RBMX

RNA binding motif protein, X-linked
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2MB0​, 2MKS​
Identifiers
Symbols	RBMX ; HNRNPG; HNRPG; RBMXP1; RBMXRT; RNMX; hnRNP-G
External IDs	OMIM: 300199 MGI: 1343044 HomoloGene: 20494 GeneCards: RBMX Gene
Gene ontology Molecular function • nucleotide binding • core promoter binding • chromatin binding • RNA binding • single-stranded RNA binding • mRNA binding • protein binding • poly(A) RNA binding Cellular component • extracellular space • nucleus • nucleoplasm • nuclear euchromatin • membrane • ribonucleoprotein complex • supraspliceosomal complex • extracellular exosome • catalytic step 2 spliceosome Biological process • regulation of alternative mRNA splicing, via spliceosome • mRNA splicing, via spliceosome • osteoblast differentiation • transcription from RNA polymerase II promoter • mRNA splice site selection • membrane protein ectodomain proteolysis • RNA splicing • gene expression • positive regulation of transcription from RNA polymerase II promoter • negative regulation of mRNA splicing, via spliceosome • positive regulation of mRNA splicing, via spliceosome • protein homooligomerization • cellular response to interleukin-1 Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	27316	19655
Ensembl	ENSG00000147274	ENSMUSG00000031134
UniProt	P38159	Q9WV02
RefSeq (mRNA)	NM_001164803	NM_001166623
RefSeq (protein)	NP_001158275	NP_001160095
Location (UCSC)	Chr X: 136.85 – 136.88 Mb	Chr X: 57.38 – 57.39 Mb
PubMed search

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 Rbmx^{tm2b(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]

Rbmx knockout mouse phenotype

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

1. Delbridge ML, Lingenfelter PA, Disteche CM, Graves JA (Jul 1999). "The candidate spermatogenesis gene RBMY has a homologue on the human X chromosome". Nature Genetics 22 (3): 223–4. doi:10.1038/10279. PMID 10391206.
2. Mazeyrat S, Saut N, Mattei MG, Mitchell MJ (Jul 1999). "RBMY evolved on the Y chromosome from a ubiquitously transcribed X-Y identical gene". Nature Genetics 22 (3): 224–6. doi:10.1038/10282. PMID 10391207.
3. "Entrez Gene: RBMX RNA binding motif protein, X-linked".
4. Hofmann Y, Wirth B (Aug 2002). "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta1". Human Molecular Genetics 11 (17): 2037–49. doi:10.1093/hmg/11.17.2037. PMID 12165565.
5. Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (Dec 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
6. 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. "International Mouse Phenotyping Consortium".
8. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
9. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
10. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
11. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
12. "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

• Le Coniat M, Soulard M, Della Valle V, Larsen CJ, Berger R (Mar 1992). "Localization of the human gene encoding heterogeneous nuclear RNA ribonucleoprotein G (hnRNP-G) to chromosome 6p12". Human Genetics 88 (5): 593–5. doi:10.1007/bf00219352. PMID 1551662.
• Soulard M, Della Valle V, Siomi MC, Piñol-Roma S, Codogno P, Bauvy C, Bellini M, Lacroix JC, Monod G, Dreyfuss G (Sep 1993). "hnRNP G: sequence and characterization of a glycosylated RNA-binding protein". Nucleic Acids Research 21 (18): 4210–7. doi:10.1093/nar/21.18.4210. PMC 310052. PMID 7692398.
• Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M (Sep 1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Research 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
• Venables JP, Vernet C, Chew SL, Elliott DJ, Cowmeadow RB, Wu J, Cooke HJ, Artzt K, Eperon IC (Jun 1999). "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. doi:10.1093/hmg/8.6.959. PMID 10332027.
• Venables JP, Elliott DJ, Makarova OV, Makarov EM, Cooke HJ, Eperon IC (Mar 2000). "RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2beta and affect splicing". Human Molecular Genetics 9 (5): 685–94. doi:10.1093/hmg/9.5.685. PMID 10749975.
• Ajuh P, Kuster B, Panov K, Zomerdijk JC, Mann M, Lamond AI (Dec 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". The EMBO Journal 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. PMC 305846. PMID 11101529.
• Lingenfelter PA, Delbridge ML, Thomas S, Hoekstra HE, Mitchell MJ, Graves JA, Disteche CM (Jul 2001). "Expression and conservation of processed copies of the RBMX gene". Mammalian Genome 12 (7): 538–45. doi:10.1007/s00335001-0003-z. PMID 11420617.
• Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ (Apr 2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis". Rna 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.
• Hofmann Y, Wirth B (Aug 2002). "hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta1". Human Molecular Genetics 11 (17): 2037–49. doi:10.1093/hmg/11.17.2037. PMID 12165565.
• Angenstein F, Evans AM, Settlage RE, Moran ST, Ling SC, Klintsova AY, Shabanowitz J, Hunt DF, Greenough WT (Oct 2002). "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. PMID 12388589.
• Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG (Nov 2003). "Regulation of alternative splicing by SRrp86 and its interacting proteins". Molecular and Cellular Biology 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMC 207616. PMID 14559993.
• 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. PMID 15144186.
• Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "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. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
• Ong SE, Mittler G, Mann M (Nov 2004). "Identifying and quantifying in vivo methylation sites by heavy methyl SILAC". Nature Methods 1 (2): 119–26. doi:10.1038/nmeth715. PMID 15782174.