Elongation factor 2 - Mus musculus (Mouse)

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P58252 (EF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:

Eef2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity.
Subcellular location	Cytoplasm.
Post-translational modification	Phosphorylation by EF-2 kinase completely inactivates EF-2 By similarity. 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.5
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 Inferred from direct assay PubMed 22157746. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell polysome Inferred from direct assay PubMed 22157746. Source: MGI
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from direct assay PubMed 22157746. Source: MGI 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

Removed Ref.3 Ref.4

Chain

2 – 858

857

Elongation factor 2

PRO_0000091002

Regions

Nucleotide binding

26 – 33

GTP By similarity

Nucleotide binding

104 – 108

GTP By similarity

Nucleotide binding

158 – 161

GTP By similarity

Amino acid modifications

Modified residue

Phosphothreonine Ref.6

Modified residue

Phosphothreonine Ref.6 Ref.7

Modified residue

Phosphothreonine Ref.7

Modified residue

235

N6-acetyllysine By similarity

Modified residue

239

N6-acetyllysine By similarity

Modified residue

272

N6-acetyllysine By similarity

Modified residue

275

N6-acetyllysine By similarity

Modified residue

435

Phosphothreonine By similarity

Modified residue

445

N6-acetyllysine By similarity

Modified residue

502

Phosphoserine By similarity

Modified residue

715

Diphthamide By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P58252 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0569DFFB9B1DB5F6
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FASTA

858

95,314

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

        70         80         90        100        110        120 
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI 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 
EGQLSAAERA KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV 

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

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

       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 EVSARQELKA 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' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Forelimb, Kidney, Liver, Mammary gland and Thymus.
[2]	"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].
[3]	Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10 AND 499-506, CLEAVAGE OF INITIATOR METHIONINE, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[4]	Lubec G., Klug S., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-10; 33-50; 163-180; 240-249; 288-308; 416-426; 581-594; 606-625; 668-688; 717-726; 728-739; 768-801 AND 846-858, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[5]	"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.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54 AND THR-57, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57 AND THR-59, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK040474 mRNA. Translation: BAC30601.1. AK077866 mRNA. Translation: BAC37041.1. AK087985 mRNA. Translation: BAC40076.1. AK145545 mRNA. Translation: BAE26498.1. AK146947 mRNA. Translation: BAE27556.1. AK151487 mRNA. Translation: BAE30440.1. AK151812 mRNA. Translation: BAE30710.1. AK151945 mRNA. Translation: BAE30820.1. AK152146 mRNA. Translation: BAE30983.1. AK152447 mRNA. Translation: BAE31226.1. AK152587 mRNA. Translation: BAE31336.1. AK152826 mRNA. Translation: BAE31527.1. AK153275 mRNA. Translation: BAE31861.1. AK155325 mRNA. Translation: BAE33192.1. AK159806 mRNA. Translation: BAE35386.1. AK163063 mRNA. Translation: BAE37177.1. AK166212 mRNA. Translation: BAE38631.1. AK166596 mRNA. Translation: BAE38882.1. AK166747 mRNA. Translation: BAE38989.1. AK166751 mRNA. Translation: BAE38992.1. AK166851 mRNA. Translation: BAE39070.1. AK166968 mRNA. Translation: BAE39151.1. AK167093 mRNA. Translation: BAE39249.1. AK167109 mRNA. Translation: BAE39257.1. AK167115 mRNA. Translation: BAE39263.1. AK167221 mRNA. Translation: BAE39346.1. AK168794 mRNA. Translation: BAE40627.1. AK168827 mRNA. Translation: BAE40654.1. AK168874 mRNA. Translation: BAE40692.1. AK169013 mRNA. Translation: BAE40810.1. BC007152 mRNA. Translation: AAH07152.1.
IPI	IPI00466069.
RefSeq	NP_031933.1. NM_007907.2.
UniGene	Mm.326799. Mm.482883.
3D structure databases
ProteinModelPortal	P58252.
SMR	P58252. Positions 2-858.
ModBase	Search...
Protein-protein interaction databases
IntAct	P58252. 6 interactions.
PTM databases
PhosphoSite	P58252.
2D gel databases
COMPLUYEAST-2DPAGE	P58252.
REPRODUCTION-2DPAGE	P58252.
Proteomic databases
PaxDb	P58252.
PRIDE	P58252.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000047864; ENSMUSP00000046101; ENSMUSG00000034994.
GeneID	13629.
KEGG	mmu:13629.
UCSC	uc007gge.2. mouse.
Organism-specific databases
CTD	1938.
MGI	MGI:95288. Eef2.
Phylogenomic databases
eggNOG	COG0480.
GeneTree	ENSGT00620000088029.
HOGENOM	HOG000231589.
HOVERGEN	HBG001838.
InParanoid	P58252.
KO	K03234.
OMA	NRHNRFY.
OrthoDB	EOG4GXFM2.
Gene expression databases
ArrayExpress	P58252.
Bgee	P58252.
CleanEx	MM_EEF2.
Genevestigator	P58252.
GermOnline	ENSMUSG00000034994. Mus musculus.
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
ChiTaRS	EEF2. mouse.
NextBio	284312.
SOURCE	Search...

Entry information

Entry name

EF2_MOUSE

Accession

Primary (citable) accession number: P58252
Secondary accession number(s): Q544E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents