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YEAST:EF3A

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Species (Taxon ID) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s) YEF3 (synonyms: EFC1, TEF3, YEF3A)
Protein Name(s) Elongation factor 3A

EF-3 EF-3A Eukaryotic elongation factor 3 eEF3 Translation elongation factor 3A Yeast elongation factor 3

External Links
UniProt P16521
EMBL J05197
J05583
U20865
AB018539
BK006945
PIR S59395
RefSeq NP_013350.1
PDB 2IW3
2IWH
2IX3
2IX8
PDBsum 2IW3
2IWH
2IX3
2IX8
ProteinModelPortal P16521
SMR P16521
BioGrid 31517
DIP DIP-2249N
IntAct P16521
MINT MINT-8285353
MaxQB P16521
PaxDb P16521
PeptideAtlas P16521
PRIDE P16521
EnsemblFungi [example_ID YLR249W]
GeneID 850951
KEGG sce:YLR249W
SGD S000004239
eggNOG COG0488
GeneTree ENSGT00550000075671
HOGENOM HOG000180957
InParanoid P16521
KO K03235
OMA FPTQEEC
OrthoDB EOG7Q2NDN
BioCyc YEAST:G3O-32354-MONOMER
UniPathway UPA00345
EvolutionaryTrace P16521
NextBio 967419
Proteomes UP000002311
Genevestigator P16521
GO GO:0010494
GO:0022626
GO:0005840
GO:0005524
GO:0016887
GO:0019843
GO:0003746
GO:0006200
GO:0006414
GO:0006415
Gene3D 1.25.10.10
3.40.50.300
InterPro IPR003593
IPR003439
IPR017871
IPR011989
IPR016024
IPR015688
IPR021133
IPR027417
PANTHER PTHR19211:SF5
Pfam PF00005
SMART SM00382
SUPFAM SSF48371
SSF52540
PROSITE PS00211
PS50893
PS50077

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0010494

cytoplasmic stress granule

PMID:26777405[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0042788

polysomal ribosome

PMID:22888004[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006469

negative regulation of protein kinase activity

PMID:22888004[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0001933

negative regulation of protein phosphorylation

PMID:22888004[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0022626

cytosolic ribosome

PMID:19666721[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:16954224[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0010494

cytoplasmic stress granule

PMID:23451152[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006415

translational termination

PMID:20534490[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006414

translational elongation

PMID:19666721[3]

ECO:0000316

genetic interaction evidence used in manual assertion

SGD:S000004140

P

Seeded From UniProt

complete

involved_in

GO:0006414

translational elongation

PMID:19666721[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005840

ribosome

PMID:9553076[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0003746

translation elongation factor activity

PMID:2670939[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003439
InterPro:IPR017871

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003439
InterPro:IPR017871

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0006412

translation

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0648

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

enables

GO:0003746

translation elongation factor activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0251

F

Seeded From UniProt

complete

enables

GO:0019843

rRNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0699

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

involved_in

GO:0006414

translational elongation

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0251
UniPathway:UPA00345

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Jain, S et al. (2016) ATPase-Modulated Stress Granules Contain a Diverse Proteome and Substructure. Cell 164 487-98 PubMed GONUTS page
  2. 2.0 2.1 2.2 Visweswaraiah, J et al. (2012) Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation. J. Biol. Chem. 287 37757-68 PubMed GONUTS page
  3. 3.0 3.1 3.2 Van Dyke, N et al. (2009) Stm1p alters the ribosome association of eukaryotic elongation factor 3 and affects translation elongation. Nucleic Acids Res. 37 6116-25 PubMed GONUTS page
  4. Anand, M et al. (2006) Domain and nucleotide dependence of the interaction between Saccharomyces cerevisiae translation elongation factors 3 and 1A. J. Biol. Chem. 281 32318-26 PubMed GONUTS page
  5. Grousl, T et al. (2013) Heat shock-induced accumulation of translation elongation and termination factors precedes assembly of stress granules in S. cerevisiae. PLoS ONE 8 e57083 PubMed GONUTS page
  6. Kurata, S et al. (2010) Ribosome recycling step in yeast cytoplasmic protein synthesis is catalyzed by eEF3 and ATP. Proc. Natl. Acad. Sci. U.S.A. 107 10854-9 PubMed GONUTS page
  7. Gontarek, RR et al. (1998) The N terminus of eukaryotic translation elongation factor 3 interacts with 18 S rRNA and 80 S ribosomes. J. Biol. Chem. 273 10249-52 PubMed GONUTS page
  8. Kamath, A & Chakraburtty, K (1989) Role of yeast elongation factor 3 in the elongation cycle. J. Biol. Chem. 264 15423-8 PubMed GONUTS page