PRO_0000190464Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Modified residuei15 – 151Phosphoserine4 Publications
      Modified residuei24 – 241Phosphoserine1 Publication
      Modified residuei41 – 411Phosphoserine1 Publication

      Keywords - PTMi

      Phosphoprotein

      Proteomic databases

      MaxQBiP09938.
      PaxDbiP09938.
      PeptideAtlasiP09938.

      Expressioni

      Inductioni

      Induced by DNA-damage.2 Publications

      Gene expression databases

      GenevestigatoriP09938.

      Interactioni

      Subunit structurei

      Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3. Interacts with DIF1.3 Publications

      Binary interactionsi

      WithEntry#Exp.IntActNotes
      RNR4P497236EBI-15240,EBI-15251

      Protein-protein interaction databases

      BioGridi33733. 50 interactions.
      DIPiDIP-5671N.
      IntActiP09938. 15 interactions.
      MINTiMINT-547064.
      STRINGi4932.YJL026W.

      Structurei

      Secondary structure

      1
      399
      Legend: HelixTurnBeta strand
      Show more details
      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Helixi27 – 3610
      Helixi38 – 4912
      Helixi51 – 6111
      Helixi63 – 7210
      Helixi73 – 753
      Helixi77 – 793
      Helixi94 – 10411
      Helixi110 – 1123
      Helixi118 – 1247
      Helixi128 – 14215
      Helixi147 – 1526
      Helixi153 – 1575
      Helixi163 – 19028
      Helixi194 – 20411
      Helixi208 – 22013
      Beta strandi223 – 2253
      Helixi228 – 24013
      Turni241 – 2433
      Helixi244 – 25512
      Helixi260 – 28526
      Helixi293 – 31220
      Helixi317 – 3204
      Helixi324 – 34017
      Turni341 – 3433
      Helixi355 – 3584

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      1JK0X-ray2.80A1-399[»]
      1SMQX-ray3.10A/B/C/D1-399[»]
      2CVYX-ray2.40B391-399[»]
      DisProtiDP00487.
      ProteinModelPortaliP09938.
      SMRiP09938. Positions 26-359.
      ModBaseiSearch...
      MobiDBiSearch...

      Miscellaneous databases

      EvolutionaryTraceiP09938.

      Family & Domainsi

      Sequence similaritiesi

      Phylogenomic databases

      eggNOGiCOG0208.
      GeneTreeiENSGT00390000013305.
      HOGENOMiHOG000255975.
      KOiK10808.
      OMAiGVMNSTK.
      OrthoDBiEOG7T1RMH.

      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.

      P09938-1 [UniParc]FASTAAdd to Basket

      « Hide

      MPKETPSKAA ADALSDLEIK DSKSNLNKEL ETLREENRVK SDMLKEKLSK    50
      DAENHKAYLK SHQVHRHKLK EMEKEEPLLN EDKERTVLFP IKYHEIWQAY 100
      KRAEASFWTA EEIDLSKDIH DWNNRMNENE RFFISRVLAF FAASDGIVNE 150
      NLVENFSTEV QIPEAKSFYG FQIMIENIHS ETYSLLIDTY IKDPKESEFL 200
      FNAIHTIPEI GEKAEWALRW IQDADALFGE RLVAFASIEG VFFSGSFASI 250
      FWLKKRGMMP GLTFSNELIC RDEGLHTDFA CLLFAHLKNK PDPAIVEKIV 300
      TEAVEIEQRY FLDALPVALL GMNADLMNQY VEFVADRLLV AFGNKKYYKV 350
      ENPFDFMENI SLAGKTNFFE KRVSDYQKAG VMSKSTKQEA GAFTFNEDF 399
      Length:399
      Mass (Da):46,147
      Last modified:November 1, 1995 - v2
      Checksum:iDB98028408292042
      GO

      Experimental Info

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Sequence conflicti101 – 1033Missing in AAA34987. (PubMed:3313004)Curated
      Sequence conflicti111 – 1111E → ETAE(PubMed:3313004)Curated

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      M17221 Genomic DNA. Translation: AAA34987.1.
      M17789 Genomic DNA. Translation: AAA34988.1.
      Z49301 Genomic DNA. Translation: CAA89317.1.
      BK006943 Genomic DNA. Translation: DAA08772.1.
      PIRiA26916.
      RefSeqiNP_012508.1. NM_001181460.1.

      Genome annotation databases

      EnsemblFungiiYJL026W; YJL026W; YJL026W.
      GeneIDi853427.
      KEGGisce:YJL026W.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      M17221 Genomic DNA. Translation: AAA34987.1 .
      M17789 Genomic DNA. Translation: AAA34988.1 .
      Z49301 Genomic DNA. Translation: CAA89317.1 .
      BK006943 Genomic DNA. Translation: DAA08772.1 .
      PIRi A26916.
      RefSeqi NP_012508.1. NM_001181460.1.

