CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041980
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L3 
Protein Synonyms/Alias
 Ribosomal protein L3, isoform CRA_e; Uncharacterized protein 
Gene Name
 RPL3 
Gene Synonyms/Alias
 ASC-1; hCG_2015191 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
260TDYDLSDKSINPLGGubiquitination[1, 2]
297KRVLTLRKSLLVQTKubiquitination[1, 3]
304KSLLVQTKRRALEKIubiquitination[3]
310TKRRALEKIDLKFIDacetylation[4, 5]
310TKRRALEKIDLKFIDubiquitination[3, 6]
314ALEKIDLKFIDTTSKacetylation[4, 7]
314ALEKIDLKFIDTTSKubiquitination[1, 2, 3, 6, 7, 8, 9]
321KFIDTTSKFGHGRFQacetylation[7]
321KFIDTTSKFGHGRFQubiquitination[1, 3, 6, 7]
333RFQTMEEKKAFMGPLubiquitination[1, 2]
334FQTMEEKKAFMGPLKubiquitination[3, 6]
341KAFMGPLKKDRIAKEubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [5] 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]
 [6] 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]
 [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]
 [8] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [9] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 351 AA 
Protein Sequence
MTHIVREVDR PGSKVNKKEV VEAVTIVETP PMVVVGIVGY VETPRGLRTF KTVFAEHISD 60
ECKRRFYKNW HKSKKKAFTK YCKKWQDEDG KKQLEKDFSS MKKYCQVIRV IAHTQMRLLP 120
LRQKKAHLME IQVNGGTVAE KLDWARERLE QQVPVNQVFG QDEMIDVIGV TKGKGYKGVT 180
SRWHTKKLPR KTHRGLRKVA CIGAWHPARV AFSVARAGQK GYHHRTEINK KIYKIGQGYL 240
IKDGKLIKNN ASTDYDLSDK SINPLGGFVH YGEVTNDFVM LKGCVVGTKK RVLTLRKSLL 300
VQTKRRALEK IDLKFIDTTS KFGHGRFQTM EEKKAFMGPL KKDRIAKEEG A 351 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005840; C:ribosome; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 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