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RNA-binding proteins (often abbreviated as RBPs) ... (CNV), for example CNV gains of BYSL in colorectal cancer cells [19] and ESRP1, CELF3 in breast cancer, ...
RNA binding protein domains in other proteins that are similar to the RNA binding domain of protein K are called K-homology or KH domains. Protein K has been the subject of study related to colorectal cancer, in which an RNA editing event inducing the expression of an isoform containing a point mutation was found to be specific to cancerous ...
Heterogeneous nuclear ribonucleoprotein H is a protein [5] that in humans is encoded by the HNRNPH1 gene. [6] [7] This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins . The hnRNPs are RNA binding proteins and they complex with heterogeneous nuclear RNA .
Recent discoveries implicating RNA in the pathogenesis of several forms of cancer and neuromuscular diseases have created a paradigm shift in drug discovery.This work combined with advances in structural characterization techniques such as NMR spectroscopy, X-ray crystallography, Cryogenic electron microscopy [1] together with computational modeling, [2] has pushed forward the realization that ...
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 ...
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]
It is now evident that RBM4 serves as an RNA-binding protein, participating in a wide array of cellular processes, which encompass the alternative splicing of pre-mRNA, translation control, and RNA silencing. Structurally, RBM4 shares similarities with other RNA-binding proteins, featuring two RNA recognition motifs and a CCHC-type zinc finger. [9]
The hnRNPs are nucleic acid binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). The interaction sites on the RNA are frequently biased towards particular sequence motifs. [ 7 ] These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and ...