dbPTM

IF4B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF4B_MOUSE
UniProt AC	Q8BGD9
Protein Name	Eukaryotic translation initiation factor 4B
Gene Name	Eif4b
Organism	Mus musculus (Mouse).
Sequence Length	611
Subcellular Localization
Protein Description	Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F (By similarity)..
Protein Sequence	MAASAKKKNKKGKTISLTDFLAEDGGTGGGSTYVPKPVSWADETDDLEGDVSTTWHSNDDDVYRAPPIDRSILPTAPRAAREPNIDRSRLPKSPPYTAFLGNLPYDVTEDSIKDFFRGLNISAVRLPREPSNPDRLKGFGYAEFEDLDSLLSALSLNEESLGNRRIRVDVADQAQDKDRDDRSFGRDRNRDSDKTDTDWRARPTTDSFDDYPPRRGDDSFGDKYRDRYDSDRYRDGYRDGYRDGPRRDMDRYGGRDRYDDRGSRDYDRGYDSRIGSGRRAFGSGYRRDDDYRGGGDRYEDRYDRRDDRSWSSRDDYSRDDYRRDDRGPPQRPRLNLKPRSAPKEDDASASTSQSSRAASIFGGAKPVDTAAREREVEERLQKEQEKLQRQLDEPKLDRRPRERHPSWRSEETQERERSRTGSESSQTGASATSGRNTRRRESEKSLENETLNKEEDCHSPTSKPPKPDQPLKVMPAPPPKENAWVKRSSNPPARSQSSDTEQPSPTSGGGKVAAVQPPEEGPSRKDGNKVDVVGATQGQAGSCSRGPGDGGSRDHWKDLDRKDGKKDQDSRSAPEPKKPEENPASKFSSASKYAALSVDGEDEDEGDDCTE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	KKNKKGKTISLTDFL CCCCCCCEEEHHHHH	25.19	26643407
16	Phosphorylation	NKKGKTISLTDFLAE CCCCCEEEHHHHHCC	30.37	26643407
18	Phosphorylation	KGKTISLTDFLAEDG CCCEEEHHHHHCCCC	20.22	26643407
52	Phosphorylation	DDLEGDVSTTWHSND CCCCCCCCCEEECCC	25.51	26643407
53	Phosphorylation	DLEGDVSTTWHSNDD CCCCCCCCEEECCCC	33.48	26643407
54	Phosphorylation	LEGDVSTTWHSNDDD CCCCCCCEEECCCCC	17.42	26643407
57	Phosphorylation	DVSTTWHSNDDDVYR CCCCEEECCCCCCCC	33.25	26643407
63	Phosphorylation	HSNDDDVYRAPPIDR ECCCCCCCCCCCCCH	14.19	-
70	Methylation	YRAPPIDRSILPTAP CCCCCCCHHHCCCCC	26.73	-
88	Phosphorylation	REPNIDRSRLPKSPP CCCCCCHHHCCCCCC	34.13	26239621
93	Phosphorylation	DRSRLPKSPPYTAFL CHHHCCCCCCCEEEC	29.21	25521595
96	Phosphorylation	RLPKSPPYTAFLGNL HCCCCCCCEEECCCC	17.68	25521595
97	Phosphorylation	LPKSPPYTAFLGNLP CCCCCCCEEECCCCC	19.39	24925903
105	Phosphorylation	AFLGNLPYDVTEDSI EECCCCCCCCCHHHH	26.64	25619855
108	Phosphorylation	GNLPYDVTEDSIKDF CCCCCCCCHHHHHHH	31.04	25619855
111	Phosphorylation	PYDVTEDSIKDFFRG CCCCCHHHHHHHHHC	25.88	25619855
131	Phosphorylation	VRLPREPSNPDRLKG EECCCCCCCHHHCCC	57.13	30352176
183	Phosphorylation	DKDRDDRSFGRDRNR CCCCCCCCCCCCCCC	38.76	26824392
192	Phosphorylation	GRDRNRDSDKTDTDW CCCCCCCCCCCCCCC	37.46	25266776
195	Phosphorylation	RNRDSDKTDTDWRAR CCCCCCCCCCCCCCC	49.47	26525534
197	Phosphorylation	RDSDKTDTDWRARPT CCCCCCCCCCCCCCC	42.57	28066266
204	Phosphorylation	TDWRARPTTDSFDDY CCCCCCCCCCCCCCC	37.37	23684622
205	Phosphorylation	DWRARPTTDSFDDYP CCCCCCCCCCCCCCC	32.12	23684622
207	Phosphorylation	RARPTTDSFDDYPPR CCCCCCCCCCCCCCC	28.60	27087446
211	Phosphorylation	TTDSFDDYPPRRGDD CCCCCCCCCCCCCCC	19.58	25159016
219	Phosphorylation	PPRRGDDSFGDKYRD CCCCCCCCCCHHHHH	35.55	26824392
223	Acetylation	GDDSFGDKYRDRYDS CCCCCCHHHHHCCCC	42.43	23806337
