dbPTM

IF4B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF4B_HUMAN
UniProt AC	P23588
Protein Name	Eukaryotic translation initiation factor 4B
Gene Name	EIF4B
Organism	Homo sapiens (Human).
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..
Protein Sequence	MAASAKKKNKKGKTISLTDFLAEDGGTGGGSTYVSKPVSWADETDDLEGDVSTTWHSNDDDVYRAPPIDRSILPTAPRAAREPNIDRSRLPKSPPYTAFLGNLPYDVTEESIKEFFRGLNISAVRLPREPSNPERLKGFGYAEFEDLDSLLSALSLNEESLGNRRIRVDVADQAQDKDRDDRSFGRDRNRDSDKTDTDWRARPATDSFDDYPPRRGDDSFGDKYRDRYDSDRYRDGYRDGYRDGPRRDMDRYGGRDRYDDRGSRDYDRGYDSRIGSGRRAFGSGYRRDDDYRGGGDRYEDRYDRRDDRSWSSRDDYSRDDYRRDDRGPPQRPKLNLKPRSTPKEDDSSASTSQSTRAASIFGGAKPVDTAAREREVEERLQKEQEKLQRQLDEPKLERRPRERHPSWRSEETQERERSRTGSESSQTGTSTTSSRNARRRESEKSLENETLNKEEDCHSPTSKPPKPDQPLKVMPAPPPKENAWVKRSSNPPARSQSSDTEQQSPTSGGGKVAPAQPSEEGPGRKDENKVDGMNAPKGQTGNSSRGPGDGGNRDHWKESDRKDGKKDQDSRSAPEPKKPEENPASKFSSASKYAALSVDGEDENEGEDYAE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Acetylation	--MAASAKKKNKKGK --CCCCCCCCCCCCC	62.88	30582825
14	Phosphorylation	KKNKKGKTISLTDFL CCCCCCCEEEHHHHH	25.19	28102081
16	Phosphorylation	NKKGKTISLTDFLAE CCCCCEEEHHHHHCC	30.37	25159151
18	Phosphorylation	KGKTISLTDFLAEDG CCCEEEHHHHHCCCC	20.22	28102081
27	Phosphorylation	FLAEDGGTGGGSTYV HHCCCCCCCCCCCEE	37.88	20068231
31	Phosphorylation	DGGTGGGSTYVSKPV CCCCCCCCCEECCCC	21.60	26074081
32	Phosphorylation	GGTGGGSTYVSKPVS CCCCCCCCEECCCCC	31.08	20068231
33	Phosphorylation	GTGGGSTYVSKPVSW CCCCCCCEECCCCCC	12.39	20068231
35	Phosphorylation	GGGSTYVSKPVSWAD CCCCCEECCCCCCCC	22.34	20068231
39	Phosphorylation	TYVSKPVSWADETDD CEECCCCCCCCCCCC	25.69	26074081
44	Phosphorylation	PVSWADETDDLEGDV CCCCCCCCCCCCCCC	35.05	27732954
52	Phosphorylation	DDLEGDVSTTWHSND CCCCCCCCCEEECCC	25.51	29978859
53	Phosphorylation	DLEGDVSTTWHSNDD CCCCCCCCEEECCCC	33.48	25159151
54	Phosphorylation	LEGDVSTTWHSNDDD CCCCCCCEEECCCCC	17.42	27732954
57	Phosphorylation	DVSTTWHSNDDDVYR CCCCEEECCCCCCCC	33.25	29978859
63	Phosphorylation	HSNDDDVYRAPPIDR ECCCCCCCCCCCCCH	14.19	29978859
70	Methylation	YRAPPIDRSILPTAP CCCCCCCHHHCCCCC	26.73	-
71	Phosphorylation	RAPPIDRSILPTAPR CCCCCCHHHCCCCCH	25.40	20068231
75	Phosphorylation	IDRSILPTAPRAARE CCHHHCCCCCHHHCC	45.94	20068231
78	Methylation	SILPTAPRAAREPNI HHCCCCCHHHCCCCC	38.11	-
88	Phosphorylation	REPNIDRSRLPKSPP CCCCCCHHHCCCCCC	34.13	23403867
92	Ubiquitination	IDRSRLPKSPPYTAF CCHHHCCCCCCCEEE	78.98	-
93	Phosphorylation	DRSRLPKSPPYTAFL CHHHCCCCCCCEEEC	29.21	25159151
96	Phosphorylation	RLPKSPPYTAFLGNL HCCCCCCCEEECCCC	17.68	30278072
97	Phosphorylation	LPKSPPYTAFLGNLP CCCCCCCEEECCCCC	19.39	28176443
105	Phosphorylation	AFLGNLPYDVTEESI EECCCCCCCCCHHHH	26.64	28176443
