CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012462
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exosome complex component RRP42 
Protein Synonyms/Alias
 Exosome component 7; Ribosomal RNA-processing protein 42; p8 
Gene Name
 EXOSC7 
Gene Synonyms/Alias
 KIAA0116; RRP42 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11VTLSEAEKVYIVHGVubiquitination[1]
52TSGSARVKLGHTDILubiquitination[1]
116LYRIFNNKSSVDLKTacetylation[2]
116LYRIFNNKSSVDLKTubiquitination[1]
122NKSSVDLKTLCISPRubiquitination[3, 4]
178LEDEEGSKDIELSDDubiquitination[1]
205PCIVTLCKIGYRHVVubiquitination[1, 3]
244TCMRKVGKGSLDPESubiquitination[1]
260FEMMETGKRVGKVLHubiquitination[1, 5]
264ETGKRVGKVLHASLQubiquitination[1]
276SLQSVVHKEESLGPKubiquitination[4, 6]
283KEESLGPKRQKVGFLubiquitination[1]
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] 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]
 [4] 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]
 [5] 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]
 [6] 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
Functional Description
 Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 116 116 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Exosome; Nucleus; Polymorphism; Reference proteome; RNA-binding; rRNA processing. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 291 AA 
Protein Sequence
MASVTLSEAE KVYIVHGVQE DLRVDGRGCE DYRCVEVETD VVSNTSGSAR VKLGHTDILV 60
GVKAEMGTPK LEKPNEGYLE FFVDCSASAT PEFEGRGGDD LGTEIANTLY RIFNNKSSVD 120
LKTLCISPRE HCWVLYVDVL LLECGGNLFD AISIAVKAAL FNTRIPRVRV LEDEEGSKDI 180
ELSDDPYDCI RLSVENVPCI VTLCKIGYRH VVDATLQEEA CSLASLLVSV TSKGVVTCMR 240
KVGKGSLDPE SIFEMMETGK RVGKVLHASL QSVVHKEESL GPKRQKVGFL G 291 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000178; C:exosome (RNase complex); IDA:UniProtKB.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0000175; F:3'-5'-exoribonuclease activity; TAS:UniProtKB.
 GO:0003723; F:RNA binding; TAS:UniProtKB.
 GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
 GO:0006364; P:rRNA processing; TAS:UniProtKB. 
Interpro
 IPR001247; ExoRNase_PH_dom1.
 IPR015847; ExoRNase_PH_dom2.
 IPR027408; PNPase/RNase_PH_dom.
 IPR020568; Ribosomal_S5_D2-typ_fold. 
Pfam
 PF01138; RNase_PH
 PF03725; RNase_PH_C 
SMART
  
PROSITE
  
PRINTS