IF2G_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF2G_MOUSE
• UniProt AC: Q9Z0N1
• Protein Name: Eukaryotic translation initiation factor 2 subunit 3, X-linked
• Gene Name: Eif2s3x
• Organism: Mus musculus (Mouse).
• Sequence Length: 472
• Protein Description: As a subunit of eukaryotic initiation factor 2 (eIF2), involved in the early steps of protein synthesis. In the presence of GTP, eIF2 forms a ternary complex with initiator tRNA Met-tRNAi and then recruits the 40S ribosomal complex, a step that determines the rate of protein translation. This step is followed by mRNA binding to form the 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex. In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (By similarity). Along with its paralog on chromosome Y, may contribute to spermatogenesis up to the round spermatid stage. [PubMed: 26823431]
• Protein Sequence: MAGGEGGVTLGQPHLSRQDLATLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGGEGGVT ------CCCCCCCCC	34.40	17242355
16	Phosphorylation	TLGQPHLSRQDLATL CCCCCCCCHHHHEEC	25.51	22817900
22	Phosphorylation	LSRQDLATLDVTKLT CCHHHHEECCCCCCC	30.68	17242355
26	Phosphorylation	DLATLDVTKLTPLSH HHEECCCCCCCCCCH	21.72	23984901
27	Ubiquitination	LATLDVTKLTPLSHE HEECCCCCCCCCCHH	50.65	-
27	Acetylation	LATLDVTKLTPLSHE HEECCCCCCCCCCHH	50.65	22826441
32	Phosphorylation	VTKLTPLSHEVISRQ CCCCCCCCHHHHCCC	20.85	-
41	Phosphorylation	EVISRQATINIGTIG HHHCCCCEEEECCCH	13.25	29514104
59	Acetylation	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	22826441
62	Phosphorylation	STVVKAISGVHTVRF CHHHHHHCCCEEEEE	39.35	28059163
66	Phosphorylation	KAISGVHTVRFKNEL HHHCCCEEEEECCHH	15.80	28059163
90	Acetylation	YANAKIYKLDDPSCP CCCCEEEECCCCCCC	49.25	22826441
90	Ubiquitination	YANAKIYKLDDPSCP CCCCEEEECCCCCCC	49.25	-
96	Glutathionylation	YKLDDPSCPRPECYR EECCCCCCCCHHHHC	3.94	24333276
101	S-nitrosylation	PSCPRPECYRSCGSS CCCCCHHHHCCCCCC	3.66	20925432
101	Glutathionylation	PSCPRPECYRSCGSS CCCCCHHHHCCCCCC	3.66	24333276
101	S-nitrosocysteine	PSCPRPECYRSCGSS CCCCCHHHHCCCCCC	3.66	-
105	S-palmitoylation	RPECYRSCGSSTPDE CHHHHCCCCCCCCCC	4.54	28526873
105	S-nitrosocysteine	RPECYRSCGSSTPDE CHHHHCCCCCCCCCC	4.54	-
105	S-nitrosylation	RPECYRSCGSSTPDE CHHHHCCCCCCCCCC	4.54	21278135
105	Glutathionylation	RPECYRSCGSSTPDE CHHHHCCCCCCCCCC	4.54	24333276
121	Ubiquitination	PTDIPGTKGNFKLVR CCCCCCCCCCEEEEE	58.74	-
125	Acetylation	PGTKGNFKLVRHVSF CCCCCCEEEEEEEEE	50.50	22826441
125	Ubiquitination	PGTKGNFKLVRHVSF CCCCCCEEEEEEEEE	50.50	-
183	Acetylation	AIEIMKLKHILILQN HHHHHHHHHHHHHHC	24.07	22826441
191	Ubiquitination	HILILQNKIDLVKES HHHHHHCHHHHHHHH	25.33	-
191	Acetylation	HILILQNKIDLVKES HHHHHHCHHHHHHHH	25.33	22826441
196	Ubiquitination	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	-
196	Malonylation	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	26320211
266	Ubiquitination	IRSFDVNKPGCEVDD EEEECCCCCCCEECC	42.51	-
266	Acetylation	IRSFDVNKPGCEVDD EEEECCCCCCCEECC	42.51	22826441
269	S-nitrosocysteine	FDVNKPGCEVDDLKG ECCCCCCCEECCCCC	6.63	-
269	S-palmitoylation	FDVNKPGCEVDDLKG ECCCCCCCEECCCCC	6.63	28526873
269	S-nitrosylation	FDVNKPGCEVDDLKG ECCCCCCCEECCCCC	6.63	20925432
269	Glutathionylation	FDVNKPGCEVDDLKG ECCCCCCCEECCCCC	6.63	24333276
275	Ubiquitination	GCEVDDLKGGVAGGS CCEECCCCCCCCCHH	61.69	-
285	Ubiquitination	VAGGSILKGVLKVGQ CCCHHHHHHHHHCCC	45.35	-
285	Acetylation	VAGGSILKGVLKVGQ CCCHHHHHHHHHCCC	45.35	22826441
289	Ubiquitination	SILKGVLKVGQEIEV HHHHHHHHCCCEEEE	41.74	-
305	Phosphorylation	PGIVSKDSEGKLMCK CCCCCCCCCCCEECH	52.57	29514104
312	Acetylation	SEGKLMCKPIFSKIV CCCCEECHHHHHHHH	27.47	23806337
312	Succinylation	SEGKLMCKPIFSKIV CCCCEECHHHHHHHH	27.47	23806337
348	S-nitrosocysteine	TKIDPTLCRADRMVG CCCCHHHHHHHHHHH	3.57	-
348	S-nitrosylation	TKIDPTLCRADRMVG CCCCHHHHHHHHHHH	3.57	21278135
399	Phosphorylation	AAKVQKLSKNEVLMV HHHHHHCCCCCEEEE	40.23	28059163
413	Phosphorylation	VNIGSLSTGGRVSAV EEECCCCCCCCCEEE	49.28	28059163
418	Phosphorylation	LSTGGRVSAVKADLG CCCCCCCEEEECCCC	26.45	24759943
421	Malonylation	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	26320211
421	Ubiquitination	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	-
434	S-nitrosylation	IVLTNPVCTEVGEKI EEECCCCCCHHHHHH	2.57	21278135
434	S-palmitoylation	IVLTNPVCTEVGEKI EEECCCCCCHHHHHH	2.57	28526873
434	S-nitrosocysteine	IVLTNPVCTEVGEKI EEECCCCCCHHHHHH	2.57	-
449	Acetylation	ALSRRVEKHWRLIGW HHHHHHHHHHEECCC	45.68	23201123

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of IF2G_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IF2G_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of IF2G_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of IF2G_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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 THR-22, AND MASSSPECTROMETRY.
PubMed: 17242355