108	Phosphorylation	GNLPYDVTEESIKEF CCCCCCCCHHHHHHH	31.01	23403867
111	Phosphorylation	PYDVTEESIKEFFRG CCCCCHHHHHHHHHC	32.50	28176443
117	Methylation	ESIKEFFRGLNISAV HHHHHHHHCCCCCEE	54.75	-
122	Phosphorylation	FFRGLNISAVRLPRE HHHCCCCCEEECCCC	21.46	28555341
131	Phosphorylation	VRLPREPSNPERLKG EECCCCCCCHHHHCC	61.33	23898821
138	Acetylation	SNPERLKGFGYAEFE CCHHHHCCCCCCCHH	26.29	-
141	Phosphorylation	ERLKGFGYAEFEDLD HHHCCCCCCCHHCHH	10.74	22115753
149	Phosphorylation	AEFEDLDSLLSALSL CCHHCHHHHHHHHCC	38.21	25338102
155	Acetylation	DSLLSALSLNEESLG HHHHHHHCCCHHHHC	28.94	-
155	Phosphorylation	DSLLSALSLNEESLG HHHHHHHCCCHHHHC	28.94	18452278
160	Phosphorylation	ALSLNEESLGNRRIR HHCCCHHHHCCCEEE	35.08	18452278
177	Acetylation	VADQAQDKDRDDRSF HHHHHHCCCCCCCCC	42.45	23236377
177	Ubiquitination	VADQAQDKDRDDRSF HHHHHHCCCCCCCCC	42.45	-
182	Methylation	QDKDRDDRSFGRDRN HCCCCCCCCCCCCCC	37.87	-
183	Phosphorylation	DKDRDDRSFGRDRNR CCCCCCCCCCCCCCC	38.76	25159151
184	Acetylation	KDRDDRSFGRDRNRD CCCCCCCCCCCCCCC	10.95	-
184	Ubiquitination	KDRDDRSFGRDRNRD CCCCCCCCCCCCCCC	10.95	21906983
192	Phosphorylation	GRDRNRDSDKTDTDW CCCCCCCCCCCCCCH	37.46	25159151
194	Acetylation	DRNRDSDKTDTDWRA CCCCCCCCCCCCHHH	52.86	23236377
195	Phosphorylation	RNRDSDKTDTDWRAR CCCCCCCCCCCHHHC	49.47	27794612
197	Phosphorylation	RDSDKTDTDWRARPA CCCCCCCCCHHHCCC	42.57	27794612
205	Phosphorylation	DWRARPATDSFDDYP CHHHCCCCCCCCCCC	34.55	22617229
207	Phosphorylation	RARPATDSFDDYPPR HHCCCCCCCCCCCCC	26.64	20044836
211	Phosphorylation	ATDSFDDYPPRRGDD CCCCCCCCCCCCCCC	19.58	25159151
219	Phosphorylation	PPRRGDDSFGDKYRD CCCCCCCCCCHHHHH	35.55	29255136
223	2-Hydroxyisobutyrylation	GDDSFGDKYRDRYDS CCCCCCHHHHHCCCC	42.43	-
223	Acetylation	GDDSFGDKYRDRYDS CCCCCCHHHHHCCCC	42.43	23236377
223	Ubiquitination	GDDSFGDKYRDRYDS CCCCCCHHHHHCCCC	42.43	21906983
224	Phosphorylation	DDSFGDKYRDRYDSD CCCCCHHHHHCCCCH	23.61	23927012
228	Phosphorylation	GDKYRDRYDSDRYRD CHHHHHCCCCHHHCC	24.88	28796482
230	Phosphorylation	KYRDRYDSDRYRDGY HHHHCCCCHHHCCCC	18.30	23401153
233	Phosphorylation	DRYDSDRYRDGYRDG HCCCCHHHCCCCCCC	20.32	29116813
237	Phosphorylation	SDRYRDGYRDGYRDG CHHHCCCCCCCCCCC	15.15	-
241	Phosphorylation	RDGYRDGYRDGPRRD CCCCCCCCCCCCCCC	15.15	-
252	Phosphorylation	PRRDMDRYGGRDRYD CCCCCHHCCCCCCCC	21.48	28060719
258	Phosphorylation	RYGGRDRYDDRGSRD HCCCCCCCCCCCCCC	26.87	30576142
261	Methylation	GRDRYDDRGSRDYDR CCCCCCCCCCCCCCC	41.93	-
263	Phosphorylation	DRYDDRGSRDYDRGY CCCCCCCCCCCCCCC	23.91	28555341
266	Phosphorylation	DDRGSRDYDRGYDSR CCCCCCCCCCCCCCC	13.36	28796482
268	Methylation	RGSRDYDRGYDSRIG CCCCCCCCCCCCCCC	39.06	-
