Eef2 (eukaryotic translation elongation factor 2) - Rat Genome Database

Send us a Message



 Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   
Search RGD Grant Resources Citing RGD About Us Contact Us
Genes QTLs Strains Markers Community Projects Genome Information Ontologies Cell Lines References Download Submit Data
OntoMate (Literature Search) JBrowse (Genome Browser) Synteny Browser (VCMap)  (beta) Variant Visualizer Multi-Ontology Enrichment (MOET) Gene-Ortholog Location Finder (GOLF) InterViewer (Protein-Protein Interactions) PhenoMiner (Quatitative Phenotypes) Gene Annotator OLGA (Gene List Generator) AllianceMine GViewer (Genome Viewer)
Aging & Age-Related Disease Cancer & Neoplastic Disease Cardiovascular Disease COVID-19 Developmental Disease Diabetes Hematologic Disease Immune & Inflammatory Disease Infectious Disease Liver Disease Neurological Disease Obesity & Metabolic Syndrome Renal Disease Respiratory Disease Sensory Organ Disease
Find Models   new Genetic Models Autism Models Rat PhenoMiner (Quantitative Phenotypes) Chinchilla PhenoMiner Expected Ranges (Quantitative Phenotype) PhenoMiner Term Comparison Hybrid Rat Diversity Panel Phenotypes GERRC (Gene Editing Rat Resource Center) Phenotypes in Other Animal Models Animal Husbandry Strain Medical Records Phylogenetics Strain Availability Calendar Rats 101 Submissions Photo Archive
Pathways
Rat Community Forum Directory of Rat Laboratories Video Tutorials News RGD Publications RGD Presentations Archive Nomenclature Guidelines Resource Links Laboratory Resources Employment Resources
Gene: Eef2 (eukaryotic translation elongation factor 2) Rattus norvegicus
Analyze
Symbol: Eef2
Name: eukaryotic translation elongation factor 2
RGD ID: 61979
Description: Enables several functions, including 5S rRNA binding activity; actin filament binding activity; and p53 binding activity. Involved in several processes, including cellular response to brain-derived neurotrophic factor stimulus; positive regulation of cytoplasmic translation; and response to ischemia. Located in cytoplasm and ribosome. Part of ribonucleoprotein complex. Is active in glutamatergic synapse. Human ortholog(s) of this gene implicated in glaucoma; spinocerebellar ataxia type 26; and stomach cancer. Orthologous to human EEF2 (eukaryotic translation elongation factor 2); PARTICIPATES IN mTOR signaling pathway; translation elongation pathway; INTERACTS WITH 1,2,4-trimethylbenzene; 17beta-estradiol; 2,3,7,8-tetrachlorodibenzodioxine.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: Ef-2; elongation factor 2; elongation factor-2
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Alliance Genes
More Info more info ...
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.278,533,248 - 8,538,518 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl78,533,116 - 8,559,183 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx711,418,330 - 11,423,600 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0713,293,816 - 13,299,086 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0711,160,262 - 11,165,532 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0711,401,501 - 11,406,771 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl711,401,501 - 11,406,771 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0711,568,907 - 11,574,177 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4710,017,061 - 10,022,331 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1710,017,060 - 10,022,331 (-)NCBI
Celera76,721,131 - 6,726,401 (-)NCBICelera
