CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007831
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L5 
Protein Synonyms/Alias
  
Gene Name
 RPL5 
Gene Synonyms/Alias
 MSTP030 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MGFVKVVKNKAYacetylation[1, 2]
5***MGFVKVVKNKAYubiquitination[3, 4, 5]
10FVKVVKNKAYFKRYQubiquitination[6, 7]
14VKNKAYFKRYQVKFRubiquitination[6, 7]
19YFKRYQVKFRRRREGubiquitination[4, 6]
27FRRRREGKTDYYARKacetylation[5]
27FRRRREGKTDYYARKubiquitination[3, 4, 5, 6, 7, 8, 9]
41KRLVIQDKNKYNTPKacetylation[5, 10]
41KRLVIQDKNKYNTPKubiquitination[4, 5, 6]
43LVIQDKNKYNTPKYRacetylation[5, 10]
43LVIQDKNKYNTPKYRubiquitination[4, 5, 6]
48KNKYNTPKYRMIVRVacetylation[1, 5]
48KNKYNTPKYRMIVRVubiquitination[4, 5]
85AYAHELPKYGVKVGLubiquitination[7]
89ELPKYGVKVGLTNYAubiquitination[4, 7]
158ARTTTGNKVFGALKGubiquitination[4]
164NKVFGALKGAVDGGLubiquitination[4, 5, 6, 7, 9, 11]
178LSIPHSTKRFPGYDSubiquitination[4, 5, 6, 7, 12]
188PGYDSESKEFNAEVHubiquitination[4, 5, 6, 7, 9]
197FNAEVHRKHIMGQNVubiquitination[4, 5, 11]
220EEDEDAYKKQFSQYIacetylation[13]
220EEDEDAYKKQFSQYIubiquitination[4, 5, 6, 7, 9]
221EDEDAYKKQFSQYIKubiquitination[4, 5, 6, 7, 11]
228KQFSQYIKNSVTPDMubiquitination[6]
241DMMEEMYKKAHAAIRacetylation[13]
242MMEEMYKKAHAAIREubiquitination[4]
255RENPVYEKKPKKEVKubiquitination[4, 5]
256ENPVYEKKPKKEVKKubiquitination[4, 5]
258PVYEKKPKKEVKKKRubiquitination[4]
270KKRWNRPKMSLAQKKubiquitination[4, 11]
276PKMSLAQKKDRVAQKubiquitination[9]
284KDRVAQKKASFLRAQubiquitination[4]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [11] 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]
 [12] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [13] 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
 Required for rRNA maturation and formation of the 60S ribosomal subunits. This protein binds 5S RNA. 
Sequence Annotation
 MOD_RES 5 5 N6-acetyllysine.
 MOD_RES 48 48 N6-acetyllysine.
 MOD_RES 272 272 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Diamond-Blackfan anemia; Direct protein sequencing; Disease mutation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 297 AA 
Protein Sequence
MGFVKVVKNK AYFKRYQVKF RRRREGKTDY YARKRLVIQD KNKYNTPKYR MIVRVTNRDI 60
ICQIAYARIE GDMIVCAAYA HELPKYGVKV GLTNYAAAYC TGLLLARRLL NRFGMDKIYE 120
GQVEVTGDEY NVESIDGQPG AFTCYLDAGL ARTTTGNKVF GALKGAVDGG LSIPHSTKRF 180
PGYDSESKEF NAEVHRKHIM GQNVADYMRY LMEEDEDAYK KQFSQYIKNS VTPDMMEEMY 240
KKAHAAIREN PVYEKKPKKE VKKKRWNRPK MSLAQKKDRV AQKKASFLRA QERAAES 297 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0008097; F:5S rRNA binding; IEA:InterPro.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
 GO:0006364; P:rRNA processing; IMP:UniProtKB.
 GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
 GO:0006414; P:translational elongation; TAS:Reactome.
 GO:0006413; P:translational initiation; TAS:Reactome.
 GO:0006415; P:translational termination; TAS:Reactome.
 GO:0019083; P:viral transcription; TAS:Reactome. 
Interpro
 IPR005485; Rbsml_L5_euk/L18_arc.
 IPR025607; Rbsml_L5e/L18P_C.
 IPR005484; Ribosomal_L18/L5. 
Pfam
 PF14204; Ribosomal_L18_c
 PF00861; Ribosomal_L18p 
SMART
  
PROSITE
  
PRINTS
 PR00058; RIBOSOMALL5.