CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018095
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DIS3-like exonuclease 1 
Protein Synonyms/Alias
  
Gene Name
 DIS3L 
Gene Synonyms/Alias
 DIS3L1; KIAA1955 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
137ERGESMEKWQTRSIYubiquitination[1]
252QGILNVNKHRAQIEAubiquitination[1]
269RLQGASSKDSDLVSDubiquitination[1, 2]
283DILIHGMKARNRSIHubiquitination[1, 2]
319CENDCDDKASGESPSubiquitination[3]
340RVVGILQKNWRDYVVubiquitination[1]
352YVVTFPSKEEVQSQGubiquitination[1, 2]
360EEVQSQGKNAQKILVubiquitination[3]
364SQGKNAQKILVTPWDubiquitination[1]
480LVFSIDPKGCEDVDDubiquitination[1]
695ANHWVAKKIWESFPHubiquitination[1]
727LRECAKAKGFFIDTRubiquitination[1]
737FIDTRSNKTLADSLDubiquitination[1]
831KGNLFSNKDLEELCRubiquitination[1]
864LFQCMYFKDKDPATEubiquitination[1]
898FIPRFGIKGAAYLKNubiquitination[1]
906GAAYLKNKDGLVISCubiquitination[1]
998LLKSELVKEVTKSVEubiquitination[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] 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]
 [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] 
Functional Description
 Putative cytoplasm-specific 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 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. 
Sequence Annotation
  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Exonuclease; Exosome; Hydrolase; Magnesium; Nuclease; Polymorphism; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1054 AA 
Protein Sequence
MLQKREKVLL LRTFQGRTLR IVREHYLRPC VPCHSPLCPQ PAACSHDGKL LSSDVTHYVI 60
PDWKVVQDYL EILEFPELKG IIFMQTACQA VQHQRGRRQY NKLRNLLKDA RHDCILFANE 120
FQQCCYLPRE RGESMEKWQT RSIYNAAVWY YHHCQDRMPI VMVTEDEEAI QQYGSETEGV 180
FVITFKNYLD NFWPDLKAAH ELCDSILQSR RERENESQES HGKEYPEHLP LEVLEAGIKS 240
GRYIQGILNV NKHRAQIEAF VRLQGASSKD SDLVSDILIH GMKARNRSIH GDVVVVELLP 300
KNEWKGRTVA LCENDCDDKA SGESPSEPMP TGRVVGILQK NWRDYVVTFP SKEEVQSQGK 360
NAQKILVTPW DYRIPKIRIS TQQAETLQDF RVVVRIDSWE STSVYPNGHF VRVLGRIGDL 420
EGEIATILVE NSISVIPFSE AQMCEMPVNT PESPWKVSPE EEQKRKDLRK SHLVFSIDPK 480
GCEDVDDTLS VRTLNNGNLE LGVHIADVTH FVAPNSYIDI EARTRATTYY LADRRYDMLP 540
SVLSADLCSL LGGVDRYAVS IMWELDKASY EIKKVWYGRT IIRSAYKLFY EAAQELLDGN 600
LSVVDDIPEF KDLDEKSRQA KLEELVWAIG KLTDIARHVR AKRDGCGALE LEGVEVCVQL 660
DDKKNIHDLI PKQPLEVHET VAECMILANH WVAKKIWESF PHQALLRQHP PPHQEFFSEL 720
RECAKAKGFF IDTRSNKTLA DSLDNANDPH DPIVNRLLRS MATQAMSNAL YFSTGSCAEE 780
EFHHYGLALD KYTHFTSPIR RYSDIVVHRL LMAAISKDKK MEIKGNLFSN KDLEELCRHI 840
NNRNQAAQHS QKQSTELFQC MYFKDKDPAT EERCISDGVI YSIRTNGVLL FIPRFGIKGA 900
AYLKNKDGLV ISCGPDSCSE WKPGSLQRFQ NKITSTTTDG ESVTFHLFDH VTVRISIQAS 960
RCHSDTIRLE IISNKPYKIP NTELIHQSSP LLKSELVKEV TKSVEEAQLA QEVKVNIIQE 1020
EYQEYRQTKG RSLYTLLEEI RDLALLDVSN NYGI 1054 
Gene Ontology
 GO:0005813; C:centrosome; IDA:HPA.
 GO:0000177; C:cytoplasmic exosome (RNase complex); IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0016075; P:rRNA catabolic process; IDA:UniProtKB. 
Interpro
 IPR001900; RNase_II/R.
 IPR022966; RNase_II/R_CS. 
Pfam
 PF00773; RNB 
SMART
 SM00955; RNB 
PROSITE
 PS01175; RIBONUCLEASE_II 
PRINTS