| + |
CSNK2A1 | up-regulates activity 
phosphorylation
|
EIF5 |
0.402 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250861 |
Ser174 |
DKENGSVsSSETPPP |
Homo sapiens |
|
| pmid |
sentence |
| 11861906 |
Mass spectrometric analysis of maximally in vitro phosphorylated eIF5 localized the major phosphorylation sites at Ser-387 and Ser-388 near the C-terminus of eIF5. These serine residues are embedded within a cluster of acidic amino acid residues and account for nearly 90% of the total in vitro eIF5 phosphorylation. A minor phosphorylation site at Ser-174 was also observed. | The results suggest that phosphorylation of eIF5 may have a role in stimulating the rate of eIF5-promoted GTP hydrolysis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2B | up-regulates activity
phosphorylation
|
EIF5 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251068 |
Ser174 |
DKENGSVsSSETPPP |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 11861906 |
Mass spectrometric analysis of maximally in vitro phosphorylated eIF5 localized the major phosphorylation sites at Ser-387 and Ser-388 near the C-terminus of eIF5. These serine residues are embedded within a cluster of acidic amino acid residues and account for nearly 90% of the total in vitro eIF5 phosphorylation. A minor phosphorylation site at Ser-174 was also observed. | The results suggest that phosphorylation of eIF5 may have a role in stimulating the rate of eIF5-promoted GTP hydrolysis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251069 |
Ser389 |
LKEAEEEsSGGEEED |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 11861906 |
Mass spectrometric analysis of maximally in vitro phosphorylated eIF5 localized the major phosphorylation sites at Ser-387 and Ser-388 near the C-terminus of eIF5. These serine residues are embedded within a cluster of acidic amino acid residues and account for nearly 90% of the total in vitro eIF5 phosphorylation. A minor phosphorylation site at Ser-174 was also observed. | The results suggest that phosphorylation of eIF5 may have a role in stimulating the rate of eIF5-promoted GTP hydrolysis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251070 |
Ser390 |
KEAEEESsGGEEEDE |
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 11861906 |
Mass spectrometric analysis of maximally in vitro phosphorylated eIF5 localized the major phosphorylation sites at Ser-387 and Ser-388 near the C-terminus of eIF5. These serine residues are embedded within a cluster of acidic amino acid residues and account for nearly 90% of the total in vitro eIF5 phosphorylation. A minor phosphorylation site at Ser-174 was also observed. | The results suggest that phosphorylation of eIF5 may have a role in stimulating the rate of eIF5-promoted GTP hydrolysis. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | up-regulates
phosphorylation
|
EIF5 |
0.402 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179542 |
Ser389 |
LKEAEEEsSGGEEED |
Homo sapiens |
|
| pmid |
sentence |
| 18649047 |
We find that eif5 is associated with ck2 when the kinase activity is at the highest level in vivo, and is phosphorylated at ser389 and ser390 by ck2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179546 |
Ser390 |
KEAEEESsGGEEEDE |
Homo sapiens |
|
| pmid |
sentence |
| 18649047 |
We find that eif5 is associated with ck2 when the kinase activity is at the highest level in vivo, and is phosphorylated at ser389 and ser390 by ck2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141159 |
Ser390 |
KEAEEESsGGEEEDE |
Homo sapiens |
|
| pmid |
sentence |
| 16227438 |
We find that eif5 is associated with ck2 when the kinase activity is at the highest level in vivo, and is phosphorylated at ser389 and ser390 by ck2. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
EIF5 | form complex 
binding
|
43S_pre_initiation_complex |
0.778 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269163 |
|
|
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 |
| + |
EIF3_complex | up-regulates activity
stabilization
|
EIF5 |
0.684 |
| 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 |
| + |
EIF5 | up-regulates activity
relocalization
|
EIF5B |
0.741 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269122 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30211544 |
eIF5B promotes ribosomal subunit joining, with the help of eIF1A. Upon subunit joining, eIF5B hydrolyzes GTP and is released together with eIF1A. We found that human eIF5 interacts with eIF5B and may help recruit eIF5B to the PIC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Initiation of Translation |
3.0
EIF5
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