| + |
EIF3_complex | down-regulates activity 
|
60S cytosolic large ribosomal subunit |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269149 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15703437 |
EIF3 and, to some extent, eIF1A have been implicated in preventing reassociation of free 40S and 60S subunits and in dissociation of empty 80S ribosomes |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Initiation of Translation, Translation elongation and termination |
| + |
EIF3F | form complex 
binding
|
EIF3_complex |
0.923 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266395 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3_complex | up-regulates activity 
stabilization
|
EIF4G2 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269156 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17581632 |
EIF3 plays many functions in initiation complex formation. It interacts with eIF1, eIF5, eIF4B and eIF4G, and the direct interaction between eIF3 and eIF4G may serve as a bridge between the 40S ribosomal subunit and eIF4F-bound mRNA (Hershey and Merrick, 2000). eIF3 stabilizes the binding of the eIF2-GTP-Met-tRNAiMet ternary complex to the 40S subunit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EIF3_complex | up-regulates activity
binding
|
40S cytosolic small ribosomal subunit |
0.603 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266401 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16920360 |
EIF3 binds 40S and inhibits the association of 60S. Structural analysis suggests that eIF3 performs this scaffolding function by binding to the 40S subunit on its solvent-exposed surface rather than on its interface with the 60S subunit, where the decoding sites exist. This location of eIF3 seems ideally suited for its other proposed regulatory functions, including reinitiating translation on polycistronic mRNAs and acting as a receptor for protein kinases that control protein synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Initiation of Translation, Translation elongation and termination |
| + |
EIF3_complex | up-regulates activity
stabilization
|
Ternary_GTP_eIF2_tRNA_complex |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269154 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17581632 |
EIF3 plays many functions in initiation complex formation. It interacts with eIF1, eIF5, eIF4B and eIF4G, and the direct interaction between eIF3 and eIF4G may serve as a bridge between the 40S ribosomal subunit and eIF4F-bound mRNA (Hershey and Merrick, 2000). eIF3 stabilizes the binding of the eIF2-GTP-Met-tRNAiMet ternary complex to the 40S subunit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Initiation of Translation |
| + |
EIF3J | form complex
binding
|
EIF3_complex |
0.779 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266391 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3_complex | form complex
binding
|
43S_pre_initiation_complex |
0.66 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269162 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35489072 |
In eukaryotes, mRNA is recruited to the 43S pre-initiation complex (43S PIC), which consists of the 40S ribosomal subunit, translation initiation factors eIF1, eIF1A, eIF3, eIF5, and a ternary complex (TC) composed of eIF2, GTP and Met-tRNAiMet. 43S PIC binds to the 5′ end of the mRNA and scans along the 5′ untranslated region (5′UTR) in the 3′ direction to find the start codon (AUG) within the context of an optimal Kozak sequence. Start codon recognition stabilizes the 48S initiation complex (48S IC), initiates dissociation of eIF1, eIF1A, eIF2 and eIF5, and promotes recruitment of the 60S ribosomal subunit to form 80S IC ready to enter the elongation cycle of protein synthesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Initiation of Translation |
| + |
EIF3G | form complex
binding
|
EIF3_complex |
0.935 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266394 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3H | form complex
binding
|
EIF3_complex |
0.916 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266393 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3_complex | up-regulates activity
stabilization
|
EIF5 |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269153 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17581632 |
EIF3 plays many functions in initiation complex formation. It interacts with eIF1, eIF5, eIF4B and eIF4G, and the direct interaction between eIF3 and eIF4G may serve as a bridge between the 40S ribosomal subunit and eIF4F-bound mRNA (Hershey and Merrick, 2000). eIF3 stabilizes the binding of the eIF2-GTP-Met-tRNAiMet ternary complex to the 40S subunit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Initiation of Translation |
| + |
EIF3I | form complex
binding
|
EIF3_complex |
0.933 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266392 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3_complex | up-regulates activity
stabilization
|
EIF4G1 |
0.631 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269155 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17581632 |
EIF3 plays many functions in initiation complex formation. It interacts with eIF1, eIF5, eIF4B and eIF4G, and the direct interaction between eIF3 and eIF4G may serve as a bridge between the 40S ribosomal subunit and eIF4F-bound mRNA (Hershey and Merrick, 2000). eIF3 stabilizes the binding of the eIF2-GTP-Met-tRNAiMet ternary complex to the 40S subunit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EIF3L | form complex
binding
|
EIF3_complex |
0.922 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266389 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3_complex | up-regulates activity
stabilization
|
EIF4G3 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269157 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17581632 |
EIF3 plays many functions in initiation complex formation. It interacts with eIF1, eIF5, eIF4B and eIF4G, and the direct interaction between eIF3 and eIF4G may serve as a bridge between the 40S ribosomal subunit and eIF4F-bound mRNA (Hershey and Merrick, 2000). eIF3 stabilizes the binding of the eIF2-GTP-Met-tRNAiMet ternary complex to the 40S subunit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EIF3B | form complex
binding
|
EIF3_complex |
0.95 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266399 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3C | form complex
binding
|
EIF3_complex |
0.931 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266398 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3A | form complex
binding
|
EIF3_complex |
0.919 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266400 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3K | form complex
binding
|
EIF3_complex |
0.922 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266390 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3_complex | up-regulates activity
stabilization
|
EIF1 |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269152 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17581632 |
EIF3 plays many functions in initiation complex formation. It interacts with eIF1, eIF5, eIF4B and eIF4G, and the direct interaction between eIF3 and eIF4G may serve as a bridge between the 40S ribosomal subunit and eIF4F-bound mRNA (Hershey and Merrick, 2000). eIF3 stabilizes the binding of the eIF2-GTP-Met-tRNAiMet ternary complex to the 40S subunit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Initiation of Translation |
| + |
EIF3M | form complex
binding
|
EIF3_complex |
0.935 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266388 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3E | form complex
binding
|
EIF3_complex |
0.941 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266396 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
EIF3_complex | up-regulates activity
stabilization
|
EIF4B |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269158 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17581632 |
EIF3 plays many functions in initiation complex formation. It interacts with eIF1, eIF5, eIF4B and eIF4G, and the direct interaction between eIF3 and eIF4G may serve as a bridge between the 40S ribosomal subunit and eIF4F-bound mRNA (Hershey and Merrick, 2000). eIF3 stabilizes the binding of the eIF2-GTP-Met-tRNAiMet ternary complex to the 40S subunit |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Initiation of Translation |
| + |
EIF3D | form complex
binding
|
EIF3_complex |
0.929 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266397 |
|
|
in vitro |
|
| pmid |
sentence |
| 16920360 |
Consistent with its diverse functions, eIF3 is the largest and most complex initiation factor: the mammalian version, for example, contains 13 nonidentical subunits that are designated eIF3a to eIF3m 8, 9, 10, 11, 12, 13 (Table 1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
EIF3_complex
CPX-6036