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P32324

- EF2_YEAST

UniProt

P32324 - EF2_YEAST

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Protein

Elongation factor 2

Gene

EFT1

more
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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.1 Publication

Enzyme regulationi

Inhibited by fusidic acid and sordarin, which prevent the release of eEF2 from the ribosome after the translocation step. While fusidic acid acts on all eukaryotic eEF2, sordarin specifically binds and inhibits only selected fungal eEF2. Inhibited by diphtheria toxin and Pseudomonas aeruginosa exotoxin A (ETA), which ADP-ribosylate the diphthamide residue.

Kineticsi

  1. KM=0.010 mM for GTP

Pathwayi

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: SGD
  2. GTP binding Source: UniProtKB-KW
  3. rRNA binding Source: UniProtKB-KW
  4. translation elongation factor activity Source: SGD

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. maintenance of translational fidelity Source: SGD
  3. positive regulation of translational elongation Source: SGD
  4. translational elongation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding, RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29933-MONOMER.
YEAST:G3O-33657-MONOMER.
ReactomeiREACT_257951. Peptide chain elongation.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 2
Short name:
EF-2
Alternative name(s):
Eukaryotic elongation factor 2
Short name:
eEF2
Ribosomal translocase
Translation elongation factor 2
Gene namesi
Name:EFT1
Ordered Locus Names:YOR133W
ORF Names:O3317, YOR3317W
AND
Name:EFT2
Ordered Locus Names:YDR385W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV, UP000002311: Chromosome XV

Organism-specific databases

CYGDiYDR385w.
YOR133w.
SGDiS000005659. EFT1.
S000002793. EFT2.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi180 – 1801R → G: Causes resistance to fusidic acid and reduces sensitivity to sordarin. 1 Publication
Mutagenesisi187 – 1871V → F: Causes resistance to fusidic acid and reduces sensitivity to sordarin. 1 Publication
Mutagenesisi490 – 4901Q → E: Reduces sensitivity to sordarin. 1 Publication
Mutagenesisi521 – 5211Y → D, N or S: Reduces sensitivity to fusidic acid and sordarin. 1 Publication
Mutagenesisi523 – 5231S → F or P: Causes resistance to fusidic acid and sordarin. 1 Publication
Mutagenesisi529 – 5291I → T: Reduces sensitivity to sordarin. 1 Publication
Mutagenesisi559 – 5591P → L or R: Causes resistance to fusidic acid and sordarin. 1 Publication
Mutagenesisi562 – 5621A → P: Reduces sensitivity to fusidic acid and causes resistance to sordarin. 1 Publication
Mutagenesisi580 – 5801P → H: Causes impaired ribosomal translocation with an increased rate of -1 programmed ribosomal frameshift read-through during translation. 1 Publication
Mutagenesisi699 – 6991H → D, E, L or M: Prevents post-translational modification of this residue to diphthamide. Results in a functional protein that is resistant to diphtheria toxin. 1 Publication
Mutagenesisi701 – 7011G → R: Prevents ADP-ribosylation of the diphthamide by diphtheria toxin. 1 Publication
Mutagenesisi727 – 7271P → S: Causes resistance to sordarin. 1 Publication
Mutagenesisi774 – 7741V → F: Causes resistance to sordarin. 1 Publication
Mutagenesisi790 – 7901Missing: Causes resistance to fusidic acid and sordarin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 842842Elongation factor 2PRO_0000091024Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei509 – 5091N6,N6,N6-trimethyllysine; by EFM3; alternate2 Publications
Modified residuei509 – 5091N6,N6-dimethyllysine; by EFM3; alternate3 Publications
Modified residuei509 – 5091N6-methyllysine; by EFM3; alternate2 Publications
Modified residuei579 – 5791Phosphoserine2 Publications
Modified residuei613 – 6131N6,N6-dimethyllysine; by EFM2; alternate2 Publications
Modified residuei613 – 6131N6-methyllysine; by EFM2; alternate2 Publications
Modified residuei699 – 6991Diphthamide1 Publication
Modified residuei713 – 7131Phosphothreonine2 Publications
Modified residuei763 – 7631Phosphothreonine2 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP32324.
PaxDbiP32324.
PRIDEiP32324.

2D gel databases

SWISS-2DPAGEP32324.

Expressioni

Gene expression databases

GenevestigatoriP32324.

Interactioni

Subunit structurei

Binds to 80S ribosomes. Interacts directly with the 40S ribosomal subunit protein RPL9A, the 60S ribosomal subunit proteins RPL12A and RPS23A, as well as the 18S rRNA and the 25S rRNA. Interacts with RPL0.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RPP0P053172EBI-6333,EBI-15447
SKP1P522862EBI-6333,EBI-4090

Protein-protein interaction databases

BioGridi32446. 133 interactions.
34529. 85 interactions.
DIPiDIP-4911N.
IntActiP32324. 138 interactions.
MINTiMINT-8285544.
STRINGi4932.YDR385W.

Structurei

Secondary structure

1
842
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi6 – 149Combined sources
Helixi16 – 183Combined sources
Beta strandi19 – 257Combined sources
Helixi28 – 303Combined sources
Helixi32 – 4312Combined sources
Beta strandi44 – 485Combined sources
Beta strandi74 – 807Combined sources
Helixi83 – 886Combined sources
Beta strandi95 – 1039Combined sources
Helixi109 – 1113Combined sources
Helixi113 – 1208Combined sources
Beta strandi123 – 1308Combined sources
Turni131 – 1333Combined sources
Helixi137 – 14812Combined sources
Beta strandi152 – 1587Combined sources
Helixi160 – 1656Combined sources
Helixi171 – 19222Combined sources
Helixi195 – 1973Combined sources
Helixi204 – 2063Combined sources
Beta strandi209 – 2135Combined sources
Turni214 – 2174Combined sources
Beta strandi218 – 2214Combined sources
Helixi222 – 2309Combined sources
Turni231 – 2344Combined sources
Helixi237 – 2437Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi249 – 2513Combined sources
Turni252 – 2554Combined sources
Beta strandi256 – 2594Combined sources
Beta strandi261 – 2633Combined sources
Turni264 – 2663Combined sources
Helixi272 – 2765Combined sources
Helixi278 – 28912Combined sources
Helixi295 – 3028Combined sources
Helixi309 – 3135Combined sources
Helixi316 – 32712Combined sources
Helixi330 – 34112Combined sources
Helixi345 – 35612Combined sources
Beta strandi357 – 3593Combined sources
Helixi364 – 3707Combined sources
Beta strandi374 – 3774Combined sources
Beta strandi379 – 39012Combined sources
Beta strandi394 – 40613Combined sources
Beta strandi410 – 4145Combined sources
Beta strandi420 – 4223Combined sources
Beta strandi426 – 4305Combined sources
Beta strandi433 – 4386Combined sources
Beta strandi441 – 4499Combined sources
Beta strandi453 – 4586Combined sources
Turni460 – 4623Combined sources
Beta strandi465 – 4717Combined sources
Beta strandi489 – 4979Combined sources
Helixi498 – 5003Combined sources
Helixi501 – 51414Combined sources
Beta strandi519 – 5224Combined sources
Beta strandi528 – 5347Combined sources
Helixi535 – 54713Combined sources
Beta strandi554 – 5574Combined sources
Beta strandi564 – 5696Combined sources
Beta strandi575 – 5784Combined sources
Beta strandi580 – 5823Combined sources
Beta strandi585 – 5928Combined sources
Helixi595 – 6028Combined sources
Beta strandi604 – 6063Combined sources
Beta strandi608 – 6103Combined sources
Helixi612 – 62110Combined sources
Helixi627 – 6315Combined sources
Beta strandi633 – 6386Combined sources
Turni639 – 6413Combined sources
Beta strandi642 – 6487Combined sources
Helixi656 – 67217Combined sources
Turni675 – 6773Combined sources
Beta strandi683 – 69210Combined sources
Helixi697 – 6993Combined sources
Helixi702 – 71918Combined sources
Beta strandi722 – 73514Combined sources
Helixi737 – 7393Combined sources
Helixi740 – 7489Combined sources
Turni749 – 7513Combined sources
Beta strandi753 – 7586Combined sources
Beta strandi766 – 7738Combined sources
Helixi774 – 7763Combined sources
Helixi780 – 7878Combined sources
Turni788 – 7903Combined sources
Beta strandi793 – 80311Combined sources
Beta strandi811 – 8133Combined sources
Helixi814 – 82512Combined sources
Helixi835 – 8384Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N0UX-ray2.12A1-842[»]
1N0VX-ray2.85C/D1-842[»]
1S1Helectron microscopy11.70T1-842[»]
1U2RX-ray2.60A1-842[»]
1ZM2X-ray3.07A/C/E1-842[»]
1ZM3X-ray3.07A/C/E1-842[»]
1ZM4X-ray2.90A/C/E1-842[»]
1ZM9X-ray2.80A/C/E1-842[»]
2E1RX-ray3.15A1-842[»]
2NPFX-ray2.90A/B1-842[»]
2P8Welectron microscopy11.30T1-842[»]
2P8Xelectron microscopy9.70T1-842[»]
2P8Yelectron microscopy11.70T1-842[»]
2P8Zelectron microscopy8.90T1-842[»]
2ZITX-ray3.00A/C/E1-842[»]
3B78X-ray2.50A/C/E1-842[»]
3B82X-ray2.35A/C/E1-842[»]
3B8HX-ray2.50A/C/E1-842[»]
3DNYelectron microscopy12.60T1-842[»]
ProteinModelPortaliP32324.
SMRiP32324. Positions 2-842.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32324.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 346330tr-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.
GeneTreeiENSGT00770000120583.
ENSGT00770000120758.
HOGENOMiHOG000231589.
InParanoidiP32324.
KOiK03234.
OMAiRWAPVPE.
OrthoDBiEOG7966SQ.