270	Phosphorylation	SRDYDRGYDSRIGSG CCCCCCCCCCCCCCC	16.19	28796482
272	Phosphorylation	DYDRGYDSRIGSGRR CCCCCCCCCCCCCCC	19.81	28796482
273	Methylation	YDRGYDSRIGSGRRA CCCCCCCCCCCCCCC	34.10	-
276	Phosphorylation	GYDSRIGSGRRAFGS CCCCCCCCCCCCCCC	27.10	26074081
279	Methylation	SRIGSGRRAFGSGYR CCCCCCCCCCCCCCC	37.48	-
283	Phosphorylation	SGRRAFGSGYRRDDD CCCCCCCCCCCCCCC	26.63	22167270
285	Phosphorylation	RRAFGSGYRRDDDYR CCCCCCCCCCCCCCC	12.27	23898821
291	Phosphorylation	GYRRDDDYRGGGDRY CCCCCCCCCCCCCCC	20.39	23403867
292	Methylation	YRRDDDYRGGGDRYE CCCCCCCCCCCCCCC	44.25	-
297	Methylation	DYRGGGDRYEDRYDR CCCCCCCCCCCCCCC	39.76	-
298	Phosphorylation	YRGGGDRYEDRYDRR CCCCCCCCCCCCCCC	27.24	28796482
302	Phosphorylation	GDRYEDRYDRRDDRS CCCCCCCCCCCCCCC	26.56	28796482
308	Methylation	RYDRRDDRSWSSRDD CCCCCCCCCCCCCCC	44.29	-
309	Phosphorylation	YDRRDDRSWSSRDDY CCCCCCCCCCCCCCC	38.00	29496963
311	Phosphorylation	RRDDRSWSSRDDYSR CCCCCCCCCCCCCCC	19.42	20068231
312	Phosphorylation	RDDRSWSSRDDYSRD CCCCCCCCCCCCCCC	33.21	20068231
316	Phosphorylation	SWSSRDDYSRDDYRR CCCCCCCCCCCCCCC	15.19	28796482
317	Phosphorylation	WSSRDDYSRDDYRRD CCCCCCCCCCCCCCC	35.91	28796482
321	Phosphorylation	DDYSRDDYRRDDRGP CCCCCCCCCCCCCCC	16.31	28796482
326	Acetylation	DDYRRDDRGPPQRPK CCCCCCCCCCCCCCC	64.90	-
333	Sumoylation	RGPPQRPKLNLKPRS CCCCCCCCCCCCCCC	52.80	-
337	Acetylation	QRPKLNLKPRSTPKE CCCCCCCCCCCCCCC	36.99	26051181
340	Phosphorylation	KLNLKPRSTPKEDDS CCCCCCCCCCCCCCC	58.55	25159151
341	Phosphorylation	LNLKPRSTPKEDDSS CCCCCCCCCCCCCCC	39.39	20044836
343	Sumoylation	LKPRSTPKEDDSSAS CCCCCCCCCCCCCCC	74.08	28112733
347	Phosphorylation	STPKEDDSSASTSQS CCCCCCCCCCCCCHH	39.88	28450419
348	Phosphorylation	TPKEDDSSASTSQST CCCCCCCCCCCCHHH	32.98	30576142
350	Phosphorylation	KEDDSSASTSQSTRA CCCCCCCCCCHHHHH	30.46	20044836
351	Phosphorylation	EDDSSASTSQSTRAA CCCCCCCCCHHHHHH	30.42	29396449
352	O-linked_Glycosylation	DDSSASTSQSTRAAS CCCCCCCCHHHHHHH	21.46	30059200
352	Phosphorylation	DDSSASTSQSTRAAS CCCCCCCCHHHHHHH	21.46	29396449
354	O-linked_Glycosylation	SSASTSQSTRAASIF CCCCCCHHHHHHHHH	21.45	30059200
354	Phosphorylation	SSASTSQSTRAASIF CCCCCCHHHHHHHHH	21.45	30576142
355	O-linked_Glycosylation	SASTSQSTRAASIFG CCCCCHHHHHHHHHC	19.38	30059200
355	Phosphorylation	SASTSQSTRAASIFG CCCCCHHHHHHHHHC	19.38	30576142
359	O-linked_Glycosylation	SQSTRAASIFGGAKP CHHHHHHHHHCCCCC	19.91	30059200
359	Phosphorylation	SQSTRAASIFGGAKP CHHHHHHHHHCCCCC	19.91	23401153
365	2-Hydroxyisobutyrylation	ASIFGGAKPVDTAAR HHHHCCCCCCCHHHH	49.18	-
365	Acetylation	ASIFGGAKPVDTAAR HHHHCCCCCCCHHHH	49.18	23236377
365	Ubiquitination	ASIFGGAKPVDTAAR HHHHCCCCCCCHHHH	49.18	-
