dbPTM

EIF3G_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF3G_HUMAN
UniProt AC	O75821
Protein Name	Eukaryotic translation initiation factor 3 subunit G {ECO:0000255\|HAMAP-Rule:MF_03006}
Gene Name	EIF3G {ECO:0000255\|HAMAP-Rule:MF_03006}
Organism	Homo sapiens (Human).
Sequence Length	320
Subcellular Localization	Cytoplasm . Nucleus . Cytoplasm, perinuclear region . Colocalizes with AIFM1 in the nucleus and perinuclear region.
Protein Description	RNA-binding 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	MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLATGDTSPEPELLPGAPLPPPKEVINGNIKTVTEYKIDEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQATQNKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPTGDFDSKP -----CCCCCCCCCC	48.35	22199227
3	O-linked_Glycosylation	-----MPTGDFDSKP -----CCCCCCCCCC	48.35	23301498
8	Phosphorylation	MPTGDFDSKPSWADQ CCCCCCCCCCCHHHH	46.59	22199227
8	O-linked_Glycosylation	MPTGDFDSKPSWADQ CCCCCCCCCCCHHHH	46.59	23301498
9	Ubiquitination	PTGDFDSKPSWADQV CCCCCCCCCCHHHHH	44.94	32015554
9	Sumoylation	PTGDFDSKPSWADQV CCCCCCCCCCHHHHH	44.94	-
11	Phosphorylation	GDFDSKPSWADQVEE CCCCCCCCHHHHHHH	38.34	25849741
24	Ubiquitination	EEEGEDDKCVTSELL HHCCCCCCCCCHHHH	42.82	29967540
27	Phosphorylation	GEDDKCVTSELLKGI CCCCCCCCHHHHCCC	26.42	27050516
28	Phosphorylation	EDDKCVTSELLKGIP CCCCCCCHHHHCCCC	13.07	28555341
38	Phosphorylation	LKGIPLATGDTSPEP HCCCCCCCCCCCCCC	43.18	29255136
41	Phosphorylation	IPLATGDTSPEPELL CCCCCCCCCCCCCCC	47.75	29255136
42	Phosphorylation	PLATGDTSPEPELLP CCCCCCCCCCCCCCC	31.82	29255136
57	Ubiquitination	GAPLPPPKEVINGNI CCCCCCCHHHCCCCC	71.09	29967540
65	Ubiquitination	EVINGNIKTVTEYKI HHCCCCCCEEEEEEE	40.73	21906983
68	Phosphorylation	NGNIKTVTEYKIDED CCCCCEEEEEEECCC	38.54	24719451
70	Phosphorylation	NIKTVTEYKIDEDGK CCCEEEEEEECCCCC	12.13	28152594
71	Succinylation	IKTVTEYKIDEDGKK CCEEEEEEECCCCCE	37.13	23954790
71	Acetylation	IKTVTEYKIDEDGKK CCEEEEEEECCCCCE	37.13	19666621
71	Ubiquitination	IKTVTEYKIDEDGKK CCEEEEEEECCCCCE	37.13	32015554
77	Ubiquitination	YKIDEDGKKFKIVRT EEECCCCCEEEEEEE	68.32	33845483
77	Acetylation	YKIDEDGKKFKIVRT EEECCCCCEEEEEEE	68.32	25953088
78	Acetylation	KIDEDGKKFKIVRTF EECCCCCEEEEEEEE	58.37	132869
78	Ubiquitination	KIDEDGKKFKIVRTF EECCCCCEEEEEEEE	58.37	-
84	Phosphorylation	KKFKIVRTFRIETRK CEEEEEEEEEEEEHH	13.33	-
94	Methylation	IETRKASKAVARRKN EEEHHHHHHHHHHHC	52.30	-
108	Phosphorylation	NWKKFGNSEFDPPGP CHHHHCCCCCCCCCC	39.77	-
123	Phosphorylation	NVATTTVSDDVSMTF CCEEEEECCCEEEEE	26.46	-
127	Phosphorylation	TTVSDDVSMTFITSK EEECCCEEEEEEECH	21.06	-
129	O-linked_Glycosylation	VSDDVSMTFITSKED ECCCEEEEEEECHHH	12.36	OGP
146	Sulfoxidation	CQEEEDPMNKLKGQK CCCCCCHHHHCCCCE	12.20	21406390