228	Phosphorylation	GDKYRDRYDSDRYRD CHHHHHCCCCHHHCC	24.88	20469934
230	Phosphorylation	KYRDRYDSDRYRDGY HHHHCCCCHHHCCCC	18.30	25266776
263	Phosphorylation	DRYDDRGSRDYDRGY CCCCCCCCCCCCCCC	23.91	24899341
266	Phosphorylation	DDRGSRDYDRGYDSR CCCCCCCCCCCCCCC	13.36	15879432
270	Phosphorylation	SRDYDRGYDSRIGSG CCCCCCCCCCCCCCC	16.19	25367039
272	Phosphorylation	DYDRGYDSRIGSGRR CCCCCCCCCCCCCCC	19.81	25367039
283	Phosphorylation	SGRRAFGSGYRRDDD CCCCCCCCCCCCCCC	26.63	25521595
285	Phosphorylation	RRAFGSGYRRDDDYR CCCCCCCCCCCCCCC	12.27	25777480
291	Phosphorylation	GYRRDDDYRGGGDRY CCCCCCCCCCCCCCC	20.39	25266776
292	Methylation	YRRDDDYRGGGDRYE CCCCCCCCCCCCCCC	44.25	-
309	Phosphorylation	YDRRDDRSWSSRDDY CCCCCCCCCCCCCCC	38.00	25521595
311	Phosphorylation	RRDDRSWSSRDDYSR CCCCCCCCCCCCCCC	19.42	25521595
312	Phosphorylation	RDDRSWSSRDDYSRD CCCCCCCCCCCCCCC	33.21	26643407
316	Phosphorylation	SWSSRDDYSRDDYRR CCCCCCCCCCCCCCC	15.19	26643407
317	Phosphorylation	WSSRDDYSRDDYRRD CCCCCCCCCCCCCCC	35.91	25367039
321	Phosphorylation	DDYSRDDYRRDDRGP CCCCCCCCCCCCCCC	16.31	25367039
340	Phosphorylation	RLNLKPRSAPKEDDA CCCCCCCCCCCCCCC	58.41	30372032
348	Phosphorylation	APKEDDASASTSQSS CCCCCCCCCCCCHHH	29.73	18779572
352	Phosphorylation	DDASASTSQSSRAAS CCCCCCCCHHHHHHH	26.10	21183079
354	Phosphorylation	ASASTSQSSRAASIF CCCCCCHHHHHHHHH	22.89	18779572
355	Phosphorylation	SASTSQSSRAASIFG CCCCCHHHHHHHHHC	20.50	18779572
359	Phosphorylation	SQSSRAASIFGGAKP CHHHHHHHHHCCCCC	19.91	26824392
365	Acetylation	ASIFGGAKPVDTAAR HHHHCCCCCCCHHHH	49.18	23806337
365	Malonylation	ASIFGGAKPVDTAAR HHHHCCCCCCCHHHH	49.18	26320211
369	Phosphorylation	GGAKPVDTAAREREV CCCCCCCHHHHHHHH	23.58	25159016
406	Phosphorylation	RPRERHPSWRSEETQ CHHHHCCCCCCHHHH	29.06	25521595
409	Phosphorylation	ERHPSWRSEETQERE HHCCCCCCHHHHHHH	33.26	27087446
412	Phosphorylation	PSWRSEETQERERSR CCCCCHHHHHHHHHC	31.51	23684622
418	Phosphorylation	ETQERERSRTGSESS HHHHHHHHCCCCCCH	29.46	27087446
420	Phosphorylation	QERERSRTGSESSQT HHHHHHCCCCCCHHC	46.43	25521595
422	Phosphorylation	RERSRTGSESSQTGA HHHHCCCCCCHHCCC	33.42	27087446
424	Phosphorylation	RSRTGSESSQTGASA HHCCCCCCHHCCCCC	29.46	25521595
425	Phosphorylation	SRTGSESSQTGASAT HCCCCCCHHCCCCCC	27.92	25521595
427	Phosphorylation	TGSESSQTGASATSG CCCCCHHCCCCCCCC	36.34	25521595
430	Phosphorylation	ESSQTGASATSGRNT CCHHCCCCCCCCCCH	33.16	21149613
432	Phosphorylation	SQTGASATSGRNTRR HHCCCCCCCCCCHHH	29.26	21149613
433	Phosphorylation	QTGASATSGRNTRRR HCCCCCCCCCCHHHH	35.16	21149613
437	Phosphorylation	SATSGRNTRRRESEK CCCCCCCHHHHHHHH	24.96	29899451
442	Phosphorylation	RNTRRRESEKSLENE CCHHHHHHHHHHHHH	48.81	27087446
445	Phosphorylation	RRRESEKSLENETLN HHHHHHHHHHHHCCC	36.54	25521595
450	Phosphorylation	EKSLENETLNKEEDC HHHHHHHCCCCCCCC	47.41	24925903
