CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009418
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 40S ribosomal protein S7 
Protein Synonyms/Alias
  
Gene Name
 RPS7 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
10SSSAKIVKPNGEKPDubiquitination[1, 2, 3]
15IVKPNGEKPDEFESGubiquitination[1, 2, 3]
37LEMNSDLKAQLRELNubiquitination[1, 4]
49ELNITAAKEIEVGGGubiquitination[1, 3, 4, 5, 6, 7, 8]
58IEVGGGRKAIIIFVPubiquitination[3]
70FVPVPQLKSFQKIQVubiquitination[2, 3, 4, 7, 8, 9]
74PQLKSFQKIQVRLVRacetylation[10]
74PQLKSFQKIQVRLVRubiquitination[1, 2, 3, 4, 7, 8, 9, 11]
85RLVRELEKKFSGKHVubiquitination[2, 3, 4]
86LVRELEKKFSGKHVVubiquitination[3]
90LEKKFSGKHVVFIAQubiquitination[1, 2, 3]
142FPSEIVGKRIRVKLDubiquitination[1, 2, 3, 4, 5, 9]
147VGKRIRVKLDGSRLIubiquitination[3]
155LDGSRLIKVHLDKAQubiquitination[2, 3, 7, 8, 11]
160LIKVHLDKAQQNNVEubiquitination[1, 3, 11]
169QQNNVEHKVETFSGVacetylation[10]
169QQNNVEHKVETFSGVubiquitination[3, 12, 13]
178ETFSGVYKKLTGKDVubiquitination[1, 2, 3, 13]
179TFSGVYKKLTGKDVNubiquitination[3, 13]
183VYKKLTGKDVNFEFPubiquitination[1, 2, 3, 4, 7, 8, 9, 12, 13]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [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]
 [11] 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]
 [12] 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]
 [13] 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
Functional Description
 Required for rRNA maturation. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 74 74 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Cytoskeleton; Diamond-Blackfan anemia; Direct protein sequencing; Reference proteome; Ribonucleoprotein; Ribosomal protein. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 194 AA 
Protein Sequence
MFSSSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGGRKAI 60
IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRT KNKQKRPRSR 120
TLTAVHDAIL EDLVFPSEIV GKRIRVKLDG SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL 180
TGKDVNFEFP EFQL 194 
Gene Ontology
 GO:0030686; C:90S preribosome; IBA:RefGenome.
 GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
 GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0032040; C:small-subunit processome; IBA:RefGenome.
 GO:0003723; F:RNA binding; NAS:UniProtKB.
 GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
 GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
 GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
 GO:0006364; P:rRNA processing; IMP:UniProtKB.
 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
 IPR000554; Ribosomal_S7e. 
Pfam
 PF01251; Ribosomal_S7e 
SMART
  
PROSITE
 PS00948; RIBOSOMAL_S7E 
PRINTS