CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003828
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L4-A 
Protein Synonyms/Alias
 L2; RP2; YL2 
Gene Name
 RPL4A 
Gene Synonyms/Alias
 RPL2; RPL2A; YBR031W; YBR0315 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
55QAYAVSEKAGHQTSAubiquitination[1, 2]
104GRMFAPTKTWRKWNVacetylation[3]
104GRMFAPTKTWRKWNVmethylation[4]
104GRMFAPTKTWRKWNVubiquitination[2]
112TWRKWNVKVNHNEKRacetylation[3]
144ARGHRVEKIPEIPLVacetylation[3]
144ARGHRVEKIPEIPLVubiquitination[1, 2]
161TDLESIQKTKEAVAAacetylation[3]
163LESIQKTKEAVAALKubiquitination[2]
170KEAVAALKAVGAHSDacetylation[3]
170KEAVAALKAVGAHSDubiquitination[2]
180GAHSDLLKVLKSKKLacetylation[3]
217AEDNGIVKALRNVPGacetylation[3]
217AEDNGIVKALRNVPGubiquitination[1, 2]
257WTEAAFTKLDQVWGSubiquitination[2]
271SETVASSKVGYTLPSubiquitination[1, 2]
308PAGQATQKRTHVLKKubiquitination[1, 2]
321KKNPLKNKQVLLRLNacetylation[3]
321KKNPLKNKQVLLRLNubiquitination[2]
332LRLNPYAKVFAAEKLacetylation[3]
332LRLNPYAKVFAAEKLubiquitination[2]
338AKVFAAEKLGSKKAEacetylation[3]
338AKVFAAEKLGSKKAEubiquitination[2]
343AEKLGSKKAEKTGTKacetylation[5]
360AVFTETLKHD*****acetylation[3]
Reference
 [1] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [4] Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications.
 Pang CN, Gasteiger E, Wilkins MR.
 BMC Genomics. 2010 Feb 5;11:92. [PMID: 20137074]
 [5] mChIP-KAT-MS, a method to map protein interactions and acetylation sites for lysine acetyltransferases.
 Mitchell L, Huard S, Cotrut M, Pourhanifeh-Lemeri R, Steunou AL, Hamza A, Lambert JP, Zhou H, Ning Z, Basu A, Côté J, Figeys DA, Baetz K.
 Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1641-50. [PMID: 23572591
Functional Description
 Participates in the regulation of the accumulation of its own mRNA. 
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 362 AA 
Protein Sequence
MSRPQVTVHS LTGEATANAL PLPAVFSAPI RPDIVHTVFT SVNKNKRQAY AVSEKAGHQT 60
SAESWGTGRA VARIPRVGGG GTGRSGQGAF GNMCRGGRMF APTKTWRKWN VKVNHNEKRY 120
ATASAIAATA VASLVLARGH RVEKIPEIPL VVSTDLESIQ KTKEAVAALK AVGAHSDLLK 180
VLKSKKLRAG KGKYRNRRWT QRRGPLVVYA EDNGIVKALR NVPGVETANV ASLNLLQLAP 240
GAHLGRFVIW TEAAFTKLDQ VWGSETVASS KVGYTLPSHI ISTSDVTRII NSSEIQSAIR 300
PAGQATQKRT HVLKKNPLKN KQVLLRLNPY AKVFAAEKLG SKKAEKTGTK PAAVFTETLK 360
HD 362 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; TAS:SGD.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; TAS:SGD.
 GO:0002181; P:cytoplasmic translation; TAS:SGD. 
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