CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007972
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L29 
Protein Synonyms/Alias
 Cell surface heparin-binding protein HIP 
Gene Name
 RPL29 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MAKSKNHTTHNQmethylation[1, 2]
33SQRYESLKGVDPKFLacetylation[3, 4]
33SQRYESLKGVDPKFLubiquitination[5, 6]
38SLKGVDPKFLRNMRFubiquitination[4, 5, 7, 8]
63KMQANNAKAMSARAEubiquitination[4, 6, 7, 9]
73SARAEAIKALVKPKEubiquitination[4, 5, 8, 9]
82LVKPKEVKPKIPKGVacetylation[3]
103LAYIAHPKLGKRARAacetylation[10]
103LAYIAHPKLGKRARAubiquitination[5, 7, 8]
106IAHPKLGKRARARIAubiquitination[7]
130AKAKAKAKDQTKAQAubiquitination[7]
134AKAKDQTKAQAAAPAacetylation[10]
134AKAKDQTKAQAAAPAubiquitination[4, 6, 7, 9, 11]
149SVPAQAPKRTQAPTKubiquitination[4, 6, 7, 11]
Reference
 [1] Post-translational processing of rat ribosomal proteins. Ubiquitous methylation of Lys22 within the zinc-finger motif of RL40 (carboxy-terminal extension protein 52) and tissue-specific methylation of Lys4 in RL29.
 Williamson NA, Raliegh J, Morrice NA, Wettenhall RE.
 Eur J Biochem. 1997 Jun 15;246(3):786-93. [PMID: 9219540]
 [2] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] 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]
 [8] 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]
 [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] 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]
 [11] 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
Functional Description
  
Sequence Annotation
 MOD_RES 5 5 N6-methyllysine.
 MOD_RES 33 33 N6-acetyllysine.
 MOD_RES 142 142 Phosphoserine.
 CROSSLNK 56 56 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Heparin-binding; Isopeptide bond; Methylation; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 159 AA 
Protein Sequence
MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN KKGLKKMQAN 60
NAKAMSARAE AIKALVKPKE VKPKIPKGVS RKLDRLAYIA HPKLGKRARA RIAKGLRLCR 120
PKAKAKAKAK DQTKAQAAAP ASVPAQAPKR TQAPTKASE 159 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
 GO:0008201; F:heparin binding; TAS:ProtInc.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
 GO:0007566; P:embryo implantation; TAS:ProtInc.
 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
 IPR002673; Ribosomal_L29e. 
Pfam
 PF01779; Ribosomal_L29e 
SMART
  
PROSITE
  
PRINTS