dbPTM

EIF3I_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF3I_HUMAN
UniProt AC	Q13347
Protein Name	Eukaryotic translation initiation factor 3 subunit I {ECO:0000255\|HAMAP-Rule:MF_03008}
Gene Name	EIF3I {ECO:0000255\|HAMAP-Rule:MF_03008}
Organism	Homo sapiens (Human).
Sequence Length	325
Subcellular Localization	Cytoplasm .
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	MKPILLQGHERSITQIKYNREGDLLFTVAKDPIVNVWYSVNGERLGTYMGHTGAVWCVDADWDTKHVLTGSADNSCRLWDCETGKQLALLKTNSAVRTCGFDFGGNIIMFSTDKQMGYQCFVSFFDLRDPSQIDNNEPYMKIPCNDSKITSAVWGPLGECIIAGHESGELNQYSAKSGEVLVNVKEHSRQINDIQLSRDMTMFVTASKDNTAKLFDSTTLEHQKTFRTERPVNSAALSPNYDHVVLGGGQEAMDVTTTSTRIGKFEARFFHLAFEEEFGRVKGHFGPINSVAFHPDGKSYSSGGEDGYVRIHYFDPQYFEFEFEA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Sumoylation	------MKPILLQGH ------CCCEEECCC	40.54	-
2	Sumoylation	------MKPILLQGH ------CCCEEECCC	40.54	-
2	Ubiquitination	------MKPILLQGH ------CCCEEECCC	40.54	21906983
14	Phosphorylation	QGHERSITQIKYNRE CCCCCEEEEEEECCC	26.03	-
17	Ubiquitination	ERSITQIKYNREGDL CCEEEEEEECCCCCE	27.01	21906983
17	Acetylation	ERSITQIKYNREGDL CCEEEEEEECCCCCE	27.01	26051181
30	Ubiquitination	DLLFTVAKDPIVNVW CEEEEEECCCEEEEE	60.75	21906983
30	Acetylation	DLLFTVAKDPIVNVW CEEEEEECCCEEEEE	60.75	7666227
65	Ubiquitination	VDADWDTKHVLTGSA EECCCCCCEEEECCC	29.28	-
69	Phosphorylation	WDTKHVLTGSADNSC CCCCEEEECCCCCCC	28.18	30108239
71	Phosphorylation	TKHVLTGSADNSCRL CCEEEECCCCCCCEE	27.49	30108239
75	Phosphorylation	LTGSADNSCRLWDCE EECCCCCCCEEEECC	10.93	30108239
77	Methylation	GSADNSCRLWDCETG CCCCCCCEEEECCCC	38.34	-
85	Acetylation	LWDCETGKQLALLKT EEECCCCCEEEEEEC	49.94	26051181
85	Ubiquitination	LWDCETGKQLALLKT EEECCCCCEEEEEEC	49.94	21906983
91	Acetylation	GKQLALLKTNSAVRT CCEEEEEECCCCCHH	46.65	25953088
91	Ubiquitination	GKQLALLKTNSAVRT CCEEEEEECCCCCHH	46.65	21890473
139	Phosphorylation	QIDNNEPYMKIPCND HCCCCCCCEECCCCC	12.59	-
140	Sulfoxidation	IDNNEPYMKIPCNDS CCCCCCCEECCCCCH	4.67	21406390
141	Acetylation	DNNEPYMKIPCNDSK CCCCCCEECCCCCHH	37.34	26051181
141	Ubiquitination	DNNEPYMKIPCNDSK CCCCCCEECCCCCHH	37.34	-
144	S-nitrosylation	EPYMKIPCNDSKITS CCCEECCCCCHHHEE	11.42	19483679
144	S-nitrosocysteine	EPYMKIPCNDSKITS CCCEECCCCCHHHEE	11.42	-
148	Ubiquitination	KIPCNDSKITSAVWG ECCCCCHHHEEEEEC	53.52	-
148	Acetylation	KIPCNDSKITSAVWG ECCCCCHHHEEEEEC	53.52	26051181
176	Ubiquitination	ELNQYSAKSGEVLVN CCCCCCCCCCCEEEE	53.72	-
185	Sumoylation	GEVLVNVKEHSRQIN CCEEEEHHHHHHHCC	44.50	-
185	Acetylation	GEVLVNVKEHSRQIN CCEEEEHHHHHHHCC	44.50	27452117
185	Sumoylation	GEVLVNVKEHSRQIN CCEEEEHHHHHHHCC	44.50	-
185	2-Hydroxyisobutyrylation	GEVLVNVKEHSRQIN CCEEEEHHHHHHHCC	44.50	-