369	Phosphorylation	GGAKPVDTAAREREV CCCCCCCHHHHHHHH	23.58	20068231
405	Acetylation	RRPRERHPSWRSEET CCCCCCCCCCCCHHH	41.63	-
406	Phosphorylation	RPRERHPSWRSEETQ CCCCCCCCCCCHHHH	29.06	22167270
409	Phosphorylation	ERHPSWRSEETQERE CCCCCCCCHHHHHHH	33.26	22167270
412	Phosphorylation	PSWRSEETQERERSR CCCCCHHHHHHHHHC	31.51	22167270
418	Phosphorylation	ETQERERSRTGSESS HHHHHHHHCCCCCCC	29.46	25159151
420	Phosphorylation	QERERSRTGSESSQT HHHHHHCCCCCCCCC	46.43	29255136
422	Phosphorylation	RERSRTGSESSQTGT HHHHCCCCCCCCCCC	33.42	21536668
424	Phosphorylation	RSRTGSESSQTGTST HHCCCCCCCCCCCCC	29.46	29255136
425	Phosphorylation	SRTGSESSQTGTSTT HCCCCCCCCCCCCCC	27.92	29255136
427	Phosphorylation	TGSESSQTGTSTTSS CCCCCCCCCCCCCHH	44.36	23401153
429	Phosphorylation	SESSQTGTSTTSSRN CCCCCCCCCCCHHHH	26.70	23401153
430	Phosphorylation	ESSQTGTSTTSSRNA CCCCCCCCCCHHHHH	30.91	23927012
431	Phosphorylation	SSQTGTSTTSSRNAR CCCCCCCCCHHHHHH	30.45	23927012
432	Phosphorylation	SQTGTSTTSSRNARR CCCCCCCCHHHHHHH	25.19	23927012
433	O-linked_Glycosylation	QTGTSTTSSRNARRR CCCCCCCHHHHHHHH	27.65	30059200
433	Phosphorylation	QTGTSTTSSRNARRR CCCCCCCHHHHHHHH	27.65	23927012
434	Phosphorylation	TGTSTTSSRNARRRE CCCCCCHHHHHHHHH	27.71	25159151
442	Phosphorylation	RNARRRESEKSLENE HHHHHHHHHHHHHHH	48.81	27273156
444	Acetylation	ARRRESEKSLENETL HHHHHHHHHHHHHCC	70.40	23236377
445	Phosphorylation	RRRESEKSLENETLN HHHHHHHHHHHHCCC	36.54	19664994
450	Phosphorylation	EKSLENETLNKEEDC HHHHHHHCCCCCCCC	47.41	29255136
453	Acetylation	LENETLNKEEDCHSP HHHHCCCCCCCCCCC	66.64	26051181
459	Phosphorylation	NKEEDCHSPTSKPPK CCCCCCCCCCCCCCC	35.88	29255136
461	Phosphorylation	EEDCHSPTSKPPKPD CCCCCCCCCCCCCCC	53.01	20201521
462	Phosphorylation	EDCHSPTSKPPKPDQ CCCCCCCCCCCCCCC	46.69	30266825
463	Acetylation	DCHSPTSKPPKPDQP CCCCCCCCCCCCCCC	68.75	26051181
463	Ubiquitination	DCHSPTSKPPKPDQP CCCCCCCCCCCCCCC	68.75	-
466	Acetylation	SPTSKPPKPDQPLKV CCCCCCCCCCCCCCC	70.52	26051181
480	Acetylation	VMPAPPPKENAWVKR CCCCCCCCCCCCHHC	70.18	26051181
486	Methylation	PKENAWVKRSSNPPA CCCCCCHHCCCCCCC	35.54	-
488	Phosphorylation	ENAWVKRSSNPPARS CCCCHHCCCCCCCCC	28.84	21601212
489	Phosphorylation	NAWVKRSSNPPARSQ CCCHHCCCCCCCCCC	58.34	25159151
495	O-linked_Glycosylation	SSNPPARSQSSDTEQ CCCCCCCCCCCCCCC	36.20	30059200
495	Phosphorylation	SSNPPARSQSSDTEQ CCCCCCCCCCCCCCC	36.20	29255136
497	Phosphorylation	NPPARSQSSDTEQQS CCCCCCCCCCCCCCC	31.28	29255136
498	Phosphorylation	PPARSQSSDTEQQSP CCCCCCCCCCCCCCC	40.70	29255136
500	Phosphorylation	ARSQSSDTEQQSPTS CCCCCCCCCCCCCCC	37.33	29255136
504	O-linked_Glycosylation	SSDTEQQSPTSGGGK CCCCCCCCCCCCCCC	29.82	30059200
