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UniProt functional annotation for Q9UMR2 | ||
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| UniProt code: Q9UMR2. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
ATP-dependent RNA helicase involved in mRNA export from the nucleus (PubMed:10428971). Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins (PubMed:10428971). {ECO:0000269|PubMed:10428971}. |
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| Catalytic activity: | |
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:10428971}; |
| Subunit: | |
Associates with the nuclear pore complex via interaction with NUP214 (PubMed:10428971, PubMed:19208808, PubMed:19219046). Interacts with NUP214 or RNA in a mutually exclusive manner (PubMed:19208808, PubMed:19219046, PubMed:19244245). {ECO:0000269|PubMed:10428971, ECO:0000269|PubMed:19208808, ECO:0000269|PubMed:19219046, ECO:0000269|PubMed:19244245}. |
| Subcellular location: | |
Cytoplasm {ECO:0000269|PubMed:10428971}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10428971}. Note=Associates with the nuclear pore complex cytoplasmic fibrils. {ECO:0000269|PubMed:10428971}. |
| Domain: | |
The N-terminal extension helix acts as an autoinhibitory domain, preventing ATP hydrolysis, unless the N-terminus of the protein is displaced by RNA binding, allowing cleft closure to bring key side chains into position for catalysis. |
| Similarity: | |
Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.