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RBM3
Identifiers
Aliases	RBM3, IS1-RNPL, RNPL, RNA binding motif (RNP1, RRM) protein 3, RNA binding motif protein 3
External IDs	OMIM: 300027; MGI: 3642874; GeneCards: RBM3
Gene location (Human) Chr. X chromosome (human) Band Xp11.23 Start 48,574,449 bp End 48,581,162 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon human penis monocyte synovial joint nipple gastric mucosa saphenous vein skin of leg body of pancreas olfactory zone of nasal mucosa n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding nucleic acid binding RNA binding mRNA 3'-UTR binding poly(U) RNA binding translation repressor activity ribosomal large subunit binding small ribosomal subunit rRNA binding Cellular component cytoplasm large ribosomal subunit dendrite cell projection nucleolus nucleus nucleoplasm spliceosomal complex ribonucleoprotein complex Biological process RNA processing regulation of translation positive regulation of translation response to cold negative regulation of translation positive regulation of mRNA splicing, via spliceosome Sources:Amigo / QuickGO
Orthologs Databases NCBI: entry; OMA: entry Species Human Mouse Entrez 5935 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.

Gene

A pseudogene exists on chromosome 1. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. RBM3 contains a poison exon whose inclusion is lowered during hypothermia.

Structure

This gene is a member of the glycine-rich RNA-binding protein family and encodes a protein with one RNA recognition motif (RRM) domain.

Function

Expression of this gene is induced by cold shock and low oxygen tension.

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

Clinical significance

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

Further reading

• Danno S, Nishiyama H, Higashitsuji H, Yokoi H, Xue JH, Itoh K, et al. (July 1997). "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): 804–807. Bibcode:1997BBRC..236..804D. doi:10.1006/bbrc.1997.7059. PMID 9245737.
• Chappell SA, Mauro VP (September 2003). "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): 33793–33800. doi:10.1074/jbc.M303495200. PMID 12824175.
• Wellmann S, Bührer C, Moderegger E, Zelmer A, Kirschner R, Koehne P, et al. (April 2004). "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a HIF-1-independent mechanism". Journal of Cell Science. 117 (Pt 9): 1785–1794. doi:10.1242/jcs.01026. PMID 15075239.
• Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC (May 2004). "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry". Analytical Chemistry. 76 (10): 2763–2772. Bibcode:2004AnaCh..76.2763B. doi:10.1021/ac035352d. PMID 15144186.
• Dellis S, Strickland KC, McCrary WJ, Patel A, Stocum E, Wright CF (November 2004). "Protein interactions among the vaccinia virus late transcription factors". Virology. 329 (2): 328–336. doi:10.1016/j.virol.2004.08.017. hdl:10161/15063. PMID 15518812.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, et al. (January 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
• Ong SE, Mittler G, Mann M (November 2004). "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nature Methods. 1 (2): 119–126. doi:10.1038/nmeth715. PMID 15782174. S2CID 6654604.
• Martínez-Arribas F, Agudo D, Pollán M, Gómez-Esquer F, Díaz-Gil G, Lucas R, et al. (April 2006). "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): 1275–1282. doi:10.1002/jcb.20725. PMID 16552754. S2CID 9804734.