CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036374
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Exosome complex component RRP45 
Protein Synonyms/Alias
 Exosome component 9, isoform CRA_f 
Gene Name
 EXOSC9 
Gene Synonyms/Alias
 hCG_38830 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
251EITELILKALENDQKubiquitination[1, 2]
258KALENDQKVRKEGGKubiquitination[2]
261ENDQKVRKEGGKFGFubiquitination[2]
265KVRKEGGKFGFAESIacetylation[3, 4]
265KVRKEGGKFGFAESIubiquitination[1, 2, 4, 5]
281NQRITAFKMEKAPIDacetylation[4, 6]
281NQRITAFKMEKAPIDubiquitination[2]
284ITAFKMEKAPIDTSDubiquitination[1, 2]
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] 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]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [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] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 423 AA 
Protein Sequence
MNLCLQRLDG RQTYDYRNIR ISFGTDYGCC IVELGKTRVL GQVSCELVSP KLNRATEGIL 60
FFNLELSQMA APAFEPGRQS DLLVKLNRLM ERCLRNSKCI DTESLCVVAG EKVWQIRVDL 120
HLLNHDGNII DAASIAAIVA LCHFRRPDVS VQGDEVTLYT PEERDPVPLS IHHMPICVSF 180
AFFQQGTYLL VDPNEREERV MDGLLVIAMN KHREICTIQS SGGIMLLKDQ VLRCSKIAGV 240
KVAEITELIL KALENDQKVR KEGGKFGFAE SIANQRITAF KMEKAPIDTS DVEEKAEEII 300
AEAEPPSEVV STPVLWTPGT AQIGEGVENS WGDLEDSEKE DDEGGGDQAI ILDGIKMDTG 360
VEVSDIGSQD APIILSDSEE EEMIILEPDK NPKKIRTQTT SAKQEKAPSK KPVKRRKKKR 420
AAN 423 
Gene Ontology
  
Interpro
 IPR001247; ExoRNase_PH_dom1.
 IPR015847; ExoRNase_PH_dom2.
 IPR020568; Ribosomal_S5_D2-typ_fold. 
Pfam
 PF01138; RNase_PH
 PF03725; RNase_PH_C 
SMART
  
PROSITE
  
PRINTS