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100043257 Ensembl ENSG00000102317 n/a UniProt P98179 n/a RefSeq (mRNA) NM_001017430 NM_001017431 NM_006743 XM_036156140 RefSeq (protein) NP_006734 n/a Location (UCSC) Chr X: 48.57 – 48.58 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Putative RNA-binding protein 3 is a protein that in humans is encoded by the RBM3 gene. Function This gene is a member of the glycine -rich RNA ...
Recent development in experimental identification of RNA-binding proteins has extended the number of RNA-binding proteins significantly [32] [33] [34] RNA-binding protein Sam68 controls the spatial and temporal compartmentalization of RNA metabolism to attain proper synaptic function in dendrites.
A shared feature of these proteins is to bind only to a subclass of the known AREs that contain the pentamer AUUUA. A convergent effort of several research teams now adds CUGBP1 (CUG binding protein 1) to the short list of ARE-Binding proteins that control mRNA stability, with the peculiarity that it binds to non-AUUUA AREs.
Pages in category "RNA-binding proteins" The following 28 pages are in this category, out of 28 total. This list may not reflect recent changes. ...
The evolutionarily conserved function of the encoded protein in invertebrates and lower vertebrates suggests that the human protein may be involved in translational regulation of embryogenesis, and cell development and differentiation. Alternatively spliced transcript variants encoding different isoforms have been described. [4]
Nuclear cap-binding protein complex is a RNA-binding protein which binds to the 5' cap of pre-mRNA.The cap and nuclear cap-binding protein have many functions in mRNA biogenesis including splicing, 3'-end formation by stabilizing the interaction of the 3'-end processing machinery, nuclear export and protection of the transcripts from nuclease degradation. [2]
The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has three repeats of quasi-RRM domains that bind to RNAs which have guanosine-rich sequences. This protein is very similar to the family member hnRNPH. Multiple alternatively spliced variants, encoding the same protein, have been identified. [6]
The atomic structure of the NFY heterotrimer in complex with dsDNA was resolved via X-ray crystallography (PDB ID 4awl). [13] Using one of the NFYA alpha helices as a template, structure inspired stapled peptides were designed to disrupt the NFY heterotrimer formation by preventing NFYA from binding to the NFYB/C heterodimer.