dbPTM

RBM4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM4_HUMAN
UniProt AC	Q9BWF3
Protein Name	RNA-binding protein 4
Gene Name	RBM4
Organism	Homo sapiens (Human).
Sequence Length	364
Subcellular Localization	Nucleus. Nucleus, nucleolus. Nucleus speckle. Cytoplasm. Cytoplasmic granule. Undergoes continuous nucleocytoplasmic shuttling. Upon nuclear import colocalizes with SR proteins in nuclear speckles. Arsenite stress-induced phosphorylation increases it
Protein Description	RNA-binding factor involved in multiple aspects of cellular processes like alternative splicing of pre-mRNA and translation regulation. Modulates alternative 5'-splice site and exon selection. Acts as a muscle cell differentiation-promoting factor. Activates exon skipping of the PTB pre-mRNA during muscle cell differentiation. Antagonizes the activity of the splicing factor PTBP1 to modulate muscle cell-specific exon selection of alpha tropomyosin. Binds to intronic pyrimidine-rich sequence of the TPM1 and MAPT pre-mRNAs. Required for the translational activation of PER1 mRNA in response to circadian clock. Binds directly to the 3'-UTR of the PER1 mRNA. Exerts a suppressive activity on Cap-dependent translation via binding to CU-rich responsive elements within the 3'UTR of mRNAs, a process increased under stress conditions or during myocytes differentiation. Recruits EIF4A1 to stimulate IRES-dependent translation initiation in respons to cellular stress. Associates to internal ribosome entry segment (IRES) in target mRNA species under stress conditions. Plays a role for miRNA-guided RNA cleavage and translation suppression by promoting association of AGO2-containing miRNPs with their cognate target mRNAs. Associates with miRNAs during muscle cell differentiation. Binds preferentially to 5'-CGCGCG[GCA]-3' motif in vitro..
Protein Sequence	MVKLFIGNLPREATEQEIRSLFEQYGKVLECDIIKNYGFVHIEDKTAAEDAIRNLHHYKLHGVNINVEASKNKSKTSTKLHVGNISPTCTNKELRAKFEEYGPVIECDIVKDYAFVHMERAEDAVEAIRGLDNTEFQGKRMHVQLSTSRLRTAPGMGDQSGCYRCGKEGHWSKECPIDRSGRVADLTEQYNEQYGAVRTPYTMSYGDSLYYNNAYGALDAYYKRCRAARSYEAVAAAAASVYNYAEQTLSQLPQVQNTAMASHLTSTSLDPYDRHLLPTSGAAATAAAAAAAAAAVTAASTSYYGRDRSPLRRATAPVPTVGEGYGYGHESELSQASAAARNSLYDMARYEREQYADRARYSAF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MVKLFIGNLP -----CCEEEECCCC	36.06	21890473
3 (in isoform 3)	Ubiquitination	-	36.06	21890473
3 (in isoform 2)	Ubiquitination	-	36.06	21890473
3 (in isoform 1)	Ubiquitination	-	36.06	21890473
3	Ubiquitination	-----MVKLFIGNLP -----CCEEEECCCC	36.06	21890473
3	Sumoylation	-----MVKLFIGNLP -----CCEEEECCCC	36.06	-
3	Sumoylation	-----MVKLFIGNLP -----CCEEEECCCC	36.06	-
