dbPTM

RBMX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBMX_HUMAN
UniProt AC	P38159
Protein Name	RNA-binding motif protein, X chromosome
Gene Name	RBMX
Organism	Homo sapiens (Human).
Sequence Length	391
Subcellular Localization	Nucleus . Component of ribonucleosomes. Localizes in numerous small granules in the nucleus.
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	MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQERGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY

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	21890473
9	2-Hydroxyisobutyrylation	VEADRPGKLFIGGLN CCCCCCCCEEECCCC	42.79	-
9	Acetylation	VEADRPGKLFIGGLN CCCCCCCCEEECCCC	42.79	25953088
9	Ubiquitination	VEADRPGKLFIGGLN CCCCCCCCEEECCCC	42.79	23000965
9	Ubiquitination	VEADRPGKLFIGGLN CCCCCCCCEEECCCC	42.79	21890473
17	Phosphorylation	LFIGGLNTETNEKAL EEECCCCCCCCHHHH	49.59	23186163
19	Phosphorylation	IGGLNTETNEKALEA ECCCCCCCCHHHHHH	46.79	30576142
22	2-Hydroxyisobutyrylation	LNTETNEKALEAVFG CCCCCCHHHHHHHHH	61.41	-
22	Acetylation	LNTETNEKALEAVFG CCCCCCHHHHHHHHH	61.41	23749302
22	Neddylation	LNTETNEKALEAVFG CCCCCCHHHHHHHHH	61.41	32015554
22	Sumoylation	LNTETNEKALEAVFG CCCCCCHHHHHHHHH	61.41	28112733
22	Ubiquitination	LNTETNEKALEAVFG CCCCCCHHHHHHHHH	61.41	23000965
30	2-Hydroxyisobutyrylation	ALEAVFGKYGRIVEV HHHHHHHHHHHHHEE	32.82	-
30	Acetylation	ALEAVFGKYGRIVEV HHHHHHHHHHHHHEE	32.82	19608861
30	Ubiquitination	ALEAVFGKYGRIVEV HHHHHHHHHHHHHEE	32.82	23000965
31	Phosphorylation	LEAVFGKYGRIVEVL HHHHHHHHHHHHEEE	16.41	22817900
41	2-Hydroxyisobutyrylation	IVEVLLMKDRETNKS HHEEEEEECCCCCCC	54.31	-
41	Ubiquitination	IVEVLLMKDRETNKS HHEEEEEECCCCCCC	54.31	23000965
47	Ubiquitination	MKDRETNKSRGFAFV EECCCCCCCCCEEEE	49.28	23000965
48	Phosphorylation	KDRETNKSRGFAFVT ECCCCCCCCCEEEEE	39.44	23882029
49	Methylation	DRETNKSRGFAFVTF CCCCCCCCCEEEEEE	45.95	-
55	Phosphorylation	SRGFAFVTFESPADA CCCEEEEEECCCHHH	18.41	30266825
58	Phosphorylation	FAFVTFESPADAKDA EEEEEECCCHHHHHH	22.61	29255136
63	2-Hydroxyisobutyrylation	FESPADAKDAARDMN ECCCHHHHHHHHHHC	48.74	-
63	Acetylation	FESPADAKDAARDMN ECCCHHHHHHHHHHC	48.74	23954790
63	Sumoylation	FESPADAKDAARDMN ECCCHHHHHHHHHHC	48.74	-
63	Ubiquitination	FESPADAKDAARDMN ECCCHHHHHHHHHHC	48.74	27667366
72	Acetylation	AARDMNGKSLDGKAI HHHHHCCCCCCCCEE	42.72	7427301
73	Phosphorylation	ARDMNGKSLDGKAIK HHHHCCCCCCCCEEE	32.84	25849741
77	Acetylation	NGKSLDGKAIKVEQA CCCCCCCCEEEEEEC	46.75	26051181
77	Ubiquitination	NGKSLDGKAIKVEQA CCCCCCCCEEEEEEC	46.75	24816145
80	Sumoylation	SLDGKAIKVEQATKP CCCCCEEEEEECCCC	44.58	-
80	2-Hydroxyisobutyrylation	SLDGKAIKVEQATKP CCCCCEEEEEECCCC	44.58	-
80	Acetylation	SLDGKAIKVEQATKP CCCCCEEEEEECCCC	44.58	23749302
80	Malonylation	SLDGKAIKVEQATKP CCCCCEEEEEECCCC	44.58	32601280
80	Sumoylation	SLDGKAIKVEQATKP CCCCCEEEEEECCCC	44.58	28112733
85	Phosphorylation	AIKVEQATKPSFESG EEEEEECCCCCCCCC	43.09	23927012
86	2-Hydroxyisobutyrylation	IKVEQATKPSFESGR EEEEECCCCCCCCCC	41.50	-
86	Acetylation	IKVEQATKPSFESGR EEEEECCCCCCCCCC	41.50	23749302
86	Malonylation	IKVEQATKPSFESGR EEEEECCCCCCCCCC	41.50	26320211
86	Sumoylation	IKVEQATKPSFESGR EEEEECCCCCCCCCC	41.50	28112733
86	Ubiquitination	IKVEQATKPSFESGR EEEEECCCCCCCCCC	41.50	33845483
88	Phosphorylation	VEQATKPSFESGRRG EEECCCCCCCCCCCC	43.11	29255136
91	Phosphorylation	ATKPSFESGRRGPPP CCCCCCCCCCCCCCC	35.27	29255136
94	Methylation	PSFESGRRGPPPPPR CCCCCCCCCCCCCCC	66.55	58859263
101	Methylation	RGPPPPPRSRGPPRG CCCCCCCCCCCCCCC	44.77	24411129
102	Phosphorylation	GPPPPPRSRGPPRGL CCCCCCCCCCCCCCC	47.57	29496963
103	Methylation	PPPPPRSRGPPRGLR CCCCCCCCCCCCCCC	64.02	58859271
107	Dimethylation	PRSRGPPRGLRGGRG CCCCCCCCCCCCCCC	60.97	-
107	Methylation	PRSRGPPRGLRGGRG CCCCCCCCCCCCCCC	60.97	116195087
110	Dimethylation	RGPPRGLRGGRGGSG CCCCCCCCCCCCCCC	48.63	-
110	Methylation	RGPPRGLRGGRGGSG CCCCCCCCCCCCCCC	48.63	83108741
113	Dimethylation	PRGLRGGRGGSGGTR CCCCCCCCCCCCCCC	49.47	-
113	Methylation	PRGLRGGRGGSGGTR CCCCCCCCCCCCCCC	49.47	83108749
116	Phosphorylation	LRGGRGGSGGTRGPP CCCCCCCCCCCCCCC	36.55	28450419
119	Phosphorylation	GRGGSGGTRGPPSRG CCCCCCCCCCCCCCC	35.66	22496350
124	Phosphorylation	GGTRGPPSRGGHMDD CCCCCCCCCCCCCCC	46.84	23401153
125	Asymmetric dimethylarginine	GTRGPPSRGGHMDDG CCCCCCCCCCCCCCC	61.97	-
125	Methylation	GTRGPPSRGGHMDDG CCCCCCCCCCCCCCC	61.97	12018769
134	Phosphorylation	GHMDDGGYSMNFNMS CCCCCCCEECCCCCC	15.41	21945579
135	Phosphorylation	HMDDGGYSMNFNMSS CCCCCCEECCCCCCC	15.55	21945579
141	Phosphorylation	YSMNFNMSSSRGPLP EECCCCCCCCCCCCC	26.68	23401153
142	Phosphorylation	SMNFNMSSSRGPLPV ECCCCCCCCCCCCCC	17.18	21945579
143	Phosphorylation	MNFNMSSSRGPLPVK CCCCCCCCCCCCCCC	33.67	21945579
144	Methylation	NFNMSSSRGPLPVKR CCCCCCCCCCCCCCC	53.34	30760813
150	2-Hydroxyisobutyrylation	SRGPLPVKRGPPPRS CCCCCCCCCCCCCCC	50.09	-
150	Acetylation	SRGPLPVKRGPPPRS CCCCCCCCCCCCCCC	50.09	23749302
150	Methylation	SRGPLPVKRGPPPRS CCCCCCCCCCCCCCC	50.09	129091
150	Ubiquitination	SRGPLPVKRGPPPRS CCCCCCCCCCCCCCC	50.09	27667366
151	Methylation	RGPLPVKRGPPPRSG CCCCCCCCCCCCCCC	64.18	54558703
156	Methylation	VKRGPPPRSGGPPPK CCCCCCCCCCCCCCC	54.42	54558719
157	Phosphorylation	KRGPPPRSGGPPPKR CCCCCCCCCCCCCCC	54.60	20363803
163	2-Hydroxyisobutyrylation	RSGGPPPKRSAPSGP CCCCCCCCCCCCCCC	65.83	-
163	Acetylation	RSGGPPPKRSAPSGP CCCCCCCCCCCCCCC	65.83	7825097
164	Methylation	SGGPPPKRSAPSGPV CCCCCCCCCCCCCCC	43.77	24381481
165	O-linked_Glycosylation	GGPPPKRSAPSGPVR CCCCCCCCCCCCCCC	51.13	31373491
165	Phosphorylation	GGPPPKRSAPSGPVR CCCCCCCCCCCCCCC	51.13	30266825
168	Phosphorylation	PPKRSAPSGPVRSSS CCCCCCCCCCCCCCC	56.28	30266825
172	Dimethylation	SAPSGPVRSSSGMGG CCCCCCCCCCCCCCC	33.67	-
172	Methylation	SAPSGPVRSSSGMGG CCCCCCCCCCCCCCC	33.67	18600931
173	Phosphorylation	APSGPVRSSSGMGGR CCCCCCCCCCCCCCC	29.14	23403867
174	Phosphorylation	PSGPVRSSSGMGGRA CCCCCCCCCCCCCCC	21.98	23403867
175	Phosphorylation	SGPVRSSSGMGGRAP CCCCCCCCCCCCCCC	33.76	22115753
180	Methylation	SSSGMGGRAPVSRGR CCCCCCCCCCCCCCC	29.95	80701015
184	Phosphorylation	MGGRAPVSRGRDSYG CCCCCCCCCCCCCCC	28.14	27174698
185	Dimethylation	GGRAPVSRGRDSYGG CCCCCCCCCCCCCCC	44.38	-
185	Methylation	GGRAPVSRGRDSYGG CCCCCCCCCCCCCCC	44.38	15782174
187	Methylation	RAPVSRGRDSYGGPP CCCCCCCCCCCCCCC	28.70	82955293
189	Phosphorylation	PVSRGRDSYGGPPRR CCCCCCCCCCCCCCC	25.07	23401153
190	Phosphorylation	VSRGRDSYGGPPRRE CCCCCCCCCCCCCCC	30.32	24732914
201	Phosphorylation	PRREPLPSRRDVYLS CCCCCCCCCCCCEEC	47.86	26074081
206	Phosphorylation	LPSRRDVYLSPRDDG CCCCCCCEECCCCCC	13.02	23927012
208	Phosphorylation	SRRDVYLSPRDDGYS CCCCCEECCCCCCCC	10.53	19664994
214	Phosphorylation	LSPRDDGYSTKDSYS ECCCCCCCCCCCCCC	21.84	23927012
215	Phosphorylation	SPRDDGYSTKDSYSS CCCCCCCCCCCCCCC	34.21	23401153
216	Phosphorylation	PRDDGYSTKDSYSSR CCCCCCCCCCCCCCC	30.32	23927012
217	2-Hydroxyisobutyrylation	RDDGYSTKDSYSSRD CCCCCCCCCCCCCCC	38.44	-
217	Acetylation	RDDGYSTKDSYSSRD CCCCCCCCCCCCCCC	38.44	23749302
217	Succinylation	RDDGYSTKDSYSSRD CCCCCCCCCCCCCCC	38.44	23954790
217	Ubiquitination	RDDGYSTKDSYSSRD CCCCCCCCCCCCCCC	38.44	23000965
219	Phosphorylation	DGYSTKDSYSSRDYP CCCCCCCCCCCCCCC	28.59	23401153
220	Phosphorylation	GYSTKDSYSSRDYPS CCCCCCCCCCCCCCC	22.31	23927012
221	Phosphorylation	YSTKDSYSSRDYPSS CCCCCCCCCCCCCCC	23.89	23401153
222	Phosphorylation	STKDSYSSRDYPSSR CCCCCCCCCCCCCCC	22.42	23927012
225	Phosphorylation	DSYSSRDYPSSRDTR CCCCCCCCCCCCCCC	12.14	28102081
227	Phosphorylation	YSSRDYPSSRDTRDY CCCCCCCCCCCCCCC	31.60	28152594
228	Phosphorylation	SSRDYPSSRDTRDYA CCCCCCCCCCCCCCC	29.66	28152594
231	Phosphorylation	DYPSSRDTRDYAPPP CCCCCCCCCCCCCCC	25.08	29116813
234	Phosphorylation	SSRDTRDYAPPPRDY CCCCCCCCCCCCCCC	20.09	21945579
241	Phosphorylation	YAPPPRDYTYRDYGH CCCCCCCCCCCCCCC	13.62	21945579
242	Phosphorylation	APPPRDYTYRDYGHS CCCCCCCCCCCCCCC	19.17	21945579
243	Phosphorylation	PPPRDYTYRDYGHSS CCCCCCCCCCCCCCC	8.68	21945579
246	Phosphorylation	RDYTYRDYGHSSSRD CCCCCCCCCCCCCCC	14.03	25463755
249	Phosphorylation	TYRDYGHSSSRDDYP CCCCCCCCCCCCCCC	26.16	22167270
250	Phosphorylation	YRDYGHSSSRDDYPS CCCCCCCCCCCCCCC	24.58	23401153
251	Phosphorylation	RDYGHSSSRDDYPSR CCCCCCCCCCCCCCC	42.62	22167270
255	Phosphorylation	HSSSRDDYPSRGYSD CCCCCCCCCCCCCCC	13.85	27273156
257	Phosphorylation	SSRDDYPSRGYSDRD CCCCCCCCCCCCCCC	31.91	21955146
258	Methylation	SRDDYPSRGYSDRDG CCCCCCCCCCCCCCC	43.49	81453613
260	Phosphorylation	DDYPSRGYSDRDGYG CCCCCCCCCCCCCCC	13.29	28152594
261	Phosphorylation	DYPSRGYSDRDGYGR CCCCCCCCCCCCCCC	29.06	25159151
263	Methylation	PSRGYSDRDGYGRDR CCCCCCCCCCCCCCC	33.06	115490871
266	Phosphorylation	GYSDRDGYGRDRDYS CCCCCCCCCCCCCCC	17.18	28152594
272	Phosphorylation	GYGRDRDYSDHPSGG CCCCCCCCCCCCCCC	19.52	27273156
273	Phosphorylation	YGRDRDYSDHPSGGS CCCCCCCCCCCCCCC	33.46	23927012
277	Phosphorylation	RDYSDHPSGGSYRDS CCCCCCCCCCCCCCC	52.98	22167270
280	Phosphorylation	SDHPSGGSYRDSYES CCCCCCCCCCCCHHH	22.11	23401153
281	Phosphorylation	DHPSGGSYRDSYESY CCCCCCCCCCCHHHH	23.01	22167270
284	Phosphorylation	SGGSYRDSYESYGNS CCCCCCCCHHHHCCC	23.08	23927012
285	Phosphorylation	GGSYRDSYESYGNSR CCCCCCCHHHHCCCC	17.12	23927012
287	Phosphorylation	SYRDSYESYGNSRSA CCCCCHHHHCCCCCC	30.06	20164059
288	Phosphorylation	YRDSYESYGNSRSAP CCCCHHHHCCCCCCC	14.37	27273156
291	Phosphorylation	SYESYGNSRSAPPTR CHHHHCCCCCCCCCC	24.21	23927012
292	Methylation	YESYGNSRSAPPTRG HHHHCCCCCCCCCCC	40.62	30760819
293	Phosphorylation	ESYGNSRSAPPTRGP HHHCCCCCCCCCCCC	44.97	30576142
297	Phosphorylation	NSRSAPPTRGPPPSY CCCCCCCCCCCCCCC	47.39	28450419
298	Methylation	SRSAPPTRGPPPSYG CCCCCCCCCCCCCCC	62.49	54558711
303	Phosphorylation	PTRGPPPSYGGSSRY CCCCCCCCCCCCCCC	42.03	28555341
304	Nitration	TRGPPPSYGGSSRYD CCCCCCCCCCCCCCC	31.14	-
304	Phosphorylation	TRGPPPSYGGSSRYD CCCCCCCCCCCCCCC	31.14	23403867
307	Phosphorylation	PPPSYGGSSRYDDYS CCCCCCCCCCCCCCC	13.79	23403867
308	Phosphorylation	PPSYGGSSRYDDYSS CCCCCCCCCCCCCCC	37.83	23403867
