Biology:RBMX
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Heterogeneous nuclear ribonucleoprotein G is a protein that in humans is encoded by the RBMX gene.[1][2][3]
Function
This gene belongs to the RBMY gene family which includes candidate Y chromosome spermatogenesis genes. This gene, an active X chromosome homolog of the Y chromosome RBMY gene, is widely expressed whereas the RBMY gene evolved a male-specific function in spermatogenesis. Pseudogenes of this gene, found on chromosomes 1, 4, 9, 11, and 6, were likely derived by retrotransposition from the original gene. Alternatively spliced transcript variants encoding different isoforms have been identified but their biological nature has not been determined.[3]
Interactions
RBMX has been shown to interact with SFRS10[4] and CDC5L.[5]
Model organisms
Model organisms have been used in the study of RBMX function. A conditional knockout mouse line called Rbmxtm2b(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute.[6] Male and female animals underwent a standardized phenotypic screen[7] to determine the effects of deletion.[8][9][10][11] Additional screens performed: - In-depth immunological phenotyping[12]
| Characteristic | Phenotype |
|---|---|
| All data available at.[7][12] | |
| Peripheral blood leukocytes 6 Weeks | Normal |
| Insulin | Normal |
| Haematology 6 Weeks | Normal |
| Homozygous viability at P14 | Normal |
| Homozygous Fertility | Normal |
| Body weight | Abnormal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Haematology 16 Weeks | Normal |
| Peripheral blood leukocytes 16 Weeks | Normal |
| Heart weight | Normal |
| Salmonella infection | Normal |
| Cytotoxic T Cell Function | Normal |
| Spleen Immunophenotyping | Normal |
| Mesenteric Lymph Node Immunophenotyping | Normal |
| Bone Marrow Immunophenotyping | Normal |
| Epidermal Immune Composition | Normal |
| Trichuris Challenge | Normal |
References
- ↑ "The candidate spermatogenesis gene RBMY has a homologue on the human X chromosome". Nature Genetics 22 (3): 223–4. Jul 1999. doi:10.1038/10279. PMID 10391206.
- ↑ "RBMY evolved on the Y chromosome from a ubiquitously transcribed X-Y identical gene". Nature Genetics 22 (3): 224–6. Jul 1999. doi:10.1038/10282. PMID 10391207.
- ↑ 3.0 3.1 "Entrez Gene: RBMX RNA binding motif protein, X-linked". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27316.
- ↑ "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta1". Human Molecular Genetics 11 (17): 2037–49. Aug 2002. doi:10.1093/hmg/11.17.2037. PMID 12165565.
- ↑ "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal 19 (23): 6569–81. Dec 2000. doi:10.1093/emboj/19.23.6569. PMID 11101529.
- ↑ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
- ↑ 7.0 7.1 "International Mouse Phenotyping Consortium". http://www.mousephenotype.org/data/search?q=Rbmx#fq=*:*&facet=gene.
- ↑ "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. Jun 2011. doi:10.1038/nature10163. PMID 21677750.
- ↑ "Mouse library set to be knockout". Nature 474 (7351): 262–3. Jun 2011. doi:10.1038/474262a. PMID 21677718.
- ↑ "A mouse for all reasons". Cell 128 (1): 9–13. Jan 2007. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
- ↑ "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell 154 (2): 452–64. Jul 2013. doi:10.1016/j.cell.2013.06.022. PMID 23870131.
- ↑ 12.0 12.1 "Infection and Immunity Immunophenotyping (3i) Consortium". http://www.immunophenotyping.org/data/search?keys=Rbmx&field_gene_construct_tid=All.
Further reading
- "Localization of the human gene encoding heterogeneous nuclear RNA ribonucleoprotein G (hnRNP-G) to chromosome 6p12". Human Genetics 88 (5): 593–5. Mar 1992. doi:10.1007/bf00219352. PMID 1551662.
- "hnRNP G: sequence and characterization of a glycosylated RNA-binding protein". Nucleic Acids Research 21 (18): 4210–7. Sep 1993. doi:10.1093/nar/21.18.4210. PMID 7692398.
- "Generation and analysis of 280,000 human expressed sequence tags". Genome Research 6 (9): 807–28. Sep 1996. doi:10.1101/gr.6.9.807. PMID 8889549.
- "T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis". Human Molecular Genetics 8 (6): 959–69. Jun 1999. doi:10.1093/hmg/8.6.959. PMID 10332027.
- "RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2beta and affect splicing". Human Molecular Genetics 9 (5): 685–94. Mar 2000. doi:10.1093/hmg/9.5.685. PMID 10749975.
- "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal 19 (23): 6569–81. Dec 2000. doi:10.1093/emboj/19.23.6569. PMID 11101529.
- "Expression and conservation of processed copies of the RBMX gene". Mammalian Genome 12 (7): 538–45. Jul 2001. doi:10.1007/s00335001-0003-z. PMID 11420617.
- "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". RNA 8 (4): 426–39. Apr 2002. doi:10.1017/S1355838202021088. PMID 11991638.
- "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta1". Human Molecular Genetics 11 (17): 2037–49. Aug 2002. doi:10.1093/hmg/11.17.2037. PMID 12165565.
- "A receptor for activated C kinase is part of messenger ribonucleoprotein complexes associated with polyA-mRNAs in neurons". The Journal of Neuroscience 22 (20): 8827–37. Oct 2002. doi:10.1523/JNEUROSCI.22-20-08827.2002. PMID 12388589.
- "Regulation of alternative splicing by SRrp86 and its interacting proteins". Molecular and Cellular Biology 23 (21): 7437–47. Nov 2003. doi:10.1128/MCB.23.21.7437-7447.2003. PMID 14559993.
- "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. https://figshare.com/articles/journal_contribution/Robust_Phosphoproteomic_Profiling_of_Tyrosine_Phosphorylation_Sites_from_Human_T_Cells_Using_Immobilized_Metal_Affinity_Chromatography_and_Tandem_Mass_Spectrometry/3339307/files/5178523.pdf.
- "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America 101 (33): 12130–5. Aug 2004. doi:10.1073/pnas.0404720101. PMID 15302935. Bibcode: 2004PNAS..10112130B.
- "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nature Methods 1 (2): 119–26. Nov 2004. doi:10.1038/nmeth715. PMID 15782174.
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