CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010523
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L24 
Protein Synonyms/Alias
 60S ribosomal protein L30 
Gene Name
 RPL24 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
2******MKVELCSFSubiquitination[1, 2, 3, 4]
12LCSFSGYKIYPGHGRubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
27RYARTDGKVFQFLNAacetylation[11]
27RYARTDGKVFQFLNAubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
35VFQFLNAKCESAFLSubiquitination[1, 2, 3, 4, 7, 9]
43CESAFLSKRNPRQINubiquitination[1, 2, 3, 4, 7, 9, 10]
61LYRRKHKKGQSEEIQubiquitination[7]
69GQSEEIQKKRTRRAVubiquitination[7, 10]
77KRTRRAVKFQRAITGacetylation[11]
77KRTRRAVKFQRAITGubiquitination[3, 7, 8, 9, 10]
93SLADIMAKRNQKPEVacetylation[11]
93SLADIMAKRNQKPEVubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
97IMAKRNQKPEVRKAQubiquitination[7, 10]
113EQAIRAAKEAKKAKQacetylation[12]
116IRAAKEAKKAKQASKacetylation[12]
117RAAKEAKKAKQASKKacetylation[12]
119AKEAKKAKQASKKTAacetylation[12]
124KAKQASKKTAMAAAKubiquitination[10]
131KTAMAAAKAPTKAAPubiquitination[2, 3, 7, 9, 10, 13, 14]
135AAAKAPTKAAPKQKIubiquitination[10]
144APKQKIVKPVKVSAPubiquitination[3, 14]
147QKIVKPVKVSAPRVGubiquitination[3, 13, 14]
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] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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] 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]
 [5] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [6] 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]
 [7] 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]
 [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] 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]
 [10] 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]
 [11] 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]
 [12] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [13] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [14] 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
  
Sequence Annotation
 MOD_RES 27 27 N6-acetyllysine.
 MOD_RES 77 77 N6-acetyllysine.
 MOD_RES 83 83 Phosphothreonine.
 MOD_RES 86 86 Phosphoserine.
 MOD_RES 93 93 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 157 AA 
Protein Sequence
MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN WTVLYRRKHK 60
KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV RKAQREQAIR AAKEAKKAKQ 120
ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA PRVGGKR 157 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 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: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
 IPR023442; Ribosomal_L24e_CS.
 IPR023441; Ribosomal_L24e_dom.
 IPR000988; Ribosomal_L24e_rel.
 IPR011017; TRASH_dom. 
Pfam
 PF01246; Ribosomal_L24e 
SMART
 SM00746; TRASH 
PROSITE
 PS01073; RIBOSOMAL_L24E 
PRINTS