185	Ubiquitination	GEVLVNVKEHSRQIN CCEEEEHHHHHHHCC	44.50	21906983
200	Sulfoxidation	DIQLSRDMTMFVTAS EEECCCCCEEEEEEC	2.58	21406390
201	Phosphorylation	IQLSRDMTMFVTASK EECCCCCEEEEEECC	16.25	20068231
202	Sulfoxidation	QLSRDMTMFVTASKD ECCCCCEEEEEECCC	1.72	30846556
205	Phosphorylation	RDMTMFVTASKDNTA CCCEEEEEECCCCCC	17.59	20068231
207	Phosphorylation	MTMFVTASKDNTAKL CEEEEEECCCCCCCC	31.04	20068231
208	Ubiquitination	TMFVTASKDNTAKLF EEEEEECCCCCCCCC	53.16	21906983
213	Ubiquitination	ASKDNTAKLFDSTTL ECCCCCCCCCCCCCC	47.88	21906983
213	2-Hydroxyisobutyrylation	ASKDNTAKLFDSTTL ECCCCCCCCCCCCCC	47.88	-
213	Sumoylation	ASKDNTAKLFDSTTL ECCCCCCCCCCCCCC	47.88	-
213	Sumoylation	ASKDNTAKLFDSTTL ECCCCCCCCCCCCCC	47.88	-
213	Acetylation	ASKDNTAKLFDSTTL ECCCCCCCCCCCCCC	47.88	25953088
217	Phosphorylation	NTAKLFDSTTLEHQK CCCCCCCCCCCEEEC	18.89	26434776
218	Phosphorylation	TAKLFDSTTLEHQKT CCCCCCCCCCEEECE	36.93	26434776
219	Phosphorylation	AKLFDSTTLEHQKTF CCCCCCCCCEEECEE	33.82	26434776
224	Ubiquitination	STTLEHQKTFRTERP CCCCEEECEECCCCC	52.09	21906983
224	Acetylation	STTLEHQKTFRTERP CCCCEEECEECCCCC	52.09	26051181
234	Phosphorylation	RTERPVNSAALSPNY CCCCCCCCCCCCCCC	18.36	-
238	Phosphorylation	PVNSAALSPNYDHVV CCCCCCCCCCCCEEE	13.33	25159151
241	Phosphorylation	SAALSPNYDHVVLGG CCCCCCCCCEEEECC	15.71	22817900
256	Phosphorylation	GQEAMDVTTTSTRIG CCEEEECEECCCCEE	21.79	26434776
257	Phosphorylation	QEAMDVTTTSTRIGK CEEEECEECCCCEEE	20.71	26434776
258	Phosphorylation	EAMDVTTTSTRIGKF EEEECEECCCCEEEE	20.80	26434776
259	Phosphorylation	AMDVTTTSTRIGKFE EEECEECCCCEEEEE	17.37	28857561
260	Phosphorylation	MDVTTTSTRIGKFEA EECEECCCCEEEEEE	24.98	28857561
264	Ubiquitination	TTSTRIGKFEARFFH ECCCCEEEEEEEHHH	37.35	21890473
264	Malonylation	TTSTRIGKFEARFFH ECCCCEEEEEEEHHH	37.35	26320211
264	Acetylation	TTSTRIGKFEARFFH ECCCCEEEEEEEHHH	37.35	19608861
282	Sumoylation	EEEFGRVKGHFGPIN HHHHCCCCCCCCCCC	45.36	-
282	Sumoylation	EEEFGRVKGHFGPIN HHHHCCCCCCCCCCC	45.36	-
282	Acetylation	EEEFGRVKGHFGPIN HHHHCCCCCCCCCCC	45.36	26051181
282	Ubiquitination	EEEFGRVKGHFGPIN HHHHCCCCCCCCCCC	45.36	21890473
298	Acetylation	VAFHPDGKSYSSGGE EEECCCCCCCCCCCC	54.31	26051181
298	2-Hydroxyisobutyrylation	VAFHPDGKSYSSGGE EEECCCCCCCCCCCC	54.31	-
298	Ubiquitination	VAFHPDGKSYSSGGE EEECCCCCCCCCCCC	54.31	21890473
299	Phosphorylation	AFHPDGKSYSSGGED EECCCCCCCCCCCCC	35.46	28152594
300	Phosphorylation	FHPDGKSYSSGGEDG ECCCCCCCCCCCCCC	15.44	28152594
301	Phosphorylation	HPDGKSYSSGGEDGY CCCCCCCCCCCCCCE	29.60	28152594
302	Phosphorylation	PDGKSYSSGGEDGYV CCCCCCCCCCCCCEE	42.45	28152594
