CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009466
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein S13 
Protein Synonyms/Alias
  
Gene Name
 RPS13 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9GRMHAPGKGLSQSALubiquitination[1, 2, 3, 4]
27RSVPTWLKLTSDDVKacetylation[5]
27RSVPTWLKLTSDDVKubiquitination[1, 3, 4, 6, 7]
34KLTSDDVKEQIYKLAubiquitination[2, 3, 6, 7]
39DVKEQIYKLAKKGLTacetylation[5]
39DVKEQIYKLAKKGLTubiquitination[2, 3]
42EQIYKLAKKGLTPSQubiquitination[2]
43QIYKLAKKGLTPSQIubiquitination[1, 2, 3, 4, 6, 7, 8, 9, 10]
70VRFVTGNKILRILKSubiquitination[1, 2, 3, 4, 7]
76NKILRILKSKGLAPDubiquitination[6]
78ILRILKSKGLAPDLPubiquitination[1, 2, 3, 4, 6, 7, 10]
93EDLYHLIKKAVAVRKacetylation[5]
93EDLYHLIKKAVAVRKubiquitination[1, 3, 4, 6, 10]
94DLYHLIKKAVAVRKHubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [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] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [9] 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]
 [10] 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
Functional Description
  
Sequence Annotation
 MOD_RES 27 27 N6-acetyllysine.
 MOD_RES 38 38 Phosphotyrosine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 151 AA 
Protein Sequence
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV 60
AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES 120
RIHRLARYYK TKRVLPPNWK YESSTASALV A 151 
Gene Ontology
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0003729; F:mRNA binding; IDA:UniProtKB.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0033119; P:negative regulation of RNA splicing; 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
 IPR012606; Ribosomal_S13/S15_N.
 IPR000589; Ribosomal_S15.
 IPR023029; Ribosomal_S15P.
 IPR009068; S15_NS1_RNA-bd. 
Pfam
 PF08069; Ribosomal_S13_N
 PF00312; Ribosomal_S15 
SMART
  
PROSITE
 PS00362; RIBOSOMAL_S15 
PRINTS