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P58252

- EF2_MOUSE

UniProt

P58252 - EF2_MOUSE

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Protein

Elongation factor 2

Gene

Eef2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 338GTPBy similarity
Nucleotide bindingi104 – 1085GTPBy similarity
Nucleotide bindingi158 – 1614GTPBy similarity

GO - Molecular functioni

  1. GTPase activity Source: MGI
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl
  4. translation activator activity Source: Ensembl
  5. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. hematopoietic progenitor cell differentiation Source: MGI
  3. positive regulation of gene expression Source: Ensembl
  4. translational elongation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 2
Short name:
EF-2
Gene namesi
Name:Eef2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:95288. Eef2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: Ensembl
  4. polysome Source: MGI
  5. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 858857Elongation factor 2PRO_0000091002Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541PhosphothreonineBy similarity
Modified residuei57 – 571PhosphothreonineBy similarity
Modified residuei59 – 591PhosphothreonineBy similarity
Modified residuei152 – 1521N6-succinyllysine1 Publication
Modified residuei235 – 2351N6-acetyllysineBy similarity
Modified residuei239 – 2391N6-acetyllysine1 Publication
Modified residuei272 – 2721N6-acetyllysine; alternate1 Publication
Modified residuei272 – 2721N6-succinyllysine; alternate1 Publication
Modified residuei275 – 2751N6-acetyllysine1 Publication
Modified residuei435 – 4351PhosphothreonineBy similarity
Modified residuei439 – 4391N6-acetyllysine1 Publication
Modified residuei445 – 4451N6-acetyllysine1 Publication
Modified residuei502 – 5021PhosphoserineBy similarity
Modified residuei572 – 5721N6-succinyllysine1 Publication
Modified residuei619 – 6191N6-acetyllysine1 Publication
Modified residuei715 – 7151DiphthamideBy similarity

Post-translational modificationi

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).By similarity
ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP58252.
PaxDbiP58252.
PRIDEiP58252.

2D gel databases

COMPLUYEAST-2DPAGEP58252.
REPRODUCTION-2DPAGEP58252.

PTM databases

PhosphoSiteiP58252.

Expressioni

Gene expression databases

BgeeiP58252.
CleanExiMM_EEF2.
ExpressionAtlasiP58252. baseline and differential.
GenevestigatoriP58252.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi199387. 8 interactions.
IntActiP58252. 11 interactions.
MINTiMINT-1862939.

Structurei

3D structure databases

ProteinModelPortaliP58252.
SMRiP58252. Positions 3-858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 362346tr-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0480.
GeneTreeiENSGT00760000119370.
HOGENOMiHOG000231589.
HOVERGENiHBG001838.
InParanoidiP58252.
KOiK03234.
OMAiRWAPVPE.
OrthoDBiEOG7WDN1S.
PhylomeDBiP58252.
TreeFamiTF300575.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR000795. 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]
PfamiPF00679. 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]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P58252-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR
60 70 80 90 100
AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI
110 120 130 140 150
NLIDSPGHVD FSSEVTAALR VTDGALVVVD CVSGVCVQTE TVLRQAIAER
160 170 180 190 200
IKPVLMMNKM DRALLELQLE PEELYQTFQR IVENVNVIIS TYGEGESGPM
210 220 230 240 250
GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG EGQLSAAERA
260 270 280 290 300
KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV
310 320 330 340 350
FDAIMNFRKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL
360 370 380 390 400
LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK
410 420 430 440 450
MVPTSDKGRF YAFGRVFSGV VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT
460 470 480 490 500
ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV KTGTITTFEH AHNMRVMKFS
510 520 530 540 550
VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE SGEHIIAGAG
560 570 580 590 600
ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN
610 620 630 640 650
RLYMKARPFP DGLAEDIDKG EVSARQELKA RARYLAEKYE WDVAEARKIW
660 670 680 690 700
CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV
710 720 730 740 750
RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ
760 770 780 790 800
CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL
810 820 830 840 850
RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA

LDNFLDKL
Length:858
Mass (Da):95,314
Last modified:January 23, 2007 - v2
Checksum:i0569DFFB9B1DB5F6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35993.1.
RefSeqiNP_031933.1. NM_007907.2.
UniGeneiMm.326799.
Mm.482883.
Mm.486637.

Genome annotation databases

EnsembliENSMUST00000047864; ENSMUSP00000046101; ENSMUSG00000034994.
GeneIDi13629.
KEGGimmu:13629.
UCSCiuc007gge.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35993.1.
RefSeqi NP_031933.1. NM_007907.2.
UniGenei Mm.326799.
Mm.482883.
Mm.486637.

3D structure databases

ProteinModelPortali P58252.
SMRi P58252. Positions 3-858.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199387. 8 interactions.
IntActi P58252. 11 interactions.
MINTi MINT-1862939.

PTM databases

PhosphoSitei P58252.

2D gel databases

COMPLUYEAST-2DPAGE P58252.
REPRODUCTION-2DPAGE P58252.

Proteomic databases

MaxQBi P58252.
PaxDbi P58252.
PRIDEi P58252.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047864 ; ENSMUSP00000046101 ; ENSMUSG00000034994 .
GeneIDi 13629.
KEGGi mmu:13629.
UCSCi uc007gge.2. mouse.

Organism-specific databases

CTDi 1938.
MGIi MGI:95288. Eef2.

Phylogenomic databases

eggNOGi COG0480.
GeneTreei ENSGT00760000119370.
HOGENOMi HOG000231589.
HOVERGENi HBG001838.
InParanoidi P58252.
KOi K03234.
OMAi RWAPVPE.
OrthoDBi EOG7WDN1S.
PhylomeDBi P58252.
TreeFami TF300575.

Miscellaneous databases

ChiTaRSi EEF2. mouse.
NextBioi 284312.
PROi P58252.
SOURCEi Search...

Gene expression databases

Bgeei P58252.
CleanExi MM_EEF2.
ExpressionAtlasi P58252. baseline and differential.
Genevestigatori P58252.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR000795. 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 ]
Pfami PF00679. 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 ]
PRINTSi PR00315. ELONGATNFCT.
SMARTi SM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiEF2_MOUSE
AccessioniPrimary (citable) accession number: P58252
Secondary accession number(s): Q544E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3