25	Phosphorylation	IRSLFEQYGKVLECD HHHHHHHHCCCEECE	16.24	29496907
27	Ubiquitination	SLFEQYGKVLECDII HHHHHHCCCEECEEH	38.42	23000965
35	Ubiquitination	VLECDIIKNYGFVHI CEECEEHHCCEEEEE	44.44	21963094
37	Phosphorylation	ECDIIKNYGFVHIED ECEEHHCCEEEEECC	13.62	25159151
45	2-Hydroxyisobutyrylation	GFVHIEDKTAAEDAI EEEEECCCCHHHHHH	27.55	-
45	Ubiquitination	GFVHIEDKTAAEDAI EEEEECCCCHHHHHH	27.55	21963094
59	Acetylation	IRNLHHYKLHGVNIN HHHHHHHEECCEEEE	29.65	-
59	Ubiquitination	IRNLHHYKLHGVNIN HHHHHHHEECCEEEE	29.65	21963094
71	Sumoylation	NINVEASKNKSKTST EEEEEECCCCCCCCC	75.37	-
71	Ubiquitination	NINVEASKNKSKTST EEEEEECCCCCCCCC	75.37	-
71	Sumoylation	NINVEASKNKSKTST EEEEEECCCCCCCCC	75.37	-
76	Phosphorylation	ASKNKSKTSTKLHVG ECCCCCCCCCEEEEC	49.04	25690035
77	Phosphorylation	SKNKSKTSTKLHVGN CCCCCCCCCEEEECC	27.55	25690035
78	Phosphorylation	KNKSKTSTKLHVGNI CCCCCCCCEEEECCC	42.74	25690035
79	Sumoylation	NKSKTSTKLHVGNIS CCCCCCCEEEECCCC	36.04	28112733
79	Acetylation	NKSKTSTKLHVGNIS CCCCCCCEEEECCCC	36.04	25953088
79	Ubiquitination	NKSKTSTKLHVGNIS CCCCCCCEEEECCCC	36.04	29967540
86	Phosphorylation	KLHVGNISPTCTNKE EEEECCCCCCCCCHH	20.39	29255136
88	Phosphorylation	HVGNISPTCTNKELR EECCCCCCCCCHHHH	25.77	29255136
90	Phosphorylation	GNISPTCTNKELRAK CCCCCCCCCHHHHHH	52.37	29255136
92	Ubiquitination	ISPTCTNKELRAKFE CCCCCCCHHHHHHHH	39.72	23000965
92	Sumoylation	ISPTCTNKELRAKFE CCCCCCCHHHHHHHH	39.72	28112733
92	Sumoylation	ISPTCTNKELRAKFE CCCCCCCHHHHHHHH	39.72	-
92	Acetylation	ISPTCTNKELRAKFE CCCCCCCHHHHHHHH	39.72	25953088
97	Sumoylation	TNKELRAKFEEYGPV CCHHHHHHHHHHCCE	47.04	-
97	Sumoylation	TNKELRAKFEEYGPV CCHHHHHHHHHHCCE	47.04	-
97	Acetylation	TNKELRAKFEEYGPV CCHHHHHHHHHHCCE	47.04	26051181
97	Ubiquitination	TNKELRAKFEEYGPV CCHHHHHHHHHHCCE	47.04	23000965
101	Phosphorylation	LRAKFEEYGPVIECD HHHHHHHHCCEEEEE	21.38	29496907
111	Ubiquitination	VIECDIVKDYAFVHM EEEEEEEECEEEEEH	45.41	29967540
113	Phosphorylation	ECDIVKDYAFVHMER EEEEEECEEEEEHHH	9.02	28796482
129	Methylation	EDAVEAIRGLDNTEF HHHHHHHHCCCCCCC	46.82	-
139	Ubiquitination	DNTEFQGKRMHVQLS CCCCCCCEEEEEEEE	35.45	27667366
139	2-Hydroxyisobutyrylation	DNTEFQGKRMHVQLS CCCCCCCEEEEEEEE	35.45	-
139	Acetylation	DNTEFQGKRMHVQLS CCCCCCCEEEEEEEE	35.45	12431749
145 (in isoform 2)	Methylation	-	6.16	-
146	Phosphorylation	KRMHVQLSTSRLRTA EEEEEEEECCCCCCC	13.77	28857561
147	Phosphorylation	RMHVQLSTSRLRTAP EEEEEEECCCCCCCC	26.85	28555341
152	Phosphorylation	LSTSRLRTAPGMGDQ EECCCCCCCCCCCCC	41.62	21406692
160 (in isoform 2)	Ubiquitination	-	35.25	-
160	Phosphorylation	APGMGDQSGCYRCGK CCCCCCCCCCCCCCC	35.25	21406692
163	Phosphorylation	MGDQSGCYRCGKEGH CCCCCCCCCCCCCCC	16.68	21406692
173	Sumoylation	GKEGHWSKECPIDRS CCCCCCCCCCCCCCC	59.13	-
173	Ubiquitination	GKEGHWSKECPIDRS CCCCCCCCCCCCCCC	59.13	22505724
173	Sumoylation	GKEGHWSKECPIDRS CCCCCCCCCCCCCCC	59.13	-
173	Acetylation	GKEGHWSKECPIDRS CCCCCCCCCCCCCCC	59.13	26051181
187	Phosphorylation	SGRVADLTEQYNEQY CCCCCHHHHHHHHHH	22.91	27642862
190	Phosphorylation	VADLTEQYNEQYGAV CCHHHHHHHHHHCCC	17.90	21945579
194	Phosphorylation	TEQYNEQYGAVRTPY HHHHHHHHCCCCCCE	10.81	21945579
201	Phosphorylation	YGAVRTPYTMSYGDS HCCCCCCEECCCCCC	17.92	20090780
205	Phosphorylation	RTPYTMSYGDSLYYN CCCEECCCCCCCCCC	17.71	-
208	Phosphorylation	YTMSYGDSLYYNNAY EECCCCCCCCCCCCH	17.57	-
210	Phosphorylation	MSYGDSLYYNNAYGA CCCCCCCCCCCCHHH	14.22	20090780
211	Phosphorylation	SYGDSLYYNNAYGAL CCCCCCCCCCCHHHH	13.77	27642862
215	Phosphorylation	SLYYNNAYGALDAYY CCCCCCCHHHHHHHH	12.68	-
221	Phosphorylation	AYGALDAYYKRCRAA CHHHHHHHHHHHHHH	14.80	-
222	Phosphorylation	YGALDAYYKRCRAAR HHHHHHHHHHHHHHH	8.15	-
223	Ubiquitination	GALDAYYKRCRAARS HHHHHHHHHHHHHHC	32.14	21963094
223	Sumoylation	GALDAYYKRCRAARS HHHHHHHHHHHHHHC	32.14	-
223	Acetylation	GALDAYYKRCRAARS HHHHHHHHHHHHHHC	32.14	26051181
272	Phosphorylation	TSTSLDPYDRHLLPT HCCCCCCCCCCCCCC	25.85	25884760
279	O-linked_Glycosylation	YDRHLLPTSGAAATA CCCCCCCCCHHHHHH	39.50	31373491
280	O-linked_Glycosylation	DRHLLPTSGAAATAA CCCCCCCCHHHHHHH	25.21	31373491
285	Phosphorylation	PTSGAAATAAAAAAA CCCHHHHHHHHHHHH	16.47	26434776
285	O-linked_Glycosylation	PTSGAAATAAAAAAA CCCHHHHHHHHHHHH	16.47	31373491
297	Phosphorylation	AAAAAAVTAASTSYY HHHHHHHHHHHHCCC	16.27	27174698
297	O-linked_Glycosylation	AAAAAAVTAASTSYY HHHHHHHHHHHHCCC	16.27	31373491
300	O-linked_Glycosylation	AAAVTAASTSYYGRD HHHHHHHHHCCCCCC	18.54	31373491
300	Phosphorylation	AAAVTAASTSYYGRD HHHHHHHHHCCCCCC	18.54	27174698
301	O-linked_Glycosylation	AAVTAASTSYYGRDR HHHHHHHHCCCCCCC	18.93	31373491
301	Phosphorylation	AAVTAASTSYYGRDR HHHHHHHHCCCCCCC	18.93	27174698
302	O-linked_Glycosylation	AVTAASTSYYGRDRS HHHHHHHCCCCCCCC	17.54	31373491
302	Phosphorylation	AVTAASTSYYGRDRS HHHHHHHCCCCCCCC	17.54	27174698
303	Phosphorylation	VTAASTSYYGRDRSP HHHHHHCCCCCCCCC	15.27	20090780
304	Phosphorylation	TAASTSYYGRDRSPL HHHHHCCCCCCCCCC	12.88	27174698
309	Phosphorylation	SYYGRDRSPLRRATA CCCCCCCCCCCCCCC	32.35	30266825
315	Phosphorylation	RSPLRRATAPVPTVG CCCCCCCCCCCCCCC	29.68	28796482
320	Phosphorylation	RATAPVPTVGEGYGY CCCCCCCCCCCCCCC	41.18	28796482
325	Phosphorylation	VPTVGEGYGYGHESE CCCCCCCCCCCCHHH	11.67	28796482
327	Phosphorylation	TVGEGYGYGHESELS CCCCCCCCCCHHHHH	13.56	28796482
331	O-linked_Glycosylation	GYGYGHESELSQASA CCCCCCHHHHHHHHH	37.86	31373491
