CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-043248
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L4 
Protein Synonyms/Alias
 Ribosomal protein L4, isoform CRA_a 
Gene Name
 RPL4 
Gene Synonyms/Alias
 hCG_2004318 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
12GRMFAPTKTWRRWHRacetylation[1]
12GRMFAPTKTWRRWHRubiquitination[2, 3, 4, 5, 6, 7, 8]
46LPALVMSKGHRIEEVubiquitination[3, 4, 5, 6, 8]
63LPLVVEDKVEGYKKTubiquitination[3, 4, 5, 6, 7, 8, 9]
68EDKVEGYKKTKEAVLubiquitination[3, 4, 6, 7, 9]
69DKVEGYKKTKEAVLLubiquitination[4, 6]
71VEGYKKTKEAVLLLKubiquitination[3, 4, 5, 6, 7, 8, 9]
78KEAVLLLKKLKAWNDubiquitination[4, 5, 6, 7, 8, 9]
79EAVLLLKKLKAWNDIubiquitination[4, 6, 8]
81VLLLKKLKAWNDIKKubiquitination[3, 4, 6, 8, 9]
87LKAWNDIKKVYASQRubiquitination[3, 4, 6, 8, 9]
88KAWNDIKKVYASQRMubiquitination[4, 6]
125NEDNGIIKAFRNIPGubiquitination[2, 3, 4, 6, 8, 9]
140ITLLNVSKLNILKLAubiquitination[2, 3, 4, 6, 7, 8]
145VSKLNILKLAPGGHVubiquitination[3, 4, 6, 8, 9]
165WTESAFRKLDELYGTubiquitination[3, 6, 8, 9]
175ELYGTWRKAASLKSNubiquitination[4, 6, 8]
180WRKAASLKSNYNLPMubiquitination[2, 3, 4, 6, 7, 8, 9]
189NYNLPMHKMINTDLSubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
200TDLSRILKSPEIQRAubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
221KIHRRVLKKNPLKNLubiquitination[6]
222IHRRVLKKNPLKNLRubiquitination[4]
226VLKKNPLKNLRIMLKubiquitination[3, 4, 6, 7, 8]
233KNLRIMLKLNPYAKTubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
239LKLNPYAKTMRRNTIubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
259NHKLRVDKAAAAAAAubiquitination[2, 3, 4, 5, 6, 7, 8, 9]
270AAAALQAKSDEKAAVacetylation[10]
270AAAALQAKSDEKAAVubiquitination[4, 5, 6, 7, 8, 9]
274LQAKSDEKAAVAGKKacetylation[8]
274LQAKSDEKAAVAGKKubiquitination[4, 5, 7, 8, 9]
280EKAAVAGKKPVVGKKubiquitination[4, 6, 8]
Reference
 [1] 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]
 [2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 333 AA 
Protein Sequence
MCRGGRMFAP TKTWRRWHRR VNTTQKRYAI CSALAASALP ALVMSKGHRI EEVPELPLVV 60
EDKVEGYKKT KEAVLLLKKL KAWNDIKKVY ASQRMRAGKG KMRNRRRIQR RGPCIIYNED 120
NGIIKAFRNI PGITLLNVSK LNILKLAPGG HVGRFCIWTE SAFRKLDELY GTWRKAASLK 180
SNYNLPMHKM INTDLSRILK SPEIQRALRA PRKKIHRRVL KKNPLKNLRI MLKLNPYAKT 240
MRRNTILRQA RNHKLRVDKA AAAAAALQAK SDEKAAVAGK KPVVGKKGKK AAVGVKKQKK 300
PLVGKKAAAT KKPAPEKKPA EKKPTTEEKK PAA 333 
Gene Ontology
 GO:0005840; C:ribosome; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR025755; Ribos_L4_C_dom.
 IPR002136; Ribosomal_L4/L1e.
 IPR013000; Ribosomal_L4/L1e_euk/arc_CS.
 IPR023574; Ribosomal_L4_dom. 
Pfam
 PF14374; Ribos_L4_asso_C
 PF00573; Ribosomal_L4 
SMART
  
PROSITE
 PS00939; RIBOSOMAL_L1E 
PRINTS