dbPTM

EIF3G_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF3G_MOUSE
UniProt AC	Q9Z1D1
Protein Name	Eukaryotic translation initiation factor 3 subunit G {ECO:0000255\|HAMAP-Rule:MF_03006}
Gene Name	Eif3g
Organism	Mus musculus (Mouse).
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. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. This subunit can bind 18S rRNA..
Protein Sequence	MPTGDFDSKPSWADQVEEEGEDDKCVTSELLKGIPLPTGDTSPEPELLPGDPLPPPKEVINGNIKTVTEYKIEEDGKKFKIVRTFRIETRKASKAVARRKNWKKFGNSEFDPPGPNVATTTVSDDVSMTFITSKEDLNCQEEEDPMNKLKGQKIVSCRICKGDHWTTRCPYKDTLGPMQKELAEQLGLSTGEKEKLPGELEPVQAAQSKTGKYVPPSLRDGASRRGESMQPNRRADDNATIRVTNLSEDTRETDLQELFRPFGSISRIYLAKDKTTGQSKGFAFISFHRREDAARAIAGVSGFGYDHLILNVEWAKPSTN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPTGDFDSKP -----CCCCCCCCCC	48.35	23684622
8	Phosphorylation	MPTGDFDSKPSWADQ CCCCCCCCCCCHHHH	46.59	30387612
11	Phosphorylation	GDFDSKPSWADQVEE CCCCCCCCHHHHHHH	38.34	30352176
38	Phosphorylation	LKGIPLPTGDTSPEP HCCCCCCCCCCCCCC	56.20	24925903
41	Phosphorylation	IPLPTGDTSPEPELL CCCCCCCCCCCCCCC	47.75	24925903
42	Phosphorylation	PLPTGDTSPEPELLP CCCCCCCCCCCCCCC	31.82	24925903
65	Ubiquitination	EVINGNIKTVTEYKI HHCCCCCCEEEEEEE	40.73	-
66	Phosphorylation	VINGNIKTVTEYKIE HCCCCCCEEEEEEEE	28.94	20469934
68	Phosphorylation	NGNIKTVTEYKIEED CCCCCEEEEEEEEEC	38.54	20469934
70	Phosphorylation	NIKTVTEYKIEEDGK CCCEEEEEEEEECCC	14.11	25367039
153	Malonylation	MNKLKGQKIVSCRIC HHHCCCCEEEEEEEC	54.46	26320211
169	Glutathionylation	GDHWTTRCPYKDTLG CCCCCCCCCCCCCCC	3.97	24333276
180	Ubiquitination	DTLGPMQKELAEQLG CCCCHHHHHHHHHHC	48.74	-
189	Phosphorylation	LAEQLGLSTGEKEKL HHHHHCCCCCCCCCC	32.35	25266776
195	Ubiquitination	LSTGEKEKLPGELEP CCCCCCCCCCCCCCC	71.67	-
208	Phosphorylation	EPVQAAQSKTGKYVP CCCCCCCCCCCCCCC	27.71	29514104
213	Phosphorylation	AQSKTGKYVPPSLRD CCCCCCCCCCHHHCC	21.38	29514104
217	Phosphorylation	TGKYVPPSLRDGASR CCCCCCHHHCCCCCC	29.93	24719451
223	Phosphorylation	PSLRDGASRRGESMQ HHHCCCCCCCCCCCC	28.21	29514104
228	Phosphorylation	GASRRGESMQPNRRA CCCCCCCCCCCCCCC	26.07	25266776
253	Phosphorylation	LSEDTRETDLQELFR CCCCCCCCCHHHHHH	38.42	22942356
264	Phosphorylation	ELFRPFGSISRIYLA HHHHHHCCEEEEEEE	20.12	26643407
266	Phosphorylation	FRPFGSISRIYLAKD HHHHCCEEEEEEEEC	17.83	26643407

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_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF3G_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EIF3G_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of EIF3G_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41, AND MASSSPECTROMETRY.	15345747 [Abstract]