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.

P32324-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVAFTVDQMR SLMDKVTNVR NMSVIAHVDH GKSTLTDSLV QRAGIISAAK
60 70 80 90 100
AGEARFTDTR KDEQERGITI KSTAISLYSE MSDEDVKEIK QKTDGNSFLI
110 120 130 140 150
NLIDSPGHVD FSSEVTAALR VTDGALVVVD TIEGVCVQTE TVLRQALGER
160 170 180 190 200
IKPVVVINKV DRALLELQVS KEDLYQTFAR TVESVNVIVS TYADEVLGDV
210 220 230 240 250
QVYPARGTVA FGSGLHGWAF TIRQFATRYA KKFGVDKAKM MDRLWGDSFF
260 270 280 290 300
NPKTKKWTNK DTDAEGKPLE RAFNMFILDP IFRLFTAIMN FKKDEIPVLL
310 320 330 340 350
EKLEIVLKGD EKDLEGKALL KVVMRKFLPA ADALLEMIVL HLPSPVTAQA
360 370 380 390 400
YRAEQLYEGP ADDANCIAIK NCDPKADLML YVSKMVPTSD KGRFYAFGRV
410 420 430 440 450
FAGTVKSGQK VRIQGPNYVP GKKDDLFIKA IQRVVLMMGR FVEPIDDCPA
460 470 480 490 500
GNIIGLVGID QFLLKTGTLT TSETAHNMKV MKFSVSPVVQ VAVEVKNAND
510 520 530 540 550
LPKLVEGLKR LSKSDPCVLT YMSESGEHIV AGTGELHLEI CLQDLEHDHA
560 570 580 590 600
GVPLKISPPV VAYRETVESE SSQTALSKSP NKHNRIYLKA EPIDEEVSLA
610 620 630 640 650
IENGIINPRD DFKARARIMA DDYGWDVTDA RKIWCFGPDG NGPNLVIDQT
660 670 680 690 700
KAVQYLHEIK DSVVAAFQWA TKEGPIFGEE MRSVRVNILD VTLHADAIHR
710 720 730 740 750
GGGQIIPTMR RATYAGFLLA DPKIQEPVFL VEIQCPEQAV GGIYSVLNKK
760 770 780 790 800
RGQVVSEEQR PGTPLFTVKA YLPVNESFGF TGELRQATGG QAFPQMVFDH
810 820 830 840
WSTLGSDPLD PTSKAGEIVL AARKRHGMKE EVPGWQEYYD KL
Length:842
Mass (Da):93,289
Last modified:October 1, 1993 - v1
Checksum:iFD2F8073CB9B66AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59369 Genomic DNA. Translation: AAA21646.1.
M59370 Genomic DNA. Translation: AAA51398.1.
X90518 Genomic DNA. Translation: CAA62116.1.
X94335 Genomic DNA. Translation: CAA64052.1.
U32274 Genomic DNA. Translation: AAB64827.1.
U28373 Genomic DNA. Translation: AAB64821.1.
Z75041 Genomic DNA. Translation: CAA99332.1.
AY497635 Genomic DNA. Translation: AAT12549.1.
BK006948 Genomic DNA. Translation: DAA10907.1.
BK006938 Genomic DNA. Translation: DAA12229.1.
PIRiA41778.
RefSeqiNP_010673.1. NM_001180693.1.
NP_014776.1. NM_001183552.1.