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      Entry Method Resolution (Å) Chain Positions PDBsum
      1JK0 X-ray 2.80 A 1-399 [» ]
      1SMQ X-ray 3.10 A/B/C/D 1-399 [» ]
      2CVY X-ray 2.40 B 391-399 [» ]
      DisProti DP00487.
      ProteinModelPortali P09938.
      SMRi P09938. Positions 26-359.
      ModBasei Search...
      MobiDBi Search...

      Protein-protein interaction databases

      BioGridi 33733. 50 interactions.
      DIPi DIP-5671N.
      IntActi P09938. 15 interactions.
      MINTi MINT-547064.
      STRINGi 4932.YJL026W.

      Proteomic databases

      MaxQBi P09938.
      PaxDbi P09938.
      PeptideAtlasi P09938.

      Protocols and materials databases

      Structural Biology Knowledgebase Search...

      Genome annotation databases

      EnsemblFungii YJL026W ; YJL026W ; YJL026W .
      GeneIDi 853427.
      KEGGi sce:YJL026W.

      Organism-specific databases

      CYGDi YJL026w.
      SGDi S000003563. RNR2.

      Phylogenomic databases

      eggNOGi COG0208.
      GeneTreei ENSGT00390000013305.
      HOGENOMi HOG000255975.
      KOi K10808.
      OMAi GVMNSTK.
      OrthoDBi EOG7T1RMH.

      Enzyme and pathway databases

      UniPathwayi UPA00326 .
      BioCyci MetaCyc:YJL026W-MONOMER.
      YEAST:YJL026W-MONOMER.
      Reactomei REACT_189247. G1/S-Specific Transcription.

      Miscellaneous databases

      EvolutionaryTracei P09938.
      NextBioi 973962.
      PROi P09938.

      Gene expression databases

      Genevestigatori P09938.

      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. "Identification and isolation of the gene encoding the small subunit of ribonucleotide reductase from Saccharomyces cerevisiae: DNA damage-inducible gene required for mitotic viability."
        Elledge S.J., Davis R.W.
        Mol. Cell. Biol. 7:2783-2793(1987) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      2. "Identification of the gene for the yeast ribonucleotide reductase small subunit and its inducibility by methyl methanesulfonate."
        Hurd H.K., Roberts C.W., Roberts J.W.
        Mol. Cell. Biol. 7:3673-3677(1987) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
      3. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
        Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
        , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
        EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
        Strain: ATCC 204508 / S288c.
      4. Cited for: GENOME REANNOTATION.
        Strain: ATCC 204508 / S288c.
      5. "Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly."
        Nguyen H.-H.T., Ge J., Perlstein D.L., Stubbe J.
        Proc. Natl. Acad. Sci. U.S.A. 96:12339-12344(1999) [PubMed] [Europe PMC] [Abstract]
        Cited for: FUNCTION, SUBUNIT.
      6. "Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit."
        Chabes A., Domkin V., Larsson G., Liu A., Graeslund A., Wijmenga S., Thelander L.
        Proc. Natl. Acad. Sci. U.S.A. 97:2474-2479(2000) [PubMed] [Europe PMC] [Abstract]
        Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
      7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
      8. "Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways."
        Yao R., Zhang Z., An X., Bucci B., Perlstein D.L., Stubbe J., Huang M.
        Proc. Natl. Acad. Sci. U.S.A. 100:6628-6633(2003) [PubMed] [Europe PMC] [Abstract]
        Cited for: SUBCELLULAR LOCATION.
      9. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
        Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
        Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
        Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
        Strain: YAL6B.
      10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
        Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
        J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
        Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
        Strain: ADR376.
      11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
        Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
        Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
        Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      12. "Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase."
        Lee Y.D., Wang J., Stubbe J., Elledge S.J.
        Mol. Cell 32:70-80(2008) [PubMed] [Europe PMC] [Abstract]
        Cited for: SUBCELLULAR LOCATION, INTERACTION WITH DIF1 AND RNR4.
      13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
        Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
        Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
        Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
        Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
        Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
        Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      15. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
      16. "Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers."
        Sommerhalter M., Voegtli W.C., Perlstein D.L., Ge J., Stubbe J., Rosenzweig A.C.
        Biochemistry 43:7736-7742(2004) [PubMed] [Europe PMC] [Abstract]
        Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).

      Entry informationi

      Entry nameiRIR2_YEAST
      AccessioniPrimary (citable) accession number: P09938
      Secondary accession number(s): D6VWF6
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: July 1, 1989
      Last sequence update: November 1, 1995
      Last modified: October 1, 2014
      This is version 160 of the entry and version 2 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programFungal Protein Annotation Program

      Miscellaneousi

      Miscellaneous

      Present with 538 molecules/cell in log phase SD medium.1 Publication

      Keywords - Technical termi

      3D-structure, Complete proteome, Reference proteome

      Documents

      1. PATHWAY comments
        Index of metabolic and biosynthesis pathways
      2. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      3. SIMILARITY comments
        Index of protein domains and families
      4. Yeast
        Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
      5. Yeast chromosome X
        Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

      External Data

      Dasty 3