Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot P13639 (EF2_HUMAN)

Last modified November 25, 2008. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Elongation factor 2
      Short name=EF-2
Gene names
Name: EEF2
Synonyms: EF2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Hide | Top

Protein attributes

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

Hide | Top

General annotation (Comments)

Function

This protein promotes the GTP-dependent translocation of the nascent protein chain from the A-site to the P-site of the ribosome.

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.

Sequence similarities

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

Hide | Top

Ontologies

Keywords

   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   PTMPhosphoprotein
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processtranslational elongation

Inferred from Experiment. Source: Reactome

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionGTP binding

Inferred from electronic annotation. Source: InterPro

GTPase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

translation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NDRG1Q925971EBI-352560,EBI-716486

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
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 By similarity
Modified residue571Phosphothreonine
Modified residue591Phosphothreonine By similarity
Modified residue2651Phosphotyrosine
Modified residue5021Phosphoserine
Modified residue7151Diphthamide

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P13639-1 [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

Hide | Top

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: 2610926] [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: 1596361] [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]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"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: 2840927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-858.
[6]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 796-801, MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[7]Bienvenut W.V.
Submitted (AUG-2001) to UniProtKB
Cited for: CLEAVAGE OF INITIATOR METHIONINE.
[8]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."
Kim J.-E., Tannenbaum S.R., White F.M.
J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, MASS SPECTROMETRY.
[10]"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.
Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-265, MASS SPECTROMETRY.
Tissue: Hepatocyte.
[11]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57, MASS SPECTROMETRY.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

X51466 mRNA. Translation: CAA35829.1.
Z11692 mRNA. Translation: CAA77750.1.
AY942181 mRNA. Translation: AAX34409.1.
BC126259 mRNA. Translation: AAI26260.1.
M19997 mRNA. Translation: AAA50388.1.
PIREFHU2. S18294.
RefSeqNP_001952.1.
UniGeneHs.515070

3D structure databases

HSSPHSSP built from PDB template 1N0U based on UniProtKB P32324.
ModBaseSearch...

Protein-protein interaction databases

IntActP13639.

PTM databases

PhosphoSiteP13639.

2-D gel databases

PMMA-2DPAGEP13639.
REPRODUCTION-2DPAGEIPI00186290.

Proteomic databases

PeptideAtlasP13639.

Genome annotation databases

EnsemblENSG00000167658. Homo sapiens. [Contig view]
GeneID1938.
KEGGhsa:1938.
NMPDRfig|9606.3.peg.15406.

Organism-specific databases

H-InvDBHIX0040078.
HGNCHGNC:3214. EEF2.
HPACAB007795.
MIM130610. gene.
PharmGKBPA27650.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMP13639.
HOVERGENP13639.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressP13639.
CleanExHS_EEF2.
GermOnlineENSG00000167658. Homo sapiens.

Family and domain databases

InterProIPR000795. ProtSyn_GTP_bd.
IPR014721. Ribosomal_S5_D2-type_fold.
IPR005225. Small_GTP_bd.
IPR000640. Transl_elong_EFG/EF2_C.
IPR005517. Transl_elong_EFG/EF2_IV.
IPR004161. Transl_elong_EFTu/EF1A_2.
[Graphical view]
Gene3DG3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 2 hits.
PfamPF00679. EFG_C. 1 hit.
PF03764. EFG_IV. 1 hit.
PF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio7853.
SOURCESearch...

Hide | Top

Entry information

Entry nameEF2_HUMAN
AccessionPrimary (citable) accession number: P13639
Secondary accession number(s): Q58J86
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 25, 2008
This is version 97 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

Human chromosome 19

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

MIM cross-references

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents