CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005977
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribonucleoside-diphosphate reductase subunit M2 
Protein Synonyms/Alias
 Ribonucleotide reductase small chain; Ribonucleotide reductase small subunit 
Gene Name
 RRM2 
Gene Synonyms/Alias
 RR2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23QLQLSPLKGLSLVDKubiquitination[1, 2, 3, 4, 5, 6, 7]
30KGLSLVDKENTPPALubiquitination[2, 3, 4, 5, 7]
46GTRVLASKTARRIFQubiquitination[2, 4, 5]
59FQEPTEPKTKAAAPGubiquitination[4, 7]
61EPTEPKTKAAAPGVEubiquitination[4, 5]
95HDIWQMYKKAEASFWubiquitination[1, 4, 5, 6]
96DIWQMYKKAEASFWTubiquitination[4]
120IQHWESLKPEERYFIubiquitination[5]
205ETMPCVKKKADWALRubiquitination[4]
206TMPCVKKKADWALRWubiquitination[4]
217ALRWIGDKEATYGERubiquitination[4]
278DFACLMFKHLVHKPSubiquitination[4]
311LTEALPVKLIGMNCTubiquitination[4]
358ENISLEGKTNFFEKRubiquitination[3]
364GKTNFFEKRVGEYQRubiquitination[3, 4, 5]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling. 
Sequence Annotation
 ACT_SITE 176 176 By similarity.
 METAL 138 138 Iron 1 (By similarity).
 METAL 169 169 Iron 1 (By similarity).
 METAL 169 169 Iron 2 (By similarity).
 METAL 172 172 Iron 1 (By similarity).
 METAL 232 232 Iron 2 (By similarity).
 METAL 266 266 Iron 2 (By similarity).
 METAL 269 269 Iron 2 (By similarity).
 MOD_RES 20 20 Phosphoserine.
 MOD_RES 33 33 Phosphothreonine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; DNA replication; Iron; Metal-binding; Oxidoreductase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 389 AA 
Protein Sequence
MLSLRVPLAP ITDPQQLQLS PLKGLSLVDK ENTPPALSGT RVLASKTARR IFQEPTEPKT 60
KAAAPGVEDE PLLRENPRRF VIFPIEYHDI WQMYKKAEAS FWTAEEVDLS KDIQHWESLK 120
PEERYFISHV LAFFAASDGI VNENLVERFS QEVQITEARC FYGFQIAMEN IHSEMYSLLI 180
DTYIKDPKER EFLFNAIETM PCVKKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF 240
ASIFWLKKRG LMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRIE 300
QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM ENISLEGKTN 360
FFEKRVGEYQ RMGVMSSPTE NSFTLDADF 389 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:UniProtKB.
 GO:0046914; F:transition metal ion binding; IEA:InterPro.
 GO:0009186; P:deoxyribonucleoside diphosphate metabolic process; IEA:InterPro.
 GO:0009263; P:deoxyribonucleotide biosynthetic process; ISS:UniProtKB.
 GO:0006260; P:DNA replication; NAS:UniProtKB.
 GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
 GO:0051290; P:protein heterotetramerization; IEA:Compara.
 GO:0000083; P:regulation of transcription involved in G1/S phase of mitotic cell cycle; TAS:Reactome. 
Interpro
 IPR009078; Ferritin-like_SF.
 IPR012348; RNR-rel.
 IPR000358; RNR_small. 
Pfam
 PF00268; Ribonuc_red_sm 
SMART
  
PROSITE
 PS00368; RIBORED_SMALL 
PRINTS