Genome annotation databases

EnsemblFungiiYDR385W; YDR385W; YDR385W.
YOR133W; YOR133W; YOR133W.
GeneIDi851993.
854301.
KEGGisce:YDR385W.
sce:YOR133W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59369 Genomic DNA. Translation: AAA21646.1 .
M59370 Genomic DNA. Translation: AAA51398.1 .
X90518 Genomic DNA. Translation: CAA62116.1 .
X94335 Genomic DNA. Translation: CAA64052.1 .
U32274 Genomic DNA. Translation: AAB64827.1 .
U28373 Genomic DNA. Translation: AAB64821.1 .
Z75041 Genomic DNA. Translation: CAA99332.1 .
AY497635 Genomic DNA. Translation: AAT12549.1 .
BK006948 Genomic DNA. Translation: DAA10907.1 .
BK006938 Genomic DNA. Translation: DAA12229.1 .
PIRi A41778.
RefSeqi NP_010673.1. NM_001180693.1.
NP_014776.1. NM_001183552.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1N0U X-ray 2.12 A 1-842 [» ]
1N0V X-ray 2.85 C/D 1-842 [» ]
1S1H electron microscopy 11.70 T 1-842 [» ]
1U2R X-ray 2.60 A 1-842 [» ]
1ZM2 X-ray 3.07 A/C/E 1-842 [» ]
1ZM3 X-ray 3.07 A/C/E 1-842 [» ]
1ZM4 X-ray 2.90 A/C/E 1-842 [» ]
1ZM9 X-ray 2.80 A/C/E 1-842 [» ]
2E1R X-ray 3.15 A 1-842 [» ]
2NPF X-ray 2.90 A/B 1-842 [» ]
2P8W electron microscopy 11.30 T 1-842 [» ]
2P8X electron microscopy 9.70 T 1-842 [» ]
2P8Y electron microscopy 11.70 T 1-842 [» ]
2P8Z electron microscopy 8.90 T 1-842 [» ]
2ZIT X-ray 3.00 A/C/E 1-842 [» ]
3B78 X-ray 2.50 A/C/E 1-842 [» ]
3B82 X-ray 2.35 A/C/E 1-842 [» ]
3B8H X-ray 2.50 A/C/E 1-842 [» ]
3DNY electron microscopy 12.60 T 1-842 [» ]
ProteinModelPortali P32324.
SMRi P32324. Positions 2-842.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32446. 133 interactions.
34529. 85 interactions.
DIPi DIP-4911N.
IntActi P32324. 138 interactions.
MINTi MINT-8285544.
STRINGi 4932.YDR385W.

2D gel databases

SWISS-2DPAGE P32324.

Proteomic databases

MaxQBi P32324.
PaxDbi P32324.
PRIDEi P32324.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR385W ; YDR385W ; YDR385W .
YOR133W ; YOR133W ; YOR133W .
GeneIDi 851993.
854301.
KEGGi sce:YDR385W.
sce:YOR133W.

Organism-specific databases

CYGDi YDR385w.
YOR133w.
SGDi S000005659. EFT1.
S000002793. EFT2.

Phylogenomic databases

eggNOGi COG0480.
GeneTreei ENSGT00770000120583.
ENSGT00770000120758.
HOGENOMi HOG000231589.
InParanoidi P32324.
KOi K03234.
OMAi RWAPVPE.
OrthoDBi EOG7966SQ.

Enzyme and pathway databases

UniPathwayi UPA00345 .
BioCyci YEAST:G3O-29933-MONOMER.
YEAST:G3O-33657-MONOMER.
Reactomei REACT_257951. Peptide chain elongation.

Miscellaneous databases

EvolutionaryTracei P32324.
NextBioi 970163.
PROi P32324.

Gene expression databases

Genevestigatori P32324.

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. "Saccharomyces cerevisiae elongation factor 2. Genetic cloning, characterization of expression, and G-domain modeling."
    Perentesis J.P., Phan L.D., Laporte D.C., Livingston D.M., Bodley J.W.
    J. Biol. Chem. 267:1190-1197(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1 AND EFT2).
  2. "Sequencing and analysis of 51 kb on the right arm of chromosome XV from Saccharomyces cerevisiae reveals 30 open reading frames."
    Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C., Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.
    Yeast 12:281-288(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1).
    Strain: ATCC 96604 / S288c / FY1679.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (EFT1).
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT2).
    Strain: ATCC 204508 / S288c.
  5. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT1).
    Strain: ATCC 204508 / S288c.
  6. Cited for: GENOME REANNOTATION (EFT1 AND EFT2).
    Strain: ATCC 204508 / S288c.
  7. Cited for: PROTEIN SEQUENCE OF 411-422 AND 505-513.
    Strain: ATCC 204508 / S288c.
  8. "Phylogeny and evolution of medical species of Candida and related taxa: a multigenic analysis."
    Diezmann S., Cox C.J., Schoenian G., Vilgalys R.J., Mitchell T.G.
    J. Clin. Microbiol. 42:5624-5635(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 586-785.
  9. "Isolation and properties of the trypsin-derived ADP-ribosyl peptide from diphtheria toxin-modified yeast elongation factor 2."
    Van Ness B.G., Howard J.B., Bodley J.W.
    J. Biol. Chem. 253:8687-8690(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 686-700, DIPHTHAMIDE AT HIS-699.
  10. "Saccharomyces cerevisiae elongation factor 2 is phosphorylated by an endogenous kinase."
    Donovan M.G., Bodley J.W.
    FEBS Lett. 291:303-306(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  11. "Expression of non-ADP-ribosylatable, diphtheria toxin-resistant elongation factor 2 in Saccharomyces cerevisiae."
    Kimata Y., Harashima S., Kohno K.
    Biochem. Biophys. Res. Commun. 191:1145-1151(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLY-701.
  12. "Saccharomyces cerevisiae elongation factor 2. Mutagenesis of the histidine precursor of diphthamide yields a functional protein that is resistant to diphtheria toxin."
    Phan L.D., Perentesis J.P., Bodley J.W.
    J. Biol. Chem. 268:8665-8668(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-699.
  13. "Elongation factor 2 as a novel target for selective inhibition of fungal protein synthesis."
    Justice M.C., Hsu M.-J., Tse B., Ku T., Balkovec J., Schmatz D., Nielsen J.
    J. Biol. Chem. 273:3148-3151(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-180; VAL-187; GLN-490; TYR-521; SER-523; ILE-529; PRO-559; ALA-562; PRO-727; VAL-774 AND GLY-790.
  14. "Characterization of interaction sites in the Saccharomyces cerevisiae ribosomal stalk components."
    Lalioti V.S., Perez-Fernandez J., Remacha M.A., Ballesta J.P.G.
    Mol. Microbiol. 46:719-729(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPL0.
  15. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  16. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  17. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579; THR-713 AND THR-763, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "A conserved eEF2 coding variant in SCA26 leads to loss of translational fidelity and increased susceptibility to proteostatic insult."
    Hekman K.E., Yu G.Y., Brown C.D., Zhu H., Du X., Gervin K., Undlien D.E., Peterson A., Stevanin G., Clark H.B., Pulst S.M., Bird T.D., White K.P., Gomez C.M.
    Hum. Mol. Genet. 21:5472-5483(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PRO-580.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases."
    Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.
    Proteomics 12:960-972(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-509.
  23. "Elongation factor methyltransferase 3 - A novel eukaryotic lysine methyltransferase."
    Zhang L., Hamey J.J., Hart-Smith G., Erce M.A., Wilkins M.R.
    Biochem. Biophys. Res. Commun. 451:229-234(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-509 BY EFM3, METHYLATION AT LYS-613 BY EFM2.
  24. "Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights into non-histone protein lysine methyltransferase activity."
    Hart-Smith G., Chia S.Z., Low J.K., McKay M.J., Molloy M.P., Wilkins M.R.
    J. Proteome Res. 13:1744-1756(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-509, METHYLATION AT LYS-613 BY EFM2.
  25. "Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase."
    Joergensen R., Ortiz P.A., Carr-Schmid A., Nissen P., Kinzy T.G., Andersen G.R.
    Nat. Struct. Biol. 10:379-385(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SORDARIN.
  26. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
    Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
    EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.7 ANGSTROMS) IN COMPLEX WITH 80S RIBOSOME AND SORDARIN, FUNCTION, INTERACTION WITH RPL9A; RPL12A; RPS23A; 18S RRNA AND 25S RRNA.
  27. "Crystal structure of ADP-ribosylated ribosomal translocase from Saccharomyces cerevisiae."
    Joergensen R., Yates S.P., Teal D.J., Nilsson J., Prentice G.A., Merrill A.R., Andersen G.R.
    J. Biol. Chem. 279:45919-45925(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF ADP-RIBOSYLATED FORM IN COMPLEX WITH GDP AND SORDARIN.

Entry informationi

Entry nameiEF2_YEAST
AccessioniPrimary (citable) accession number: P32324
Secondary accession number(s): D6VT19, Q6JEF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 26, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 160782 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eEF2 in yeast.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
  6. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3