P13639 (EF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Elongation factor 2
Short name=EF-2

Gene names

Name:	EEF2
Synonyms:	EF2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	858 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.12
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. ISGylated. Ref.9
Sequence similarities	Belongs to the GTP-binding elongation factor family. EF-G/EF-2 subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Molecular function	Elongation factor
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	translational elongation Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome polysome Inferred from electronic annotation. Source: Compara ribonucleoprotein complex Inferred from direct assay PubMed 18809582. Source: MGI
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: Compara translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 858	857	Elongation factor 2		PRO_0000091000
Regions
	Nucleotide binding	26 – 33	8	GTP By similarity
	Nucleotide binding	104 – 108	5	GTP By similarity
	Nucleotide binding	158 – 161	4	GTP By similarity
Amino acid modifications
	Modified residue	54	1	Phosphothreonine Ref.16
	Modified residue	57	1	Phosphothreonine Ref.14 Ref.16
	Modified residue	59	1	Phosphothreonine Ref.14 Ref.16
	Modified residue	235	1	N6-acetyllysine Ref.13
	Modified residue	239	1	N6-acetyllysine Ref.13
	Modified residue	272	1	N6-acetyllysine Ref.13
	Modified residue	275	1	N6-acetyllysine Ref.13
	Modified residue	435	1	Phosphothreonine Ref.11 Ref.14
	Modified residue	445	1	N6-acetyllysine Ref.13
	Modified residue	502	1	Phosphoserine Ref.11
	Modified residue	715	1	Diphthamide

Sequences

	Sequence		Length	Mass (Da)
	P13639 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 78BD1710236C0D9C	FASTA	858	95,338
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"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, MASS SPECTROMETRY.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00186290.
PIR	EFHU2. S18294.
RefSeq	NP_001952.1. NM_001961.3.
UniGene	Hs.515070.
3D structure databases
ProteinModelPortal	P13639.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13639. 36 interactions.
MINT	MINT-4999025.
STRING	9606.ENSP00000307940.
PTM databases
PhosphoSite	P13639.
Polymorphism databases
DMDM	119172.
2D gel databases
REPRODUCTION-2DPAGE	IPI00186290.
Proteomic databases
PaxDb	P13639.
PeptideAtlas	P13639.
PRIDE	P13639.
Protocols and materials databases
DNASU	1938.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000309311; ENSP00000307940; ENSG00000167658.
GeneID	1938.
KEGG	hsa:1938.
UCSC	uc002lze.3. human.
Organism-specific databases
CTD	1938.
GeneCards	GC19M003976.
HGNC	HGNC:3214. EEF2.
HPA	CAB007795.
MIM	130610. gene.
neXtProt	NX_P13639.
PharmGKB	PA27650.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0480.
HOGENOM	HOG000231589.
HOVERGEN	HBG001838.
InParanoid	P13639.
KO	K03234.
OMA	NRHNRFY.
OrthoDB	EOG4GXFM2.
PhylomeDB	P13639.
Enzyme and pathway databases
Pathway_Interaction_DB	mtor_4pathway. mTOR signaling pathway.
Reactome	REACT_17015. Metabolism of proteins. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P13639.
Bgee	P13639.
CleanEx	HS_EEF2.
Genevestigator	P13639.
GermOnline	ENSG00000167658. Homo sapiens.
Family and domain databases
Gene3D	3.30.230.10. 1 hit. 3.30.70.240. 1 hit.
InterPro	IPR000795. EF_GTP-bd_dom. IPR009022. EFG_III-V. IPR000640. EFG_V. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR005225. Small_GTP-bd_dom. IPR005517. Transl_elong_EFG/EF2_IV. IPR004161. Transl_elong_EFTu/EF1A_2. IPR009000. Transl_elong_init/rib_B-barrel. [Graphical view]
Pfam	PF00679. EFG_C. 1 hit. PF03764. EFG_IV. 1 hit. PF00009. GTP_EFTU. 1 hit. PF03144. GTP_EFTU_D2. 1 hit. [Graphical view]
PRINTS	PR00315. ELONGATNFCT.
SMART	SM00838. EFG_C. 1 hit. SM00889. EFG_IV. 1 hit. [Graphical view]
SUPFAM	SSF54980. EFG_III_V. 2 hits. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. SSF50447. Translat_factor. 1 hit.
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS00301. EFACTOR_GTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL1795108.
ChiTaRS	EEF2. human.
GenomeRNAi	1938.
NextBio	7853.
SOURCE	Search...

Entry information

Entry name

EF2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 147 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.