Cytogenetic Map7q11NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(1->4)-beta-D-glucan  (ISO)
(S)-amphetamine  (ISO)
(S)-nicotine  (ISO)
(Z)-3-butylidenephthalide  (ISO)
1,2,4-trimethylbenzene  (EXP)
1,2-dimethylhydrazine  (ISO)
1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine  (ISO)
17alpha-ethynylestradiol  (ISO)
17beta-estradiol  (EXP)
17beta-hydroxy-17-methylestra-4,9,11-trien-3-one  (ISO)
2,2',4,4',5,5'-hexachlorobiphenyl  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,4-dibromophenyl 2,4,5-tribromophenyl ether  (EXP,ISO)
2-nitrofluorene  (EXP)
3,4-methylenedioxymethamphetamine  (ISO)
3,5-diethoxycarbonyl-1,4-dihydrocollidine  (ISO)
3-chloropropane-1,2-diol  (EXP)
3-isobutyl-1-methyl-7H-xanthine  (ISO)
3H-1,2-dithiole-3-thione  (EXP)
4,4'-sulfonyldiphenol  (EXP,ISO)
4-(N-nitrosomethylamino)-1-(3-pyridyl)butan-1-one  (EXP)
4-hydroxynon-2-enal  (EXP)
6-propyl-2-thiouracil  (EXP)
7,12-dimethyltetraphene  (ISO)
acetaldehyde  (EXP)
acrylamide  (ISO)
aflatoxin B1  (EXP,ISO)
aldehydo-D-glucose  (ISO)
amitrole  (EXP)
ammonium chloride  (EXP)
aniline  (EXP)
aristolochic acid A  (ISO)
arsane  (ISO)
arsenic atom  (ISO)
arsenous acid  (ISO)
atropine  (ISO)
benzene  (EXP)
benzo[a]pyrene  (ISO)
bis(2-ethylhexyl) phthalate  (EXP)
bisphenol A  (EXP,ISO)
Bisphenol B  (ISO)
bisphenol F  (EXP,ISO)
Brodifacoum  (EXP)
caffeine  (ISO)
calcitriol  (EXP)
calcium atom  (EXP)
calcium(0)  (EXP)
capsaicin  (EXP)
carbachol  (ISO)
carbon nanotube  (ISO)
cefaloridine  (EXP)
CGP 52608  (ISO)
chlorohydrocarbon  (EXP)
chloropicrin  (ISO)
chlorpyrifos  (ISO)
ciguatoxin CTX1B  (ISO)
cisplatin  (ISO)
clobetasol  (ISO)
clofibrate  (ISO)
coumarin  (ISO)
cumene hydroperoxide  (EXP)
cyclophosphamide  (EXP)
cyclosporin A  (ISO)
cytarabine  (ISO)
D-glucose  (ISO)
decabromodiphenyl ether  (ISO)
dexamethasone  (ISO)
diarsenic trioxide  (ISO)
dibutyl phthalate  (EXP)
dichlorine  (EXP)
diethylstilbestrol  (EXP)
disodium selenite  (ISO)
doxorubicin  (ISO)
endosulfan  (EXP)
enzyme inhibitor  (ISO)
epoxiconazole  (ISO)
ethanol  (ISO)
fenthion  (ISO)
fluoxetine  (EXP)
fulvestrant  (ISO)
genistein  (ISO)
gentamycin  (EXP)
glucose  (ISO)
glyphosate  (ISO)
gold atom  (ISO)
gold(0)  (ISO)
hyaluronic acid  (EXP)
hydrogen peroxide  (EXP)
indometacin  (ISO)
ivermectin  (ISO)
lovastatin  (ISO)
malonaldehyde  (EXP)
methapyrilene  (EXP)
methimazole  (EXP)
methylparaben  (ISO)
N-nitrosodimethylamine  (EXP)
N-nitrosomorpholine  (EXP)
naphthalene  (ISO)
nickel dichloride  (ISO)
nickel subsulfide  (ISO)
nicotine  (ISO)
ochratoxin A  (ISO)
ozone  (EXP)
paclitaxel  (ISO)
paracetamol  (ISO)
PCB138  (EXP)
perfluorohexanesulfonic acid  (ISO)
perfluorononanoic acid  (ISO)
perfluorooctane-1-sulfonic acid  (ISO)
perfluorooctanoic acid  (ISO)
phenethyl isothiocyanate  (EXP)
phorbol 13-acetate 12-myristate  (ISO)
piperonyl butoxide  (EXP)
pirinixic acid  (EXP)
pregnenolone 16alpha-carbonitrile  (EXP)
prostaglandin A1  (ISO)
protein kinase inhibitor  (ISO)
pyrogallol  (ISO)
quinoline  (ISO)
resveratrol  (EXP,ISO)
rotenone  (EXP)
rottlerin  (EXP)
silicon dioxide  (ISO)
sirolimus  (ISO)
sodium arsenite  (ISO)
sodium fluoride  (ISO)
sulfadimethoxine  (EXP)
sunitinib  (ISO)
T-2 toxin  (EXP)
tanespimycin  (ISO)
tert-butyl hydroperoxide  (EXP)
tetrachloroethene  (ISO)
thapsigargin  (EXP)
titanium dioxide  (ISO)
torin 1  (ISO)
tremolite asbestos  (ISO)
trichloroethene  (EXP,ISO)
trimellitic anhydride  (ISO)
U0126  (ISO)
urethane  (ISO)
valproic acid  (ISO)
vinclozolin  (EXP)
vitamin E  (EXP)
warfarin  (ISO)

Gene Ontology Annotations     Click to see Annotation Detail View

Cellular Component
aggresome  (IEA,ISO)
cytoplasm  (IDA,ISO)
cytosol  (IBA,IEA,ISO)
glutamatergic synapse  (IDA,IEP)
nucleus  (ISO)
plasma membrane  (IEA,ISO)
polysome  (IEA)
postsynapse  (IEA)
ribonucleoprotein complex  (IBA,IDA,ISO)
ribosome  (IDA,ISO)
synapse  (IEA,ISO)

Molecular Function

Molecular Pathway Annotations     Click to see Annotation Detail View
References

References - curated
# Reference Title Reference Citation
1. The mechanics of ribosomal translocation. Achenbach J and Nierhaus KH, Biochimie. 2014 Dec 13. pii: S0300-9084(14)00376-9. doi: 10.1016/j.biochi.2014.12.003.
2. Localization of translational components at the ultramicroscopic level at postsynaptic sites of the rat brain. Asaki C, etal., Brain Res. 2003 May 16;972(1-2):168-76.
3. Role of calmodulin-dependent phosphorylation of elongation factor 2 in the proliferation of rat glial cells. Bagaglio DM and Hait WN, Cell Growth Differ. 1994 Dec;5(12):1403-8.
4. Interactions of eukaryotic elongation factor 2 with actin: a possible link between protein synthetic machinery and cytoskeleton. Bektas M, etal., FEBS Lett. 1994 Dec 12;356(1):89-93.
5. Estrogen regulation of the rat anterior pituitary gland proteome. Blake CA, etal., Exp Biol Med (Maywood). 2005 Dec;230(11):800-7.
6. A pharmacoproteomic approach implicates eukaryotic elongation factor 2 kinase in ER stress-induced cell death. Boyce M, etal., Cell Death Differ. 2008 Mar;15(3):589-99. doi: 10.1038/sj.cdd.4402296. Epub 2008 Jan 11.
7. Functional properties of phosphorylated elongation factor 2. Carlberg U, etal., Eur J Biochem. 1990 Aug 17;191(3):639-45.
8. Sumoylation of eukaryotic elongation factor 2 is vital for protein stability and anti-apoptotic activity in lung adenocarcinoma cells. Chen CY, etal., Cancer Sci. 2011 Aug;102(8):1582-9. doi: 10.1111/j.1349-7006.2011.01975.x. Epub 2011 Jun 23.
9. Chronic fluoxetine induces region-specific changes in translation factor eIF4E and eEF2 activity in the rat brain. Dagestad G, etal., Eur J Neurosci. 2006 May;23(10):2814-8.
10. Protein macroarray profiling of serum autoantibodies in pseudoexfoliation glaucoma. Dervan EW, etal., Invest Ophthalmol Vis Sci. 2010 Jun;51(6):2968-75. doi: 10.1167/iovs.09-4898. Epub 2010 Jan 27.
11. Does phosphorylation of eukaryotic elongation factor eEF2 regulate protein synthesis in ischemic preconditioning? Garcia L, etal., J Neurosci Res. 2004 Jul 15;77(2):292-8.
12. Effect of prenatal exposure to ethanol on hepatic elongation factor-2 and proteome in 21 d old rats: protective effect of folic acid. Garcia-Rodriguez S, etal., Free Radic Biol Med. 2003 Aug 15;35(4):428-37.
13. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, etal., Brief Bioinform. 2011 Sep;12(5):449-62. doi: 10.1093/bib/bbr042. Epub 2011 Aug 27.
14. Post-transcriptional effects and interactions between chronic mild stress and acute sleep deprivation: regulation of translation factor and cytoplasmic polyadenylation element-binding protein phosphorylation. Gronli J, etal., Behav Brain Res. 2012 Dec 1;235(2):251-62. doi: 10.1016/j.bbr.2012.08.008. Epub 2012 Aug 16.
15. Gastric Adenocarcinoma Predictive Long Intergenic Non-Coding RNA Promotes Tumor Occurrence and Progression in Non-Small Cell Lung Cancer via Regulation of the miR-661/eEF2K Signaling Pathway. Gu H, etal., Cell Physiol Biochem. 2018;51(5):2136-2147. doi: 10.1159/000495831. Epub 2018 Dec 6.
16. In vitro interaction of eukaryotic elongation factor 2 with synthetic oligoribonucleotide that mimics GTPase domain of rat 28S ribosomal RNA. He WJ, etal., Int J Biochem Cell Biol 2002 Mar;34(3):263-8.
17. Heterogeneity of cardiac rat and human elongation factor 2. Jager D, etal., Electrophoresis. 2000 Jul;21(13):2729-36.
18. Increased phosphorylation of elongation factor 2 in Alzheimer's disease. Johnson G, etal., Brain Res Mol Brain Res. 1992 Oct;15(3-4):319-26.
19. Levels of mTOR and its downstream targets 4E-BP1, eEF2, and eEF2 kinase in relationships with tau in Alzheimer's disease brain. Li X, etal., FEBS J. 2005 Aug;272(16):4211-20.
20. ATP depletion increases phosphorylation of elongation factor eEF2 in adult cardiomyocytes independently of inhibition of mTOR signalling. McLeod LE and Proud CG, FEBS Lett 2002 Nov 20;531(3):448-52.
21. Overexpression of eukaryotic elongation factor eEF2 in gastrointestinal cancers and its involvement in G2/M progression in the cell cycle. Nakamura J, etal., Int J Oncol. 2009 May;34(5):1181-9.
22. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
23. The ribosomal binding site for eukaryotic elongation factor EF-2 contains 5 S ribosomal RNA. Nygard O and Nilsson L, Biochim Biophys Acta. 1987 Jan 28;908(1):46-53.
24. The translation elongation factor eEF2 is a novel tumor‑associated antigen overexpressed in various types of cancers. Oji Y, etal., Int J Oncol. 2014 May;44(5):1461-9. doi: 10.3892/ijo.2014.2318. Epub 2014 Mar 4.
25. Primary structure of rat liver elongation factor 2 deduced from the cDNA sequence. Oleinikov AV, etal., FEBS Lett 1989 May 8;248(1-2):131-6.
26. OMIM Disease Annotation Pipeline OMIM Disease Annotation Pipeline
27. PID Annotation Import Pipeline Pipeline to import Pathway Interaction Database annotations from NCI into RGD
28. GOA pipeline RGD automated data pipeline
29. ClinVar Automated Import and Annotation Pipeline RGD automated import pipeline for ClinVar variants, variant-to-disease annotations and gene-to-disease annotations
30. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
31. A Ca(2+)-calmodulin-eEF2K-eEF2 signalling cascade, but not AMPK, contributes to the suppression of skeletal muscle protein synthesis during contractions. Rose AJ, etal., J Physiol. 2009 Apr 1;587(Pt 7):1547-63. doi: 10.1113/jphysiol.2008.167528. Epub 2009 Feb 2.
32. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Strausberg RL, etal., Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.
33. Clinical value of eukaryotic elongation factor 2 (eEF2) in non-small cell lung cancer patients. Sun HG, etal., Asian Pac J Cancer Prev. 2014 Jan;14(11):6533-5. doi: 10.7314/apjcp.2013.14.11.6533.
34. Brain-derived neurotrophic factor enhances the basal rate of protein synthesis by increasing active eukaryotic elongation factor 2 levels and promoting translation elongation in cortical neurons. Takei N, etal., J Biol Chem. 2009 Sep 25;284(39):26340-8. doi: 10.1074/jbc.M109.023010. Epub 2009 Jul 22.
35. Eukaryotic elongation factor 2 can bind to the synthetic oligoribonucleotide that mimics sarcin/ricin domain of rat 28S ribosomal RNA. Tang S, etal., Mol Cell Biochem. 2001 Jul;223(1-2):117-21.
36. Impaired overload-induced muscle growth is associated with diminished translational signalling in aged rat fast-twitch skeletal muscle. Thomson DM and Gordon SE, J Physiol. 2006 Jul 1;574(Pt 1):291-305. Epub 2006 Apr 20.
37. Differential expression of elongation factor-2, alpha4 phosphoprotein and Cdc5-like protein in prolactin-dependent/independent rat lymphoid cells. Too CK Mol Cell Endocrinol 1997 Aug 8;131(2):221-32.
38. Role of elongation factor 2 in regulating peptide-chain elongation in the heart. Vary TC, etal., Am J Physiol. 1994 Apr;266(4 Pt 1):E628-34.
39. Muscarinic acetylcholine receptors regulate the dephosphorylation of eukaryotic translation elongation factor 2 in SNU-407 colon cancer cells. Vasamsetti BMK, etal., Biochem Biophys Res Commun. 2019 Aug 20;516(2):424-429. doi: 10.1016/j.bbrc.2019.06.059. Epub 2019 Jun 19.
40. Synaptic activity controls dendritic spine morphology by modulating eEF2-dependent BDNF synthesis. Verpelli C, etal., J Neurosci. 2010 Apr 28;30(17):5830-42. doi: 10.1523/JNEUROSCI.0119-10.2010.
41. Structural basis of the translational elongation cycle. Voorhees RM and Ramakrishnan V, Annu Rev Biochem. 2013;82:203-36. doi: 10.1146/annurev-biochem-113009-092313.
42. Phosphorylation of eukaryotic elongation factor 2 can be regulated by phosphoinositide 3-kinase in the early stages of myoblast differentiation. Woo JH and Kim HS, Mol Cells. 2006 Apr 30;21(2):294-301.
43. Cytoplasmic complex of p53 and eEF2. Yin X, etal., J Cell Physiol. 2003 Sep;196(3):474-82.
Additional References at PubMed
PMID:3014523   PMID:3693353   PMID:4368673   PMID:10559001   PMID:12426392   PMID:12644453   PMID:12920134   PMID:15158453   PMID:15489334   PMID:16025302   PMID:16396499   PMID:16452087  
PMID:16854843   PMID:17522089   PMID:17665640   PMID:18187610   PMID:18809582   PMID:19056867   PMID:19182904   PMID:19199708   PMID:19946888   PMID:20458337   PMID:21088871   PMID:21172375  
PMID:21630459   PMID:22082260   PMID:22157746   PMID:22462727   PMID:22658674   PMID:22681889   PMID:22871113   PMID:23041477   PMID:23106098   PMID:23184662   PMID:23376485   PMID:23533145  
PMID:23823123   PMID:23979707   PMID:24029230   PMID:24625528   PMID:25064856   PMID:25468996   PMID:26316108   PMID:27292877   PMID:28726101   PMID:29476059   PMID:30826070   PMID:30987676  
PMID:31904090   PMID:32357304  


Genomics

Comparative Map Data
Eef2
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.278,533,248 - 8,538,518 (-)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl78,533,116 - 8,559,183 (-)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx711,418,330 - 11,423,600 (-)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0713,293,816 - 13,299,086 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0711,160,262 - 11,165,532 (-)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0711,401,501 - 11,406,771 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl711,401,501 - 11,406,771 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0711,568,907 - 11,574,177 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.4710,017,061 - 10,022,331 (-)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.1710,017,060 - 10,022,331 (-)NCBI
Celera76,721,131 - 6,726,401 (-)NCBICelera
Cytogenetic Map7q11NCBI
EEF2
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh38193,976,056 - 3,985,463 (-)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl193,976,056 - 3,985,463 (-)EnsemblGRCh38hg38GRCh38
GRCh37193,976,054 - 3,985,461 (-)NCBIGRCh37GRCh37hg19GRCh37
Build 36193,927,054 - 3,936,461 (-)NCBINCBI36Build 36hg18NCBI36
Build 34193,927,054 - 3,936,446NCBI
Celera193,912,125 - 3,921,537 (-)NCBICelera
Cytogenetic Map19p13.3NCBI
HuRef193,738,145 - 3,747,558 (-)NCBIHuRef
CHM1_1193,974,658 - 3,985,048 (-)NCBICHM1_1
T2T-CHM13v2.0193,954,240 - 3,963,657 (-)NCBIT2T-CHM13v2.0
Eef2
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm391081,012,465 - 81,018,343 (+)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl1081,012,465 - 81,018,332 (+)EnsemblGRCm39 Ensembl
GRCm381081,176,631 - 81,182,509 (+)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl1081,176,631 - 81,182,498 (+)EnsemblGRCm38mm10GRCm38
MGSCv371080,639,376 - 80,645,254 (+)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv361080,579,789 - 80,585,625 (+)NCBIMGSCv36mm8
Celera1082,196,988 - 82,202,866 (+)NCBICelera
Cytogenetic Map10C1NCBI
cM Map1039.72NCBI
Eef2
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_0049554954,799,922 - 4,807,252 (+)EnsemblChiLan1.0
ChiLan1.0NW_0049554954,800,103 - 4,807,714 (+)NCBIChiLan1.0ChiLan1.0
EEF2
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1197,604,824 - 7,614,023 (-)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v0193,000,608 - 3,009,918 (-)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.1193,950,772 - 3,960,200 (-)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl193,950,772 - 3,960,172 (-)Ensemblpanpan1.1panPan2
EEF2
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.12055,577,413 - 55,586,422 (+)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl2055,522,213 - 55,586,126 (+)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha2055,303,183 - 55,312,190 (+)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.02056,237,756 - 56,246,765 (+)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl2056,237,827 - 56,246,765 (+)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.12055,293,742 - 55,302,746 (+)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.02055,775,305 - 55,784,515 (+)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.02055,973,982 - 55,983,220 (+)NCBIUU_Cfam_GSD_1.0
Eef2
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_024405118215,567,040 - 215,575,661 (+)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_0049365882,258,309 - 2,266,609 (-)EnsemblSpeTri2.0
SpeTri2.0NW_0049365882,259,236 - 2,267,692 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
EEF2
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl274,747,080 - 74,756,680 (+)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.1274,746,541 - 74,756,687 (+)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.2275,290,872 - 75,300,980 (+)NCBISscrofa10.2Sscrofa10.2susScr3
EEF2
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.163,733,056 - 3,742,526 (-)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl63,732,425 - 3,742,826 (-)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_0236660814,504,441 - 4,513,956 (+)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Eef2
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_0046248285,601,444 - 5,611,405 (+)EnsemblHetGla_female_1.0HetGla_female_1.0 EnsemblhetGla2
HetGla 1.0NW_0046248285,601,906 - 5,609,978 (+)NCBIHetGla_female_1.0HetGla 1.0hetGla2

Variants

.
Variants in Eef2
17 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:57
Count of miRNA genes:47
Interacting mature miRNAs:54
Transcripts:ENSRNOT00000047450
Prediction methods:Miranda, Rnahybrid, Targetscan
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (http://mirgate.bioinfo.cnio.es/).
For more information about miRGate, see PMID:25858286 or access the full paper here.


QTLs in Region (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
2298550Neuinf6Neuroinflammation QTL 63.3nervous system integrity trait (VT:0010566)spinal cord RT1-B protein level (CMO:0002132)7127829089Rat
7411566Bw136Body weight QTL 13610.40.001body mass (VT:0001259)body weight gain (CMO:0000420)7131962314Rat
9590142Scort5Serum corticosterone level QTL 524.40.001blood corticosterone amount (VT:0005345)plasma corticosterone level (CMO:0001173)7131962314Rat
724560Plsm3Polydactyly-luxate syndrome (PLS) morphotypes QTL 30.0003tibia length (VT:0004357)tibia length (CMO:0000450)7134000259Rat
2317047Wbc4White blood cell count QTL 40.01leukocyte quantity (VT:0000217)white blood cell count (CMO:0000027)7135342956Rat
61410Bw19Body weight QTL 196.20.001body mass (VT:0001259)body weight (CMO:0000012)7144782185Rat
631503Bp102Blood pressure QTL 1021.9arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)7144822433Rat
1300176Hrtrt10Heart rate QTL 103.19heart pumping trait (VT:2000009)heart rate (CMO:0000002)766427026029351Rat
634336Anxrr17Anxiety related response QTL 173.66locomotor behavior trait (VT:0001392)number of entries into a discrete space in an experimental apparatus (CMO:0000960)7924703115097879Rat
10755438Coatc9Coat color QTL 90coat/hair pigmentation trait (VT:0010463)pigmented ventral coat/hair area to total ventral coat/hair area ratio (CMO:0001812)7352928048529280Rat
9590102Sffal5Serum free fatty acids level QTL 58.620.001blood free fatty acid amount (VT:0001553)plasma free fatty acids level (CMO:0000546)7532901950329019Rat
10755440Coatc10Coat color QTL 100coat/hair pigmentation trait (VT:0010463)pigmented ventral coat/hair area to total ventral coat/hair area ratio (CMO:0001812)7749649952496499Rat
10059592Kidm45Kidney mass QTL 453.950.025kidney mass (VT:0002707)both kidneys wet weight to body weight ratio (CMO:0000340)7757398552573985Rat

Markers in Region
RH143325  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.278,535,643 - 8,535,785 (+)MAPPERmRatBN7.2
mRatBN7.23110,342,376 - 110,342,518 (+)MAPPERmRatBN7.2
Rnor_6.03115,231,382 - 115,231,523NCBIRnor6.0
Rnor_6.0711,403,897 - 11,404,038NCBIRnor6.0
Rnor_5.0711,571,303 - 11,571,444UniSTSRnor5.0
Rnor_5.03121,770,572 - 121,770,713UniSTSRnor5.0
RGSC_v3.43110,195,303 - 110,195,444UniSTSRGSC3.4
RGSC_v3.4710,019,457 - 10,019,598UniSTSRGSC3.4
Celera76,723,527 - 6,723,668UniSTS
Celera3109,226,989 - 109,227,130UniSTS
Cytogenetic Map3q35UniSTS
Cytogenetic Map7q11UniSTS
RH140185  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.278,536,045 - 8,536,437 (+)MAPPERmRatBN7.2
Rnor_6.0711,404,299 - 11,404,690NCBIRnor6.0
Rnor_5.0711,571,705 - 11,572,096UniSTSRnor5.0
RGSC_v3.4710,019,859 - 10,020,250UniSTSRGSC3.4
Celera76,723,929 - 6,724,320UniSTS
Cytogenetic Map7q11UniSTS


Expression


RNA-SEQ Expression
High: > 1000 TPM value   Medium: Between 11 and 1000 TPM
Low: Between 0.5 and 10 TPM   Below Cutoff: < 0.5 TPM

alimentary part of gastrointestinal system circulatory system endocrine system exocrine system hemolymphoid system hepatobiliary system integumental system musculoskeletal system nervous system renal system reproductive system respiratory system appendage
High 2 24 27 20 17 20 1 55 18 34 2
Medium 1 19 30 21 2 21 8 10 19 17 7 9 8
Low
Below cutoff

Sequence


Reference Sequences
RefSeq Acc Id: ENSRNOT00000047450   ⟹   ENSRNOP00000041821
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl78,533,118 - 8,559,183 (-)Ensembl
Rnor_6.0 Ensembl711,401,501 - 11,406,771 (-)Ensembl
RefSeq Acc Id: ENSRNOT00000096642   ⟹   ENSRNOP00000088535
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl78,533,116 - 8,537,680 (-)Ensembl
RefSeq Acc Id: ENSRNOT00000110754   ⟹   ENSRNOP00000092424
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl78,533,116 - 8,538,049 (-)Ensembl
RefSeq Acc Id: NM_017245   ⟹   NP_058941
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.278,533,248 - 8,538,518 (-)NCBI
Rnor_6.0711,401,501 - 11,406,771 (-)NCBI
Rnor_5.0711,568,907 - 11,574,177 (-)NCBI
RGSC_v3.4710,017,061 - 10,022,331 (-)RGD
Celera76,721,131 - 6,726,401 (-)RGD
Sequence:
Reference Protein Sequences
RefSeq Acc Id: NP_058941   ⟸   NM_017245
- UniProtKB: P97619 (UniProtKB/Swiss-Prot),   P05197 (UniProtKB/Swiss-Prot),   A6K8B6 (UniProtKB/TrEMBL),   A0A8I6A8A4 (UniProtKB/TrEMBL)
- Sequence:
RefSeq Acc Id: ENSRNOP00000041821   ⟸   ENSRNOT00000047450
RefSeq Acc Id: ENSRNOP00000088535   ⟸   ENSRNOT00000096642
RefSeq Acc Id: ENSRNOP00000092424   ⟸   ENSRNOT00000110754
Protein Domains
tr-type G

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-P05197-F1-model_v2 AlphaFold P05197 1-858 view protein structure

Transcriptome

eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen

Promoters
RGD ID:13694986
Promoter ID:EPDNEW_R5510
Type:multiple initiation site
Name:Eef2_1
Description:eukaryotic translation elongation factor 2
SO ACC ID:SO:0000170
Source:EPDNEW (Eukaryotic Promoter Database, http://epd.vital-it.ch/)
Experiment Methods:Single-end sequencing.
Position:
Rat AssemblyChrPosition (strand)Source
Rnor_6.0711,406,789 - 11,406,849EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:61979 AgrOrtholog
BioCyc Gene G2FUF-35004 BioCyc
Ensembl Genes ENSRNOG00000020266 Ensembl, ENTREZGENE, UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000047450 ENTREZGENE, UniProtKB/Swiss-Prot
  ENSRNOT00000096642.1 UniProtKB/TrEMBL
  ENSRNOT00000110754.1 UniProtKB/TrEMBL
Gene3D-CATH 3.30.230.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.30.70.240 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.40.50.300 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Elongation Factor G (Translational Gtpase), domain 3 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Translation factors UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Yeast translation eEF2 (G' domain) UniProtKB/TrEMBL
IMAGE_CLONE IMAGE:5623322 IMAGE-MGC_LOAD
InterPro EFG_II UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EFG_III/V UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EFG_V-like UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EFTu-like_2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  G_TR_CS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  P-loop_NTPase UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Ribosomal_S5_D2-typ_fold UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Ribosomal_S5_D2-typ_fold_subgr UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Small_GTP-bd_dom UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  T_Tr_GTP-bd_dom UniProtKB/TrEMBL, UniProtKB/Swiss-Prot
  Transl_B-barrel_sf UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Transl_elong_EFG/EF2_IV UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:29565 UniProtKB/Swiss-Prot
MGC_CLONE MGC:72505 IMAGE-MGC_LOAD
NCBI Gene 29565 ENTREZGENE
PANTHER ELONGATION FACTOR 2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  TRANSLATION ELONGATION FACTOR-RELATED UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam EFG_C UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EFG_II UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EFG_IV UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  GTP_EFTU UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  GTP_EFTU_D2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Eef2 PhenoGen
PRINTS ELONGATNFCT UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PROSITE G_TR_1 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  G_TR_2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000020266 RatGTEx
SMART EFG_C UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  EFG_IV UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Superfamily-SCOP SSF50447 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF52540 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF54211 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  SSF54980 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
UniProt A0A8I6A8A4 ENTREZGENE, UniProtKB/TrEMBL
  A0A8I6AFH4_RAT UniProtKB/TrEMBL
  A6K8B6 ENTREZGENE, UniProtKB/TrEMBL
  EF2_RAT UniProtKB/Swiss-Prot, ENTREZGENE
  P97619 ENTREZGENE
UniProt Secondary P97619 UniProtKB/Swiss-Prot


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2002-06-10 Eef2  eukaryotic translation elongation factor 2      Name updated 70584 APPROVED

RGD Curation Notes
Note Type Note Reference