331	Phosphorylation	GYGYGHESELSQASA CCCCCCHHHHHHHHH	37.86	28796482
334	Phosphorylation	YGHESELSQASAAAR CCCHHHHHHHHHHHH	21.46	25849741
337	Phosphorylation	ESELSQASAAARNSL HHHHHHHHHHHHHHH	15.71	28796482
343	Phosphorylation	ASAAARNSLYDMARY HHHHHHHHHHHHHHH	23.82	28796482
345	Phosphorylation	AAARNSLYDMARYER HHHHHHHHHHHHHHH	11.95	25159151
350	Phosphorylation	SLYDMARYEREQYAD HHHHHHHHHHHHHHH	15.14	-
355	Phosphorylation	ARYEREQYADRARYS HHHHHHHHHHHHHHH	13.01	-
358	Methylation	EREQYADRARYSAF- HHHHHHHHHHHHCC-	16.88	83108829
361	Phosphorylation	QYADRARYSAF---- HHHHHHHHHCC----	11.90	20736484
362	Phosphorylation	YADRARYSAF----- HHHHHHHHCC-----	20.04	22210691

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
309	S	Phosphorylation	Kinase	SRPK1	Q96SB4	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
309	S	Phosphorylation	17284590
Phosphorylated in vitro on Ser-309 by SRPK1.
309	S	Phosphorylation	17284590
Phosphorylation on Ser-309 is induced upon cell muscle differentiation (By similarity).
309	S	Phosphorylation	17284590
Phosphorylation on Ser-309 is induced upon cell stress signaling, which alters its subcellular localization and may modulate its activity on IRES-mediated mRNA translation.

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 RBM4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRCC1_HUMAN	XRCC1	physical	22939629
TM189_HUMAN	TMEM189	physical	22939629
SUCB1_HUMAN	SUCLA2	physical	22939629
TPR_HUMAN	TPR	physical	22939629
RU1C_HUMAN	SNRPC	physical	22365833
SF3B4_HUMAN	SF3B4	physical	22365833
U2AF2_HUMAN	U2AF2	physical	22365833
RBM10_HUMAN	RBM10	physical	22365833
SF01_HUMAN	SF1	physical	22365833
RBM23_HUMAN	RBM23	physical	22365833
PRP31_HUMAN	PRPF31	physical	22365833
RBM22_HUMAN	RBM22	physical	22365833
AQR_HUMAN	AQR	physical	22365833
DGC14_HUMAN	DGCR14	physical	22365833
RBM7_HUMAN	RBM7	physical	22365833
DDX17_HUMAN	DDX17	physical	22365833
DDX5_HUMAN	DDX5	physical	22365833
HNRPK_HUMAN	HNRNPK	physical	22365833
HNRL1_HUMAN	HNRNPUL1	physical	22365833
DHX9_HUMAN	DHX9	physical	22365833
HNRPM_HUMAN	HNRNPM	physical	22365833
HNRPF_HUMAN	HNRNPF	physical	22365833
HNRH2_HUMAN	HNRNPH2	physical	22365833
HNRH3_HUMAN	HNRNPH3	physical	22365833
RBM42_HUMAN	RBM42	physical	22365833
CX056_HUMAN	CXorf56	physical	22365833
PABP1_HUMAN	PABPC1	physical	22365833
PTBP2_HUMAN	PTBP2	physical	22365833
PEPL_HUMAN	PPL	physical	26496610
PPM1G_HUMAN	PPM1G	physical	26496610
KITM_HUMAN	TK2	physical	26496610
TLN1_HUMAN	TLN1	physical	26496610
RM24_HUMAN	MRPL24	physical	26496610
IPO4_HUMAN	IPO4	physical	26496610
ZN668_HUMAN	ZNF668	physical	26496610
MILK1_HUMAN	MICALL1	physical	26496610
WDR3_HUMAN	WDR3	physical	28514442
