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THEX1
RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs. Note: This description may include information from UniProtKB.
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| Protein type: EC 3.1.-.-; Hydrolase; Nucleolus |
| Chromosomal Location of mouse Ortholog: 8|8 A4 |
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Cellular Component:
cytoplasm; histone pre-mRNA 3'end processing complex; nucleolus; nucleus
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Molecular Function:
3'-5' exonuclease activity; 3'-5'-exoribonuclease activity; exonuclease activity; histone pre-mRNA stem-loop binding; hydrolase activity; metal ion binding; nuclease activity; nucleic acid binding; protein binding; ribosome binding; RNA binding; rRNA binding
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Biological Process:
DNA catabolic process, exonucleolytic; exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); gene silencing by RNA; rRNA 3'-end processing; rRNA processing
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Reference #:
Q7TMF2
(UniProtKB)
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Alt. Names/Synonyms: 3'-5' exonuclease ERI1; 3'-5' exoribonuclease 1; 3'exo; 3'hexo; 3110010F15Rik; enhanced RNAi protein 1; eri-1; Eri-1 homolog; Eri1; exoribonuclease 1; histone mRNA 3' end-specific exonuclease; Histone mRNA 3'-exonuclease 1; Thex1; three prime histone mRNA exonuclease 1
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Gene Symbols: Eri1
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Molecular weight:
39,493 Da
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Basal Isoelectric point:
8.56
Predict pI for various phosphorylation states
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Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology®
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