dbPTM

IF2G_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF2G_HUMAN
UniProt AC	P41091
Protein Name	Eukaryotic translation initiation factor 2 subunit 3
Gene Name	EIF2S3
Organism	Homo sapiens (Human).
Sequence Length	472
Subcellular Localization
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 (By similarity)..
Protein Sequence	MAGGEAGVTLGQPHLSRQDLTTLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGTKGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIMKLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIVKKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGIVSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGAVGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAVKADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGGEAGVT ------CCCCCCCCC	34.40	-
9	Phosphorylation	AGGEAGVTLGQPHLS CCCCCCCCCCCCCCC	25.01	30108239
16	Phosphorylation	TLGQPHLSRQDLTTL CCCCCCCCCCCCCCC	25.51	29255136
21	Phosphorylation	HLSRQDLTTLDVTKL CCCCCCCCCCCCCCC	33.33	26657352
22	Phosphorylation	LSRQDLTTLDVTKLT CCCCCCCCCCCCCCC	28.40	30576142
26	Phosphorylation	DLTTLDVTKLTPLSH CCCCCCCCCCCCCCH	21.72	30108239
27	Ubiquitination	LTTLDVTKLTPLSHE CCCCCCCCCCCCCHH	50.65	27667366
27	2-Hydroxyisobutyrylation	LTTLDVTKLTPLSHE CCCCCCCCCCCCCHH	50.65	-
27	Ubiquitination	LTTLDVTKLTPLSHE CCCCCCCCCCCCCHH	50.65	21890473
27	Ubiquitination	LTTLDVTKLTPLSHE CCCCCCCCCCCCCHH	50.65	21890473
27	Ubiquitination	LTTLDVTKLTPLSHE CCCCCCCCCCCCCHH	50.65	21890473
27	Acetylation	LTTLDVTKLTPLSHE CCCCCCCCCCCCCHH	50.65	23236377
27	Ubiquitination	LTTLDVTKLTPLSHE CCCCCCCCCCCCCHH	50.65	21890473
29	Phosphorylation	TLDVTKLTPLSHEVI CCCCCCCCCCCHHHH	24.60	21406692
32	Phosphorylation	VTKLTPLSHEVISRQ CCCCCCCCHHHHCCC	20.85	21406692
37	Phosphorylation	PLSHEVISRQATINI CCCHHHHCCCCEEEE	24.42	21406692
41	Phosphorylation	EVISRQATINIGTIG HHHCCCCEEEECCCH	13.25	29083192
54	Ubiquitination	IGHVAHGKSTVVKAI CHHHHCCCCHHHHHH	32.84	21963094
55	Phosphorylation	GHVAHGKSTVVKAIS HHHHCCCCHHHHHHC	30.90	21854064
56	Phosphorylation	HVAHGKSTVVKAISG HHHCCCCHHHHHHCC	32.57	21854064
59	Methylation	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	-
59	Ubiquitination	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	27667366
59	Malonylation	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	26320211
59	Ubiquitination	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	21890473
59	Ubiquitination	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	21890473
59	Ubiquitination	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	21890473
59	Acetylation	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	25953088
59	Ubiquitination	HGKSTVVKAISGVHT CCCCHHHHHHCCCEE	35.35	21890473
66	Phosphorylation	KAISGVHTVRFKNEL HHHCCCEEEEECCHH	15.80	21854064
70	Ubiquitination	GVHTVRFKNELERNI CCEEEEECCHHHHCE	38.66	21906983
70	2-Hydroxyisobutyrylation	GVHTVRFKNELERNI CCEEEEECCHHHHCE	38.66	-
70	Ubiquitination	GVHTVRFKNELERNI CCEEEEECCHHHHCE	38.66	21890473
70	Ubiquitination	GVHTVRFKNELERNI CCEEEEECCHHHHCE	38.66	21890473
70	Ubiquitination	GVHTVRFKNELERNI CCEEEEECCHHHHCE	38.66	21890473
70	Acetylation	GVHTVRFKNELERNI CCEEEEECCHHHHCE	38.66	26051181
70	Ubiquitination	GVHTVRFKNELERNI CCEEEEECCHHHHCE	38.66	21890473
80	Ubiquitination	LERNITIKLGYANAK HHHCEEEEEECCCCE	27.49	21963094
80	Acetylation	LERNITIKLGYANAK HHHCEEEEEECCCCE	27.49	25953088
83	Phosphorylation	NITIKLGYANAKIYK CEEEEEECCCCEEEE	13.71	29496907
87	Ubiquitination	KLGYANAKIYKLDDP EEECCCCEEEECCCC	46.50	23000965
87	Acetylation	KLGYANAKIYKLDDP EEECCCCEEEECCCC	46.50	26051181
89	Phosphorylation	GYANAKIYKLDDPSC ECCCCEEEECCCCCC	12.56	28152594
90	Acetylation	YANAKIYKLDDPSCP CCCCEEEECCCCCCC	49.25	23749302
90	Ubiquitination	YANAKIYKLDDPSCP CCCCEEEECCCCCCC	49.25	23000965
90	Ubiquitination	YANAKIYKLDDPSCP CCCCEEEECCCCCCC	49.25	21890473
90	Ubiquitination	YANAKIYKLDDPSCP CCCCEEEECCCCCCC	49.25	21890473
90	Ubiquitination	YANAKIYKLDDPSCP CCCCEEEECCCCCCC	49.25	21890473
90	Ubiquitination	YANAKIYKLDDPSCP CCCCEEEECCCCCCC	49.25	21890473
102	Phosphorylation	SCPRPECYRSCGSST CCCCHHHHCCCCCCC	12.14	29496907
104	Phosphorylation	PRPECYRSCGSSTPD CCHHHHCCCCCCCCC	9.06	21712546
105	Glutathionylation	RPECYRSCGSSTPDE CHHHHCCCCCCCCCC	4.54	22555962
105	S-nitrosylation	RPECYRSCGSSTPDE CHHHHCCCCCCCCCC	4.54	22126794
105	S-palmitoylation	RPECYRSCGSSTPDE CHHHHCCCCCCCCCC	4.54	26865113
107	Phosphorylation	ECYRSCGSSTPDEFP HHHCCCCCCCCCCCC	35.05	23186163
108	Phosphorylation	CYRSCGSSTPDEFPT HHCCCCCCCCCCCCC	29.28	21815630
109	Phosphorylation	YRSCGSSTPDEFPTD HCCCCCCCCCCCCCC	36.13	21815630
121	Ubiquitination	PTDIPGTKGNFKLVR CCCCCCCCCCEEEEE	58.74	27667366
121	Acetylation	PTDIPGTKGNFKLVR CCCCCCCCCCEEEEE	58.74	26051181
125	Ubiquitination	PGTKGNFKLVRHVSF CCCCCCEEEEEEEEE	50.50	21963094
125	Acetylation	PGTKGNFKLVRHVSF CCCCCCEEEEEEEEE	50.50	25953088
181	Ubiquitination	LAAIEIMKLKHILIL HHHHHHHHHHHHHHH	61.11	22817900
183	Ubiquitination	AIEIMKLKHILILQN HHHHHHHHHHHHHHC	24.07	21963094
183	2-Hydroxyisobutyrylation	AIEIMKLKHILILQN HHHHHHHHHHHHHHC	24.07	-
183	Acetylation	AIEIMKLKHILILQN HHHHHHHHHHHHHHC	24.07	26051181
191	Ubiquitination	HILILQNKIDLVKES HHHHHHCHHHHHHHH	25.33	21906983
191	2-Hydroxyisobutyrylation	HILILQNKIDLVKES HHHHHHCHHHHHHHH	25.33	-
196	Ubiquitination	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	27667366
196	2-Hydroxyisobutyrylation	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	-
196	Malonylation	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	26320211
196	Ubiquitination	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	21890473
196	Ubiquitination	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	21890473
