Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P09938 (RIR2_YEAST)

Last modified June 16, 2009. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Ribonucleoside-diphosphate reductase small chain 1
    EC=1.17.4.1
Alternative name(s):
    Ribonucleotide reductase small subunit 1
    Ribonucleotide reductase R2 subunit 1
Gene names
Name: RNR2
Synonyms: CRT6
Ordered Locus Names: YJL026W
ORF Names: J1271
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Hide | Top

Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR2 provides the diiron-tyrosyl radical center. Ref.4

Catalytic activity

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

Cofactor

Binds 2 iron ions per subunit.

Pathway

Genetic information processing; DNA replication.

Subunit structure

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. Ref.4 Ref.5

Subcellular location

Nucleus. 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. Ref.7

Induction

Induced by DNA-damage. Ref.1 Ref.2

Miscellaneous

Present with 538 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Belongs to the ribonucleoside diphosphate reductase small chain family.

Biophysicochemical properties

Kinetic parameters:

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

Temperature dependence:

Optimum temperature is 30 degrees Celsius.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself1EBI-15240,EBI-15240
P382541EBI-15240,EBI-21533
P429371EBI-15240,EBI-23470
Q061371EBI-15240,EBI-33827
ACB1P317871EBI-15240,EBI-2060
ADE4P040461EBI-15240,EBI-14238
ALO1P547831EBI-15240,EBI-2519
APC9Q121071EBI-15240,EBI-36475
ARP2P323811EBI-15240,EBI-2927
ATX1P386361EBI-15240,EBI-2046026
BBC1P470681EBI-15240,EBI-3437
BCY1P072781EBI-15240,EBI-9475
CAP2P135171EBI-15240,EBI-4013
CCR4P313841EBI-15240,EBI-4396
CDC28P005461EBI-15240,EBI-4253
CKA1P157901EBI-15240,EBI-9533
CKB1P436391EBI-15240,EBI-9563
CKI1P204851EBI-15240,EBI-9699
CMK1P274661EBI-15240,EBI-9592
CMK2P225171EBI-15240,EBI-9600
CNA2P147471EBI-15240,EBI-12778
CSL4P538591EBI-15240,EBI-1731
CTT1P061151EBI-15240,EBI-4065
DCP2P535501EBI-15240,EBI-270
DCS1Q061511EBI-15240,EBI-38973
DHH1P395171EBI-15240,EBI-158
DPB4Q046031EBI-15240,EBI-29938
FAP7Q120551EBI-15240,EBI-22197
FBP26P326041EBI-15240,EBI-6749
FCY1Q121781EBI-15240,EBI-6851
FUM1P084171EBI-15240,EBI-7165
GAD1Q047921EBI-15240,EBI-5668
GCY1P140651EBI-15240,EBI-7505
GDH2P333271EBI-15240,EBI-5815
GET3Q121541EBI-15240,EBI-2989
GLO2Q055841EBI-15240,EBI-7672
GLR1P419211EBI-15240,EBI-7920
GPD2P419111EBI-15240,EBI-7791
GPM2Q120081EBI-15240,EBI-2063839
GPX2P381431EBI-15240,EBI-7863
GRE3P387151EBI-15240,EBI-7884
GSY2P274721EBI-15240,EBI-8036
HCH1P538341EBI-15240,EBI-28288
HOG1P324851EBI-15240,EBI-8437
HSP30P256191EBI-15240,EBI-8563
HUG1Q6Q5K61EBI-15240,EBI-392766
HYR1P405811EBI-15240,EBI-7869
IDI1P154961EBI-15240,EBI-8902
IMD3P500951EBI-15240,EBI-9190
INO1P119861EBI-15240,EBI-9257
KAP104P382171EBI-15240,EBI-9152
KRE1P172601EBI-15240,EBI-2068892
KTI11Q3E8401EBI-15240,EBI-2055307
LIA1P471201EBI-15240,EBI-25526
LSB1P532811EBI-15240,EBI-23329
LSM4P400701EBI-15240,EBI-188
MCM5P294961EBI-15240,EBI-10549
MPT5P390161EBI-15240,EBI-2052996
NOT1P256551EBI-15240,EBI-12139
PGM2P370121EBI-15240,EBI-13296
PHO13P198811EBI-15240,EBI-35376
PLP2Q120171EBI-15240,EBI-39032
PRE10P212421EBI-15240,EBI-13963
PST2Q123351EBI-15240,EBI-14064
PTC2P399661EBI-15240,EBI-12795
RAD25Q005781EBI-15240,EBI-14683
RAS2P011201EBI-15240,EBI-14838
RCK2P386231EBI-15240,EBI-14885
RDI1Q124341EBI-15240,EBI-7525
RFA2P267541EBI-15240,EBI-14976
RNR4P497233EBI-15240,EBI-15251
RPB2P085181EBI-15240,EBI-15767
RRP4P387921EBI-15240,EBI-1757
RRP43P253591EBI-15240,EBI-1773
RVS161P253431EBI-15240,EBI-14490
SAP155P436121EBI-15240,EBI-16370
SDS22P360471EBI-15240,EBI-16783
SDS24P383141EBI-15240,EBI-20977
SEM1O947421EBI-15240,EBI-31337
SER3P400541EBI-15240,EBI-16961
SGT1Q084461EBI-15240,EBI-17070
SKI8Q027931EBI-15240,EBI-17260
SLA1P327901EBI-15240,EBI-17313
SLT2Q007721EBI-15240,EBI-17372
SMI1P325661EBI-15240,EBI-17452
SNC2P333281EBI-15240,EBI-17512
SNX4P470571EBI-15240,EBI-17610
SOL3P388581EBI-15240,EBI-17685
SRV2P175551EBI-15240,EBI-4024
SSD1P242761EBI-15240,EBI-18153
TFG2P418961EBI-15240,EBI-18916
TIP41Q121991EBI-15240,EBI-38123
TPD3P313831EBI-15240,EBI-1936
TPK1P062441EBI-15240,EBI-9458
TRP2P008991EBI-15240,EBI-19575
TSA2Q041201EBI-15240,EBI-19631
TVP15Q038601EBI-15240,EBI-37537
UBC13P524901EBI-15240,EBI-19777
UGA2P380671EBI-15240,EBI-20027
URA7P282741EBI-15240,EBI-20128
VHS2P404631EBI-15240,EBI-25234
VPS21P360171EBI-15240,EBI-29399
WTM2Q122062EBI-15240,EBI-20571
YCK1P232911EBI-15240,EBI-4718
YHB1P396761EBI-15240,EBI-6905
YKL054CP357321EBI-15240,EBI-26695
YNK1P360101EBI-15240,EBI-11968
YPT1P011231EBI-15240,EBI-29496
YVH1Q022561EBI-15240,EBI-14322
ZPR1P533031EBI-15240,EBI-29657

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Ribonucleoside-diphosphate reductase small chain 1
PRO_0000190464

Sites

Active site1831
Metal binding1451Iron 1
Metal binding1761Iron 1
Metal binding1761Iron 2
Metal binding1791Iron 1
Metal binding2391Iron 2
Metal binding2731Iron 2
Metal binding2761Iron 2

Amino acid modifications

Modified residue71Phosphoserine Ref.13
Modified residue151Phosphoserine Ref.13 Ref.8 Ref.9 Ref.10 Ref.12
Modified residue221Phosphoserine Ref.13 Ref.12
Modified residue241Phosphoserine Ref.13
Modified residue411Phosphoserine Ref.11
Modified residue3741Phosphoserine Ref.13 Ref.12

Experimental info

Sequence conflict101 – 1033Missing in AAA34987. Ref.1
Sequence conflict1111E → ETAE Ref.1

Secondary structure

1 .............................................. 399
Helix Strand Turn

Details...

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P09938-1 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: DB98028408292042

FASTA39946,147
        10         20         30         40         50         60 
MPKETPSKAA ADALSDLEIK DSKSNLNKEL ETLREENRVK SDMLKEKLSK DAENHKAYLK 

        70         80         90        100        110        120 
SHQVHRHKLK EMEKEEPLLN EDKERTVLFP IKYHEIWQAY KRAEASFWTA EEIDLSKDIH 

       130        140        150        160        170        180 
DWNNRMNENE RFFISRVLAF FAASDGIVNE NLVENFSTEV QIPEAKSFYG FQIMIENIHS 

       190        200        210        220        230        240 
ETYSLLIDTY IKDPKESEFL FNAIHTIPEI GEKAEWALRW IQDADALFGE RLVAFASIEG 

       250        260        270        280        290        300 
VFFSGSFASI FWLKKRGMMP GLTFSNELIC RDEGLHTDFA CLLFAHLKNK PDPAIVEKIV 

       310        320        330        340        350        360 
TEAVEIEQRY FLDALPVALL GMNADLMNQY VEFVADRLLV AFGNKKYYKV ENPFDFMENI 

       370        380        390 
SLAGKTNFFE KRVSDYQKAG VMSKSTKQEA GAFTFNEDF

« Hide

Hide | Top

References

« Hide 'large scale' references
[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: 3313004] [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: 3316984] [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. expand/collapse author list , 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: 8641269] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[4]"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: 10535923] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[5]"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: 10716984] [Abstract]
Cited for: SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"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: 12732713] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[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: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
[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: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, MASS SPECTROMETRY.
[12]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-22 AND SER-374, MASS SPECTROMETRY.
[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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-15; SER-22; SER-24 AND SER-374, MASS SPECTROMETRY.
[14]"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer."
Voegtli W.C., Ge J., Perlstein D.L., Stubbe J., Rosenzweig A.C.
Proc. Natl. Acad. Sci. U.S.A. 98:10073-10078(2001) [PubMed: 11526233] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[15]"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: 15196016] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

M17221 Genomic DNA. Translation: AAA34987.1.
M17789 Genomic DNA. Translation: AAA34988.1.
Z49301 Genomic DNA. Translation: CAA89317.1.
PIRA26916.
RefSeqNP_012508.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JK0X-ray2.80A1-399[»]
1SMQX-ray3.10A/B/C/D1-399[»]
2CVYX-ray2.40B391-399[»]
DisProtDP00487.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5671N.
IntActP09938. 159 interactions.

Proteomic databases

PeptideAtlasP09938.
PRIDEP09938.

Genome annotation databases

EnsemblYJL026W. Saccharomyces cerevisiae. [Contig view]
GeneID853427.
GenomeReviewsGene locus YJL026W in contig Y13136_GR.
KEGGsce:YJL026W.
NMPDRfig|4932.3.peg.3482.

Organism-specific databases

CYGDYJL026w.
SGDS000003563. RNR2.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP09938.
OMAP09938. GTPENDQ.

Enzyme and pathway databases

BRENDA1.17.4.1. 250.

Gene expression databases

GermOnlineYJL026W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR012348. Ribncl_red_rel.
IPR000358. Ribonucl_redctse.
[Graphical view]
Gene3DG3DSA:1.10.620.20. Ribncl_red_rel. 1 hit.
PANTHERPTHR23409. Ribonucl_redctse. 1 hit.
PfamPF00268. Ribonuc_red_sm. 1 hit.
[Graphical view]
PROSITEPS00368. RIBORED_SMALL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio973962.

Hide | Top

Entry information

Entry nameRIR2_YEAST
AccessionPrimary (citable) accession number: P09938
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents