Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Eukaryotic translation initiation factor 2 subunit 3  

UniProtKB / Swiss-Prot ID :  IF2G_HUMAN

Gene Name (Synonyms) : 
EIF2S3, EIF2G  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S preinitiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. 

Protein Sequence MAGGEAGVTLGQPHLSRQDLTTLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKAISGVHTVRFK...
Predicted Secondary Structure CCCCCCCCCCCCCCCCHHHHHCCCCCCCCCCCHHHCCCCCEEEEEEEEEEECCHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
125K -> R (in dbSNP:rs16997659). VAR_002352
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine; partial.---MAGGEA
---CCCCCC
34.40UniProtKB
Link-
21PhosphothreonineRQDLTTLDV
HHHHHCCCC
33.33HPRD
Link-
27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LDVTKLTPL
CCCCCCCCC
50.65Phosphositeplus
Link-
55PhosphoserineAHGKSTVVK
ECCHHHHHH
30.90Phosphositeplus
Link-
56PhosphothreonineHGKSTVVKA
CCHHHHHHH
32.57Phosphositeplus
Link-
66PhosphothreonineSGVHTVRFK
HHHHHHHHH
15.80Phosphositeplus
Link-
87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YANAKIYKL
CCEEHHHHH
46.50Phosphositeplus
Link-
90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AKIYKLDDP
EHHHHHCCC
49.25Phosphositeplus
Link-
109PhosphothreonineCGSSTPDEF
EEEEEEEEE
36.13Phosphositeplus
Link-
196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IDLVKESQA
CCCCCHHHH
59.97Phosphositeplus
Link-
236S-nitrosocysteineIEVVCEYIV
HHHHHHHHH
3.87dbSNO
Link-
289Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KGVLKVGQE
EEEECCCCE
41.74Phosphositeplus
Link-
303Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GIVSKDSEG
CCEEEEEEE
55.14Phosphositeplus
Link-
412PhosphoserineIGSLSTGGR
EEEECCCEE
27.06Phosphositeplus
Link-
413PhosphothreonineGSLSTGGRV
EEECCCEEE
49.28Phosphositeplus
Link-
418PhosphoserineGGRVSAVKA
CEEEEEECC
26.45Phosphositeplus
Link-
421Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VSAVKADLG
EEEECCCCE
35.58Phosphositeplus
Link-
435PhosphothreonineNPVCTEVGE
CCEEECCCC
33.66Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
IF2B_HUMANdirect interaction
direct interaction
direct interaction
direct interaction
EBI-1226316
EBI-1226135
EBI-1
intact16288713
16288713
16288713
16288713
IF2A_HUMANdirect interaction
direct interaction
direct interaction
direct interaction
EBI-1226316
EBI-1226156
EBI-1
intact16288713
16288713
16288713
16288713
NDRG1_HUMANphysical interactionEBI-1190929
intact17220478
1B42_HUMANphysical interactionEBI-1080036
intact17353931
RS20_HUMANENSP00000253039STRING
RS5_HUMANENSP00000253039STRING
RS18_HUMANENSP00000253039STRING
EIF3D_HUMANENSP00000253039STRING
IF5_HUMANENSP00000253039STRING
EIF3E_HUMANENSP00000253039STRING
RS19_HUMANENSP00000253039STRING
RS13_HUMANENSP00000253039STRING
EI2BA_HUMANENSP00000253039STRING
RS12_HUMANENSP00000253039STRING
RS15_HUMANENSP00000253039STRING
RS25_HUMANENSP00000253039STRING
EIF3K_HUMANENSP00000253039STRING
RS4Y1_HUMANENSP00000253039STRING
RS16_HUMANENSP00000253039STRING
EIF3G_HUMANENSP00000253039STRING
IF2A_HUMANENSP00000253039STRING
EIF3J_HUMANENSP00000253039STRING
IF4B_HUMANENSP00000253039STRING
IF4H_HUMANENSP00000253039STRING
EI2BB_HUMANENSP00000253039STRING
RS11_HUMANENSP00000253039STRING
RL13A_HUMANENSP00000253039STRING
RS27A_HUMANENSP00000253039STRING
UBIQ_HUMANENSP00000253039STRING
EI2BE_HUMANENSP00000253039STRING
EIF3H_HUMANENSP00000253039STRING
RS3_HUMANENSP00000253039STRING
UBIM_HUMANENSP00000253039STRING
RS30_HUMANENSP00000253039STRING
IF4E_HUMANENSP00000253039STRING
RS23_HUMANENSP00000253039STRING
RS9_HUMANENSP00000253039STRING
EIF3F_HUMANENSP00000253039STRING
EIF3F_HUMANENSP00000253039STRING
RS14_HUMANENSP00000253039STRING
PABP1_HUMANENSP00000253039STRING
RS15A_HUMANENSP00000253039STRING
IF4G1_HUMANENSP00000253039STRING
IF4A2_HUMANENSP00000253039STRING
EIF3C_HUMANENSP00000253039STRING
RS7_HUMANENSP00000253039STRING
RS2_HUMANENSP00000253039STRING
RS17_HUMANENSP00000253039STRING
RS3A_HUMANENSP00000253039STRING
RSSA_HUMANENSP00000253039STRING
RS26_HUMANENSP00000253039STRING
RS28_HUMANENSP00000253039STRING
EI2BG_HUMANENSP00000253039STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures