CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017096
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DIS3-like exonuclease 2 
Protein Synonyms/Alias
 hDIS3L2 
Gene Name
 DIS3L2 
Gene Synonyms/Alias
 FAM6A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
252RAATGFLKLLADKNSacetylation[1]
283PRIYVPLKDCPQDFVubiquitination[2]
376SKRRDLRKDCIFTIDubiquitination[2]
397LDDALSCKPLADGNFubiquitination[2]
507MIESPTEKIPAKELPubiquitination[3]
596ANMAVAHKIHRAFPEubiquitination[2]
652TQTFGDDKYSLARKEubiquitination[2]
Reference
 [1] 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]
 [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] 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] 
Functional Description
 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of both mRNAs and miRNAs that have been polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. Mediates degradation of uridylated pre-let-7 miRNAs, contributing to the maintenance of embryonic stem (ES) cells. Essential for correct mitosis, and negatively regulates cell proliferation. 
Sequence Annotation
 MOD_RES 31 31 Phosphoserine.
 MOD_RES 194 194 Phosphoserine (By similarity).
 MOD_RES 252 252 N6-acetyllysine.
 MOD_RES 875 875 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Disease mutation; Exonuclease; Hydrolase; Magnesium; Manganese; Mitosis; Nuclease; Phosphoprotein; Polymorphism; Reference proteome; RNA-binding; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 885 AA 
Protein Sequence
MSHPDYRMNL RPLGTPRGVS AVAGPHDIGA SPGDKKSKNR STRGKKKSIF ETYMSKEDVS 60
EGLKRGTLIQ GVLRINPKKF HEAFIPSPDG DRDIFIDGVV ARNRALNGDL VVVKLLPEEH 120
WKVVKPESND KETEAAYESD IPEELCGHHL PQQSLKSYND SPDVIVEAQF DGSDSEDGHG 180
ITQNVLVDGV KKLSVCVSEK GREDGDAPVT KDETTCISQD TRALSEKSLQ RSAKVVYILE 240
KKHSRAATGF LKLLADKNSE LFRKYALFSP SDHRVPRIYV PLKDCPQDFV ARPKDYANTL 300
FICRIVDWKE DCNFALGQLA KSLGQAGEIE PETEGILTEY GVDFSDFSSE VLECLPQGLP 360
WTIPPEEFSK RRDLRKDCIF TIDPSTARDL DDALSCKPLA DGNFKVGVHI ADVSYFVPEG 420
SDLDKVAAER ATSVYLVQKV VPMLPRLLCE ELCSLNPMSD KLTFSVIWTL TPEGKILDEW 480
FGRTIIRSCT KLSYEHAQSM IESPTEKIPA KELPPISPEH SSEEVHQAVL NLHGIAKQLR 540
QQRFVDGALR LDQLKLAFTL DHETGLPQGC HIYEYRESNK LVEEFMLLAN MAVAHKIHRA 600
FPEQALLRRH PPPQTRMLSD LVEFCDQMGL PVDFSSAGAL NKSLTQTFGD DKYSLARKEV 660
LTNMCSRPMQ MALYFCSGLL QDPAQFRHYA LNVPLYTHFT SPIRRFADVL VHRLLAAALG 720
YRERLDMAPD TLQKQADHCN DRRMASKRVQ ELSTSLFFAV LVKESGPLES EAMVMGILKQ 780
AFDVLVLRYG VQKRIYCNAL ALRSHHFQKV GKKPELTLVW EPEDMEQEPA QQVITIFSLV 840
EVVLQAESTA LKYSAILKRP GTQGHLGPEK EEEESDGEPE DSSTS 885 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
 GO:0004540; F:ribonuclease activity; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0051306; P:mitotic sister chromatid separation; IMP:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB. 
Interpro
 IPR001900; RNase_II/R.
 IPR022966; RNase_II/R_CS. 
Pfam
 PF00773; RNB 
SMART
 SM00955; RNB 
PROSITE
 PS01175; RIBONUCLEASE_II 
PRINTS