CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009616
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein S3 
Protein Synonyms/Alias
  
Gene Name
 Rps3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
62TQNVLGEKGRRIRELacetylation[1]
62TQNVLGEKGRRIRELubiquitination[2]
75ELTAVVQKRFGFPEGubiquitination[2]
108QAESLRYKLLGGLAVacetylation[1]
108QAESLRYKLLGGLAVubiquitination[2]
187GVLGIKVKIMLPWDPacetylation[3]
197LPWDPSGKIGPKKPLacetylation[1, 3]
197LPWDPSGKIGPKKPLubiquitination[2]
201PSGKIGPKKPLPDHVphosphoglycerylation[4]
201PSGKIGPKKPLPDHVubiquitination[2]
202SGKIGPKKPLPDHVSubiquitination[2]
214HVSIVEPKDEILPTTubiquitination[2]
Reference
 [1] 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]
 [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]
 [4] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 
Functional Description
  
Sequence Annotation
 DOMAIN 21 92 KH type-2.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 62 62 N6-acetyllysine (By similarity).
 MOD_RES 221 221 Phosphothreonine.
 MOD_RES 224 224 Phosphoserine (By similarity).
 MOD_RES 242 242 Phosphothreonine (By similarity).
 CROSSLNK 90 90 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 202 202 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Isopeptide bond; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 243 AA 
Protein Sequence
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG 60
EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY 120
GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG 180
VLGIKVKIML PWDPSGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV 240
PTA 243 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
 GO:0015935; C:small ribosomal subunit; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0006412; P:translation; IEA:InterPro. 
Interpro
 IPR004087; KH_dom.
 IPR015946; KH_dom-like_a/b.
 IPR004044; KH_dom_type_2.
 IPR009019; KH_prok-type.
 IPR001351; Ribosomal_S3_C.
 IPR018280; Ribosomal_S3_CS.
 IPR005703; Ribosomal_S3_euk/arc. 
Pfam
 PF07650; KH_2
 PF00189; Ribosomal_S3_C 
SMART
 SM00322; KH 
PROSITE
 PS50823; KH_TYPE_2
 PS00548; RIBOSOMAL_S3 
PRINTS