dbPTM

RBMX_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBMX_MOUSE
UniProt AC	Q9WV02
Protein Name	RNA-binding motif protein, X chromosome
Gene Name	Rbmx
Organism	Mus musculus (Mouse).
Sequence Length	391
Subcellular Localization	Nucleus. Localizes in numerous small granules in the nucleus (By similarity). Component of ribonucleosomes..
Protein Description	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. Plays also 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..
Protein Sequence	MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGLPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFTMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGLGGRAPVSRGRDGYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSREYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQERGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MVEADRPG -------CCCCCCCC	5.77	-
2	Acetylation	------MVEADRPGK ------CCCCCCCCC	9.26	-
9	Ubiquitination	VEADRPGKLFIGGLN CCCCCCCCEEECCCC	42.79	22790023
22	Ubiquitination	LNTETNEKALEAVFG CCCCCCHHHHHHHHH	61.41	22790023
30	Acetylation	ALEAVFGKYGRIVEV HHHHHHHHHHHHHEE	32.82	23806337
30	Ubiquitination	ALEAVFGKYGRIVEV HHHHHHHHHHHHHEE	32.82	22790023
55	Phosphorylation	SRGFAFVTFESPADA CCCEEEEEECCCCHH	18.41	23984901
58	Phosphorylation	FAFVTFESPADAKDA EEEEEECCCCHHHHH	22.61	26824392
73	Phosphorylation	ARDMNGKSLDGKAIK HHHHCCCCCCCCEEE	32.84	-
85	Phosphorylation	AIKVEQATKPSFESG EEEEEECCCCCCCCC	43.09	25619855
86	Ubiquitination	IKVEQATKPSFESGR EEEEECCCCCCCCCC	41.50	27667366
86	Malonylation	IKVEQATKPSFESGR EEEEECCCCCCCCCC	41.50	26320211
88	Phosphorylation	VEQATKPSFESGRRG EEECCCCCCCCCCCC	43.11	23684622
91	Phosphorylation	ATKPSFESGRRGLPP CCCCCCCCCCCCCCC	35.27	23684622
94	Methylation	PSFESGRRGLPPPPR CCCCCCCCCCCCCCH	55.30	58859261
101	Methylation	RGLPPPPRSRGPPRG CCCCCCCHHCCCCCC	44.77	24411133
103	Methylation	LPPPPRSRGPPRGLR CCCCCHHCCCCCCCC	64.02	58859269
116	Phosphorylation	LRGGRGGSGGTRGPP CCCCCCCCCCCCCCC	36.55	25266776
119	Phosphorylation	GRGGSGGTRGPPSRG CCCCCCCCCCCCCCC	35.66	30635358
124	Phosphorylation	GGTRGPPSRGGHMDD CCCCCCCCCCCCCCC	46.84	25266776
125	Methylation	GTRGPPSRGGHMDDG CCCCCCCCCCCCCCC	61.97	12018773
125	Asymmetric dimethylarginine	GTRGPPSRGGHMDDG CCCCCCCCCCCCCCC	61.97	-
144	Methylation	NFTMSSSRGPLPVKR EEEECCCCCCCCCCC	53.34	24129315
150	Ubiquitination	SRGPLPVKRGPPPRS CCCCCCCCCCCCCCC	50.09	27667366
150	Acetylation	SRGPLPVKRGPPPRS CCCCCCCCCCCCCCC	50.09	4264811
150	Malonylation	SRGPLPVKRGPPPRS CCCCCCCCCCCCCCC	50.09	26320211
157	Phosphorylation	KRGPPPRSGGPPPKR CCCCCCCCCCCCCCC	54.60	19854140
164	Methylation	SGGPPPKRSAPSGPV CCCCCCCCCCCCCCC	43.77	24129315
165	Phosphorylation	GGPPPKRSAPSGPVR CCCCCCCCCCCCCCC	51.13	-
168	Phosphorylation	PPKRSAPSGPVRSSS CCCCCCCCCCCCCCC	56.28	19144319
172	Methylation	SAPSGPVRSSSGLGG CCCCCCCCCCCCCCC	33.67	24129315
173	Phosphorylation	APSGPVRSSSGLGGR CCCCCCCCCCCCCCC	29.14	29899451
174	Phosphorylation	PSGPVRSSSGLGGRA CCCCCCCCCCCCCCC	20.19	25521595
175	Phosphorylation	SGPVRSSSGLGGRAP CCCCCCCCCCCCCCC	39.00	20415495
184	Phosphorylation	LGGRAPVSRGRDGYG CCCCCCCCCCCCCCC	28.14	27600695
185	Methylation	GGRAPVSRGRDGYGG CCCCCCCCCCCCCCC	44.38	-
201	Phosphorylation	PRREPLPSRRDVYLS CCCCCCCCCCCCEEC	47.86	29176673
206	Phosphorylation	LPSRRDVYLSPRDDG CCCCCCCEECCCCCC	13.02	24925903
208	Phosphorylation	SRRDVYLSPRDDGYS CCCCCEECCCCCCCC	10.53	24925903
214	Phosphorylation	LSPRDDGYSTKDSYS ECCCCCCCCCCCCCC	21.84	28833060
215	Phosphorylation	SPRDDGYSTKDSYSS CCCCCCCCCCCCCCC	34.21	24925903
216	Phosphorylation	PRDDGYSTKDSYSSR CCCCCCCCCCCCCCC	30.32	28833060
217	Acetylation	RDDGYSTKDSYSSRE CCCCCCCCCCCCCCC	38.44	23806337
217	Ubiquitination	RDDGYSTKDSYSSRE CCCCCCCCCCCCCCC	38.44	22790023
219	Phosphorylation	DGYSTKDSYSSREYP CCCCCCCCCCCCCCC	28.59	23684622
221	Phosphorylation	YSTKDSYSSREYPSS CCCCCCCCCCCCCCC	27.20	23684622
228	Phosphorylation	SSREYPSSRDTRDYA CCCCCCCCCCCCCCC	29.66	29899451
243	Phosphorylation	PPPRDYTYRDYGHSS CCCCCCCCCCCCCCC	8.68	-
246	Phosphorylation	RDYTYRDYGHSSSRD CCCCCCCCCCCCCCC	14.03	29472430
249	Phosphorylation	TYRDYGHSSSRDDYP CCCCCCCCCCCCCCC	26.16	23684622
250	Phosphorylation	YRDYGHSSSRDDYPS CCCCCCCCCCCCCCC	24.58	29899451
251	Phosphorylation	RDYGHSSSRDDYPSR CCCCCCCCCCCCCCC	42.62	27681418
255	Phosphorylation	HSSSRDDYPSRGYSD CCCCCCCCCCCCCCC	13.85	29899451
260	Phosphorylation	DDYPSRGYSDRDGYG CCCCCCCCCCCCCCC	13.29	-
261	Phosphorylation	DYPSRGYSDRDGYGR CCCCCCCCCCCCCCC	29.06	-
272	Phosphorylation	GYGRDRDYSDHPSGG CCCCCCCCCCCCCCC	19.52	25367039
273	Phosphorylation	YGRDRDYSDHPSGGS CCCCCCCCCCCCCCC	33.46	23684622
277	Phosphorylation	RDYSDHPSGGSYRDS CCCCCCCCCCCCCCC	52.98	26643407
280	Phosphorylation	SDHPSGGSYRDSYES CCCCCCCCCCCCHHH	22.11	26643407
281	Phosphorylation	DHPSGGSYRDSYESY CCCCCCCCCCCHHHC	23.01	26643407
284	Phosphorylation	SGGSYRDSYESYGNS CCCCCCCCHHHCCCC	23.08	26643407
285	Phosphorylation	GGSYRDSYESYGNSR CCCCCCCHHHCCCCC	17.12	25159016
287	Phosphorylation	SYRDSYESYGNSRSA CCCCCHHHCCCCCCC	30.06	25159016
288	Phosphorylation	YRDSYESYGNSRSAP CCCCHHHCCCCCCCC	14.37	26643407
291	Phosphorylation	SYESYGNSRSAPPTR CHHHCCCCCCCCCCC	24.21	27841257
293	Phosphorylation	ESYGNSRSAPPTRGP HHCCCCCCCCCCCCC	44.97	26643407
297	Phosphorylation	NSRSAPPTRGPPPSY CCCCCCCCCCCCCCC	47.39	29514104
298	Methylation	SRSAPPTRGPPPSYG CCCCCCCCCCCCCCC	62.49	54558713
303	Phosphorylation	PTRGPPPSYGGSSRY CCCCCCCCCCCCCCC	42.03	27149854
307	Phosphorylation	PPPSYGGSSRYDDYS CCCCCCCCCCCCCCC	13.79	27149854
310	Phosphorylation	SYGGSSRYDDYSSSR CCCCCCCCCCCCCCC	18.34	25777480
313	Phosphorylation	GSSRYDDYSSSRDGY CCCCCCCCCCCCCCC	13.93	26643407
314	Phosphorylation	SSRYDDYSSSRDGYG CCCCCCCCCCCCCCC	28.91	26643407
315	Phosphorylation	SRYDDYSSSRDGYGG CCCCCCCCCCCCCCC	24.14	26525534
316	Phosphorylation	RYDDYSSSRDGYGGS CCCCCCCCCCCCCCC	28.57	25521595
320	Phosphorylation	YSSSRDGYGGSRDSY CCCCCCCCCCCCCCC	23.70	25159016
323	Phosphorylation	SRDGYGGSRDSYSSS CCCCCCCCCCCCCCC	28.66	25159016
326	Phosphorylation	GYGGSRDSYSSSRSD CCCCCCCCCCCCHHH	26.29	23527152
327	Phosphorylation	YGGSRDSYSSSRSDL CCCCCCCCCCCHHHH	19.50	25619855
328	Phosphorylation	GGSRDSYSSSRSDLY CCCCCCCCCCHHHHH	26.28	23527152
329	Phosphorylation	GSRDSYSSSRSDLYS CCCCCCCCCHHHHHH	22.87	25168779
330	Phosphorylation	SRDSYSSSRSDLYSS CCCCCCCCHHHHHHC	29.84	25521595
332	Phosphorylation	DSYSSSRSDLYSSGR CCCCCCHHHHHHCCC	33.64	21082442
335	Phosphorylation	SSSRSDLYSSGRDRV CCCHHHHHHCCCCCC	13.04	25619855
336	Phosphorylation	SSRSDLYSSGRDRVG CCHHHHHHCCCCCCC	33.35	25619855
337	Phosphorylation	SRSDLYSSGRDRVGR CHHHHHHCCCCCCCC	25.04	25619855
352	Phosphorylation	QERGLPPSMERGYPP CCCCCCCHHHCCCCC	31.19	27087446
357	Phosphorylation	PPSMERGYPPPRDSY CCHHHCCCCCCCCCC	20.84	23984901
361	Methylation	ERGYPPPRDSYSSSS HCCCCCCCCCCCCCC	51.81	16188517

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of RBMX_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
182	R	Methylation		-
Arg-182 is dimethylated, probably to asymmetric dimethylarginine.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of RBMX_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RBMX_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RBMX_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-208, ANDMASS SPECTROMETRY.	19144319 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.	16452087 [Abstract]

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