308	Nitration	SSGGEDGYVRIHYFD CCCCCCCEEEEEEEC	10.01	-
308	Phosphorylation	SSGGEDGYVRIHYFD CCCCCCCEEEEEEEC	10.01	20090780
318	Phosphorylation	IHYFDPQYFEFEFEA EEEECCCEEEEEEEC	15.51	27642862

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 EIF3I_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF3I_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 EIF3I_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF3K_HUMAN	EIF3K	physical	22939629
EIF3M_HUMAN	EIF3M	physical	22939629
EIF3L_HUMAN	EIF3L	physical	22939629
EIF3B_HUMAN	EIF3B	physical	22863883
EIF3B_HUMAN	EIF3B	physical	26186194
EIF3K_HUMAN	EIF3K	physical	26186194
HERC2_HUMAN	HERC2	physical	26186194
IF4G1_HUMAN	EIF4G1	physical	26186194
EIF3A_HUMAN	EIF3A	physical	26186194
EIF3H_HUMAN	EIF3H	physical	26186194
E41L1_HUMAN	EPB41L1	physical	26186194
PRC2B_HUMAN	PRRC2B	physical	26186194
EIF3F_HUMAN	EIF3F	physical	26186194
EIFCL_HUMAN	EIF3CL	physical	26186194
EIF3C_HUMAN	EIF3C	physical	26186194
EIF3M_HUMAN	EIF3M	physical	26186194
EIF3L_HUMAN	EIF3L	physical	26186194
EIF3D_HUMAN	EIF3D	physical	26186194
EIF3E_HUMAN	EIF3E	physical	26186194
EIF3J_HUMAN	EIF3J	physical	26186194
TRIPC_HUMAN	TRIP12	physical	26186194
DNJA4_HUMAN	DNAJA4	physical	26186194
DCA10_HUMAN	DCAF10	physical	26186194
EI2BE_HUMAN	EIF2B5	physical	26344197
NUMA1_HUMAN	NUMA1	physical	26344197
PDCD4_HUMAN	PDCD4	physical	26344197
RPAC1_HUMAN	POLR1C	physical	26344197
RAN_HUMAN	RAN	physical	26344197
RL37A_HUMAN	RPL37A	physical	26344197
4F2_HUMAN	SLC3A2	physical	26344197
SRRM1_HUMAN	SRRM1	physical	26344197
SRSF6_HUMAN	SRSF6	physical	26344197
SRSF7_HUMAN	SRSF7	physical	26344197
TCP4_HUMAN	SUB1	physical	26344197
TMED2_HUMAN	TMED2	physical	26344197
TGFR2_HUMAN	TGFBR2	physical	9813058
EIF3H_HUMAN	EIF3H	physical	28514442
EIFCL_HUMAN	EIF3CL	physical	28514442
EIF3M_HUMAN	EIF3M	physical	28514442
PRC2B_HUMAN	PRRC2B	physical	28514442
EIF3E_HUMAN	EIF3E	physical	28514442
EIF3F_HUMAN	EIF3F	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
TRIPC_HUMAN	TRIP12	physical	28514442
EIF3J_HUMAN	EIF3J	physical	28514442
E41L1_HUMAN	EPB41L1	physical	28514442
IF4G1_HUMAN	EIF4G1	physical	28514442
DNJA4_HUMAN	DNAJA4	physical	28514442
IF4A1_HUMAN	EIF4A1	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 EIF3I_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-264, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND MASSSPECTROMETRY.	18083107 [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-308, AND MASSSPECTROMETRY.	15592455 [Abstract]
Ubiquitylation
Reference	PubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-282, AND MASSSPECTROMETRY.	18781797 [Abstract]