Details for: RBMX
Associated with
Significant Cells
Cell Significance Index (CSI) scores for the chosen context(s)
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CSI 111.36rCSI 74.02%PRS 21.26
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CSI 87.98rCSI 79.45%PRS 15.88
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CSI 81.34rCSI 65.77%PRS 17.67
-
CSI 77.43rCSI 61.2%PRS 12.1
-
CSI 71rCSI 81.99%PRS 15.47
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CSI 69.85rCSI 83.84%PRS 17.31
-
CSI 65.92rCSI 63.57%PRS 12.64
-
CSI 63.5rCSI 88.21%PRS 18.09
-
CSI 62.87rCSI 65.71%PRS 18.47
-
CSI 62.72rCSI 55.09%PRS 20.25
-
CSI 59.35rCSI 67.94%PRS 35.81
-
CSI 57.89rCSI 72.65%PRS 22.85
-
CSI 52.21rCSI 45.21%PRS 19.87
-
CSI 47.64rCSI 55.95%PRS 20.59
-
CSI 46.3rCSI 66.07%PRS 19.81
-
CSI 45.23rCSI 37.5%PRS 16.71
-
CSI 43.39rCSI 59.12%PRS 15.68
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CSI 40.92rCSI 33.89%PRS 17.88
-
CSI 37.57rCSI 48.22%PRS 17.11
-
CSI 36.66rCSI 30.73%PRS 21.08
-
CSI 34.18rCSI 49.05%PRS 13.65
-
CSI 33.8rCSI 48.75%PRS 24.74
-
CSI 31.07rCSI 49.57%PRS 15.14
-
CSI 29.19rCSI 39%PRS 33.54
-
CSI 28.51rCSI 27.44%PRS 18.28
-
CSI 28.39rCSI 38.82%PRS 27.9
-
CSI 25.98rCSI 74.18%PRS 30.34
-
CSI 25.5rCSI 70.06%PRS 28.98
-
CSI 25.49rCSI 25.98%PRS 25.38
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CSI 25.25rCSI 81.01%PRS 25.44
-
CSI 24.68rCSI 87.73%PRS 52.53
-
CSI 23.99rCSI 57.02%PRS 26.43
-
CSI 22.48rCSI 43.72%PRS 18.05
-
CSI 22.35rCSI 38.29%PRS 23.98
-
CSI 20.98rCSI 56.55%PRS 22.83
-
CSI 20.45rCSI 27.18%PRS 19.33
-
CSI 20.35rCSI 79.2%PRS 29.07
-
CSI 19.37rCSI 16.84%PRS 22.07
-
CSI 18.34rCSI 53.11%PRS 19.94
-
CSI 17.91rCSI 92.5%PRS 34.33
-
CSI 16.28rCSI 14.31%PRS 12.83
-
CSI 15.92rCSI 38.31%PRS 27.98
-
CSI 15.37rCSI 32.7%PRS 28.49
-
CSI 15.35rCSI 20.97%PRS 19.56
-
CSI 14.7rCSI 22.59%PRS 24.37
-
CSI 13.76rCSI 28.24%PRS 38.69
-
CSI 13.7rCSI 73.1%PRS 59.39
-
CSI 13.09rCSI 85.88%PRS 44.3
-
CSI 12.94rCSI 32.87%PRS 17.81
-
CSI 12.31rCSI 29.59%PRS 26.17
-
CSI 12.23rCSI 11.29%PRS 18.23
-
CSI 12.22rCSI 36.44%PRS 41.39
-
CSI 11.87rCSI 18.12%PRS 17.76
-
CSI 11.83rCSI 29.64%PRS 48.23
-
CSI 11.71rCSI 17.92%PRS 28.58
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CSI 11.11rCSI 7.73%PRS 21.03
-
CSI 11.01rCSI 38.64%PRS 31.03
-
CSI 10.4rCSI 9.23%PRS 17.73
-
CSI 10.29rCSI 45.18%PRS 32.74
-
CSI 9.89rCSI 6.9%PRS 18.78
-
CSI 9.32rCSI 54.21%PRS 26.32
-
CSI 9.09rCSI 25.48%PRS 27.32
-
CSI 8.9rCSI 11.33%PRS 20.52
-
CSI 8.89rCSI 41.68%PRS 44.37
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CSI 8.5rCSI 54.48%PRS 26.65
-
CSI 8.42rCSI 24.85%PRS 21.3
-
CSI 8.42rCSI 6.53%PRS 16.9
-
CSI 8.27rCSI 17.49%PRS 35.26
-
CSI 8.22rCSI 8.61%PRS 18.86
-
CSI 8.12rCSI 43.8%PRS 31.46
-
CSI 8.02rCSI 7.02%PRS 23.51
-
CSI 7.5rCSI 15.42%PRS 17.61
-
CSI 7.13rCSI 40.88%PRS 26.9
-
CSI 6.76rCSI 8.41%PRS 18.72
-
CSI 6.59rCSI 14.44%PRS 23.66
-
CSI 6.54rCSI 7.36%PRS 28.37
-
CSI 6.47rCSI 9.55%PRS 27.59
-
CSI 6.32rCSI 6.5%PRS 28.67
-
CSI 6.27rCSI 92.7%PRS 42.33
-
CSI 6.24rCSI 20.9%PRS 12.34
-
CSI 5.83rCSI 43.78%PRS 32.11
-
CSI 5.51rCSI 5.21%PRS 18.47
-
CSI 5.48rCSI 52%PRS 63.44
-
CSI 5.43rCSI 18.35%PRS 28.57
-
CSI 5.41rCSI 9.84%PRS 26.91
-
CSI 5.4rCSI 15.79%PRS 51.76
-
CSI 5.32rCSI 15.39%PRS 37.81
-
CSI 5.27rCSI 6.1%PRS 12.97
-
CSI 5.15rCSI 10.35%PRS 13.06
-
CSI 5.08rCSI 13.2%PRS 44.67
-
CSI 4.99rCSI 6.83%PRS 19.99
-
CSI 4.93rCSI 6.82%PRS 25.13
-
CSI 4.87rCSI 89.16%PRS 50.11
-
CSI 4.86rCSI 9.65%PRS 18.7
-
CSI 4.82rCSI 6.05%PRS 64.08
-
CSI 4.76rCSI 3.75%PRS 21.31
-
CSI 4.74rCSI 7.25%PRS 22.71
-
CSI 4.7rCSI 3.53%PRS 18.66
-
CSI 4.55rCSI 3.2%PRS 42.16
-
CSI 4.34rCSI 4.49%PRS 20.76
-
CSI -5.3rCSI -9.9%PRS 12.7%
-
CSI -4.3rCSI -12.7%PRS 24.9%
-
CSI -3.6rCSI -3.3%PRS 20.6%
-
CSI -2.8rCSI -3.2%PRS 23.9%
-
CSI -2.4rCSI -6.3%PRS 21.1%
-
CSI -2.3rCSI -6.9%PRS 16.0%
-
CSI -1.7rCSI -2.1%PRS 10.9%
-
CSI -1.4rCSI -8.2%PRS 22.7%
-
CSI -1.1rCSI -1.8%PRS 11.3%
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CSI -1.0rCSI -2.9%PRS 31.0%
-
CSI -0.8rCSI -1.8%PRS 20.4%
-
CSI -0.8rCSI -5.1%PRS 44.9%
-
CSI -0.8rCSI -1.9%PRS 10.2%
-
CSI -0.8rCSI -3.8%PRS 21.7%
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CSI -0.8rCSI -1.0%PRS 23.2%
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CSI -0.7rCSI -1.8%PRS 16.2%
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CSI -0.6rCSI -6.2%PRS 19.8%
-
CSI -0.6rCSI -11.2%PRS 79.4%
-
CSI -0.6rCSI -2.5%PRS 16.8%
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CSI -0.6rCSI -1.8%PRS 13.6%
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CSI -0.5rCSI -4.0%PRS 10.8%
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CSI -0.3rCSI -0.6%PRS 10.4%
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CSI -0.3rCSI -0.8%PRS 26.1%
-
CSI -0.3rCSI -0.4%PRS 25.1%
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CSI -0.2rCSI -0.2%PRS 9.7%
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CSI -0.1rCSI -0.4%PRS 25.9%
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CSI 0.0rCSI 0.1%PRS 60.7%
-
CSI 0.0rCSI 0.1%PRS 10.8%
-
CSI 0.1rCSI 0.2%PRS 11.1%
-
CSI 0.1rCSI 1.6%PRS 14.9%
-
CSI 0.1rCSI 0.1%PRS 20.2%
-
CSI 0.1rCSI 0.7%PRS 60.9%
-
CSI 0.1rCSI 2.2%PRS 71.6%
-
CSI 0.1rCSI 1.5%PRS 54.5%
-
CSI 0.1rCSI 1.7%PRS 89.6%
-
CSI 0.1rCSI 0.3%PRS 44.0%
-
CSI 0.1rCSI 0.2%PRS 18.7%
-
CSI 0.2rCSI 0.9%PRS 9.1%
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CSI 0.2rCSI 1.6%PRS 54.0%
-
CSI 0.2rCSI 0.3%PRS 17.8%
-
CSI 0.2rCSI 3.2%PRS 50.4%
-
CSI 0.2rCSI 1.1%PRS 13.7%
-
CSI 0.2rCSI 1.5%PRS 52.4%
-
CSI 0.2rCSI 1.1%PRS 63.0%
-
CSI 0.2rCSI 0.9%PRS 24.0%
-
CSI 0.3rCSI 1.3%PRS 39.8%
-
CSI 0.3rCSI 5.9%PRS 13.8%
-
CSI 0.3rCSI 0.6%PRS 39.1%
-
CSI 0.3rCSI 1.7%PRS 10.9%
-
CSI 0.3rCSI 6.4%PRS 77.7%
-
CSI 0.3rCSI 1.3%PRS 24.1%
-
CSI 0.3rCSI 0.7%PRS 34.6%
-
CSI 0.3rCSI 1.9%PRS 55.7%
-
CSI 0.3rCSI 0.7%PRS 39.3%
-
CSI 0.4rCSI 0.6%PRS 16.3%
-
CSI 0.4rCSI 0.8%PRS 31.5%
-
CSI 0.4rCSI 1.6%PRS 17.3%
-
CSI 0.4rCSI 9.6%PRS 68.1%
-
CSI 0.4rCSI 0.5%PRS 30.8%
-
CSI 0.4rCSI 1.8%PRS 36.5%
-
CSI 0.4rCSI 1.7%PRS 15.0%
-
CSI 0.4rCSI 3.0%PRS 49.6%
-
CSI 0.4rCSI 2.0%PRS 9.9%
-
CSI 0.5rCSI 0.6%PRS 17.5%
-
CSI 0.5rCSI 5.0%PRS 53.5%
-
CSI 0.5rCSI 2.8%PRS 44.0%
-
CSI 0.5rCSI 1.2%PRS 17.4%
-
CSI 0.5rCSI 0.8%PRS 23.2%
-
CSI 0.5rCSI 1.4%PRS 20.4%
-
CSI 0.5rCSI 2.5%PRS 23.3%
-
CSI 0.5rCSI 1.9%PRS 10.7%
-
CSI 0.5rCSI 5.4%PRS 23.4%
-
CSI 0.5rCSI 1.3%PRS 13.4%
-
CSI 0.5rCSI 1.3%PRS 34.2%
-
CSI 0.5rCSI 0.7%PRS 27.2%
-
CSI 0.5rCSI 0.7%PRS 24.4%
-
CSI 0.5rCSI 2.1%PRS 24.3%
-
CSI 0.5rCSI 1.3%PRS 71.3%
-
CSI 0.5rCSI 2.3%PRS 31.0%
-
CSI 0.5rCSI 0.4%PRS 18.7%
-
CSI 0.5rCSI 1.9%PRS 9.8%
-
CSI 0.5rCSI 3.4%PRS 53.3%
-
CSI 0.5rCSI 3.6%PRS 18.2%
-
CSI 0.6rCSI 1.0%PRS 13.5%
-
CSI 0.6rCSI 1.2%PRS 12.6%
-
CSI 0.6rCSI 2.7%PRS 13.1%
-
CSI 0.6rCSI 2.1%PRS 24.3%
-
CSI 0.6rCSI 1.4%PRS 16.3%
-
CSI 0.6rCSI 2.2%PRS 56.9%
-
CSI 0.6rCSI 1.1%PRS 14.6%
-
CSI 0.6rCSI 0.7%PRS 25.8%
-
CSI 0.6rCSI 0.7%PRS 10.2%
-
CSI 0.6rCSI 3.5%PRS 45.7%
-
CSI 0.6rCSI 3.7%PRS 58.1%
-
CSI 0.6rCSI 6.1%PRS 46.9%
-
CSI 0.6rCSI 1.0%PRS 31.1%
-
CSI 0.6rCSI 4.6%PRS 46.2%
-
CSI 0.6rCSI 3.5%PRS 31.4%
-
CSI 0.6rCSI 2.0%PRS 26.4%
-
CSI 0.7rCSI 1.1%PRS 20.8%
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration
Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.
Legend:
- Query Gene
-
Node Color (Target Cell CSI, relative to current network):
- Very High
- High
- Medium
- Low
- Very Low
- CSI N/A
- Node Size: Proportional to Target Cell CSI magnitude
- STRING PPI Edge
- Shared Pathway Edge (ONTOLOGY)
Other Information
This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.
Genular Protein ID: 617492948
Symbol: RBMX_HUMAN
Name: RNA-binding motif protein, X chromosome
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 7692398
Title: hnRNP G: sequence and characterization of a glycosylated RNA-binding protein.
PubMed ID: 7692398
PubMed ID: 11420617
Title: Expression and conservation of processed copies of the RBMX gene.
PubMed ID: 11420617
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 15772651
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 10332027
Title: T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis.
PubMed ID: 10332027
DOI: 10.1093/hmg/8.6.959
PubMed ID: 11991638
Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
PubMed ID: 11991638
PubMed ID: 12165565
Title: hnRNP-G promotes exon 7 inclusion of survival motor neuron (SMN) via direct interaction with Htra2-beta1.
PubMed ID: 12165565
PubMed ID: 12761049
Title: HnRNP G and Tra2beta: opposite effects on splicing matched by antagonism in RNA binding.
PubMed ID: 12761049
DOI: 10.1093/hmg/ddg136
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16707624
Title: Heterogeneous nuclear ribonucleoprotein G shows tumor suppressive effect against oral squamous cell carcinoma cells.
PubMed ID: 16707624
PubMed ID: 17890166
Title: The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.
PubMed ID: 17890166
PubMed ID: 18445477
Title: An association between RBMX, a heterogeneous nuclear ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release.
PubMed ID: 18445477
PubMed ID: 18541147
Title: hnRNP G elicits tumor-suppressive activity in part by upregulating the expression of Txnip.
PubMed ID: 18541147
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19282290
Title: Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA.
PubMed ID: 19282290
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 21327109
Title: Novel domains in the hnRNP G/RBMX protein with distinct roles in RNA binding and targeting nascent transcripts.
PubMed ID: 21327109
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25678563
Title: Peptidylprolyl isomerase A governs TARDBP function and assembly in heterogeneous nuclear ribonucleoprotein complexes.
PubMed ID: 25678563
DOI: 10.1093/brain/awv005
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
PubMed ID: 25256757
Title: The RBMX gene as a candidate for the Shashi X-linked intellectual disability syndrome.
PubMed ID: 25256757
DOI: 10.1111/cge.12511
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 37277488
Title: Gustavson syndrome is caused by an in-frame deletion in RBMX associated with potentially disturbed SH3 domain interactions.
PubMed ID: 37277488
Sequence Information:
- Length: 391
- Mass: 42332
- Checksum: 904FEB9BFC573546
- Sequence:
MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEVLLM KDRETNKSRG FAFVTFESPA DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGRGGSGGTR GPPSRGGHMD DGGYSMNFNM SSSRGPLPVK RGPPPRSGGP PPKRSAPSGP VRSSSGMGGR APVSRGRDSY GGPPRREPLP SRRDVYLSPR DDGYSTKDSY SSRDYPSSRD TRDYAPPPRD YTYRDYGHSS SRDDYPSRGY SDRDGYGRDR DYSDHPSGGS YRDSYESYGN SRSAPPTRGP PPSYGGSSRY DDYSSSRDGY GGSRDSYSSS RSDLYSSGRD RVGRQERGLP PSMERGYPPP RDSYSSSSRG APRGGGRGGS RSDRGGGRSR Y