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P13639 (EF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor 2

Short name=EF-2
Gene names
Name:EEF2
Synonyms:EF2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length858 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9. Ref.13

Subcellular location

Cytoplasm.

Post-translational modification

Phosphorylation by EF-2 kinase completely inactivates EF-2.

Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis By similarity.

ISGylated. Ref.9

Involvement in disease

Spinocerebellar ataxia 26 (SCA26) [MIM:609306]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   DiseaseDisease mutation
Neurodegeneration
Spinocerebellar ataxia
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

positive regulation of gene expression

Inferred from genetic interaction PubMed 23184662. Source: UniProt

positive regulation of translation

Inferred from genetic interaction PubMed 23184662. Source: UniProt

translation

Traceable author statement. Source: Reactome

translational elongation

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

polysome

Inferred from electronic annotation. Source: Ensembl

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: Ensembl

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 23823123. Source: UniProt

translation activator activity

Inferred from genetic interaction PubMed 23184662. Source: UniProt

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 858857Elongation factor 2
PRO_0000091000

Regions

Nucleotide binding26 – 338GTP By similarity
Nucleotide binding104 – 1085GTP By similarity
Nucleotide binding158 – 1614GTP By similarity

Amino acid modifications

Modified residue541Phosphothreonine Ref.17
Modified residue571Phosphothreonine Ref.15 Ref.17
Modified residue591Phosphothreonine Ref.15 Ref.17
Modified residue1521N6-succinyllysine By similarity
Modified residue2351N6-acetyllysine Ref.14
Modified residue2391N6-acetyllysine Ref.14
Modified residue2721N6-acetyllysine; alternate Ref.14
Modified residue2721N6-succinyllysine; alternate By similarity
Modified residue2751N6-acetyllysine Ref.14
Modified residue4351Phosphothreonine Ref.11 Ref.15
Modified residue4391N6-acetyllysine By similarity
Modified residue4451N6-acetyllysine Ref.14
Modified residue5021Phosphoserine Ref.11
Modified residue5721N6-succinyllysine By similarity
Modified residue6191N6-acetyllysine By similarity
Modified residue7151Diphthamide By similarity

Natural variations

Natural variant5961P → H in SCA26; compromises the mechanics of translocation. Ref.19
VAR_070792

Sequences

Sequence LengthMass (Da)Tools
P13639 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 78BD1710236C0D9C

FASTA85895,338
        10         20         30         40         50         60 
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR 

        70         80         90        100        110        120 
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGAGFLI 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 
EGQLGPAERA KKVEDMMKKL WGDRYFDPAN GKFSKSATSP EGKKLPRTFC QLILDPIFKV 

       310        320        330        340        350        360 
FDAIMNFKKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS 

       370        380        390        400        410        420 
PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK MVPTSDKGRF YAFGRVFSGL 

       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 EVSARQELKQ 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 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells."
Rapp G., Klaudiny J., Hagendorff G., Luck M.R., Heinz K.
Biol. Chem. Hoppe-Seyler 370:1071-1075(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"Construction of a plasmid containing the complete coding region of human elongation factor 2."
Hanes J., Freudenstein J., Rapp G., Scheit K.H.
Biol. Chem. Hoppe-Seyler 373:201-204(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Ustek D., Bektas M., Cakiris A., Oku B., Bermek E.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[6]"Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2."
Rapp G., Mucha J., Einspanier R., Luck M., Scheit K.H.
Biol. Chem. Hoppe-Seyler 369:247-250(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-858.
[7]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 796-801, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[8]Bienvenut W.V.
Submitted (AUG-2001) to UniProtKB
Cited for: CLEAVAGE OF INITIATOR METHIONINE.
[9]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435 AND SER-502, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay."
Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S.
Genes Dev. 23:1091-1105(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SURF COMPLEX.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-235; LYS-239; LYS-272; LYS-275 AND LYS-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; THR-59 AND THR-435, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; THR-57 AND THR-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult."
Hekman K.E., Yu G.Y., Brown C.D., Zhu H., Du X., Gervin K., Undlien D.E., Peterson A., Stevanin G., Clark H.B., Pulst S.M., Bird T.D., White K.P., Gomez C.M.
Hum. Mol. Genet. 21:5472-5483(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCA26 HIS-596, CHARACTERIZATION OF VARIANT SCA26 HIS-596.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51466 mRNA. Translation: CAA35829.1.
Z11692 mRNA. Translation: CAA77750.1.
AY942181 mRNA. Translation: AAX34409.1.
CH471139 Genomic DNA. Translation: EAW69274.1.
CH471139 Genomic DNA. Translation: EAW69275.1.
BC126259 mRNA. Translation: AAI26260.1.
BC136313 mRNA. Translation: AAI36314.1.
M19997 mRNA. Translation: AAA50388.1.
PIREFHU2. S18294.
RefSeqNP_001952.1. NM_001961.3.
UniGeneHs.515070.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00z1-858[»]
ProteinModelPortalP13639.
SMRP13639. Positions 3-858.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108258. 123 interactions.
IntActP13639. 46 interactions.
MINTMINT-4999025.
STRING9606.ENSP00000307940.

Chemistry

ChEMBLCHEMBL1795108.

PTM databases

PhosphoSiteP13639.

Polymorphism databases

DMDM119172.

2D gel databases

REPRODUCTION-2DPAGEIPI00186290.

Proteomic databases

PaxDbP13639.
PeptideAtlasP13639.
PRIDEP13639.

Protocols and materials databases

DNASU1938.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309311; ENSP00000307940; ENSG00000167658.
GeneID1938.
KEGGhsa:1938.
UCSCuc002lze.3. human.

Organism-specific databases

CTD1938.
GeneCardsGC19M003976.
HGNCHGNC:3214. EEF2.
HPACAB007795.
MIM130610. gene.
609306. phenotype.
neXtProtNX_P13639.
Orphanet101112. Spinocerebellar ataxia type 26.
PharmGKBPA27650.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0480.
HOGENOMHOG000231589.
HOVERGENHBG001838.
InParanoidP13639.
KOK03234.
OMAYACCLTA.
OrthoDBEOG7WDN1S.
PhylomeDBP13639.
TreeFamTF300575.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP13639.
BgeeP13639.
CleanExHS_EEF2.
GenevestigatorP13639.

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProIPR000795. EF_GTP-bd_dom.
IPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
PfamPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SMARTSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEEF2. human.
GeneWikiEEF2.
GenomeRNAi1938.
NextBio7853.
PROP13639.
SOURCESearch...

Entry information

Entry nameEF2_HUMAN
AccessionPrimary (citable) accession number: P13639
Secondary accession number(s): B2RMP5, D6W618, Q58J86
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 158 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM