CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009459
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein S18 
Protein Synonyms/Alias
 Ke-3; Ke3 
Gene Name
 RPS18 
Gene Synonyms/Alias
 D6S218E 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MSLVIPEKFQHILRVacetylation[1, 2]
8MSLVIPEKFQHILRVubiquitination[3, 4, 5, 6, 7]
25TNIDGRRKIAFAITAubiquitination[5]
34AFAITAIKGVGRRYAubiquitination[4, 5, 8, 9]
47YAHVVLRKADIDLTKubiquitination[5, 9, 10]
54KADIDLTKRAGELTEubiquitination[5, 7, 8, 9, 10, 11]
78MQNPRQYKIPDWFLNacetylation[1]
78MQNPRQYKIPDWFLNubiquitination[3, 4, 5, 6, 9, 10, 11, 12]
94QKDVKDGKYSQVLANacetylation[1, 13]
94QKDVKDGKYSQVLANubiquitination[3, 4, 5, 6, 9, 10, 11, 12]
106LANGLDNKLREDLERacetylation[1]
106LANGLDNKLREDLERubiquitination[3, 5, 6, 9, 10]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [10] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [11] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [12] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [13] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
Functional Description
 Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity). 
Sequence Annotation
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 94 94 N6-acetyllysine.
 MOD_RES 106 106 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Reference proteome; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 152 AA 
Protein Sequence
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT 60
EDEVERVITI MQNPRQYKIP DWFLNRQKDV KDGKYSQVLA NGLDNKLRED LERLKKIRAH 120
RGLRHFWGLR VRGQHTKTTG RRGRTVGVSK KK 152 
Gene Ontology
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
 GO:0003735; F:structural constituent of ribosome; IBA:RefGenome.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0042254; P:ribosome biogenesis; IBA:RefGenome.
 GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
 GO:0006414; P:translational elongation; TAS:Reactome.
 GO:0006413; P:translational initiation; TAS:Reactome.
 GO:0006415; P:translational termination; TAS:Reactome.
 GO:0019083; P:viral transcription; TAS:Reactome. 
Interpro
 IPR027437; 30s_Rbsml_prot_S13_C.
 IPR001892; Ribosomal_S13.
 IPR010979; Ribosomal_S13-like_H2TH.
 IPR018269; Ribosomal_S13_CS. 
Pfam
 PF00416; Ribosomal_S13 
SMART
  
PROSITE
 PS00646; RIBOSOMAL_S13_1
 PS50159; RIBOSOMAL_S13_2 
PRINTS