Tchem EEF2 Elongation factor 2

Protein Classes

PANTHER Classes

Protein / Nucleic Acid Binding / Rna Binding Protein / Translation Factor / Translation Initiation Factor / Elongation Factor 2

Protein / Nucleic Acid Binding / Rna Binding Protein / Translation Factor / Translation Elongation Factor / Elongation Factor 2

Protein / Hydrolase / Elongation Factor 2

Protein / Enzyme Modulator / G-protein / Elongation Factor 2

DTO Classes

Protein / Enzyme / Hydrolase / Elongation Factor 2

Protein Summary

Description

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome. This protein is completely inactivated by EF-2 kinase phosporylation. [provided by RefSeq, Jul 2008]

Uniprot Accession IDs

• P13639
• B2RMP5
• D6W618
• Q58J86
• EF-2

Gene Name

• EEF2

Ensembl ID

• ENST00000309311
• ENSP00000307940
• ENSG00000167658

Symbol

• EF2
• EF2
• EF-2
• EEF-2
• SCA26

Knowledge Table

Most Knowledge About	Knowledge Value (0 to 1 scale)
disease perturbation	1
interacting protein	1
protein domain	1
kinase perturbation	0.98
molecular function	0.98

IDG Development Level Summary

Tdark

These are targets about which virtually nothing is known. They do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:

Pubmed score: 1059.35   (req: < 5)

Gene RIFs: 28   (req: <= 3)

Antibodies: 493   (req: <= 50)

Tbio

These targets do not have known drug or small molecule activities
- AND - satisfy two or more of the following criteria:

Pubmed score: 1059.35   (req: >= 5)

Gene RIFs: 28   (req: > 3)

Antibodies: 493   (req: > 50)

- OR - satisfy the following criterion:

Gene Ontology Terms: 26

Tchem

Target has at least one ChEMBL compound with an activity cutoff of < 30 nM - AND - satisfies the preceding conditions

Active Ligand: 1

Tclin

Target has at least one approved drug - AND - satisfies the preceding conditions

Active Drug: 0

Active Ligands (1)

Explore Active Ligands

1 – 1 of 1

M5717

EEF2Tchem

EC50: 9

Protein Data Bank (2)

1 – 2 of 2

PDB Structure Id	Ligand	Method	Resolution (Å)	M.W. (kDa)	Pub Year	Title

PDB Structure Id	M.W.	Resolution	Pub Year

Pathways (21)

Reactome (15)

KEGG (2)

PathwayCommons (1)

WikiPathways (3)

Disease (R-HSA-1643685)

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Items per page:

5

1 – 5 of 15

Data Source	Name	Explore in Pharos	Explore in Source
Reactome	Disease	1105 targets	R-HSA-1643685
Reactome	Eukaryotic Translation Elongation	96 targets	R-HSA-156842
Reactome	Gamma carboxylation, hypusine formation and arylsulfatase activation	39 targets	R-HSA-163841
Reactome	Immune System	2246 targets	R-HSA-168256
Reactome	Infectious disease	408 targets	R-HSA-5663205

Name	Explore in Pharos	Explore in Source
Disease	1105 targets	R-HSA-1643685
Eukaryotic Translation Elongation	96 targets	R-HSA-156842
Gamma carboxylation, hypusine formation and arylsulfatase activation	39 targets	R-HSA-163841
Immune System	2246 targets	R-HSA-168256
Infectious disease	408 targets	R-HSA-5663205

Gene Ontology Terms (40)

Functions (10)

Components (14)

Processes (16)

Items per page:

10

1 – 10 of 10

GO Term	Evidence	Assigned by
protein kinase binding	Inferred from Physical Interaction (IPI)	UniProtKB
cadherin binding	Inferred from High Throughput Direct Assay (HDA)	BHF-UCL
RNA binding	Inferred from High Throughput Direct Assay (HDA)	UniProtKB
translation elongation factor activity	Inferred from Biological aspect of Ancestor (IBA)	GO_Central
5S rRNA binding	Inferred from Electronic Annotation (IEA)	Ensembl
actin filament binding	Inferred from Electronic Annotation (IEA)	Ensembl
GTP binding	Inferred from Electronic Annotation (IEA)	UniProtKB-KW
GTPase activity	Inferred from Electronic Annotation (IEA)	Ensembl
p53 binding	Inferred from Electronic Annotation (IEA)	Ensembl
ribosome binding	Inferred from Electronic Annotation (IEA)	Ensembl

Protein-Protein Interactions (631)

Explore Interacting Targets

1 – 10 of 631

• See Interactions on String-DB

FBXO9

Tbio

Novelty: 0.45236398

p_int: 0.992246252

p_ni: 0.007753748

Score: 0.563

Data Source: BioPlex,STRINGDB

DEFA1

Tbio

Novelty: 0.01616437

p_int: 0.991584763

p_ni: 0.008415237

Data Source: BioPlex

EEF2KMT

Tdark

Family: Enzyme

Novelty: 0.39473684

p_int: 0.894189881

p_ni: 0.105810119

Score: 0.986

Data Source: BioPlex,Reactome,STRINGDB

SLC25A48

Tdark

Family: Transporter

Novelty: 2.57142857

p_int: 0.764772671

p_ni: 0.235227329

Score: 0.267

Data Source: BioPlex,STRINGDB

RPL6

Tbio

Novelty: 0.02335748

Score: 0.999

Data Source: STRINGDB

RPL26

Tbio

Novelty: 0.02081491

Score: 0.999

Data Source: STRINGDB

RPL7

Tbio

Novelty: 0.00758123

Score: 0.999

Data Source: STRINGDB

RPL18A

Tbio

Novelty: 0.05603159

Score: 0.999

Data Source: STRINGDB

RPL17

Tbio

Novelty: 0.06372809

Score: 0.999

Data Source: STRINGDB

RPL10A

Tbio

Novelty: 0.02288439

Score: 0.999

Data Source: STRINGDB

Publication Statistics

PubMed Score  1059.35

PubMed score by year

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PubTator Score  452.5

PubTator score by year

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Amino Acid Sequence

Residue Counts

Sequence

MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITI

1-70

KSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTE

70-140

TVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLG

140-210

TVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSP

210-280

EGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDAL

280-350

LQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGL

350-420

VSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEH

420-490

AHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKD

490-560

LEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQ

560-630

RARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGV

630-700

RFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHV

700-770

FEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRK

770-840

RKGLKEGIPALDNFLDKL

840-858

MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGLVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL

Find similar targets by:

Uniprot Keyword

3D-structure
Acetylation
Complete proteome
Cytoplasm
Direct protein sequencing
Disease mutation
Elongation factor
GTP-binding
Isopeptide bond
Methylation