Biology:RBM3

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Putative RNA-binding protein 3 is a protein that in humans is encoded by the RBM3 gene.[1][2]

Function

This gene is a member of the glycine-rich RNA-binding protein family and encodes a protein with one RNA recognition motif (RRM) domain. Expression of this gene is induced by cold shock and low oxygen tension. A pseudogene exists on chromosome 1. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[2]

RBM3 is cold-induced RNA binding protein and is involved in mRNA biogenesis exerts anti-apoptotic effects.[3] According to antibody-based profiling and transcriptomics analysis, RBM3 protein is present in all analysed human tissues[4] and based on confocal microscopy mainly localised to the nucleoplasm.[5]

Clinical significance

RBM3 is a proto-oncogene that is associated with tumor progression and metastasis and is a potential cancer biomarker.[3] Based on patient survival data, high levels of RBM3 protein in tumor cells is a favourable prognostic biomarker in colorectal cancer.[6]

References

Further reading

  • "Increased transcript level of RBM3, a member of the glycine-rich RNA-binding protein family, in human cells in response to cold stress". Biochemical and Biophysical Research Communications 236 (3): 804–7. July 1997. doi:10.1006/bbrc.1997.7059. PMID 9245737. 
  • "The internal ribosome entry site (IRES) contained within the RNA-binding motif protein 3 (Rbm3) mRNA is composed of functionally distinct elements". The Journal of Biological Chemistry 278 (36): 33793–800. September 2003. doi:10.1074/jbc.M303495200. PMID 12824175. 
  • "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a HIF-1-independent mechanism". Journal of Cell Science 117 (Pt 9): 1785–94. April 2004. doi:10.1242/jcs.01026. PMID 15075239. 
  • "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Analytical Chemistry 76 (10): 2763–72. May 2004. doi:10.1021/ac035352d. PMID 15144186. 
  • "Protein interactions among the vaccinia virus late transcription factors". Virology 329 (2): 328–36. November 2004. doi:10.1016/j.virol.2004.08.017. PMID 15518812. 
  • "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. January 2005. doi:10.1038/nature03207. PMID 15635413. Bibcode2005Natur.433...77A. 
  • "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nature Methods 1 (2): 119–26. November 2004. doi:10.1038/nmeth715. PMID 15782174. 
  • "Positive correlation between the expression of X-chromosome RBM genes (RBMX, RBM3, RBM10) and the proapoptotic Bax gene in human breast cancer". Journal of Cellular Biochemistry 97 (6): 1275–82. April 2006. doi:10.1002/jcb.20725. PMID 16552754.