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RBM10 encodes a nuclear protein that belongs to a family proteins that contain an RNA-binding motif. Additionally we are shipping RBM10 Antibodies (42) and many more products for this protein.
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RBM10-TFE3 (show TFE3 Proteins) fusion variant (from chromosome X paracentric inversion), therefore, appears to be a recurrent molecular event in Xp11.2 RCCs. RBM10-TFE3 (show TFE3 Proteins) fusion should be added in the list of screened fusion transcripts in targeted molecular diagnostic multiplex RT-PCR
RBM10 is a tumor suppressor that represses Notch (show NOTCH1 Proteins) signaling and cell proliferation through the regulation of NUMB (show NUMB Proteins) alternative splicing
Src (show SRC Proteins) family tyrosine kinase (show TXK Proteins) signaling may regulate FilGAP (show ARHGAP24 Proteins) through association with RBM10
The ability of RBM10v1 to regulate alternative splicing depends, at least in part, on a structural alteration within the second RNA recognition motif domain, and correlates with preferential expression of the NUMB (show NUMB Proteins) exon 11 inclusion variant.
RBM10 regulates alternative splicing of Fas (show FAS Proteins) and Bcl-x (show BCL2L1 Proteins) genes.
Antagonizes the effects of RBM5 (show RBM5 Proteins), RBM6 (show RBM6 Proteins), and RBM10 in cell colony formation.
This study established RBM10 as an important regulator of alternative splicing, presented a mechanistic model for RBM10-mediated splicing regulation and provided a molecular link to understanding a human congenital disorder.
S1-1 contains multiple nuclear localisation sequence that act cooperatively.
Massively parallel sequencing of exons on the X chromosome identifies RBM10 as the gene that causes a syndromic form of cleft palate.
From these results, it seems that the X-chromosome, through its RBM (show RBMY1A1 Proteins) genes, plays a formerly unknown role in the regulation of programmed cell death (apoptosis) in breast cancer.
Expression of Rbm5 (show RBM5 Proteins) and Rbm10 RNA remained constant during C2C12 myogenesis, but protein levels significantly decreased.
S1-1 constitutes hundreds of nuclear domains, which dynamically change their structures in a reversible manner; upon globally reducing RNA polymerase II transcription, S1-1 nuclear bodies enlarge and decrease in number.
This gene encodes a nuclear protein that belongs to a family proteins that contain an RNA-binding motif. The encoded protein associates with hnRNP proteins and may be involved in regulating alternative splicing. Defects in this gene are the cause of the X-linked recessive disorder, TARP syndrome. Alternate splicing results in multiple transcript variants.
RNA binding motif protein 10
, RNA-binding protein 10-like
, RNA-binding protein 10
, RNA-binding protein S1-1
, g patch domain-containing protein 9
, RNA-binding motif protein 10
, S1-1 protein from liver