504	Phosphorylation	SSDTEQQSPTSGGGK CCCCCCCCCCCCCCC	29.82	29255136
506	Phosphorylation	DTEQQSPTSGGGKVA CCCCCCCCCCCCCCC	45.29	30266825
507	Phosphorylation	TEQQSPTSGGGKVAP CCCCCCCCCCCCCCC	38.53	30266825
511	Acetylation	SPTSGGGKVAPAQPS CCCCCCCCCCCCCCC	38.20	26051181
518	Phosphorylation	KVAPAQPSEEGPGRK CCCCCCCCCCCCCCC	35.88	25159151
537	Acetylation	VDGMNAPKGQTGNSS CCCCCCCCCCCCCCC	62.33	26051181
537	Ubiquitination	VDGMNAPKGQTGNSS CCCCCCCCCCCCCCC	62.33	-
540	Phosphorylation	MNAPKGQTGNSSRGP CCCCCCCCCCCCCCC	47.18	21406692
543	Phosphorylation	PKGQTGNSSRGPGDG CCCCCCCCCCCCCCC	23.82	21406692
544	Phosphorylation	KGQTGNSSRGPGDGG CCCCCCCCCCCCCCC	45.30	28985074
547	Acetylation	TGNSSRGPGDGGNRD CCCCCCCCCCCCCHH	36.27	-
570	Phosphorylation	DGKKDQDSRSAPEPK CCCCCCCCCCCCCCC	23.62	25159151
572	Phosphorylation	KKDQDSRSAPEPKKP CCCCCCCCCCCCCCC	52.72	25159151
578	Acetylation	RSAPEPKKPEENPAS CCCCCCCCCCCCCHH	69.26	19608861
585	Phosphorylation	KPEENPASKFSSASK CCCCCCHHHCCCCCC	35.18	23403867
586	Acetylation	PEENPASKFSSASKY CCCCCHHHCCCCCCE	51.91	19608861
586	Ubiquitination	PEENPASKFSSASKY CCCCCHHHCCCCCCE	51.91	19608861
588	Phosphorylation	ENPASKFSSASKYAA CCCHHHCCCCCCEEE	28.82	23403867
589	Phosphorylation	NPASKFSSASKYAAL CCHHHCCCCCCEEEE	39.43	23403867
591	O-linked_Glycosylation	ASKFSSASKYAALSV HHHCCCCCCEEEEEC	28.31	30059200
591	Phosphorylation	ASKFSSASKYAALSV HHHCCCCCCEEEEEC	28.31	26074081
592	Ubiquitination	SKFSSASKYAALSVD HHCCCCCCEEEEECC	38.33	-
593	Phosphorylation	KFSSASKYAALSVDG HCCCCCCEEEEECCC	8.46	23927012
597	Phosphorylation	ASKYAALSVDGEDEN CCCEEEEECCCCCCC	17.28	23927012
609	Phosphorylation	DENEGEDYAE----- CCCCCCCCCC-----	14.34	23927012

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
230	S	Phosphorylation	Kinase	MAP3K7	O43318	GPS
406	S	Phosphorylation	Kinase	MELK	Q14680	PSP
422	S	Phosphorylation	Kinase	P90RSK	Q15418	PSP
422	S	Phosphorylation	Kinase	KS6B1	P23443	PhosphoELM
422	S	Phosphorylation	Kinase	MELK	Q14680	PSP
422	S	Phosphorylation	Kinase	P70-SUBFAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
422	S	Phosphorylation		15071500
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PABP1_HUMAN	PABPC1	physical	11274152
IF4B_HUMAN	EIF4B	physical	8816444
EIF3A_HUMAN	EIF3A	physical	8816444
IF4G1_HUMAN	EIF4G1	physical	22939629
RL29_HUMAN	RPL29	physical	22939629
PHAX_HUMAN	PHAX	physical	22939629
IF4G2_HUMAN	EIF4G2	physical	22939629
MYH9_HUMAN	MYH9	physical	22939629
NU107_HUMAN	NUP107	physical	22939629
NU153_HUMAN	NUP153	physical	22939629
NADAP_HUMAN	SLC4A1AP	physical	22939629
TCPW_HUMAN	CCT6B	physical	22939629
RPAC1_HUMAN	POLR1C	physical	22939629
ANM3_HUMAN	PRMT3	physical	22863883
