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UniProtKB/Swiss-Prot entry P49723


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RIR4_YEAST
Primary accession number P49723
Secondary accession number Q66R92
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 92)
Name and origin of the protein
Protein name Ribonucleoside-diphosphate reductase small chain 2
Synonyms EC 1.17.4.1
Ribonucleotide reductase small subunit 2
Ribonucleotide reductase R2 subunit 2
Gene name
Name: RNR4
Synonyms: CRT3
OrderedLocusNames: YGR180C
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=ATCC 204508 / S288c;
PubMed=9315671 [NCBI, ExPASy, EBI, Israel, Japan]
Wang P.J., Chabes A., Casagrande R., Tian X.C., Thelander L., Huffaker T.C.;
"Rnr4p, a novel ribonucleotide reductase small-subunit protein.";
Mol. Cell. Biol. 17:6114-6121(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9169869 [NCBI, ExPASy, EBI, Israel, Japan]
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
PROTEIN SEQUENCE OF 1-9; 150-158; 167-178; 219-235 AND 294-312, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
Bienvenut W.V., Peters C.;
Submitted (JUN-2005) to UniProtKB.
[5]
FUNCTION, AND SUBUNIT.
DOI=10.1073/pnas.96.22.12339; PubMed=10535923 [NCBI, ExPASy, EBI, Israel, Japan]
Nguyen H.-H.T., Ge J., Perlstein D.L., Stubbe J.;
"Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly.";
Proc. Natl. Acad. Sci. U.S.A. 96:12339-12344(1999).
[6]
SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1073/pnas.97.6.2474; PubMed=10716984 [NCBI, ExPASy, EBI, Israel, Japan]
Chabes A., Domkin V., Larsson G., Liu A., Graeslund A., Wijmenga S., Thelander L.;
"Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit.";
Proc. Natl. Acad. Sci. U.S.A. 97:2474-2479(2000).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
SUBCELLULAR LOCATION.
DOI=10.1073/pnas.1131932100; PubMed=12732713 [NCBI, ExPASy, EBI, Israel, Japan]
Yao R., Zhang Z., An X., Bucci B., Perlstein D.L., Stubbe J., Huang M.;
"Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways.";
Proc. Natl. Acad. Sci. U.S.A. 100:6628-6633(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55 AND SER-169, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; SER-169; SER-330; SER-332; THR-334 AND SER-336, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
DOI=10.1073/pnas.181336398; PubMed=11526233 [NCBI, ExPASy, EBI, Israel, Japan]
Voegtli W.C., Ge J., Perlstein D.L., Stubbe J., Rosenzweig A.C.;
"Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer.";
Proc. Natl. Acad. Sci. U.S.A. 98:10073-10078(2001).
[14]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
DOI=10.1021/bi049510m; PubMed=15196016 [NCBI, ExPASy, EBI, Israel, Japan]
Sommerhalter M., Voegtli W.C., Perlstein D.L., Ge J., Stubbe J., Rosenzweig A.C.;
"Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers.";
Biochemistry 43:7736-7742(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U30385; AAB72236.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z72965; CAA97206.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY723819; AAU09736.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S59744; S59744.
RefSeq NP_011696.1; -.
3D structure databases
PDB
1JK0; X-ray; 2.80 A; B=1-345.[ExPASy / RCSB / EBI]
1SMS; X-ray; 3.10 A; A/B=1-345.[ExPASy / RCSB / EBI]
1ZZD; X-ray; 2.60 A; B=337-345.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JK0; -.
1SMS; -.
1ZZD; -.
DisProt DP00488; -.
ModBase P49723.
Protein-protein interaction databases
DIP DIP:5381N; -.
IntAct P49723; 21.
Organism-specific databases
CYGD YGR180c; -.
SGD S000003412; RNR4.
Yeast-GFP YGR180C.
Gene expression databases
GermOnline YGR180C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005971; Cellular component: ribonucleoside-diphosphate reductase complex (inferred from direct assay from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004748; Molecular function: ribonucleoside-diphosphate reductase activity (inferred from electronic annotation from InterPro).
GO:0046914; Molecular function: transition metal ion binding (inferred from electronic annotation from InterPro).
GO:0051188; Biological process: cofactor biosynthetic process (inferred from mutant phenotype from SGD).
GO:0009186; Biological process: deoxyribonucleoside diphosphate metabolic process (inferred from electronic annotation from InterPro).
GO:0009263; Biological process: deoxyribonucleotide biosynthetic process (inferred from direct assay from SGD).
GO:0006260; Biological process: DNA replication (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012348; Ribncl_red_rel.
IPR000358; Ribonucl_redctse.
Graphical view of domain structure.
Gene3D G3DSA:1.10.620.20; Ribncl_red_rel; 1.
PANTHER PTHR23409; Ribonucl_redctse; 1.
Pfam PF00268; Ribonuc_red_sm; 1.
Pfam graphical view of domain structure.
PROSITE PS00368; RIBORED_SMALL; 1.
Proteomic databases
PeptideAtlas P49723; -.
Proteomics databases
PRIDE P49723; -.
Genome annotation databases
Ensembl YGR180C; Saccharomyces cerevisiae. [Contig view]
GeneID 853091; -.
GenomeReviews Y13135_GR; YGR180C.
KEGG sce:YGR180C; -.
NMPDR fig|4932.3.peg.2823; -.
Phylogenomic databases
HOGENOM P49723; -.
Other
LinkHub P49723; -.
NextBio 973076; -.
ProtoNet P49723.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Complete proteome; Direct protein sequencing; DNA replication; Nucleus; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   345  345     Ribonucleoside-diphosphate reductase small chain 2. PRO_0000190465
ACT_SITE   131   131        By similarity. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   55    55        Phosphoserine. 
MOD_RES   91    91        Phosphoserine. 
MOD_RES   169   169        Phosphoserine. 
MOD_RES   330   330        Phosphoserine. 
MOD_RES   332   332        Phosphoserine. 
MOD_RES   334   334        Phosphothreonine. 
MOD_RES   336   336        Phosphoserine. 
CONFLICT   127   127        Y -> H (in Ref. 3; AAU09736). 
HELIX   4     9  6      
HELIX   13    21  9      
TURN   22    24  3      
TURN   26    28  3      
HELIX   43    54  12      
HELIX   59    61  3      
TURN   65    67  3      
TURN   69    73  5      
HELIX   78    89  12      
HELIX   101   107  7      
HELIX   111   138  28      
HELIX   148   151  4      
HELIX   155   166  12      
STRAND   169   172  4      
HELIX   175   187  13      
TURN   188   190  3      
HELIX   191   200  10      
STRAND   202   205  4      
HELIX   207   232  26      
HELIX   240   258  19      
HELIX   277   288  12      
HELIX   316   322  7      
Sequence information
Length: 345 AA [This is the length of the unprocessed precursor] Molecular weight: 40055 Da [This is the MW of the unprocessed precursor] CRC64: 712853F2D87D3972 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEAHNQFLKT FQKERHDMKE AEKDEILLME NSRRFVMFPI KYHEIWAAYK KVEASFWTAE 

        70         80         90        100        110        120 
EIELAKDTED FQKLTDDQKT YIGNLLALSI SSDNLVNKYL IENFSAQLQN PEGKSFYGFQ 

       130        140        150        160        170        180 
IMMENIYSEV YSMMVDAFFK DPKNIPLFKE IANLPEVKHK AAFIERWISN DDSLYAERLV 

       190        200        210        220        230        240 
AFAAKEGIFQ AGNYASMFWL TDKKIMPGLA MANRNICRDR GAYTDFSCLL FAHLRTKPNP 

       250        260        270        280        290        300 
KIIEKIITEA VEIEKEYYSN SLPVEKFGMD LKSIHTYIEF VADGLLQGFG NEKYYNAVNP 

       310        320        330        340 
FEFMEDVATA GKTTFFEKKV SDYQKASDMS KSATPSKEIN FDDDF 

P49723 in FASTA format

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