dbPTM

IF4A1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF4A1_HUMAN
UniProt AC	P60842
Protein Name	Eukaryotic initiation factor 4A-I
Gene Name	EIF4A1
Organism	Homo sapiens (Human).
Sequence Length	406
Subcellular Localization
Protein Description	ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon..
Protein Sequence	MSASQDSRSRDNGPDGMEPEGVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEKPSAIQQRAILPCIKGYDVIAQAQSGTGKTATFAISILQQIELDLKATQALVLAPTRELAQQIQKVVMALGDYMGASCHACIGGTNVRAEVQKLQMEAPHIIVGTPGRVFDMLNRRYLSPKYIKMFVLDEADEMLSRGFKDQIYDIFQKLNSNTQVVLLSATMPSDVLEVTKKFMRDPIRILVKKEELTLEGIRQFYINVEREEWKLDTLCDLYETLTITQAVIFINTRRKVDWLTEKMHARDFTVSAMHGDMDQKERDVIMREFRSGSSRVLITTDLLARGIDVQQVSLVINYDLPTNRENYIHRIGRGGRFGRKGVAINMVTEEDKRTLRDIETFYNTSIEEMPLNVADLI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSASQDSRS ------CCCCCCCCC	36.31	21406692
4	Phosphorylation	----MSASQDSRSRD ----CCCCCCCCCCC	27.49	21406692
40	Phosphorylation	SFDDMNLSESLLRGI CCCCCCCCHHHHHHH	21.82	18452278
42	Phosphorylation	DDMNLSESLLRGIYA CCCCCCHHHHHHHHH	29.36	18452278
48	Phosphorylation	ESLLRGIYAYGFEKP HHHHHHHHHHCCCCC	9.15	28152594
50	Phosphorylation	LLRGIYAYGFEKPSA HHHHHHHHCCCCCCH	12.84	28152594
54	Methylation	IYAYGFEKPSAIQQR HHHHCCCCCCHHHHH	41.85	19608861
54	Acetylation	IYAYGFEKPSAIQQR HHHHCCCCCCHHHHH	41.85	22642845
54	Sumoylation	IYAYGFEKPSAIQQR HHHHCCCCCCHHHHH	41.85	-
54	Ubiquitination	IYAYGFEKPSAIQQR HHHHCCCCCCHHHHH	41.85	27667366
54	Sumoylation	IYAYGFEKPSAIQQR HHHHCCCCCCHHHHH	41.85	19608861
54	Malonylation	IYAYGFEKPSAIQQR HHHHCCCCCCHHHHH	41.85	26320211
56	Phosphorylation	AYGFEKPSAIQQRAI HHCCCCCCHHHHHCH	49.42	28152594
66	S-nitrosocysteine	QQRAILPCIKGYDVI HHHCHHHHHCCCEEE	4.50	-
66	S-nitrosylation	QQRAILPCIKGYDVI HHHCHHHHHCCCEEE	4.50	19483679
68	Sumoylation	RAILPCIKGYDVIAQ HCHHHHHCCCEEEEE	59.12	-
68	Ubiquitination	RAILPCIKGYDVIAQ HCHHHHHCCCEEEEE	59.12	23000965
68	Sumoylation	RAILPCIKGYDVIAQ HCHHHHHCCCEEEEE	59.12	-
68	Neddylation	RAILPCIKGYDVIAQ HCHHHHHCCCEEEEE	59.12	32015554
68	Acetylation	RAILPCIKGYDVIAQ HCHHHHHCCCEEEEE	59.12	25953088
70	Phosphorylation	ILPCIKGYDVIAQAQ HHHHHCCCEEEEEEC	11.31	20090780
70	Nitration	ILPCIKGYDVIAQAQ HHHHHCCCEEEEEEC	11.31	-
78	Phosphorylation	DVIAQAQSGTGKTAT EEEEEECCCCCHHHH	41.14	20873877
80	Phosphorylation	IAQAQSGTGKTATFA EEEECCCCCHHHHHH	40.53	20873877
82	Ubiquitination	QAQSGTGKTATFAIS EECCCCCHHHHHHHH	34.52	16196087
99	Sumoylation	QQIELDLKATQALVL HHHCCCCHHHHHHHH	49.40	-
109	Phosphorylation	QALVLAPTRELAQQI HHHHHHCHHHHHHHH	31.04	20068231
118	Acetylation	ELAQQIQKVVMALGD HHHHHHHHHHHHHHH	38.12	19608861
118	Ubiquitination	ELAQQIQKVVMALGD HHHHHHHHHHHHHHH	38.12	22817900
121	Sulfoxidation	QQIQKVVMALGDYMG HHHHHHHHHHHHHCC	2.59	30846556
127	Sulfoxidation	VMALGDYMGASCHAC HHHHHHHCCCCCCCC	4.26	30846556
130	Phosphorylation	LGDYMGASCHACIGG HHHHCCCCCCCCCCC	10.74	-
146	Acetylation	NVRAEVQKLQMEAPH HHHHHHHHHHHCCCE	45.95	23954790
146	Ubiquitination	NVRAEVQKLQMEAPH HHHHHHHHHHHCCCE	45.95	27667366
146	Sumoylation	NVRAEVQKLQMEAPH HHHHHHHHHHHCCCE	45.95	28112733
146	Malonylation	NVRAEVQKLQMEAPH HHHHHHHHHHHCCCE	45.95	26320211
149	Sulfoxidation	AEVQKLQMEAPHIIV HHHHHHHHCCCEEEE	7.41	21406390
158	Phosphorylation	APHIIVGTPGRVFDM CCEEEEECCCHHHHH	16.21	25159151
165	Sulfoxidation	TPGRVFDMLNRRYLS CCCHHHHHHCCCCCC	2.13	21406390
168	Methylation	RVFDMLNRRYLSPKY HHHHHHCCCCCCHHH	25.34	-
172	Phosphorylation	MLNRRYLSPKYIKMF HHCCCCCCHHHEEEE	15.48	24719451
174	Acetylation	NRRYLSPKYIKMFVL CCCCCCHHHEEEEEC	57.12	19608861
174	Ubiquitination	NRRYLSPKYIKMFVL CCCCCCHHHEEEEEC	57.12	23000965
174	Malonylation	NRRYLSPKYIKMFVL CCCCCCHHHEEEEEC	57.12	26320211
177	Ubiquitination	YLSPKYIKMFVLDEA CCCHHHEEEEECHHH	24.16	23000965
178	Sulfoxidation	LSPKYIKMFVLDEAD CCHHHEEEEECHHHH	1.72	21406390
187	Sulfoxidation	VLDEADEMLSRGFKD ECHHHHHHHHCCCHH	4.19	30846556
189	Phosphorylation	DEADEMLSRGFKDQI HHHHHHHHCCCHHHH	29.10	23911959
193	Methylation	EMLSRGFKDQIYDIF HHHHCCCHHHHHHHH	52.10	-
193	Acetylation	EMLSRGFKDQIYDIF HHHHCCCHHHHHHHH	52.10	23954790
193	Sumoylation	EMLSRGFKDQIYDIF HHHHCCCHHHHHHHH	52.10	-
193	Ubiquitination	EMLSRGFKDQIYDIF HHHHCCCHHHHHHHH	52.10	23000965
193	Sumoylation	EMLSRGFKDQIYDIF HHHHCCCHHHHHHHH	52.10	-
193	Succinylation	EMLSRGFKDQIYDIF HHHHCCCHHHHHHHH	52.10	23954790
197	Phosphorylation	RGFKDQIYDIFQKLN CCCHHHHHHHHHHCC	9.43	27273156
197	Nitration	RGFKDQIYDIFQKLN CCCHHHHHHHHHHCC	9.43	-
202	Ubiquitination	QIYDIFQKLNSNTQV HHHHHHHHCCCCCEE	38.60	29967540
202	Sumoylation	QIYDIFQKLNSNTQV HHHHHHHHCCCCCEE	38.60	-
205	Phosphorylation	DIFQKLNSNTQVVLL HHHHHCCCCCEEEEE	52.25	20068231
207	Phosphorylation	FQKLNSNTQVVLLSA HHHCCCCCEEEEEEC	23.67	20068231
213	Phosphorylation	NTQVVLLSATMPSDV CCEEEEEECCCCHHH	19.96	20068231
215	Phosphorylation	QVVLLSATMPSDVLE EEEEEECCCCHHHHH	26.66	20068231
216	Sulfoxidation	VVLLSATMPSDVLEV EEEEECCCCHHHHHH	2.75	28465586
218	Phosphorylation	LLSATMPSDVLEVTK EEECCCCHHHHHHHH	29.54	21082442
224	Phosphorylation	PSDVLEVTKKFMRDP CHHHHHHHHHHHCCC	21.09	20068231
225	Sumoylation	SDVLEVTKKFMRDPI HHHHHHHHHHHCCCE	49.54	-
225	Ubiquitination	SDVLEVTKKFMRDPI HHHHHHHHHHHCCCE	49.54	21906983
225	Sumoylation	SDVLEVTKKFMRDPI HHHHHHHHHHHCCCE	49.54	28112733
225	Neddylation	SDVLEVTKKFMRDPI HHHHHHHHHHHCCCE	49.54	32015554
225	Acetylation	SDVLEVTKKFMRDPI HHHHHHHHHHHCCCE	49.54	25953088
226	Ubiquitination	DVLEVTKKFMRDPIR HHHHHHHHHHCCCEE	34.72	22817900
226	Malonylation	DVLEVTKKFMRDPIR HHHHHHHHHHCCCEE	34.72	26320211
226	Acetylation	DVLEVTKKFMRDPIR HHHHHHHHHHCCCEE	34.72	25953088
237	Ubiquitination	DPIRILVKKEELTLE CCEEEEEECCEECHH	51.53	23000965
237	Malonylation	DPIRILVKKEELTLE CCEEEEEECCEECHH	51.53	26320211
