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P58252 (EF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3 Ref.4
Chain2 – 858857Elongation factor 2
PRO_0000091002

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 By similarity
Modified residue591Phosphothreonine By similarity
Modified residue1521N6-succinyllysine Ref.6
Modified residue2351N6-acetyllysine By similarity
Modified residue2391N6-acetyllysine Ref.6
Modified residue2721N6-acetyllysine; alternate Ref.6
Modified residue2721N6-succinyllysine; alternate Ref.6
Modified residue2751N6-acetyllysine Ref.6
Modified residue4351Phosphothreonine By similarity
Modified residue4391N6-acetyllysine Ref.6
Modified residue4451N6-acetyllysine Ref.6
Modified residue5021Phosphoserine By similarity
Modified residue5721N6-succinyllysine Ref.6
Modified residue6191N6-acetyllysine Ref.6
Modified residue7151Diphthamide By similarity

Sequences

Sequence LengthMass (Da)Tools
P58252 [UniParc].

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

FASTA85895,314
        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' 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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239; LYS-272; LYS-275; LYS-439; LYS-445 AND LYS-619, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-152; LYS-272 AND LYS-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+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.
RefSeqNP_031933.1. NM_007907.2.
UniGeneMm.326799.
Mm.482883.
Mm.486637.

3D structure databases

ProteinModelPortalP58252.
SMRP58252. Positions 3-858.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199387. 7 interactions.
IntActP58252. 11 interactions.
MINTMINT-1862939.

PTM databases

PhosphoSiteP58252.

2D gel databases

COMPLUYEAST-2DPAGEP58252.
REPRODUCTION-2DPAGEP58252.

Proteomic databases

PaxDbP58252.
PRIDEP58252.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000047864; ENSMUSP00000046101; ENSMUSG00000034994.
GeneID13629.
KEGGmmu:13629.
UCSCuc007gge.2. mouse.

Organism-specific databases

CTD1938.
MGIMGI:95288. Eef2.

Phylogenomic databases

eggNOGCOG0480.
GeneTreeENSGT00750000117652.
HOGENOMHOG000231589.
HOVERGENHBG001838.
InParanoidP58252.
KOK03234.
OMAYACCLTA.
OrthoDBEOG7WDN1S.
PhylomeDBP58252.
TreeFamTF300575.

Gene expression databases

ArrayExpressP58252.
BgeeP58252.
CleanExMM_EEF2.
GenevestigatorP58252.

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. mouse.
NextBio284312.
PROP58252.
SOURCESearch...

Entry information

Entry nameEF2_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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