dbPTM

EIF3E_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF3E_HUMAN
UniProt AC	P60228
Protein Name	Eukaryotic translation initiation factor 3 subunit E {ECO:0000255\|HAMAP-Rule:MF_03004}
Gene Name	EIF3E {ECO:0000255\|HAMAP-Rule:MF_03004}
Organism	Homo sapiens (Human).
Sequence Length	445
Subcellular Localization	Cytoplasm. Nucleus, PML body.
Protein Description	Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. [PubMed: 17581632]
Protein Sequence	MAEYDLTTRIAHFLDRHLVFPLLEFLSVKEIYNEKELLQGKLDLLSDTNMVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEYDLTTR ------CCCCCCHHH	24.85	17322308
4	Phosphorylation	----MAEYDLTTRIA ----CCCCCCHHHHH	13.50	24043423
7	Phosphorylation	-MAEYDLTTRIAHFL -CCCCCCHHHHHHHH	15.90	30387612
8	Phosphorylation	MAEYDLTTRIAHFLD CCCCCCHHHHHHHHH	27.63	30387612
29	Ubiquitination	LLEFLSVKEIYNEKE HHHHHCHHHHHCHHH	34.71	23000965
32	Phosphorylation	FLSVKEIYNEKELLQ HHCHHHHHCHHHHHC	20.54	28152594
35	Acetylation	VKEIYNEKELLQGKL HHHHHCHHHHHCCHH	50.45	23954790
35	Ubiquitination	VKEIYNEKELLQGKL HHHHHCHHHHHCCHH	50.45	23000965
35	2-Hydroxyisobutyrylation	VKEIYNEKELLQGKL HHHHHCHHHHHCCHH	50.45	-
41	Ubiquitination	EKELLQGKLDLLSDT HHHHHCCHHCHHCCC	26.35	23000965
50	Sulfoxidation	DLLSDTNMVDFAMDV CHHCCCCHHHHHHHH	3.12	30846556
55	Sulfoxidation	TNMVDFAMDVYKNLY CCHHHHHHHHHHHHC	3.46	30846556
57	Ubiquitination	MVDFAMDVYKNLYSD HHHHHHHHHHHHCCC	4.75	23000965
59	Ubiquitination	DFAMDVYKNLYSDDI HHHHHHHHHHCCCCC	40.08	29967540
62	Phosphorylation	MDVYKNLYSDDIPHA HHHHHHHCCCCCCHH	21.32	28152594
63	Ubiquitination	DVYKNLYSDDIPHAL HHHHHHCCCCCCHHH	31.79	23000965
63	Phosphorylation	DVYKNLYSDDIPHAL HHHHHHCCCCCCHHH	31.79	28152594
69	Ubiquitination	YSDDIPHALREKRTT CCCCCCHHHHHCHHH	11.71	23000965
75	Phosphorylation	HALREKRTTVVAQLK HHHHHCHHHHHHHHH	34.70	21406692
76	Phosphorylation	ALREKRTTVVAQLKQ HHHHCHHHHHHHHHH	19.60	21406692
82	Ubiquitination	TTVVAQLKQLQAETE HHHHHHHHHHHHHCC	36.56	23000965
82	Acetylation	TTVVAQLKQLQAETE HHHHHHHHHHHHHCC	36.56	25953088
87	Ubiquitination	QLKQLQAETEPIVKM HHHHHHHHCCCHHHH	40.52	17623298
93	Ubiquitination	AETEPIVKMFEDPET HHCCCHHHHHCCHHH	38.29	21906983
94	Sulfoxidation	ETEPIVKMFEDPETT HCCCHHHHHCCHHHH	2.85	21406390
110	Ubiquitination	QMQSTRDGRMLFDYL HHHHCCCCHHHHHHH	17.38	23000965
116	Phosphorylation	DGRMLFDYLADKHGF CCHHHHHHHHHHCCC	9.10	23312004
120	Ubiquitination	LFDYLADKHGFRQEY HHHHHHHHCCCCHHH	39.77	23000965
120	Acetylation	LFDYLADKHGFRQEY HHHHHHHHCCCCHHH	39.77	21466224
121	Ubiquitination	FDYLADKHGFRQEYL HHHHHHHCCCCHHHH	40.97	21963094
136	Ubiquitination	DTLYRYAKFQYECGN HHHHHHHCCCCCCCC	24.86	21963094
148	Ubiquitination	CGNYSGAAEYLYFFR CCCCCCHHHHHHHHE	14.97	23000965
161	Phosphorylation	FRVLVPATDRNALSS HEECCCCCCHHHHHH	29.44	20068231
163	Methylation	VLVPATDRNALSSLW ECCCCCCHHHHHHHH	26.43	-
164	Ubiquitination	LVPATDRNALSSLWG CCCCCCHHHHHHHHH	48.30	21963094
172	Ubiquitination	ALSSLWGKLASEILM HHHHHHHHHHHHHHH	29.33	17623298
190	Phosphorylation	DAAMEDLTRLKETID HHHHHHHHHHHHHHC	46.40	20068231
193	Acetylation	MEDLTRLKETIDNNS HHHHHHHHHHHCCCC	49.90	20167786
193	Ubiquitination	MEDLTRLKETIDNNS HHHHHHHHHHHCCCC	49.90	21906983
193	2-Hydroxyisobutyrylation	MEDLTRLKETIDNNS HHHHHHHHHHHCCCC	49.90	-
195	Phosphorylation	DLTRLKETIDNNSVS HHHHHHHHHCCCCCC	31.85	26846344
200	Ubiquitination	KETIDNNSVSSPLQS HHHHCCCCCCCHHHH	29.63	17623298
200	Phosphorylation	KETIDNNSVSSPLQS HHHHCCCCCCCHHHH	29.63	26846344
202	Phosphorylation	TIDNNSVSSPLQSLQ HHCCCCCCCHHHHHH	26.51	30624053
203	Phosphorylation	IDNNSVSSPLQSLQQ HCCCCCCCHHHHHHH	27.72	21815630
207	Phosphorylation	SVSSPLQSLQQRTWL CCCCHHHHHHHHHHH	35.51	26846344
212	Phosphorylation	LQSLQQRTWLIHWSL HHHHHHHHHHHHHHH	21.93	26074081
218	Phosphorylation	RTWLIHWSLFVFFNH HHHHHHHHHHHHHCC	9.58	26074081
221	Ubiquitination	LIHWSLFVFFNHPKG HHHHHHHHHHCCCCC	6.94	27667366
256	Phosphorylation	MCPHILRYLTTAVIT HCHHHHHHHHHHHHC	12.64	28152594
258	Phosphorylation	PHILRYLTTAVITNK HHHHHHHHHHHHCCH	12.08	28152594
265	Ubiquitination	TTAVITNKDVRKRRQ HHHHHCCHHHHHHHH	49.29	27667366
265	Malonylation	TTAVITNKDVRKRRQ HHHHHCCHHHHHHHH	49.29	26320211
265	Acetylation	TTAVITNKDVRKRRQ HHHHHCCHHHHHHHH	49.29	26051181
269	Ubiquitination	ITNKDVRKRRQVLKD HCCHHHHHHHHHHHH	52.35	22817900
275	Acetylation	RKRRQVLKDLVKVIQ HHHHHHHHHHHHHHH	50.59	23749302
275	Ubiquitination	RKRRQVLKDLVKVIQ HHHHHHHHHHHHHHH	50.59	22817900
275	Malonylation	RKRRQVLKDLVKVIQ HHHHHHHHHHHHHHH	50.59	26320211
279	Ubiquitination	QVLKDLVKVIQQESY HHHHHHHHHHHHCCC	40.70	21906983
286	Phosphorylation	KVIQQESYTYKDPIT HHHHHCCCCCCCCHH	17.21	-
293	Ubiquitination	YTYKDPITEFVECLY CCCCCCHHHHHHHHE	28.85	27667366
297	Ubiquitination	DPITEFVECLYVNFD CCHHHHHHHHEEECC	24.91	22817900
303	Ubiquitination	VECLYVNFDFDGAQK HHHHEEECCCCCHHH	7.65	22817900
307	Ubiquitination	YVNFDFDGAQKKLRE EEECCCCCHHHHHHH	29.87	22817900
359	Ubiquitination	SINMLADKLNMTPEE HHHHHHHHCCCCHHH	35.83	21963094
359	Acetylation	SINMLADKLNMTPEE HHHHHHHHCCCCHHH	35.83	26051181
362	Sulfoxidation	MLADKLNMTPEEAER HHHHHCCCCHHHHHH	10.82	21406390
363	Phosphorylation	LADKLNMTPEEAERW HHHHCCCCHHHHHHH	26.86	21815630
383	Ubiquitination	RNARLDAKIDSKLGH HHHCCCCCCCCCCCC	46.87	21906983
387	Ubiquitination	LDAKIDSKLGHVVMG CCCCCCCCCCCEEEC	55.53	27667366
387	2-Hydroxyisobutyrylation	LDAKIDSKLGHVVMG CCCCCCCCCCCEEEC	55.53	-
387	Acetylation	LDAKIDSKLGHVVMG CCCCCCCCCCCEEEC	55.53	25953088
393	Sulfoxidation	SKLGHVVMGNNAVSP CCCCCEEECCCCCCH	4.65	30846556
399	Phosphorylation	VMGNNAVSPYQQVIE EECCCCCCHHHHHHH	18.58	22167270
401	Phosphorylation	GNNAVSPYQQVIEKT CCCCCCHHHHHHHHH	12.22	22167270
407	Ubiquitination	PYQQVIEKTKSLSFR HHHHHHHHHHCCCHH	50.56	21906983
407	Malonylation	PYQQVIEKTKSLSFR HHHHHHHHHHCCCHH	50.56	26320211
407	Acetylation	PYQQVIEKTKSLSFR HHHHHHHHHHCCCHH	50.56	25953088
409	Sumoylation	QQVIEKTKSLSFRSQ HHHHHHHHCCCHHHH	61.54	-
409	Ubiquitination	QQVIEKTKSLSFRSQ HHHHHHHHCCCHHHH	61.54	27667366
409	Sumoylation	QQVIEKTKSLSFRSQ HHHHHHHHCCCHHHH	61.54	-
409	2-Hydroxyisobutyrylation	QQVIEKTKSLSFRSQ HHHHHHHHCCCHHHH	61.54	-
409	Malonylation	QQVIEKTKSLSFRSQ HHHHHHHHCCCHHHH	61.54	26320211
410	Phosphorylation	QVIEKTKSLSFRSQM HHHHHHHCCCHHHHH	34.18	26434776
411	Ubiquitination	VIEKTKSLSFRSQML HHHHHHCCCHHHHHH	6.30	21963094
412	Phosphorylation	IEKTKSLSFRSQMLA HHHHHCCCHHHHHHH	26.21	25159151
415	Ubiquitination	TKSLSFRSQMLAMNI HHCCCHHHHHHHHHH	20.24	27667366
415	Phosphorylation	TKSLSFRSQMLAMNI HHCCCHHHHHHHHHH	20.24	29888752
417	Sulfoxidation	SLSFRSQMLAMNIEK CCCHHHHHHHHHHHH	2.44	21406390
420	Sulfoxidation	FRSQMLAMNIEKKLN HHHHHHHHHHHHHHC	4.58	30846556
424	Ubiquitination	MLAMNIEKKLNQNSR HHHHHHHHHHCCCCC	59.78	27667366
424	Acetylation	MLAMNIEKKLNQNSR HHHHHHHHHHCCCCC	59.78	25953088
425	Ubiquitination	LAMNIEKKLNQNSRS HHHHHHHHHCCCCCC	39.62	21906983
432	Phosphorylation	KLNQNSRSEAPNWAT HHCCCCCCCCCCCCC	37.62	24247654
435	Ubiquitination	QNSRSEAPNWATQDS CCCCCCCCCCCCCCC	32.61	27667366
437	Ubiquitination	SRSEAPNWATQDSGF CCCCCCCCCCCCCCC	10.30	27667366
439	Phosphorylation	SEAPNWATQDSGFY- CCCCCCCCCCCCCC-	25.23	23403867
442	Phosphorylation	PNWATQDSGFY---- CCCCCCCCCCC----	22.45	23403867
445	Phosphorylation	ATQDSGFY------- CCCCCCCC-------	22.59	28152594
452	Ubiquitination	Y-------------- C--------------		27667366
453	Ubiquitination	--------------- ---------------		21963094

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 EIF3E_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF3E_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 EIF3E_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRC2A_HUMAN	PRRC2A	physical	14667819
GPBL1_HUMAN	GPBP1L1	physical	16189514
RUN3A_HUMAN	RUNDC3A	physical	16189514
HAP1_HUMAN	HAP1	physical	16169070
EIF3A_HUMAN	EIF3A	physical	11590142
CASK_HUMAN	CSN3	physical	12220626
CSN6_HUMAN	COPS6	physical	12220626
IFIT1_HUMAN	IFIT1	physical	10644362
TRI27_HUMAN	TRIM27	physical	10504338
PSD12_HUMAN	PSMD12	physical	20890303
EIF3D_HUMAN	EIF3D	physical	20890303
PRS10_HUMAN	PSMC6	physical	20890303
FBXW7_HUMAN	FBXW7	physical	20890303
NCOA3_HUMAN	NCOA3	physical	20890303
EIF3B_HUMAN	EIF3B	physical	18599441
ATM_HUMAN	ATM	physical	22508697
