CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004384
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein S2 
Protein Synonyms/Alias
 40S ribosomal protein S4; Protein LLRep3 
Gene Name
 RPS2 
Gene Synonyms/Alias
 RPS4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
54GRGARGGKAEDKEWMubiquitination[1, 2]
58RGGKAEDKEWMPVTKubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
65KEWMPVTKLGRLVKDubiquitination[1, 2, 3, 4, 6, 7, 8]
76LVKDMKIKSLEEIYLubiquitination[1, 2, 3, 4, 7, 8]
108SLKDEVLKIMPVQKQubiquitination[3, 4, 7, 8]
114LKIMPVQKQTRAGQRubiquitination[1, 3, 8]
145GLGVKCSKEVATAIRubiquitination[1]
173RRGYWGNKIGKPHTVubiquitination[1]
176YWGNKIGKPHTVPCKubiquitination[1]
211IVSAPVPKKLLMMAGubiquitination[1, 6]
212VSAPVPKKLLMMAGIubiquitination[1]
238ATLGNFAKATFDAISubiquitination[1, 6]
246ATFDAISKTYSYLTPubiquitination[1, 2, 3, 4, 8, 9]
257YLTPDLWKETVFTKSubiquitination[1, 2, 3, 4, 7, 8]
263WKETVFTKSPYQEFTacetylation[10]
263WKETVFTKSPYQEFTubiquitination[1, 2, 3, 4, 6, 7, 8]
275EFTDHLVKTHTRVSVacetylation[10]
275EFTDHLVKTHTRVSVubiquitination[1, 2, 3, 4, 6, 7, 8]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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] 
Functional Description
  
Sequence Annotation
 DOMAIN 102 165 S5 DRBM.
 MOD_RES 77 77 Phosphoserine (By similarity).
 MOD_RES 82 82 Phosphotyrosine (By similarity).
 MOD_RES 85 85 Phosphoserine (By similarity).
 MOD_RES 133 133 Phosphotyrosine (By similarity).
 MOD_RES 263 263 N6-acetyllysine.
 MOD_RES 264 264 Phosphoserine.
 MOD_RES 275 275 N6-acetyllysine.
 MOD_RES 281 281 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Citrullination; Complete proteome; Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 293 AA 
Protein Sequence
MADDAGAAGG PGGPGGPGMG NRGGFRGGFG SGIRGRGRGR GRGRGRGRGA RGGKAEDKEW 60
MPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA SLKDEVLKIM PVQKQTRAGQ 120
RTRFKAFVAI GDYNGHVGLG VKCSKEVATA IRGAIILAKL SIVPVRRGYW GNKIGKPHTV 180
PCKVTGRCGS VLVRLIPAPR GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT 240
FDAISKTYSY LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT 293 
Gene Ontology
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 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
 IPR014720; dsRNA-bd-like_dom.
 IPR000851; Ribosomal_S5.
 IPR005324; Ribosomal_S5_C.
 IPR020568; Ribosomal_S5_D2-typ_fold.
 IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
 IPR005711; Ribosomal_S5_euk/arc.
 IPR013810; Ribosomal_S5_N.
 IPR018192; Ribosomal_S5_N_CS. 
Pfam
 PF00333; Ribosomal_S5
 PF03719; Ribosomal_S5_C 
SMART
  
PROSITE
 PS00585; RIBOSOMAL_S5
 PS50881; S5_DSRBD 
PRINTS