237	Acetylation	DPIRILVKKEELTLE CCEEEEEECCEECHH	51.53	26051181
238	Acetylation	PIRILVKKEELTLEG CEEEEEECCEECHHH	49.28	23954790
238	Sumoylation	PIRILVKKEELTLEG CEEEEEECCEECHHH	49.28	-
238	Ubiquitination	PIRILVKKEELTLEG CEEEEEECCEECHHH	49.28	23000965
238	Sumoylation	PIRILVKKEELTLEG CEEEEEECCEECHHH	49.28	28112733
238	Malonylation	PIRILVKKEELTLEG CEEEEEECCEECHHH	49.28	26320211
242	Phosphorylation	LVKKEELTLEGIRQF EEECCEECHHHHHHE	26.50	21815630
250	Phosphorylation	LEGIRQFYINVEREE HHHHHHEEEEECCHH	5.35	28152594
255	Methylation	QFYINVEREEWKLDT HEEEEECCHHHCHHH	42.74	-
262	Phosphorylation	REEWKLDTLCDLYET CHHHCHHHHHHHHHH	39.46	20068231
267	Phosphorylation	LDTLCDLYETLTITQ HHHHHHHHHHHCEEE	8.13	20068231
284	Ubiquitination	IFINTRRKVDWLTEK HHHCCCCCCHHHHHH	41.05	21963094
284	Malonylation	IFINTRRKVDWLTEK HHHCCCCCCHHHHHH	41.05	26320211
284	Acetylation	IFINTRRKVDWLTEK HHHCCCCCCHHHHHH	41.05	26051181
291	Acetylation	KVDWLTEKMHARDFT CCHHHHHHHHHCCCC	30.65	23236377
291	Sumoylation	KVDWLTEKMHARDFT CCHHHHHHHHHCCCC	30.65	-
291	Ubiquitination	KVDWLTEKMHARDFT CCHHHHHHHHHCCCC	30.65	27667366
291	Sumoylation	KVDWLTEKMHARDFT CCHHHHHHHHHCCCC	30.65	19608861
291	Malonylation	KVDWLTEKMHARDFT CCHHHHHHHHHCCCC	30.65	26320211
298	Phosphorylation	KMHARDFTVSAMHGD HHHHCCCCCEECCCC	20.17	25101063
300	Phosphorylation	HARDFTVSAMHGDMD HHCCCCCEECCCCCC	19.47	25101063
302	Sulfoxidation	RDFTVSAMHGDMDQK CCCCCEECCCCCCHH	2.57	30846556
306	Sulfoxidation	VSAMHGDMDQKERDV CEECCCCCCHHHHHH	7.52	30846556
309	Acetylation	MHGDMDQKERDVIMR CCCCCCHHHHHHHHH	50.91	23954790
309	Ubiquitination	MHGDMDQKERDVIMR CCCCCCHHHHHHHHH	50.91	27667366
309	Malonylation	MHGDMDQKERDVIMR CCCCCCHHHHHHHHH	50.91	26320211
309	Sumoylation	MHGDMDQKERDVIMR CCCCCCHHHHHHHHH	50.91	28112733
316	Methylation	KERDVIMREFRSGSS HHHHHHHHHHHCCCC	28.86	-
320 (in isoform 2)	Phosphorylation	-	48.63	27174698
322	O-linked_Glycosylation	MREFRSGSSRVLITT HHHHHCCCCCEEEEH	19.06	23301498
322 (in isoform 2)	Phosphorylation	-	19.06	27174698
323	O-linked_Glycosylation	REFRSGSSRVLITTD HHHHCCCCCEEEEHH	29.90	23301498
323 (in isoform 2)	Phosphorylation	-	29.90	27174698
328	Phosphorylation	GSSRVLITTDLLARG CCCCEEEEHHHHHCC	15.31	21712546
328 (in isoform 2)	Phosphorylation	-	15.31	27174698
329	Phosphorylation	SSRVLITTDLLARGI CCCEEEEHHHHHCCC	20.04	21712546
329 (in isoform 2)	Phosphorylation	-	20.04	27174698
336 (in isoform 2)	Phosphorylation	-	3.80	27174698
341 (in isoform 2)	Phosphorylation	-	2.39	27174698
353	Methylation	NYDLPTNRENYIHRI ECCCCCCCHHHCHHC	35.70	-
369	Ubiquitination	RGGRFGRKGVAINMV CCCCCCCCCEEEEEC	59.10	21906983
369	Acetylation	RGGRFGRKGVAINMV CCCCCCCCCEEEEEC	59.10	26051181
369	Sumoylation	RGGRFGRKGVAINMV CCCCCCCCCEEEEEC	59.10	28112733
375	Sulfoxidation	RKGVAINMVTEEDKR CCCEEEEECCHHHHH	3.01	30846556