148	Acetylation	EEEDPMNKLKGQKIV CCCCHHHHCCCCEEE	45.37	25953088
148	Ubiquitination	EEEDPMNKLKGQKIV CCCCHHHHCCCCEEE	45.37	27667366
150	Ubiquitination	EDPMNKLKGQKIVSC CCHHHHCCCCEEEEE	61.99	-
153	Ubiquitination	MNKLKGQKIVSCRIC HHHCCCCEEEEEEEC	54.46	27667366
161	Acetylation	IVSCRICKGDHWTTR EEEEEECCCCCCCCC	66.07	20167786
161	2-Hydroxyisobutyrylation	IVSCRICKGDHWTTR EEEEEECCCCCCCCC	66.07	-
161	Ubiquitination	IVSCRICKGDHWTTR EEEEEECCCCCCCCC	66.07	-
172	Acetylation	WTTRCPYKDTLGPMQ CCCCCCCCCCCCHHH	29.40	20167786
174	Phosphorylation	TRCPYKDTLGPMQKE CCCCCCCCCCHHHHH	29.48	28555341
178	Sulfoxidation	YKDTLGPMQKELAEQ CCCCCCHHHHHHHHH	9.37	30846556
180	Ubiquitination	DTLGPMQKELAEQLG CCCCHHHHHHHHHHC	48.74	21906983
189	Phosphorylation	LAEQLGLSTGEKEKL HHHHHCCCCCCCCCC	32.35	25159151
190	Phosphorylation	AEQLGLSTGEKEKLP HHHHCCCCCCCCCCC	55.17	21815630
193	Acetylation	LGLSTGEKEKLPGEL HCCCCCCCCCCCCCC	62.59	20167786
193	Ubiquitination	LGLSTGEKEKLPGEL HCCCCCCCCCCCCCC	62.59	32015554
193	Succinylation	LGLSTGEKEKLPGEL HCCCCCCCCCCCCCC	62.59	23954790
193	2-Hydroxyisobutyrylation	LGLSTGEKEKLPGEL HCCCCCCCCCCCCCC	62.59	-
195	Ubiquitination	LSTGEKEKLPGELEP CCCCCCCCCCCCCEE	71.67	21906983
206	Phosphorylation	ELEPVQATQNKTGKY CCEEEECCCCCCCCC	18.64	25159151
209	Malonylation	PVQATQNKTGKYVPP EEECCCCCCCCCCCC	49.16	26320211
209	Ubiquitination	PVQATQNKTGKYVPP EEECCCCCCCCCCCC	49.16	22817900
210	Phosphorylation	VQATQNKTGKYVPPS EECCCCCCCCCCCCH	46.59	26074081
212	Acetylation	ATQNKTGKYVPPSLR CCCCCCCCCCCCHHC	48.59	21339330
212	Ubiquitination	ATQNKTGKYVPPSLR CCCCCCCCCCCCHHC	48.59	22817900
213	Phosphorylation	TQNKTGKYVPPSLRD CCCCCCCCCCCHHCC	21.38	26074081
217	Phosphorylation	TGKYVPPSLRDGASR CCCCCCCHHCCCCCC	29.93	29396449
223	Phosphorylation	PSLRDGASRRGESMQ CHHCCCCCCCCCCCC	28.21	26074081
225	Methylation	LRDGASRRGESMQPN HCCCCCCCCCCCCCC	51.22	-
240	Phosphorylation	RRADDNATIRVTNLS CCCCCCCEEEEECCC	18.64	-
244	Phosphorylation	DNATIRVTNLSEDTR CCCEEEEECCCCCCC	22.16	25137130
253	Phosphorylation	LSEDTRETDLQELFR CCCCCCCCCHHHHHH	38.42	23403867
264	Phosphorylation	ELFRPFGSISRIYLA HHHHHHCCEEEEEEE	20.12	22617229
266	Phosphorylation	FRPFGSISRIYLAKD HHHHCCEEEEEEEEC	17.83	21712546
269	Phosphorylation	FGSISRIYLAKDKTT HCCEEEEEEEECCCC	10.25	29496907
272	Succinylation	ISRIYLAKDKTTGQS EEEEEEEECCCCCCC	58.10	23954790
272	2-Hydroxyisobutyrylation	ISRIYLAKDKTTGQS EEEEEEEECCCCCCC	58.10	-
274	Ubiquitination	RIYLAKDKTTGQSKG EEEEEECCCCCCCCC	47.48	33845483
280	Acetylation	DKTTGQSKGFAFISF CCCCCCCCCEEEEEE	50.59	26051181
280	Malonylation	DKTTGQSKGFAFISF CCCCCCCCCEEEEEE	50.59	32601280
280	Ubiquitination	DKTTGQSKGFAFISF CCCCCCCCCEEEEEE	50.59	33845483
