CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002841
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonucleoside-diphosphate reductase small chain 1 
Protein Synonyms/Alias
 Ribonucleotide reductase R2 subunit 1; Ribonucleotide reductase small subunit 1 
Gene Name
 RNR2 
Gene Synonyms/Alias
 CRT6; YJL026W; J1271 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
8MPKETPSKAAADALSacetylation[1]
20ALSDLEIKDSKSNLNacetylation[1]
20ALSDLEIKDSKSNLNubiquitination[2]
28DSKSNLNKELETLREacetylation[1]
74HKLKEMEKEEPLLNEacetylation[1]
92RTVLFPIKYHEIWQAubiquitination[2]
101HEIWQAYKRAEASFWubiquitination[2]
290LFAHLKNKPDPAIVEubiquitination[2]
371GKTNFFEKRVSDYQKubiquitination[2]
378KRVSDYQKAGVMSKSubiquitination[2]
384QKAGVMSKSTKQEAGubiquitination[2]
387GVMSKSTKQEAGAFTubiquitination[2]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301
Functional Description
 Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR2 provides the diiron-tyrosyl radical center. 
Sequence Annotation
 ACT_SITE 183 183
 METAL 145 145 Iron 1.
 METAL 176 176 Iron 1.
 METAL 176 176 Iron 2.
 METAL 179 179 Iron 1.
 METAL 239 239 Iron 2.
 METAL 273 273 Iron 2.
 METAL 276 276 Iron 2.
 MOD_RES 15 15 Phosphoserine.
 MOD_RES 24 24 Phosphoserine.
 MOD_RES 41 41 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; DNA replication; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 399 AA 
Protein Sequence
MPKETPSKAA ADALSDLEIK DSKSNLNKEL ETLREENRVK SDMLKEKLSK DAENHKAYLK 60
SHQVHRHKLK EMEKEEPLLN EDKERTVLFP IKYHEIWQAY KRAEASFWTA EEIDLSKDIH 120
DWNNRMNENE RFFISRVLAF FAASDGIVNE NLVENFSTEV QIPEAKSFYG FQIMIENIHS 180
ETYSLLIDTY IKDPKESEFL FNAIHTIPEI GEKAEWALRW IQDADALFGE RLVAFASIEG 240
VFFSGSFASI FWLKKRGMMP GLTFSNELIC RDEGLHTDFA CLLFAHLKNK PDPAIVEKIV 300
TEAVEIEQRY FLDALPVALL GMNADLMNQY VEFVADRLLV AFGNKKYYKV ENPFDFMENI 360
SLAGKTNFFE KRVSDYQKAG VMSKSTKQEA GAFTFNEDF 399 
Gene Ontology
 GO:0005634; C:nucleus; IDA:SGD.
 GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:SGD.
 GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:SGD.
 GO:0046914; F:transition metal ion binding; IEA:InterPro.
 GO:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:InterPro.
 GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:SGD.
 GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway. 
Interpro
 IPR009078; Ferritin-like_SF.
 IPR012348; RNR-rel.
 IPR000358; RNR_small. 
Pfam
 PF00268; Ribonuc_red_sm 
SMART
  
PROSITE
 PS00368; RIBORED_SMALL 
PRINTS