310	Phosphorylation	SYGGSSRYDDYSSSR CCCCCCCCCCCCCCC	18.34	20007894
313	Phosphorylation	GSSRYDDYSSSRDGY CCCCCCCCCCCCCCC	13.93	21955146
314	Phosphorylation	SSRYDDYSSSRDGYG CCCCCCCCCCCCCCC	28.91	23401153
315	Phosphorylation	SRYDDYSSSRDGYGG CCCCCCCCCCCCCCC	24.14	23401153
316	Phosphorylation	RYDDYSSSRDGYGGS CCCCCCCCCCCCCCC	28.57	23401153
317	Methylation	YDDYSSSRDGYGGSR CCCCCCCCCCCCCCC	43.23	-
320	Phosphorylation	YSSSRDGYGGSRDSY CCCCCCCCCCCCCCC	23.70	22167270
323	Phosphorylation	SRDGYGGSRDSYSSS CCCCCCCCCCCCCCC	28.66	22167270
326	Phosphorylation	GYGGSRDSYSSSRSD CCCCCCCCCCCCHHH	26.29	22167270
327	Phosphorylation	YGGSRDSYSSSRSDL CCCCCCCCCCCHHHH	19.50	21945579
328	Phosphorylation	GGSRDSYSSSRSDLY CCCCCCCCCCHHHHH	26.28	22167270
329	Phosphorylation	GSRDSYSSSRSDLYS CCCCCCCCCHHHHHH	22.87	22167270
330	Phosphorylation	SRDSYSSSRSDLYSS CCCCCCCCHHHHHHC	29.84	22167270
332	Phosphorylation	DSYSSSRSDLYSSGR CCCCCCHHHHHHCCC	33.64	29255136
335	Phosphorylation	SSSRSDLYSSGRDRV CCCHHHHHHCCCCCC	13.04	21945579
336	Phosphorylation	SSRSDLYSSGRDRVG CCHHHHHHCCCCCCC	33.35	21945579
337	Phosphorylation	SRSDLYSSGRDRVGR CHHHHHHCCCCCCCC	25.04	21945579
339	Methylation	SDLYSSGRDRVGRQE HHHHHCCCCCCCCCC	30.43	80701023
347	Methylation	DRVGRQERGLPPSME CCCCCCCCCCCCHHH	43.54	115490879
352	Phosphorylation	QERGLPPSMERGYPP CCCCCCCHHHCCCCC	31.19	29255136
355	Methylation	GLPPSMERGYPPPRD CCCCHHHCCCCCCCC	41.10	115490855
357	Phosphorylation	PPSMERGYPPPRDSY CCHHHCCCCCCCCCC	20.84	30576142
363	Phosphorylation	GYPPPRDSYSSSSRG CCCCCCCCCCCCCCC	28.35	26074081
364	Phosphorylation	YPPPRDSYSSSSRGA CCCCCCCCCCCCCCC	19.50	26074081
369	Dimethylation	DSYSSSSRGAPRGGG CCCCCCCCCCCCCCC	47.44	-
369	Methylation	DSYSSSSRGAPRGGG CCCCCCCCCCCCCCC	47.44	24395529
373	Dimethylation	SSSRGAPRGGGRGGS CCCCCCCCCCCCCCC	56.72	-
373	Methylation	SSSRGAPRGGGRGGS CCCCCCCCCCCCCCC	56.72	81471837
377	Dimethylation	GAPRGGGRGGSRSDR CCCCCCCCCCCCCCC	49.96	-
377	Methylation	GAPRGGGRGGSRSDR CCCCCCCCCCCCCCC	49.96	115490839
380	Phosphorylation	RGGGRGGSRSDRGGG CCCCCCCCCCCCCCC	31.28	-
381	Dimethylation	GGGRGGSRSDRGGGR CCCCCCCCCCCCCCC	45.94	-
381	Methylation	GGGRGGSRSDRGGGR CCCCCCCCCCCCCCC	45.94	115490847

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
216	T	Phosphorylation	Kinase	MAP3K7	O43318	GPS
326	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
1	M	Acetylation
If Met-1 is not removed, it is acetylated.
2	V	Acetylation	-
If it is removed, Val-2 is acetylated.
