CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009334
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein S3a 
Protein Synonyms/Alias
 v-fos transformation effector protein; Fte-1 
Gene Name
 RPS3A 
Gene Synonyms/Alias
 FTE1; MFTL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
19GGKKGAKKKVVDPFSubiquitination[1]
20GKKGAKKKVVDPFSKubiquitination[1]
27KVVDPFSKKDWYDVKacetylation[2]
27KVVDPFSKKDWYDVKubiquitination[1, 3, 4]
28VVDPFSKKDWYDVKAubiquitination[1]
34KKDWYDVKAPAMFNIacetylation[2]
34KKDWYDVKAPAMFNIubiquitination[1, 3, 4, 5, 6, 7, 8]
46FNIRNIGKTLVTRTQubiquitination[1, 3, 4, 5, 6, 7, 8]
56VTRTQGTKIASDGLKubiquitination[1, 3, 4]
63KIASDGLKGRVFEVSubiquitination[1, 4]
85EVAFRKFKLITEDVQubiquitination[1]
94ITEDVQGKNCLTNFHubiquitination[1, 5, 8]
109GMDLTRDKMCSMVKKubiquitination[1]
144LFCVGFTKKRNNQIRacetylation[2]
144LFCVGFTKKRNNQIRubiquitination[1]
145FCVGFTKKRNNQIRKubiquitination[1]
152KRNNQIRKTSYAQHQubiquitination[1, 3, 4]
166QQVRQIRKKMMEIMTubiquitination[1]
167QVRQIRKKMMEIMTRubiquitination[1, 5, 8]
182EVQTNDLKEVVNKLIubiquitination[1, 3, 4, 5, 8]
187DLKEVVNKLIPDSIGubiquitination[1, 5, 8]
195LIPDSIGKDIEKACQubiquitination[1]
199SIGKDIEKACQSIYPubiquitination[1]
227KPKFELGKLMELHGEubiquitination[1, 5, 8]
240GEGSSSGKATGDETGubiquitination[1, 3, 7]
249TGDETGAKVERADGYacetylation[2]
249TGDETGAKVERADGYsumoylation[9]
249TGDETGAKVERADGYubiquitination[1, 3, 8, 10]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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] Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.
 Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenschuh H, Thibault P.
 Mol Cell Proteomics. 2013 Jun 7;. [PMID: 23750026]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 
Functional Description
 May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity). 
Sequence Annotation
 MOD_RES 34 34 N6-acetyllysine.
 MOD_RES 249 249 N6-acetyllysine.
 MOD_RES 256 256 Phosphotyrosine.
 MOD_RES 263 263 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Differentiation; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 264 AA 
Protein Sequence
MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD 60
GLKGRVFEVS LADLQNDEVA FRKFKLITED VQGKNCLTNF HGMDLTRDKM CSMVKKWQTM 120
IEAHVDVKTT DGYLLRLFCV GFTKKRNNQI RKTSYAQHQQ VRQIRKKMME IMTREVQTND 180
LKEVVNKLIP DSIGKDIEKA CQSIYPLHDV FVRKVKMLKK PKFELGKLME LHGEGSSSGK 240
ATGDETGAKV ERADGYEPPV QESV 264 
Gene Ontology
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0003723; F:RNA binding; NAS:UniProtKB.
 GO:0003735; F:structural constituent of ribosome; IEA:HAMAP.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0097194; P:execution phase of apoptosis; IMP: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:UniProtKB.
 GO:0006415; P:translational termination; TAS:Reactome.
 GO:0019083; P:viral transcription; TAS:Reactome. 
Interpro
 IPR027500; Ribosomal_S1/3_euk.
 IPR001593; Ribosomal_S3Ae.
 IPR018281; Ribosomal_S3Ae_CS. 
Pfam
 PF01015; Ribosomal_S3Ae 
SMART
  
PROSITE
 PS01191; RIBOSOMAL_S3AE 
PRINTS