CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009587
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein S24 
Protein Synonyms/Alias
  
Gene Name
 Rps24 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
21TNRLLQRKQMVIDVLubiquitination[1]
37PGKATVPKTEIREKLacetylation[2, 3, 4]
37PGKATVPKTEIREKLubiquitination[1]
68RTHFGGGKTTGFGMIacetylation[5]
83YDSLDYAKKNEPKHRacetylation[4, 5, 6]
83YDSLDYAKKNEPKHRubiquitination[1, 7]
84DSLDYAKKNEPKHRLubiquitination[7]
88YAKKNEPKHRLARHGubiquitination[7]
122KKVRGTAKANVGAGKacetylation[8]
122KKVRGTAKANVGAGKsuccinylation[8]
Reference
 [1] 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]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
 [8] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337
Functional Description
 Required for processing of pre-rRNA and maturation of 40S ribosomal subunits (By similarity). 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 9 9 Phosphothreonine (By similarity).
 MOD_RES 81 81 Phosphotyrosine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 133 AA 
Protein Sequence
MNDTVTIRTR KFMTNRLLQR KQMVIDVLHP GKATVPKTEI REKLAKMYKT TPDVIFVFGF 60
RTHFGGGKTT GFGMIYDSLD YAKKNEPKHR LARHGLYEKK KTSRKQRKER KNRMKKVRGT 120
AKANVGAGKK PKE 133 
Gene Ontology
 GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
 GO:0005730; C:nucleolus; IBA:RefGenome.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003735; F:structural constituent of ribosome; ISO:MGI.
 GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:RefGenome.
 GO:0006414; P:translational elongation; IBA:RefGenome. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR012678; Ribosomal_L23/L15e_core_dom.
 IPR001976; Ribosomal_S24e.
 IPR018098; Ribosomal_S24e_CS. 
Pfam
 PF01282; Ribosomal_S24e 
SMART
  
PROSITE
 PS00529; RIBOSOMAL_S24E 
PRINTS