459	Phosphorylation	NKEEDCHSPTSKPPK CCCCCCCCCCCCCCC	35.88	24925903
461	Phosphorylation	EEDCHSPTSKPPKPD CCCCCCCCCCCCCCC	53.01	25521595
462	Phosphorylation	EDCHSPTSKPPKPDQ CCCCCCCCCCCCCCC	46.69	24925903
480	Acetylation	VMPAPPPKENAWVKR CCCCCCCCCCCCHHC	70.18	23806337
488	Phosphorylation	ENAWVKRSSNPPARS CCCCHHCCCCCCCCC	28.84	22324799
489	Phosphorylation	NAWVKRSSNPPARSQ CCCHHCCCCCCCCCC	58.34	27087446
495	Phosphorylation	SSNPPARSQSSDTEQ CCCCCCCCCCCCCCC	36.20	25521595
497	Phosphorylation	NPPARSQSSDTEQPS CCCCCCCCCCCCCCC	31.28	27087446
498	Phosphorylation	PPARSQSSDTEQPSP CCCCCCCCCCCCCCC	40.70	27087446
500	Phosphorylation	ARSQSSDTEQPSPTS CCCCCCCCCCCCCCC	38.17	25521595
504	Phosphorylation	SSDTEQPSPTSGGGK CCCCCCCCCCCCCCC	40.27	27087446
506	Phosphorylation	DTEQPSPTSGGGKVA CCCCCCCCCCCCCEE	44.32	25521595
507	Phosphorylation	TEQPSPTSGGGKVAA CCCCCCCCCCCCEEE	38.53	27742792
523	Phosphorylation	QPPEEGPSRKDGNKV CCCCCCCCCCCCCEE	63.92	26160508
536	Phosphorylation	KVDVVGATQGQAGSC EECEEECCCCCCCCC	27.57	29472430
542	Phosphorylation	ATQGQAGSCSRGPGD CCCCCCCCCCCCCCC	16.37	25619855
543	S-palmitoylation	TQGQAGSCSRGPGDG CCCCCCCCCCCCCCC	2.92	26165157
543	Glutathionylation	TQGQAGSCSRGPGDG CCCCCCCCCCCCCCC	2.92	24333276
544	Phosphorylation	QGQAGSCSRGPGDGG CCCCCCCCCCCCCCC	41.80	25619855
552	Phosphorylation	RGPGDGGSRDHWKDL CCCCCCCCHHHHHHC	39.81	25266776
557	Malonylation	GGSRDHWKDLDRKDG CCCHHHHHHCCCCCC	45.02	26320211
557	Acetylation	GGSRDHWKDLDRKDG CCCHHHHHHCCCCCC	45.02	23806337
570	Phosphorylation	DGKKDQDSRSAPEPK CCCCCCCCCCCCCCC	23.62	29899451
572	Phosphorylation	KKDQDSRSAPEPKKP CCCCCCCCCCCCCCC	52.72	25338131
585	Phosphorylation	KPEENPASKFSSASK CCCCCCHHHCCCCCC	35.18	29899451
586	Acetylation	PEENPASKFSSASKY CCCCCHHHCCCCCCE	51.91	23806337
588	Phosphorylation	ENPASKFSSASKYAA CCCHHHCCCCCCEEE	28.82	29514104
593	Phosphorylation	KFSSASKYAALSVDG HCCCCCCEEEEECCC	8.46	25619855
597	Phosphorylation	ASKYAALSVDGEDED CCCEEEEECCCCCCC	17.28	25521595
610	Phosphorylation	EDEGDDCTE------ CCCCCCCCC------	52.29	24925903

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
422	S	Phosphorylation	Kinase	AKT1	P31749	PSP
422	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
422	S	Phosphorylation	Kinase	RPS6KB1	P23443	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
422	S	Phosphorylation		21183079
Phosphorylated at Ser-422 by RPS6KA1 and RPS6KB1; phosphorylation enhances the affinity of EIF4B for the EIF3 complex.

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 IF4B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of IF4B_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of IF4B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-597, AND MASSSPECTROMETRY.	15345747 [Abstract]

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