196	Ubiquitination	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	21890473
196	Acetylation	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	26051181
196	Ubiquitination	QNKIDLVKESQAKEQ HCHHHHHHHHHHHHH	59.97	21890473
201	Ubiquitination	LVKESQAKEQYEQIL HHHHHHHHHHHHHHH	37.40	22817900
236	S-nitrosocysteine	KYNIEVVCEYIVKKI CCCHHHHHHHHHHCC	3.87	-
236	S-nitrosylation	KYNIEVVCEYIVKKI CCCHHHHHHHHHHCC	3.87	22178444
238	Phosphorylation	NIEVVCEYIVKKIPV CHHHHHHHHHHCCCC	13.09	28152594
241	Ubiquitination	VVCEYIVKKIPVPPR HHHHHHHHCCCCCCC	35.11	21963094
241	Acetylation	VVCEYIVKKIPVPPR HHHHHHHHCCCCCCC	35.11	26051181
242	Ubiquitination	VCEYIVKKIPVPPRD HHHHHHHCCCCCCCC	41.15	22817900
266	Ubiquitination	IRSFDVNKPGCEVDD EEEECCCCCCCEECC	42.51	21963094
266	2-Hydroxyisobutyrylation	IRSFDVNKPGCEVDD EEEECCCCCCCEECC	42.51	-
266	Acetylation	IRSFDVNKPGCEVDD EEEECCCCCCCEECC	42.51	26822725
275	Ubiquitination	GCEVDDLKGGVAGGS CCEECCCCCCCCCHH	61.69	23000965
275	Ubiquitination	GCEVDDLKGGVAGGS CCEECCCCCCCCCHH	61.69	-
275	2-Hydroxyisobutyrylation	GCEVDDLKGGVAGGS CCEECCCCCCCCCHH	61.69	-
275	Acetylation	GCEVDDLKGGVAGGS CCEECCCCCCCCCHH	61.69	25953088
282	Phosphorylation	KGGVAGGSILKGVLK CCCCCCHHHHHHHHH	24.67	24719451
285	Ubiquitination	VAGGSILKGVLKVGQ CCCHHHHHHHHHCCC	45.35	23000965
285	Ubiquitination	VAGGSILKGVLKVGQ CCCHHHHHHHHHCCC	45.35	-
285	2-Hydroxyisobutyrylation	VAGGSILKGVLKVGQ CCCHHHHHHHHHCCC	45.35	-
285	Succinylation	VAGGSILKGVLKVGQ CCCHHHHHHHHHCCC	45.35	23954790
289	Ubiquitination	SILKGVLKVGQEIEV HHHHHHHHCCCEEEE	41.74	23000965
289	Ubiquitination	SILKGVLKVGQEIEV HHHHHHHHCCCEEEE	41.74	21890473
289	Ubiquitination	SILKGVLKVGQEIEV HHHHHHHHCCCEEEE	41.74	21890473
289	Ubiquitination	SILKGVLKVGQEIEV HHHHHHHHCCCEEEE	41.74	21890473
289	Ubiquitination	SILKGVLKVGQEIEV HHHHHHHHCCCEEEE	41.74	21890473
302	Phosphorylation	EVRPGIVSKDSEGKL EECCCCCCCCCCCCE	28.91	23911959
303	Acetylation	VRPGIVSKDSEGKLM ECCCCCCCCCCCCEE	55.14	26051181
303	Ubiquitination	VRPGIVSKDSEGKLM ECCCCCCCCCCCCEE	55.14	27667366
303	2-Hydroxyisobutyrylation	VRPGIVSKDSEGKLM ECCCCCCCCCCCCEE	55.14	-
303	Malonylation	VRPGIVSKDSEGKLM ECCCCCCCCCCCCEE	55.14	26320211
305	Phosphorylation	PGIVSKDSEGKLMCK CCCCCCCCCCCEECH	52.57	29507054
308	Ubiquitination	VSKDSEGKLMCKPIF CCCCCCCCEECHHHH	29.06	21963094
308	Acetylation	VSKDSEGKLMCKPIF CCCCCCCCEECHHHH	29.06	25953088
312	Acetylation	SEGKLMCKPIFSKIV CCCCEECHHHHHHHH	27.47	25825284
312	Ubiquitination	SEGKLMCKPIFSKIV CCCCEECHHHHHHHH	27.47	21963094
316	Phosphorylation	LMCKPIFSKIVSLFA EECHHHHHHHHHHHH	23.38	24719451
317	Ubiquitination	MCKPIFSKIVSLFAE ECHHHHHHHHHHHHH	36.06	21963094
320	O-linked_Glycosylation	PIFSKIVSLFAEHND HHHHHHHHHHHHCCC	22.65	23301498
330	Phosphorylation	AEHNDLQYAAPGGLI HHCCCCCCCCCCCEE	16.42	27642862