286	Phosphorylation	SKGFAFISFHRREDA CCCEEEEEEECHHHH	14.46	-
318	Phosphorylation	NVEWAKPSTN----- ECEECCCCCC-----	39.62	27251275
319	Phosphorylation	VEWAKPSTN------ CEECCCCCC------	54.17	27251275

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 EIF3G_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF3G_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 EIF3G_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF5_HUMAN	EIF5	physical	9973622
41_HUMAN	EPB41	physical	10887144
EIF3G_HUMAN	EIF3G	physical	9822659
A4_HUMAN	APP	physical	21832049
EIF3H_HUMAN	EIF3H	physical	22939629
EIF3K_HUMAN	EIF3K	physical	22939629
EIF3I_HUMAN	EIF3I	physical	22939629
EIF3L_HUMAN	EIF3L	physical	22939629
EIF3M_HUMAN	EIF3M	physical	22939629
DC1I2_HUMAN	DYNC1I2	physical	22863883
EIF3B_HUMAN	EIF3B	physical	22863883
EIF3I_HUMAN	EIF3I	physical	22863883
NUCL_HUMAN	NCL	physical	22863883
FAM9B_HUMAN	FAM9B	physical	25416956
EIF3I_HUMAN	EIF3I	physical	26186194
EIF3B_HUMAN	EIF3B	physical	26186194
EIF3A_HUMAN	EIF3A	physical	26186194
EIF3H_HUMAN	EIF3H	physical	26186194
EIF3F_HUMAN	EIF3F	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
EIF3B_HUMAN	EIF3B	physical	24396066
EIF3A_HUMAN	EIF3A	physical	24396066
EIF3C_HUMAN	EIF3C	physical	24396066
EIF3B_HUMAN	EIF3B	physical	26344197
EIF3C_HUMAN	EIF3C	physical	26344197
EIF3F_HUMAN	EIF3F	physical	26344197
EIF3H_HUMAN	EIF3H	physical	26344197
EIF3I_HUMAN	EIF3I	physical	26344197
EIF3K_HUMAN	EIF3K	physical	26344197
IF5_HUMAN	EIF5	physical	26344197
MSI2H_HUMAN	MSI2	physical	26344197
C1TC_HUMAN	MTHFD1	physical	26344197
EIF3I_HUMAN	EIF3I	physical	28514442
EIF3H_HUMAN	EIF3H	physical	28514442
EIF3M_HUMAN	EIF3M	physical	28514442
EIF3E_HUMAN	EIF3E	physical	28514442
EIF3F_HUMAN	EIF3F	physical	28514442
EIF3A_HUMAN	EIF3A	physical	28514442
EIF3L_HUMAN	EIF3L	physical	28514442
EIF3B_HUMAN	EIF3B	physical	28514442
EIF3C_HUMAN	EIF3C	physical	28514442
EIF3D_HUMAN	EIF3D	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 EIF3G_HUMAN

Related Literatures of Post-Translational Modification

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 THR-38; THR-41 AND SER-42,AND MASS SPECTROMETRY.	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 THR-38; THR-41 AND SER-42,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 THR-38; THR-41 AND SER-42,AND MASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.	19367720 [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 THR-41 AND SER-42, AND MASSSPECTROMETRY.	17287340 [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, PHOSPHORYLATION AT THR-41AND SER-42, AND MASS SPECTROMETRY.	17322308 [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-42, AND MASSSPECTROMETRY.	15302935 [Abstract]