CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-044567
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosomal protein L19 
Protein Synonyms/Alias
  
Gene Name
 RPL19 
Gene Synonyms/Alias
 hCG_31402 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
18SVLRCGKKKVWLDPNubiquitination[1, 2]
19VLRCGKKKVWLDPNEubiquitination[2, 3, 4, 5, 6]
41NSRQQIRKLIKDGLIubiquitination[2, 3, 6, 7]
44QQIRKLIKDGLIIRKubiquitination[1, 2, 3, 4, 5, 6, 7]
51KDGLIIRKPVTVHSRubiquitination[1, 5]
78GRHMGIGKRKGTANAacetylation[6]
90ANARMPEKVTWMRRMubiquitination[1, 2, 3, 4, 5, 6]
124MYHSLYLKVKGNVFKubiquitination[2, 5, 7]
126HSLYLKVKGNVFKNKubiquitination[2, 4, 5, 6]
131KVKGNVFKNKRILMEubiquitination[4]
142ILMEHIHKLKADKARubiquitination[2, 3, 4, 6]
144MEHIHKLKADKARKKubiquitination[2, 6]
150LKADKARKKLLADQAubiquitination[1, 2, 6, 8]
151KADKARKKLLADQAEubiquitination[1, 2, 3, 4, 6, 8]
178REERLQAKKEEIIKTacetylation[6, 9]
178REERLQAKKEEIIKTubiquitination[1, 2, 4, 5, 6]
179EERLQAKKEEIIKTLubiquitination[2, 3, 4, 5, 6]
184AKKEEIIKTLSKEEEacetylation[9]
184AKKEEIIKTLSKEEEubiquitination[1, 2, 3, 4, 5, 6]
188EIIKTLSKEEETKK*acetylation[6, 10]
188EIIKTLSKEEETKK*ubiquitination[4, 5]
193LSKEEETKK******ubiquitination[1, 4]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [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] 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]
 [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] 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]
 [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
 194 AA 
Protein Sequence
MLRLQKRLAS SVLRCGKKKV WLDPNETNEI ANANSRQQIR KLIKDGLIIR KPVTVHSRAR 60
CRKNTLARRK GRHMGIGKRK GTANARMPEK VTWMRRMRIL RRLLRRYRES KKIDRHMYHS 120
LYLKVKGNVF KNKRILMEHI HKLKADKARK KLLADQAEAR RSKTKEARKR REERLQAKKE 180
EIIKTLSKEE ETKK 194 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IEA:Compara.
 GO:0003735; F:structural constituent of ribosome; IEA:Compara.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR027547; Ribosomal_L19/L19e.
 IPR023638; Ribosomal_L19/L19e_CS.
 IPR000196; Ribosomal_L19/L19e_dom.
 IPR015972; Ribosomal_L19/L19e_dom1.
 IPR015974; Ribosomal_L19/L19e_dom3. 
Pfam
 PF01280; Ribosomal_L19e 
SMART
  
PROSITE
 PS00526; RIBOSOMAL_L19E 
PRINTS