342	Ubiquitination	GLIGVGTKIDPTLCR CEEEECCCCCHHHHH	38.90	21963094
346	Phosphorylation	VGTKIDPTLCRADRM ECCCCCHHHHHHHHH	34.44	24043423
369	Phosphorylation	GALPEIFTELEISYF CCCHHHHHHHHHHHH	45.37	24043423
374	Phosphorylation	IFTELEISYFLLRRL HHHHHHHHHHHHHHH	10.64	24043423
375	Phosphorylation	FTELEISYFLLRRLL HHHHHHHHHHHHHHH	12.14	24043423
397	Ubiquitination	KKAAKVQKLSKNEVL HHHHHHHHCCCCCEE	58.68	22817900
399	Phosphorylation	AAKVQKLSKNEVLMV HHHHHHCCCCCEEEE	40.23	21406692
400	Ubiquitination	AKVQKLSKNEVLMVN HHHHHCCCCCEEEEE	68.51	21963094
405	Sulfoxidation	LSKNEVLMVNIGSLS CCCCCEEEEEECCCC	2.34	28183972
410	Phosphorylation	VLMVNIGSLSTGGRV EEEEEECCCCCCCCC	18.49	21406692
412	Phosphorylation	MVNIGSLSTGGRVSA EEEECCCCCCCCCEE	27.06	21406692
413	Phosphorylation	VNIGSLSTGGRVSAV EEECCCCCCCCCEEE	49.28	21406692
418	Phosphorylation	LSTGGRVSAVKADLG CCCCCCCEEEECCCC	26.45	21854064
421	Ubiquitination	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	27667366
421	Malonylation	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	26320211
421	Ubiquitination	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	21890473
421	Ubiquitination	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	21890473
421	Ubiquitination	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	21890473
421	Ubiquitination	GGRVSAVKADLGKIV CCCCEEEECCCCCEE	35.58	21890473
426	Ubiquitination	AVKADLGKIVLTNPV EEECCCCCEEECCCC	36.62	21963094
426	2-Hydroxyisobutyrylation	AVKADLGKIVLTNPV EEECCCCCEEECCCC	36.62	-
426	Malonylation	AVKADLGKIVLTNPV EEECCCCCEEECCCC	36.62	26320211
426	Acetylation	AVKADLGKIVLTNPV EEECCCCCEEECCCC	36.62	26051181
435	Phosphorylation	VLTNPVCTEVGEKIA EECCCCCCHHHHHHH	33.66	21854064
440	Ubiquitination	VCTEVGEKIALSRRV CCCHHHHHHHHHHHH	27.61	21963094
440	2-Hydroxyisobutyrylation	VCTEVGEKIALSRRV CCCHHHHHHHHHHHH	27.61	-
440	Acetylation	VCTEVGEKIALSRRV CCCHHHHHHHHHHHH	27.61	25953088
444	Phosphorylation	VGEKIALSRRVEKHW HHHHHHHHHHHHHHH	14.71	24719451
449	Ubiquitination	ALSRRVEKHWRLIGW HHHHHHHHHHEECCC	45.68	21963094
449	Acetylation	ALSRRVEKHWRLIGW HHHHHHHHHHEECCC	45.68	25953088
466	Ubiquitination	IRRGVTIKPTVDDD- CCCCEEECCCCCCC-	25.85	21906983
466	Acetylation	IRRGVTIKPTVDDD- CCCCEEECCCCCCC-	25.85	25953088

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
66	T	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF2G_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 IF2G_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AIMP1_HUMAN	AIMP1	physical	22863883
IMDH2_HUMAN	IMPDH2	physical	22863883
IQGA1_HUMAN	IQGAP1	physical	22863883
CCAR2_HUMAN	CCAR2	physical	22863883
PLD3_HUMAN	PLD3	physical	22863883
RS4X_HUMAN	RPS4X	physical	26344197
PYM1_HUMAN	WIBG	physical	26344197

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 IF2G_HUMAN

Related Literatures of Post-Translational Modification