| Tag | Content |
|---|
| CPLM ID | CPLM-016893 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | DIS3-like exonuclease 2 |
Protein Synonyms/Alias | |
Gene Name | Dis3l2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 644 | ALNKSLTKTFGDDKY | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
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 (By similarity).
MOD_RES 192 192 Phosphoserine.
MOD_RES 250 250 N6-acetyllysine (By similarity).
MOD_RES 864 864 Phosphoserine. |
Keyword | Acetylation; Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Magnesium; Manganese; Mitosis; Nuclease; Phosphoprotein; Reference proteome; RNA-binding; Tumor suppressor. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 870 AA |
Protein Sequence | MNHPDYKLNL RSPGTPRGVS SVVGPSAVGA SPGDKKSKNK SMRGKKKSIF ETYMSKEDVS 60
EGLKRGTLIQ GVLRINPKKF HEAFIPSPDG DRDIFIDGVV ARNRALNGDL VVVKLLPEDQ 120
WKAVKPESND KEIEATYEAD IPEEGCGHHP LQQSRKGWSG PDVIIEAQFD DSDSEDRHGN 180
TSGLVDGVKK LSISTPDRGK EDSSTPVMKD ENTPIPQDTR GLSEKSLQKS AKVVYILEKK 240
HSRAATGILK LLADKNSDLF KKYALFSPSD HRVPRIYVPL KDCPQDFMTR PKDFANTLFI 300
CRIIDWKEDC NFALGQLAKS LGQAGEIEPE TEGILTEYGV DFSDFSSEVL ECLPQSLPWT 360
IPPDEVGKRR DLRKDCIFTI DPSTARDLDD ALACRRLTDG TFEVGVHIAD VSYFVPEGSS 420
LDKVAAERAT SVYLVQKVVP MLPRLLCEEL CSLNPMTDKL TFSVIWKLTP EGKILEEWFG 480
RTIIRSCTKL SYDHAQSMIE NPTEKIPEEE LPPISPEHSV EEVHQAVLNL HSIAKQLRRQ 540
RFVDGALRLD QLKLAFTLDH ETGLPQGCHI YEYRDSNKLV EEFMLLANMA VAHKIFRTFP 600
EQALLRRHPP PQTKMLSDLV EFCDQMGLPM DVSSAGALNK SLTKTFGDDK YSLARKEVLT 660
NMYSRPMQMA LYFCSGMLQD QEQFRHYALN VPLYTHFTSP IRRFADVIVH RLLAAALGYS 720
EQPDVEPDTL QKQADHCNDR RMASKRVQEL SIGLFFAVLV KESGPLESEA MVMGVLNQAF 780
DVLVLRFGVQ KRIYCNALAL RSYSFQKVGK KPELTLVWEP DDLEEEPTQQ VITIFSLVDV 840
VLQAEATALK YSAILKRPGL EKASDEEPED 870 |
Gene Ontology | GO:0005737; C:cytoplasm; ISS:UniProtKB. GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. GO:0004540; F:ribonuclease activity; ISS:UniProtKB. GO:0003723; F:RNA binding; IEA:UniProtKB-KW. GO:0051301; P:cell division; IEA:UniProtKB-KW. GO:0051306; P:mitotic sister chromatid separation; ISS:UniProtKB. GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |