CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005600
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L3 
Protein Synonyms/Alias
 J1 protein 
Gene Name
 Rpl3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
66EVDRPGSKVNKKEVVacetylation[1]
103PRGLRTFKTVFAEHIacetylation[2]
136AFTKYCKKWQDDTGKacetylation[3]
143KWQDDTGKKQLEKDFacetylation[1, 4]
148TGKKQLEKDFNSMKKacetylation[1]
229VTKGKGYKGVTSRWHacetylation[3]
229VTKGKGYKGVTSRWHsuccinylation[3]
283HRTEINKKIYKIGQGubiquitination[5]
286EINKKIYKIGQGYLIacetylation[2, 3]
286EINKKIYKIGQGYLIsuccinylation[3]
286EINKKIYKIGQGYLIubiquitination[5]
294IGQGYLIKDGKLIKNacetylation[2, 4]
294IGQGYLIKDGKLIKNubiquitination[5]
300IKDGKLIKNNASTDYubiquitination[5]
356KSLLVQTKRRALEKIacetylation[3]
356KSLLVQTKRRALEKIsuccinylation[3]
356KSLLVQTKRRALEKIubiquitination[5]
362TKRRALEKIDLKFIDacetylation[1, 2, 4]
366ALEKIDLKFIDTTSKacetylation[1, 2, 3, 4, 6]
366ALEKIDLKFIDTTSKsuccinylation[3]
366ALEKIDLKFIDTTSKubiquitination[5]
373KFIDTTSKFGHGRFQacetylation[2, 3]
393KAFMGPLKKDRIAKEacetylation[3]
Reference
 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 The L3 protein is a component of the large subunit of cytoplasmic ribosomes. 
Sequence Annotation
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 294 294 N6-acetyllysine (By similarity).
 MOD_RES 304 304 Phosphoserine (By similarity).
 MOD_RES 366 366 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 403 AA 
Protein Sequence
MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDASKP VHLTAFLGYK AGMTHIVREV 60
DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR TFKTVFAEHI SDECKRRFYK 120
NWHKSKKKAF TKYCKKWQDD TGKKQLEKDF NSMKKYCQVI RIIAHTQMRL LPLRQKKAHL 180
MEIQVNGGTV AEKLDWARER LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL 240
PRKTHRGLRK VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK 300
NNASTDYDLS DKSINPLGGF VHYGEVTNDF IMLKGCVVGT KKRVLTLRKS LLVQTKRRAL 360
EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE EGA 403 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IEA:Compara.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0071353; P:cellular response to interleukin-4; IDA:MGI.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR000597; Ribosomal_L3.
 IPR019926; Ribosomal_L3_CS.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00297; Ribosomal_L3 
SMART
  
PROSITE
 PS00474; RIBOSOMAL_L3 
PRINTS