CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-034055
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 MCG49189 
Protein Synonyms/Alias
 Uncharacterized protein 
Gene Name
 Rpl12-ps1 
Gene Synonyms/Alias
 mCG_49189 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
40GPLGLSPKKVGEDIAacetylation[1]
54AKATGDWKGLRITVKacetylation[1]
61KGLRITVKLTIQNRQubiquitination[2]
83SASALIIKALKEPPRacetylation[3]
83SASALIIKALKEPPRubiquitination[2]
Reference
 [1] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 165 AA 
Protein Sequence
MPPKFAPNEI KIVYLRCIGE EVGATSALTP KIGPLGLSPK KVGEDIAKAT GDWKGLRITV 60
KLTIQNRQAQ IEVVPSASAL IIKALKEPPR DRKKQKNIKH SGNITFDEII NIARQMRHRS 120
LARELSGTIK EILGTAQSVG CNVDGHHPHD IIDDINSGAV ECPAS 165 
Gene Ontology
 GO:0005840; C:ribosome; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR000911; Ribosomal_L11.
 IPR020783; Ribosomal_L11_C.
 IPR020785; Ribosomal_L11_CS.
 IPR020784; Ribosomal_L11_N. 
Pfam
 PF00298; Ribosomal_L11
 PF03946; Ribosomal_L11_N 
SMART
 SM00649; RL11 
PROSITE
 PS00359; RIBOSOMAL_L11 
PRINTS