EIF3A_HUMAN	EIF3A	physical	17403899
EIF3B_HUMAN	EIF3B	physical	17403899
EIF3C_HUMAN	EIF3C	physical	17403899
EIF3D_HUMAN	EIF3D	physical	17403899
EIF3F_HUMAN	EIF3F	physical	17403899
EIF3G_HUMAN	EIF3G	physical	17403899
EIF3H_HUMAN	EIF3H	physical	17403899
EIF3I_HUMAN	EIF3I	physical	17403899
EIF3J_HUMAN	EIF3J	physical	17403899
EIF3K_HUMAN	EIF3K	physical	17403899
EIF3L_HUMAN	EIF3L	physical	17403899
EIF3H_HUMAN	EIF3H	physical	22939629
EIF3F_HUMAN	EIF3F	physical	22939629
EIF3L_HUMAN	EIF3L	physical	22939629
EIF3K_HUMAN	EIF3K	physical	22939629
EIF3G_HUMAN	EIF3G	physical	22939629
EIF3I_HUMAN	EIF3I	physical	22939629
EIF3M_HUMAN	EIF3M	physical	22939629
NP1L4_HUMAN	NAP1L4	physical	22939629
NPM_HUMAN	NPM1	physical	21988832
EIF3C_HUMAN	EIF3C	physical	22863883
EIF3D_HUMAN	EIF3D	physical	22863883
EIF3K_HUMAN	EIF3K	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
RS25_HUMAN	RPS25	physical	22863883
RS28_HUMAN	RPS28	physical	22863883
RS8_HUMAN	RPS8	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
RUN3A_HUMAN	RUNDC3A	physical	25416956
CD019_HUMAN	C4orf19	physical	25416956
AN32A_HUMAN	ANP32A	physical	26344197
DIEXF_HUMAN	DIEXF	physical	26344197
EIF3A_HUMAN	EIF3A	physical	26344197
EIF3B_HUMAN	EIF3B	physical	26344197
EIF3C_HUMAN	EIF3C	physical	26344197
EIFCL_HUMAN	EIF3CL	physical	26344197
EIF3D_HUMAN	EIF3D	physical	26344197
EIF3F_HUMAN	EIF3F	physical	26344197
EIF3G_HUMAN	EIF3G	physical	26344197
EIF3H_HUMAN	EIF3H	physical	26344197
EIF3K_HUMAN	EIF3K	physical	26344197
EIF3L_HUMAN	EIF3L	physical	26344197
EIF3M_HUMAN	EIF3M	physical	26344197
NIP7_HUMAN	NIP7	physical	26344197
NUMA1_HUMAN	NUMA1	physical	26344197
SPT4H_HUMAN	SUPT4H1	physical	26344197
EIF3M_HUMAN	EIF3M	physical	17403899
MISSL_HUMAN	MAPK1IP1L	physical	21516116
EIFCL_HUMAN	EIF3CL	physical	28514442
EIF3L_HUMAN	EIF3L	physical	28514442
EIF3A_HUMAN	EIF3A	physical	28514442
EIF3C_HUMAN	EIF3C	physical	28514442
EIF3B_HUMAN	EIF3B	physical	28514442
EIF3D_HUMAN	EIF3D	physical	28514442
EIF3K_HUMAN	EIF3K	physical	28514442
PRC2B_HUMAN	PRRC2B	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 EIF3E_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry."; Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.; Mol. Cell. Proteomics 6:1135-1146(2007). Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, ANDMASS SPECTROMETRY.	17322308 [Abstract]
"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-275, 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 SER-399, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, AND MASSSPECTROMETRY.	18691976 [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-445, AND MASSSPECTROMETRY.	15592455 [Abstract]