P58252
PR
Gene name |
Eef2 |
Protein name |
Elongation factor 2 |
Names |
EF-2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:13629 |
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
3 structures for P58252
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 7LS1 | EM | 330 A | m | 1-858 | PDB |
| 7LS2 | EM | 310 A | m | 1-858 | PDB |
| AF-P58252-F1 | Predicted | AlphaFoldDB |
54 variants for P58252
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389114878 | 25 | I>V | No | EVA | |
| rs580943629 | 36 | T>N | No | EVA | |
| rs3400215813 | 43 | A>G | No | EVA | |
| rs585502790 | 50 | R>G | No | EVA | |
| rs1132570692 | 83 | E>K | No | EVA | |
| rs1133717694 | 88 | F>C | No | EVA | |
| rs1134550530 | 88 | F>L | No | EVA | |
| rs13460391 | 105 | S>P | No | EVA | |
| rs3389127594 | 106 | P>Q | No | EVA | |
| rs3389116489 | 120 | R>G | No | EVA | |
| rs3413120388 | 122 | T>S | No | EVA | |
| rs1133922698 | 126 | L>P | No | EVA | |
| rs3389117342 | 136 | C>R | No | EVA | |
| rs1134728916 | 141 | T>I | No | EVA | |
| rs3389121689 | 156 | M>K | No | EVA | |
| rs13460378 | 179 | Q>R | No | EVA | |
| rs3389117370 | 182 | V>A | No | EVA | |
| rs244383484 | 192 | Y>D | No | EVA | |
| rs1133227589 | 211 | T>A | No | EVA | |
| rs233030361 | 245 | S>G | No | EVA | |
| rs1134394463 | 247 | A>T | No | EVA | |
| rs3389104084 | 262 | G>R | No | EVA | |
| rs3389116484 | 269 | A>T | No | EVA | |
| rs3389117334 | 303 | A>V | No | EVA | |
| rs13460390 | 322 | K>N | No | EVA | |
| rs3389116409 | 335 | L>F | No | EVA | |
| rs3389116456 | 348 | D>E | No | EVA | |
| rs3389116525 | 368 | R>L | No | EVA | |
| rs3389104078 | 373 | Y>* | No | EVA | |
| rs3389058064 | 392 | G>V | No | EVA | |
| rs239718203 | 506 | R>S | No | EVA | |
| rs3389093850 | 521 | V>M | No | EVA | |
| rs3389118717 | 535 | Q>* | No | EVA | |
| rs3389116215 | 538 | I>N | No | EVA | |
| rs3389116369 | 588 | N>D | No | EVA | |
| rs3389121742 | 598 | K>N | No | EVA | |
| rs3401362533 | 611 | D>E | No | EVA | |
| rs3389104138 | 632 | A>T | No | EVA | |
| rs3389127633 | 641 | W>C | No | EVA | |
| rs3389121752 | 674 | E>V | No | EVA | |
| rs3389104097 | 678 | S>N | No | EVA | |
| rs1133198872 | 683 | F>Y | No | EVA | |
| rs3389108220 | 691 | A>V | No | EVA | |
| rs3389113039 | 695 | E>V | No | EVA | |
| rs3389121719 | 716 | R>P | No | EVA | |
| rs3389093849 | 741 | M>K | No | EVA | |
| rs3389113004 | 766 | K>M | No | EVA | |
| rs3389127575 | 768 | G>A | No | EVA | |
| rs3389108137 | 784 | V>L | No | EVA | |
| rs3389089422 | 789 | P>H | No | EVA | |
| rs1133723986 | 805 | G>S | No | EVA | |
| rs1135312781 | 806 | G>S | No | EVA | |
| rs1135032140 | 813 | V>E | No | EVA | |
| rs1132127764 | 826 | D>V | No | EVA |
No associated diseases with P58252
7 regional properties for P58252
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Elongation factor EFG, domain V-like | 739 - 828 | IPR000640 |
| domain | Translational (tr)-type GTP-binding domain | 17 - 362 | IPR000795 |
| domain | Translation elongation factor EFTu-like, domain 2 | 411 - 485 | IPR004161 |
| domain | Small GTP-binding protein domain | 19 - 164 | IPR005225 |
| domain | Translation elongation factor EFG/EF2, domain IV | 621 - 737 | IPR005517 |
| conserved_site | Tr-type G domain, conserved site | 58 - 73 | IPR031157 |
| domain | Elongation Factor G, domain II | 503 - 564 | IPR041095 |
Functions
9 GO annotations of cellular component
| Name | Definition |
|---|---|
| aggresome | An inclusion body formed by dynein-dependent retrograde transport of an aggregated protein on microtubules. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| membrane raft | Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| polysomal ribosome | A ribosome bound to mRNA that forms part of a polysome. |
| polysome | A multiribosomal structure representing a linear array of ribosomes held together by messenger RNA. They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro. |
| ribonucleoprotein complex | A macromolecular complex that contains both RNA and protein molecules. |
| synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
9 GO annotations of molecular function
| Name | Definition |
|---|---|
| 5S rRNA binding | Binding to a 5S ribosomal RNA, the smallest RNA constituent of a ribosome. |
| actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| p53 binding | Binding to one of the p53 family of proteins. |
| protein kinase binding | Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate. |
| ribosome binding | Binding to a ribosome. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| translation elongation factor activity | Functions in chain elongation during polypeptide synthesis at the ribosome. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| hematopoietic progenitor cell differentiation | The process in which precursor cell type acquires the specialized features of a hematopoietic progenitor cell, a class of cell types including myeloid progenitor cells and lymphoid progenitor cells. |
| positive regulation of cytoplasmic translation | Any process that activates or increases the frequency, rate or extent of cytoplasmic translation. |
| positive regulation of translation | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
| translational elongation | The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVNFTVDQIR | AIMDKKANIR | NMSVIAHVDH | GKSTLTDSLV | CKAGIIASAR | AGETRFTDTR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KDEQERCITI | KSTAISLFYE | LSENDLNFIK | QSKDGSGFLI | NLIDSPGHVD | FSSEVTAALR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VTDGALVVVD | CVSGVCVQTE | TVLRQAIAER | IKPVLMMNKM | DRALLELQLE | PEELYQTFQR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IVENVNVIIS | TYGEGESGPM | GNIMIDPVLG | TVGFGSGLHG | WAFTLKQFAE | MYVAKFAAKG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EGQLSAAERA | KKVEDMMKKL | WGDRYFDPAN | GKFSKSANSP | DGKKLPRTFC | QLILDPIFKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FDAIMNFRKE | ETAKLIEKLD | IKLDSEDKDK | EGKPLLKAVM | RRWLPAGDAL | LQMITIHLPS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PVTAQKYRCE | LLYEGPPDDE | AAMGIKSCDP | KGPLMMYISK | MVPTSDKGRF | YAFGRVFSGV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VSTGLKVRIM | GPNYTPGKKE | DLYLKPIQRT | ILMMGRYVEP | IEDVPCGNIV | GLVGVDQFLV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KTGTITTFEH | AHNMRVMKFS | VSPVVRVAVE | AKNPADLPKL | VEGLKRLAKS | DPMVQCIIEE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| SGEHIIAGAG | ELHLEICLKD | LEEDHACIPI | KKSDPVVSYR | ETVSEESNVL | CLSKSPNKHN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RLYMKARPFP | DGLAEDIDKG | EVSARQELKA | RARYLAEKYE | WDVAEARKIW | CFGPDGTGPN |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ILTDITKGVQ | YLNEIKDSVV | AGFQWATKEG | ALCEENMRGV | RFDVHDVTLH | ADAIHRGGGQ |
| 730 | 740 | 750 | 760 | 770 | 780 |
| IIPTARRCLY | ASVLTAQPRL | MEPIYLVEIQ | CPEQVVGGIY | GVLNRKRGHV | FEESQVAGTP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| MFVVKAYLPV | NESFGFTADL | RSNTGGQAFP | QCVFDHWQIL | PGDPFDNSSR | PSQVVAETRK |
| 850 | |||||
| RKGLKEGIPA | LDNFLDKL |