| Tag | Content |
|---|
| CPLM ID | CPLM-016894 |
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 |
|---|
| 658 | 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
WKPRITLSLP GVLGLQAVKP ESNDKEIEAT YEADIPEEGC GHHPLQQSRK GWSGPDVIIE 180
AQFDDSDSED RHGNTSGLVD GVKKLSISTP DRGKEDSSTP VMKDENTPIP QDTRGLSEKS 240
LQKSAKVVYI LEKKHSRAAT GILKLLADKN SDLFKKYALF SPSDHRVPRI YVPLKDCPQD 300
FMTRPKDFAN TLFICRIIDW KEDCNFALGQ LAKSLGQAGE IEPETEGILT EYGVDFSDFS 360
SEVLECLPQS LPWTIPPDEV GKRRDLRKDC IFTIDPSTAR DLDDALACRR LTDGTFEVGV 420
HIADVSYFVP EGSSLDKVAA ERATSVYLVQ KVVPMLPRLL CEELCSLNPM TDKLTFSVIW 480
KLTPEGKILE EWFGRTIIRS CTKLSYDHAQ SMIENPTEKI PEEELPPISP EHSVEEVHQA 540
VLNLHSIAKQ LRRQRFVDGA LRLDQLKLAF TLDHETGLPQ GCHIYEYRDS NKLVEEFMLL 600
ANMAVAHKIF RTFPEQALLR RHPPPQTKML SDLVEFCDQM GLPMDVSSAG ALNKSLTKTF 660
GDDKYSLARK EVLTNMYSRP MQMALYFCSG MLQDQEQFRH YALNVPLYTH FTSPIRRFAD 720
VIVHRLLAAA LGYSEQPDVE PDTLQKQADH CNDRRMASKR VQELSIGLFF AVLVKESGPL 780
ESEAMVMGVL NQAFDVLVLR FGVQKRIYCN ALALRSYSFQ KVGKKPELTL VWEPDDLEEE 840
PTQQVITIFS LVDVVLQAEA TALKYSAILK RPGLEKASDE EPED 884 |
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 | |