185	R	Methylation	-
Arg-185 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CCD33_HUMAN	CCDC33	physical	16189514
RAM_HUMAN	FAM103A1	physical	16189514
LNX1_HUMAN	LNX1	physical	16189514
KHDR2_HUMAN	KHDRBS2	physical	16189514
ZN490_HUMAN	ZNF490	physical	20211142
HNRPK_HUMAN	HNRNPK	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
HNRPR_HUMAN	HNRNPR	physical	22939629
SF3B2_HUMAN	SF3B2	physical	22939629
SF3B3_HUMAN	SF3B3	physical	22939629
SF3B1_HUMAN	SF3B1	physical	22939629
HNRPM_HUMAN	HNRNPM	physical	22939629
RBM8A_HUMAN	RBM8A	physical	22939629
SF3B4_HUMAN	SF3B4	physical	22939629
SF3B6_HUMAN	SF3B6	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
RALY_HUMAN	RALY	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
IF4A3_HUMAN	EIF4A3	physical	22939629
SAFB1_HUMAN	SAFB	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
RS28_HUMAN	RPS28	physical	22939629
NUCKS_HUMAN	NUCKS1	physical	22939629
NXF1_HUMAN	NXF1	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RBM14_HUMAN	RBM14	physical	22939629
RIR2_HUMAN	RRM2	physical	22939629
ZCH18_HUMAN	ZC3H18	physical	22939629
TRA2B_HUMAN	TRA2B	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
IL7RA_HUMAN	IL7R	physical	23151878
STA5A_HUMAN	STAT5A	physical	21988832
SOCS3_HUMAN	SOCS3	physical	21988832
RBMX_HUMAN	RBMX	physical	25416956
ABC3C_HUMAN	APOBEC3C	physical	25416956
MGN2_HUMAN	MAGOHB	physical	25416956
ROBO3_HUMAN	ROBO3	physical	25416956
SOSB2_HUMAN	NABP1	physical	25416956
PRR3_HUMAN	PRR3	physical	25416956
RBY1F_HUMAN	RBMY1F	physical	25416956
KHDR2_HUMAN	KHDRBS2	physical	25416956
NIF3L_HUMAN	NIF3L1	physical	26186194
F120A_HUMAN	FAM120A	physical	26186194
HPPD_HUMAN	HPD	physical	26186194
PTCD1_HUMAN	PTCD1	physical	26186194
NGRN_HUMAN	NGRN	physical	26186194
SYYM_HUMAN	YARS2	physical	26186194
SAFB2_HUMAN	SAFB2	physical	26186194
ELAV2_HUMAN	ELAVL2	physical	26186194
TRUB2_HUMAN	TRUB2	physical	26186194
PEO1_HUMAN	C10orf2	physical	26186194
MTEF3_HUMAN	MTERF3	physical	26186194
PAIP1_HUMAN	PAIP1	physical	26186194
RBM45_HUMAN	RBM45	physical	26186194
FAKD2_HUMAN	FASTKD2	physical	26186194
QKI_HUMAN	QKI	physical	26186194
DHX36_HUMAN	DHX36	physical	26186194
P3H2_HUMAN	P3H2	physical	26186194
RALY_HUMAN	RALY	physical	26186194
FABD_HUMAN	MCAT	physical	26186194
GID8_HUMAN	GID8	physical	26186194
NCOA5_HUMAN	NCOA5	physical	26186194
MASU1_HUMAN	MALSU1	physical	26186194
YTDC1_HUMAN	YTHDC1	physical	26186194
HNRPK_HUMAN	HNRNPK	physical	21516116
HPPD_HUMAN	HPD	physical	28514442
RBM45_HUMAN	RBM45	physical	28514442
P3H2_HUMAN	P3H2	physical	28514442
PEO1_HUMAN	C10orf2	physical	28514442
NIF3L_HUMAN	NIF3L1	physical	28514442
NCOA5_HUMAN	NCOA5	physical	28514442
SYYM_HUMAN	YARS2	physical	28514442
NGRN_HUMAN	NGRN	physical	28514442
TRUB2_HUMAN	TRUB2	physical	28514442
MTEF3_HUMAN	MTERF3	physical	28514442
RU17_HUMAN	SNRNP70	physical	28514442
PTCD1_HUMAN	PTCD1	physical	28514442
MASU1_HUMAN	MALSU1	physical	28514442
YTDC1_HUMAN	YTHDC1	physical	28514442
F120A_HUMAN	FAM120A	physical	28514442

Drug and Disease Associations

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

Regulatory Network of RBMX_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND MASS SPECTROMETRY.	19608861 [Abstract]
Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-185, AND MASS SPECTROMETRY.	15782174 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-88; SER-124 ANDTYR-134, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208 AND SER-352, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-88; SER-208;SER-277; SER-326; TYR-327; SER-329; SER-330; SER-332 AND SER-352, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-280, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-332, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.	16964243 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-208 AND SER-352,AND MASS SPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.	16083285 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.	15144186 [Abstract]

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