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RBPMS encodes a member of the RRM family of RNA-binding proteins. Additionally we are shipping RBPMS Antibodies (78) and RBPMS Kits (5) and many more products for this protein.
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Cytoplasmic granule containing HERMES (show CD44 Proteins), NonO (show NONO Proteins), PSF (show IL-3 Proteins), and G3BP1 (show G3BP1 Proteins) is a neuronal RNA-protein granule that is transported in neurites during retinal differentiation.
The possible involvement of the GC box 1 at position - 54 in transcriptional regulation of Rbpms was corroborated by EMSA, which showed formation of a DNA-protein complex in the presence of the oligonucleotide corresponding to this Sp1 (show PSG1 Proteins)-binding site.
Data indicate RNA Binding Protein with Multiple Splicing (RBPMS), Regulator of Chromosome Condensation and POZ Domain Containing Protein 1 (RCBTB1), and Zinc Finger protein 608 (ZNF608) as miR-21-3p target genes.
Conserved binding of GCAC motifs by MEC (show CCL28 Proteins)-8, couch potato, and the RBPMS protein family has been reported.
ERG (show ERG Proteins) is recruited to mRNAs via interaction with the RNA-binding protein (show PTBP1 Proteins) RBPMS, and it promotes mRNA decay by binding CNOT2 (show CNOT2 Proteins), a component of the CCR4 (show CCR4 Proteins)-NOT deadenylation complex.
observation of a strong in vivo erythropoietic effect for RBPMS but not for GTF2E2, supporting the statistical fine-mapping at this locus and demonstrating that RBPMS is a regulator of erythropoiesis
Study indicates that the RNA binding increases the stability of RNA-recognition motif (RRM) in RBPMS domain, but residue mutations of RRM domain induce the fluctuation of complex systems through weakening of hydrogen bonds, conformational change or loss of binding affinity.
RBPMS1 is a critical repressor of AP-1 (show FOSB Proteins) signaling and RBPMS1 activation may be a useful strategy for cancer treatment.
The work presented here reveals a novel function for the RNA-binding protein Hermes in regulating the topographic sorting of retinal ganglion cell (RGC) axons in the optic tract and tectum
Hermes loss of function in Xenopus laevis embryos leads to a significant reduction in retinal axon arbor complexity in the optic tectum
We propose that as an RNA-binding protein, Hermes may be involved in maturation, cleavage events at the vegetal pole and germ cell development by negatively regulating the expression of RINGO/Spy, Mos (show MOS Proteins), and Xcat2 mRNAs.
This gene encodes a member of the RRM family of RNA-binding proteins. The RRM domain is between 80-100 amino acids in length and family members contain one to four copies of the domain. The RRM domain consists of two short stretches of conserved sequence called RNP1 and RNP2, as well as a few highly conserved hydrophobic residues. The protein encoded by this gene has a single, putative RRM domain in its N-terminus. Alternative splicing results in multiple transcript variants encoding different isoforms.
HEart, RRM Expressed Sequence
, RNA-binding protein gene with multiple splicing
, RNA-binding protein with multiple splicing
, RNA-binding protein with multiple splicing (RBP-MS)
, heart and RRM expressed sequence
, RNA binding protein gene with multiple splicing