General Information of Target

Target ID LDTP03850
Target Name RNA-binding motif protein, X chromosome (RBMX)
Gene Name RBMX
Gene ID 27316
Synonyms
HNRPG; RBMXP1; RNA-binding motif protein, X chromosome; Glycoprotein p43; Heterogeneous nuclear ribonucleoprotein G; hnRNP G) [Cleaved into: RNA-binding motif protein, X chromosome, N-terminally processed]
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPA
DAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGRGGSGGTR
GPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGR
APVSRGRDSYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRD
YTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGP
PPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQERGLPPSMERGYPPP
RDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY
Target Bioclass
Other
Subcellular location
Nucleus
Function
RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment.
Uniprot ID
P38159
Ensemble ID
ENST00000320676.11
HGNC ID
HGNC:9910

Target Site Mutations in Different Cell Lines

Cell line Mutation details Probe for labeling this protein in this cell
786O SNV: p.T19K .
AN3CA SNV: p.M177T .
DU145 SNV: p.G319A .
JURKAT SNV: p.R252H .
LNCaP clone FGC Deletion: p.Y357TfsTer82 .

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 18 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
A-EBA
 Probe Info 
3.66  LDD0215  [1]
TH211
 Probe Info 
Y272(20.00); Y246(17.43); Y241(14.01); Y310(13.32)  LDD0260  [2]
C-Sul
 Probe Info 
8.42  LDD0066  [3]
AZ-9
 Probe Info 
D312(0.95); E36(1.21)  LDD2208  [4]
ONAyne
 Probe Info 
K86(0.00); K163(0.00)  LDD0273  [5]
OPA-S-S-alkyne
 Probe Info 
K63(1.66); K86(2.06); K163(3.88); K217(8.01)  LDD3494  [6]
Probe 1
 Probe Info 
Y190(32.20); Y206(38.76); Y214(93.32); Y225(21.11)  LDD3495  [7]
5E-2FA
 Probe Info 
H275(0.00); H248(0.00); H128(0.00)  LDD2235  [8]
AMP probe
 Probe Info 
N.A.  LDD0200  [9]
ATP probe
 Probe Info 
K80(0.00); K86(0.00); K77(0.00); K30(0.00)  LDD0199  [9]
m-APA
 Probe Info 
H275(0.00); H128(0.00)  LDD2231  [8]
ATP probe
 Probe Info 
K86(0.00); K41(0.00)  LDD0035  [10]
1d-yne
 Probe Info 
K80(0.00); K63(0.00); K77(0.00)  LDD0356  [11]
NHS
 Probe Info 
K63(0.00); K30(0.00); K86(0.00); K9(0.00)  LDD0010  [12]
OSF
 Probe Info 
Y357(0.00); Y304(0.00); Y234(0.00); Y335(0.00)  LDD0029  [13]
SF
 Probe Info 
K63(0.00); Y313(0.00); Y288(0.00); Y243(0.00)  LDD0028  [13]
STPyne
 Probe Info 
K86(0.00); K217(0.00)  LDD0009  [12]
1c-yne
 Probe Info 
K80(0.00); K9(0.00)  LDD0228  [11]
PAL-AfBPP Probe
Click To Hide/Show 29 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
C040
 Probe Info 
6.59  LDD1740  [14]
C041
 Probe Info 
6.82  LDD1741  [14]
C063
 Probe Info 
12.73  LDD1760  [14]
C087
 Probe Info 
9.32  LDD1779  [14]
C139
 Probe Info 
10.63  LDD1821  [14]
C145
 Probe Info 
8.75  LDD1827  [14]
C165
 Probe Info 
18.51  LDD1845  [14]
C232
 Probe Info 
47.50  LDD1905  [14]
C302
 Probe Info 
5.70  LDD1971  [14]
C313
 Probe Info 
14.62  LDD1980  [14]
C314
 Probe Info 
11.16  LDD1981  [14]
C338
 Probe Info 
19.03  LDD2001  [14]
C346
 Probe Info 
10.63  LDD2007  [14]
C348
 Probe Info 
11.71  LDD2009  [14]
C353
 Probe Info 
7.67  LDD2014  [14]
C355
 Probe Info 
32.22  LDD2016  [14]
C361
 Probe Info 
25.81  LDD2022  [14]
C390
 Probe Info 
21.11  LDD2049  [14]
C391
 Probe Info 
18.51  LDD2050  [14]
FFF probe11
 Probe Info 
13.55  LDD0471  [15]
FFF probe12
 Probe Info 
5.79  LDD0473  [15]
FFF probe13
 Probe Info 
18.11  LDD0475  [15]
FFF probe14
 Probe Info 
11.65  LDD0477  [15]
FFF probe2
 Probe Info 
17.95  LDD0463  [15]
FFF probe3
 Probe Info 
12.88  LDD0464  [15]
FFF probe6
 Probe Info 
5.22  LDD0467  [15]
FFF probe9
 Probe Info 
6.19  LDD0470  [15]
JN0003
 Probe Info 
11.71  LDD0469  [15]
OEA-DA
 Probe Info 
7.36  LDD0046  [16]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Enzyme
Click To Hide/Show 3 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
DNA dC->dU-editing enzyme APOBEC-3C (APOBEC3C) Cytidine and deoxycytidylate deaminase family Q9NRW3
Dual specificity protein kinase CLK3 (CLK3) CMGC Ser/Thr protein kinase family P49761
E3 ubiquitin-protein ligase LNX (LNX1) . Q8TBB1
Transporter and channel
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Metal transporter CNNM3 (CNNM3) ACDP family Q8NE01
Transcription factor
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
Myb-related transcription factor, partner of profilin (MYPOP) . Q86VE0
Cytokine and receptor
Click To Hide/Show 1 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
CKLF-like MARVEL transmembrane domain-containing protein 6 (CMTM6) Chemokine-like factor family Q9NX76
Other
Click To Hide/Show 21 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
KH domain-containing, RNA-binding, signal transduction-associated protein 2 (KHDRBS2) KHDRBS family Q5VWX1
KH domain-containing, RNA-binding, signal transduction-associated protein 3 (KHDRBS3) KHDRBS family O75525
Protein mago nashi homolog 2 (MAGOHB) Mago nashi family Q96A72
U4/U6 small nuclear ribonucleoprotein Prp31 (PRPF31) PRP31 family Q8WWY3
RNA-binding protein FUS (FUS) RRM TET family P35637
U1 small nuclear ribonucleoprotein A (SNRPA) RRM U1 A/B'' family P09012
Nyctalopin (NYX) Small leucine-rich proteoglycan (SLRP) family Q9GZU5
SOSS complex subunit B2 (NABP1) SOSS-B family Q96AH0
Serine/arginine-rich splicing factor 3 (SRSF3) Splicing factor SR family P84103
Serine/arginine-rich splicing factor 9 (SRSF9) Splicing factor SR family Q13242
Transformer-2 protein homolog beta (TRA2B) Splicing factor SR family P62995
Cold-inducible RNA-binding protein (CIRBP) . Q14011
Heterogeneous nuclear ribonucleoprotein K (HNRNPK) . P61978
Proline-rich protein 3 (PRR3) . P79522
Protocadherin beta-14 (PCDHB14) . Q9Y5E9
RNA-binding motif protein, X chromosome (RBMX) . P38159
RNA-binding motif protein, Y chromosome, family 1 member A1 (RBMY1A1) . P0DJD3
RNA-binding motif protein, Y chromosome, family 1 member E (RBMY1E) . A6NEQ0
RNA-binding motif protein, Y chromosome, family 1 member F/J (RBMY1F; RBMY1J) . Q15415
RNA-binding protein 3 (RBM3) . P98179
TAR DNA-binding protein 43 (TARDBP) . Q13148

References

1 2-Ethynylbenzaldehyde-Based, Lysine-Targeting Irreversible Covalent Inhibitors for Protein Kinases and Nonkinases. J Am Chem Soc. 2023 Feb 12. doi: 10.1021/jacs.2c11595. Online ahead of print.
Mass spectrometry data entry: PXD037665
2 Chemoproteomic profiling of kinases in live cells using electrophilic sulfonyl triazole probes. Chem Sci. 2021 Jan 21;12(9):3295-3307. doi: 10.1039/d0sc06623k.
3 Low-Toxicity Sulfonium-Based Probes for Cysteine-Specific Profiling in Live Cells. Anal Chem. 2022 Mar 15;94(10):4366-4372. doi: 10.1021/acs.analchem.1c05129. Epub 2022 Mar 4.
4 2H-Azirine-Based Reagents for Chemoselective Bioconjugation at Carboxyl Residues Inside Live Cells. J Am Chem Soc. 2020 Apr 1;142(13):6051-6059. doi: 10.1021/jacs.9b12116. Epub 2020 Mar 23.
5 A Paal-Knorr agent for chemoproteomic profiling of targets of isoketals in cells. Chem Sci. 2021 Oct 15;12(43):14557-14563. doi: 10.1039/d1sc02230j. eCollection 2021 Nov 10.
Mass spectrometry data entry: PXD028270
6 A chemical proteomics approach for global mapping of functional lysines on cell surface of living cell. Nat Commun. 2024 Apr 8;15(1):2997. doi: 10.1038/s41467-024-47033-w.
Mass spectrometry data entry: PXD042888
7 An Azo Coupling-Based Chemoproteomic Approach to Systematically Profile the Tyrosine Reactivity in the Human Proteome. Anal Chem. 2021 Jul 27;93(29):10334-10342. doi: 10.1021/acs.analchem.1c01935. Epub 2021 Jul 12.
8 Global profiling of functional histidines in live cells using small-molecule photosensitizer and chemical probe relay labelling. Nat Chem. 2024 Jun 4. doi: 10.1038/s41557-024-01545-6. Online ahead of print.
Mass spectrometry data entry: PXD042377
9 Targeted Proteomic Approaches for Proteome-Wide Characterizations of the AMP-Binding Capacities of Kinases. J Proteome Res. 2022 Aug 5;21(8):2063-2070. doi: 10.1021/acs.jproteome.2c00225. Epub 2022 Jul 12.
10 Comparison of Quantitative Mass Spectrometry Platforms for Monitoring Kinase ATP Probe Uptake in Lung Cancer. J Proteome Res. 2018 Jan 5;17(1):63-75. doi: 10.1021/acs.jproteome.7b00329. Epub 2017 Nov 22.
Mass spectrometry data entry: PXD006095 , PXD006096
11 Tunable Amine-Reactive Electrophiles for Selective Profiling of Lysine. Angew Chem Int Ed Engl. 2022 Jan 26;61(5):e202112107. doi: 10.1002/anie.202112107. Epub 2021 Dec 16.
12 A modification-centric assessment tool for the performance of chemoproteomic probes. Nat Chem Biol. 2022 Aug;18(8):904-912. doi: 10.1038/s41589-022-01074-8. Epub 2022 Jul 21.
Mass spectrometry data entry: PXD027758 , PXD027755 , PXD027760 , PXD027762 , PXD027756 , PXD027591 , PXD007149 , PXD030064 , PXD032392 , PXD027789 , PXD027767 , PXD027764
13 Solid Phase Synthesis of Fluorosulfate Containing Macrocycles for Chemoproteomic Workflows. bioRxiv [Preprint]. 2023 Feb 18:2023.02.17.529022. doi: 10.1101/2023.02.17.529022.
Mass spectrometry data entry: PXD039931
14 Large-scale chemoproteomics expedites ligand discovery and predicts ligand behavior in cells. Science. 2024 Apr 26;384(6694):eadk5864. doi: 10.1126/science.adk5864. Epub 2024 Apr 26.
Mass spectrometry data entry: PXD041587
15 Ligand and Target Discovery by Fragment-Based Screening in Human Cells. Cell. 2017 Jan 26;168(3):527-541.e29. doi: 10.1016/j.cell.2016.12.029. Epub 2017 Jan 19.
16 Mapping Protein Targets of Bioactive Small Molecules Using Lipid-Based Chemical Proteomics. ACS Chem Biol. 2017 Oct 20;12(10):2671-2681. doi: 10.1021/acschembio.7b00581. Epub 2017 Sep 20.
Mass spectrometry data entry: PXD007570