ZN420_HUMAN	ZNF420	physical	28514442
WDR36_HUMAN	WDR36	physical	28514442
XRN1_HUMAN	XRN1	physical	28514442
RPP40_HUMAN	RPP40	physical	28514442
WDR43_HUMAN	WDR43	physical	28514442
RPP29_HUMAN	POP4	physical	28514442
CENPC_HUMAN	CENPC	physical	28514442
RL26L_HUMAN	RPL26L1	physical	28514442
ZFP62_HUMAN	ZFP62	physical	28514442
RL36L_HUMAN	RPL36AL	physical	28514442
RRP5_HUMAN	PDCD11	physical	28514442
RPF2_HUMAN	RPF2	physical	28514442
REXO4_HUMAN	REXO4	physical	28514442
SFR19_HUMAN	SCAF1	physical	28514442
WDR75_HUMAN	WDR75	physical	28514442
CENPU_HUMAN	CENPU	physical	28514442
RRP8_HUMAN	RRP8	physical	28514442
NOP2_HUMAN	NOP2	physical	28514442
EBP2_HUMAN	EBNA1BP2	physical	28514442
POP1_HUMAN	POP1	physical	28514442
TDIF2_HUMAN	DNTTIP2	physical	28514442
BUD13_HUMAN	BUD13	physical	28514442
PK1IP_HUMAN	PAK1IP1	physical	28514442
NLE1_HUMAN	NLE1	physical	28514442
DDX54_HUMAN	DDX54	physical	28514442
DDX24_HUMAN	DDX24	physical	28514442
ZN121_HUMAN	ZNF121	physical	28514442
RBM28_HUMAN	RBM28	physical	28514442
RPP38_HUMAN	RPP38	physical	28514442
H2A2B_HUMAN	HIST2H2AB	physical	28514442
NO40_HUMAN	ZCCHC17	physical	28514442
PWP2_HUMAN	PWP2	physical	28514442
NOP56_HUMAN	NOP56	physical	28514442
DDX51_HUMAN	DDX51	physical	28514442
RL32_HUMAN	RPL32	physical	28514442
CARM1_HUMAN	CARM1	physical	28514442
UTP15_HUMAN	UTP15	physical	28514442
NVL_HUMAN	NVL	physical	28514442
NOG2_HUMAN	GNL2	physical	28514442
TEX10_HUMAN	TEX10	physical	28514442
DKC1_HUMAN	DKC1	physical	28514442
NPA1P_HUMAN	URB1	physical	28514442
POP7_HUMAN	POP7	physical	28514442
RP25L_HUMAN	RPP25L	physical	28514442
TBL3_HUMAN	TBL3	physical	28514442
NOG1_HUMAN	GTPBP4	physical	28514442
RL1D1_HUMAN	RSL1D1	physical	28514442
RL5_HUMAN	RPL5	physical	28514442
URB2_HUMAN	URB2	physical	28514442
GLYR1_HUMAN	GLYR1	physical	28514442
BRX1_HUMAN	BRIX1	physical	28514442
EXOG_HUMAN	EXOG	physical	28514442
ZBT24_HUMAN	ZBTB24	physical	28514442
CENPN_HUMAN	CENPN	physical	28514442
RBBP6_HUMAN	RBBP6	physical	28514442
DDX21_HUMAN	DDX21	physical	28514442
UTP23_HUMAN	UTP23	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 RBM4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Cell stress modulates the function of splicing regulatory proteinRBM4 in translation control."; Lin J.C., Hsu M., Tarn W.Y.; Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007). Cited for: FUNCTION, INTERACTION WITH EIF4A1 AND EIF4G1, PHOSPHORYLATION ATSER-309, ASSOCIATION WITH IRES OF MRNAS, SUBCELLULAR LOCATION, ANDMUTAGENESIS OF SER-309.	17284590 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-190 AND TYR-194, ANDMASS SPECTROMETRY.	15592455 [Abstract]

show

show

show