Putative RNA-binding protein 3 is a
protein that in humans is encoded by the RBM3gene.[4][5]
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.[5]
RBM3 is cold-induced RNA binding protein and is involved in mRNA biogenesis exerts anti-
apoptotic effects.[6] According to
antibody-based profiling and
transcriptomics analysis, RBM3 protein is present in all analysed human tissues[7] and based on
confocal microscopy mainly localised to the
nucleoplasm.[8]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Derry JM, Kerns JA, Francke U (December 1995). "RBM3, a novel human gene in Xp11.23 with a putative RNA-binding domain". Human Molecular Genetics. 4 (12): 2307–11.
doi:
10.1093/hmg/4.12.2307.
PMID8634703.
Danno S, Nishiyama H, Higashitsuji H, Yokoi H, Xue JH, Itoh K, Matsuda T, Fujita J (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): 804–7.
doi:
10.1006/bbrc.1997.7059.
PMID9245737.
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): 2763–72.
doi:
10.1021/ac035352d.
PMID15144186.
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): 328–36.
doi:
10.1016/j.virol.2004.08.017.
hdl:10161/15063.
PMID15518812.
Ong SE, Mittler G, Mann M (November 2004). "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nature Methods. 1 (2): 119–26.
doi:
10.1038/nmeth715.
PMID15782174.
S2CID6654604.
Martínez-Arribas F, Agudo D, Pollán M, Gómez-Esquer F, Díaz-Gil G, Lucas R, Schneider J (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): 1275–82.
doi:
10.1002/jcb.20725.
PMID16552754.
S2CID9804734.
Putative RNA-binding protein 3 is a
protein that in humans is encoded by the RBM3gene.[4][5]
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.[5]
RBM3 is cold-induced RNA binding protein and is involved in mRNA biogenesis exerts anti-
apoptotic effects.[6] According to
antibody-based profiling and
transcriptomics analysis, RBM3 protein is present in all analysed human tissues[7] and based on
confocal microscopy mainly localised to the
nucleoplasm.[8]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Derry JM, Kerns JA, Francke U (December 1995). "RBM3, a novel human gene in Xp11.23 with a putative RNA-binding domain". Human Molecular Genetics. 4 (12): 2307–11.
doi:
10.1093/hmg/4.12.2307.
PMID8634703.
Danno S, Nishiyama H, Higashitsuji H, Yokoi H, Xue JH, Itoh K, Matsuda T, Fujita J (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): 804–7.
doi:
10.1006/bbrc.1997.7059.
PMID9245737.
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): 2763–72.
doi:
10.1021/ac035352d.
PMID15144186.
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): 328–36.
doi:
10.1016/j.virol.2004.08.017.
hdl:10161/15063.
PMID15518812.
Ong SE, Mittler G, Mann M (November 2004). "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nature Methods. 1 (2): 119–26.
doi:
10.1038/nmeth715.
PMID15782174.
S2CID6654604.
Martínez-Arribas F, Agudo D, Pollán M, Gómez-Esquer F, Díaz-Gil G, Lucas R, Schneider J (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): 1275–82.
doi:
10.1002/jcb.20725.
PMID16552754.
S2CID9804734.