377	Phosphorylation	GVAINMVTEEDKRTL CEEEEECCHHHHHHH	23.92	20068231
381	Acetylation	NMVTEEDKRTLRDIE EECCHHHHHHHHHHH	51.03	23954790
381	Ubiquitination	NMVTEEDKRTLRDIE EECCHHHHHHHHHHH	51.03	27667366
381	Sumoylation	NMVTEEDKRTLRDIE EECCHHHHHHHHHHH	51.03	28112733
389	Phosphorylation	RTLRDIETFYNTSIE HHHHHHHHHHCCCHH	31.58	20068231
391	Phosphorylation	LRDIETFYNTSIEEM HHHHHHHHCCCHHHC	25.58	20068231
393	Phosphorylation	DIETFYNTSIEEMPL HHHHHHCCCHHHCCC	21.50	20068231
394	Phosphorylation	IETFYNTSIEEMPLN HHHHHCCCHHHCCCC	25.10	20068231
398	Sulfoxidation	YNTSIEEMPLNVADL HCCCHHHCCCCHHHC	2.72	30846556

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 IF4A1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF4A1_HUMAN !!

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 IF4A1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF4G1_HUMAN	EIF4G1	physical	17353931
PDCD4_HUMAN	PDCD4	physical	17353931
EIF3A_HUMAN	EIF3A	physical	17353931
IF4G3_HUMAN	EIF4G3	physical	17353931
IF4E_HUMAN	EIF4E	physical	17353931
PDCD4_HUMAN	PDCD4	physical	17053147
IF4G1_HUMAN	EIF4G1	physical	17053147
EIF3B_HUMAN	EIF3B	physical	17053147
PDCD4_HUMAN	PDCD4	physical	22586265
IF4G1_HUMAN	EIF4G1	physical	22586265
IF4G1_HUMAN	EIF4G1	physical	22939629
IF4G2_HUMAN	EIF4G2	physical	22939629
IF4G3_HUMAN	EIF4G3	physical	22939629
IF4H_HUMAN	EIF4H	physical	22939629
IF4B_HUMAN	EIF4B	physical	22939629
IF4A2_HUMAN	EIF4A2	physical	22939629
RSSA_HUMAN	RPSA	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RL19_HUMAN	RPL19	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
TMM43_HUMAN	TMEM43	physical	22939629
MRP2_HUMAN	ABCC2	physical	22939629
VDAC3_HUMAN	VDAC3	physical	22939629
ZBT43_HUMAN	ZBTB43	physical	22939629
ILF2_HUMAN	ILF2	physical	22939629
VATA_HUMAN	ATP6V1A	physical	22939629
UCRI_HUMAN	UQCRFS1	physical	22939629
RAI3_HUMAN	GPRC5A	physical	22939629
NDUBB_HUMAN	NDUFB11	physical	22939629
LAGE3_HUMAN	LAGE3	physical	26344197
NFYB_HUMAN	NFYB	physical	26344197
IBTK_HUMAN	IBTK	physical	28514442
IF4G3_HUMAN	EIF4G3	physical	28514442
PDCD4_HUMAN	PDCD4	physical	28514442
IF4G2_HUMAN	EIF4G2	physical	28514442
IF4G1_HUMAN	EIF4G1	physical	28514442
IF4A2_HUMAN	EIF4A2	physical	28514442
CAF17_HUMAN	IBA57	physical	28514442
IF4A3_HUMAN	EIF4A3	physical	28514442
EIF3A_HUMAN	EIF3A	physical	28514442
EIF3E_HUMAN	EIF3E	physical	28514442
EIF3M_HUMAN	EIF3M	physical	28514442
RP25L_HUMAN	RPP25L	physical	28514442
EIF3C_HUMAN	EIF3C	physical	28514442
EIF3B_HUMAN	EIF3B	physical	28514442
IF4E3_HUMAN	EIF4E3	physical	28514442
EIF3D_HUMAN	EIF3D	physical	28514442
KIF1B_HUMAN	KIF1B	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 IF4A1_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-118; LYS-174 AND LYS-309,AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 THR-158, AND MASSSPECTROMETRY.	18669648 [Abstract]