CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009606
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L30 
Protein Synonyms/Alias
  
Gene Name
 RPL30 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MVAAKKTKKSLESINubiquitination[1]
9VAAKKTKKSLESINSubiquitination[1, 2, 3, 4, 5]
23SRLQLVMKSGKYVLGubiquitination[1, 3, 4, 5]
26QLVMKSGKYVLGYKQacetylation[6]
26QLVMKSGKYVLGYKQubiquitination[1, 2, 3, 4, 5, 7]
32GKYVLGYKQTLKMIRubiquitination[1, 2, 3, 4, 5]
36LGYKQTLKMIRQGKAubiquitination[1, 3]
44MIRQGKAKLVILANNubiquitination[1, 2, 4]
57NNCPALRKSEIEYYAubiquitination[1, 2]
68EYYAMLAKTGVHHYSubiquitination[1, 2]
87ELGTACGKYYRVCTLubiquitination[8]
115MPEQTGEK*******ubiquitination[3, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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] 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 10 10 Phosphoserine.
 MOD_RES 26 26 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 115 AA 
Protein Sequence
MVAAKKTKKS LESINSRLQL VMKSGKYVLG YKQTLKMIRQ GKAKLVILAN NCPALRKSEI 60
EYYAMLAKTG VHHYSGNNIE LGTACGKYYR VCTLAIIDPG DSDIIRSMPE QTGEK 115 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0003723; F:RNA binding; TAS:UniProtKB.
 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
 IPR000231; Ribosomal_L30e.
 IPR022991; Ribosomal_L30e_CS.
 IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45. 
Pfam
 PF01248; Ribosomal_L7Ae 
SMART
  
PROSITE
 PS00709; RIBOSOMAL_L30E_1
 PS00993; RIBOSOMAL_L30E_2 
PRINTS