Q95L46
Gene name |
EIF4G2 |
Protein name |
Eukaryotic translation initiation factor 4 gamma 2 |
Names |
eIF-4-gamma 2, eIF-4G 2, eIF4G 2, p97 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:286870 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q95L46
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q95L46-F1 | Predicted | AlphaFoldDB |
No variants for Q95L46
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q95L46 | |||||
No associated diseases with Q95L46
10 regional properties for Q95L46
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dbl homology (DH) domain | 538 - 729 | IPR000219 |
| domain | FERM domain | 44 - 324 | IPR000299 |
| domain | Pleckstrin homology domain | 758 - 857 | IPR001849-1 |
| domain | Pleckstrin homology domain | 930 - 1029 | IPR001849-2 |
| domain | FERM adjacent | 332 - 378 | IPR014847 |
| domain | FERM, N-terminal | 48 - 110 | IPR018979 |
| conserved_site | FERM conserved site | 98 - 127 | IPR019747 |
| domain | FERM central domain | 129 - 234 | IPR019748 |
| domain | Band 4.1 domain | 40 - 234 | IPR019749 |
| domain | FARP1/FARP2/FRMD7, FERM domain C-lobe | 221 - 341 | IPR041788 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| eukaryotic translation initiation factor 4F complex | The eukaryotic translation initiation factor 4F complex is composed of eIF4E, eIF4A and eIF4G; it is involved in the recognition of the mRNA cap, ATP-dependent unwinding of the 5'-terminal secondary structure and recruitment of the mRNA to the ribosome. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| translation factor activity, RNA binding | Functions during translation by binding to RNA during polypeptide synthesis at the ribosome. |
| translation initiation factor activity | Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| regulation of translational initiation | Any process that modulates the frequency, rate or extent of translational initiation. |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9H074 | PAIP1 | Polyadenylate-binding protein-interacting protein 1 | Homo sapiens (Human) | PR |
| O43432 | EIF4G3 | Eukaryotic translation initiation factor 4 gamma 3 | Homo sapiens (Human) | EV |
| Q04637 | EIF4G1 | Eukaryotic translation initiation factor 4 gamma 1 | Homo sapiens (Human) | EV |
| P78344 | EIF4G2 | Eukaryotic translation initiation factor 4 gamma 2 | Homo sapiens (Human) | PR |
| Q8VE62 | Paip1 | Polyadenylate-binding protein-interacting protein 1 | Mus musculus (Mouse) | PR |
| Q6NZJ6 | Eif4g1 | Eukaryotic translation initiation factor 4 gamma 1 | Mus musculus (Mouse) | SS |
| Q80XI3 | Eif4g3 | Eukaryotic translation initiation factor 4 gamma 3 | Mus musculus (Mouse) | SS |
| Q62448 | Eif4g2 | Eukaryotic translation initiation factor 4 gamma 2 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MESAIAEGGA | SRFSASSGGG | GSRGAPQHYP | KTAGNSEFLG | KTPGQNAQKW | IPARSTRRDD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NSAANNSANE | KERHDAIFRK | VRGILNKLTP | EKFDKLCLEL | LNVGVESKLI | LKGVILLIVD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KALEEPKYSS | LYAQLCLRLA | EDAPNFDGPA | AEGQPGQKQS | TTFRRLLISK | LQDEFENRTR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NVDVYDKREN | PLLPEEEEQR | AIAKIKMLGN | IKFIGELGKL | DLIHESILHK | CIKTLLEKKK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RVQLKDMGED | LECLCQIMRT | VGPRLDHERA | KSLMDQYFAR | MCSLMLSKEL | PARIRFLLQD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TVELREHHWV | PRKAFLDNGP | KTINQIRQDA | VKDLGVFIPA | PMAQGMRSDF | FLEGPFMPPR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| MKMDRDPLGG | LADMFGQMPG | SGIGTGPGVI | QDRFSPTMGR | HRSNQLFNGH | GGHIMPPTQS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QFGEMGGKFM | KSQGLSQLYH | NQSQGLLSQL | QGQSKDMPPR | FSKKGQLNAD | EISLRPAQSF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LMNKNQVPKL | QPQITMIPPS | AQPPRTQTPP | LGQTPQLGLK | TNPPLIQEKP | AKTSKKPPPS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KEELLKLTET | VVTEYLNSGN | ANEAVNGVRE | MRAPKHFLPE | MLSKVIILSL | DRSDEDKEKA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SSLISLLKQE | GIATSDNFMQ | AFLNVLDQCP | KLEVDIPLVK | SYLAQFAARA | IISELVSISE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LAQPLESGTH | FPLFLLCLQQ | LAKLQDREWL | TELFQQSKVN | MQKMLPEIDQ | NKDRMLEILE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| GKGLSFLFPL | LKLEKELLKQ | IKLDPSPQTI | YKWIKDNISP | KLHVDKGFVN | ILMTSFLQYI |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SSEVNPPSDE | TDSSSAPSKE | QLEQEKQLLL | SFKPVMQKFL | HDHVDLQVSA | LYALQVHCYN |
| 850 | 860 | 870 | 880 | 890 | 900 |
| SNFPKGMLLR | FFVHFYDMEI | IEEEAFLAWK | EDITQEFPGK | GKALFQVNQW | LTWLETAEEE |
| ESEEEAD |