SF01_HUMAN	SF1	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
TCPZ_HUMAN	CCT6A	physical	26344197
COF1_HUMAN	CFL1	physical	26344197
CSTF2_HUMAN	CSTF2	physical	26344197
PYRG1_HUMAN	CTPS1	physical	26344197
DX39A_HUMAN	DDX39A	physical	26344197
DOHH_HUMAN	DOHH	physical	26344197
IF4G1_HUMAN	EIF4G1	physical	26344197
ERF3A_HUMAN	GSPT1	physical	26344197
HSPB1_HUMAN	HSPB1	physical	26344197
IMDH2_HUMAN	IMPDH2	physical	26344197
FUBP2_HUMAN	KHSRP	physical	26344197
PABP1_HUMAN	PABPC1	physical	26344197
1433S_HUMAN	SFN	physical	26344197
1433T_HUMAN	YWHAQ	physical	26344197
1433Z_HUMAN	YWHAZ	physical	26344197

Drug and Disease Associations

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

Regulatory Network of IF4B_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-586, AND MASS SPECTROMETRY.	19608861 [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-597, AND MASSSPECTROMETRY.	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-16; SER-93; THR-420;SER-422; SER-424; SER-425; SER-459; THR-461; SER-462; SER-498;THR-500; SER-504 AND SER-597, AND MASS 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-93; SER-219; SER-283;SER-459; SER-495; SER-498; SER-504 AND SER-597, AND MASS 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-406, AND MASSSPECTROMETRY.	18220336 [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-422, AND MASSSPECTROMETRY.	17924679 [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-192; SER-459; THR-461AND SER-495, AND MASS SPECTROMETRY.	17287340 [Abstract]
"The mTOR/PI3K and MAPK pathways converge on eIF4B to control itsphosphorylation and activity."; Shahbazian D., Roux P.P., Mieulet V., Cohen M.S., Raught B.,Taunton J., Hershey J.W., Blenis J., Pende M., Sonenberg N.; EMBO J. 25:2781-2791(2006). Cited for: PHOSPHORYLATION AT SER-422.	16763566 [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-406; SER-445; SER-459AND SER-504, 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-422; SER-425 ANDSER-504, AND MASS SPECTROMETRY.	16083285 [Abstract]
"Phosphorylation of eucaryotic translation initiation factor 4B Ser422is modulated by S6 kinases."; Raught B., Peiretti F., Gingras A.C., Livingstone M., Shahbazian D.,Mayeur G.L., Polakiewicz R.D., Sonenberg N., Hershey J.W.; EMBO J. 23:1761-1769(2004). Cited for: PHOSPHORYLATION AT SER-422.	15071500 [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-93; SER-498 AND SER-504,AND MASS SPECTROMETRY.	15302935 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-211, AND MASSSPECTROMETRY.	17389395 [Abstract]

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