CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003742
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 60S ribosomal protein L2-A 
Protein Synonyms/Alias
 L5; RP8; YL6 
Gene Name
 RPL2A 
Gene Synonyms/Alias
 RPL5B; YFR031C-A; YFR031BC 
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
10RVIRNQRKGAGSIFTubiquitination[1]
46GYIRGIVKQIVHDSGacetylation[2]
46GYIRGIVKQIVHDSGubiquitination[1, 3]
60GRGAPLAKVVFRDPYacetylation[2]
68VVFRDPYKYRLREEIacetylation[2]
68VVFRDPYKYRLREEIubiquitination[3]
93QFIYAGKKASLNVGNubiquitination[1, 3]
119IVSNVEEKPGDRGALacetylation[2]
119IVSNVEEKPGDRGALubiquitination[1, 3]
145GHNPDENKTRVRLPSacetylation[2]
145GHNPDENKTRVRLPSubiquitination[1, 3]
155VRLPSGAKKVISSDAacetylation[4]
156RLPSGAKKVISSDARubiquitination[1]
177AGGGRVDKPLLKAGRubiquitination[1]
181RVDKPLLKAGRAFHKubiquitination[1, 3]
198LKRNSWPKTRGVAMNubiquitination[1]
221GNHQHIGKASTISRGacetylation[2]
221GNHQHIGKASTISRGubiquitination[1]
234RGAVSGQKAGLIAARubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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
  
Sequence Annotation
 MOD_RES 95 95 Phosphoserine.
 MOD_RES 159 159 Phosphoserine.
 MOD_RES 160 160 Phosphoserine.
 MOD_RES 249 249 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 254 AA 
Protein Sequence
MGRVIRNQRK GAGSIFTSHT RLRQGAAKLR TLDYAERHGY IRGIVKQIVH DSGRGAPLAK 60
VVFRDPYKYR LREEIFIANE GVHTGQFIYA GKKASLNVGN VLPLGSVPEG TIVSNVEEKP 120
GDRGALARAS GNYVIIIGHN PDENKTRVRL PSGAKKVISS DARGVIGVIA GGGRVDKPLL 180
KAGRAFHKYR LKRNSWPKTR GVAMNPVDHP HGGGNHQHIG KASTISRGAV SGQKAGLIAA 240
RRTGLLRGSQ KTQD 254 
Gene Ontology
 GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
 GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; IDA:SGD.
 GO:0002181; P:cytoplasmic translation; IDA:SGD. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR022666; Rbsml_prot_L2_RNA-bd_dom.
 IPR014722; Rib_L2_dom2.
 IPR002171; Ribosomal_L2.
 IPR022669; Ribosomal_L2_C.
 IPR022671; Ribosomal_L2_CS.
 IPR014726; Ribosomal_L2_dom3.
 IPR008991; Translation_prot_SH3-like. 
Pfam
 PF00181; Ribosomal_L2
 PF03947; Ribosomal_L2_C 
SMART
  
PROSITE
 PS00467; RIBOSOMAL_L2 
PRINTS