Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P32471 (EF1B_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 1-beta

Short name=EF-1-beta
Alternative name(s):
Eukaryotic elongation factor 1Balpha
Short name=eEF1Balpha
Translation elongation factor 1B alpha
Gene names
Name:EFB1
Synonyms:TEF5
Ordered Locus Names:YAL003W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic subunit of the guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) of the eukaryotic elongation factor 1 complex (eEF1). Stimulates the exchange of GDP for GTP on elongation factor 1A (eEF1A), probably by displacing GDP from the nucleotide binding pocket in eEF1A. The 30-fold higher concentration of GTP compared to GDP in cells favors the formation of eEF1A-GTP, which rapidly forms a ternary complex with aminoacyl-tRNA that in turn displaces eEF1B from the complex. Ref.8

Pathway

Protein biosynthesis; polypeptide chain elongation.

Subunit structure

The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. eEF1Balpha interacts directly with eEF1A. eEF1Balpha and eEF1Bgamma form the eEF1B subcomplex with the GEF activity.

Domain

The C-terminus (pos. 119-205) exhibits guanine nucleotide exchange activity.

Post-translational modification

S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis.

Sequence similarities

Belongs to the EF-1-beta/EF-1-delta family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 206205Elongation factor 1-beta
PRO_0000155042

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue311Phosphoserine Ref.13
Modified residue861Phosphoserine Ref.12 Ref.13 Ref.14

Experimental info

Mutagenesis120 – 1223KSI → R in TEF5-7; reduces translation efficiency and enhances translation fidelity.
Mutagenesis1211S → I, L or N: Reduces translation efficiency and enhances translation fidelity. Ref.8
Mutagenesis1631F → A: Temperature-sensitive. Ref.16
Mutagenesis2051K → A: Loss of catalytic activity, but still binds to eEF1A. Ref.17
Sequence conflict491S → F in BAA03165. Ref.1
Sequence conflict571S → F in BAA03165. Ref.1
Sequence conflict981L → W in BAA03165. Ref.1
Sequence conflict1681L → E AA sequence Ref.6

Secondary structure

............... 206
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32471 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: BEA764852CE125F7

FASTA20622,627
        10         20         30         40         50         60 
MASTDFSKIE TLKQLNASLA DKSYIEGTAV SQADVTVFKA FQSAYPEFSR WFNHIASKAD 

        70         80         90        100        110        120 
EFDSFPAASA AAAEEEEDDD VDLFGSDDEE ADAEAEKLKA ERIAAYNAKK AAKPAKPAAK 

       130        140        150        160        170        180 
SIVTLDVKPW DDETNLEEMV ANVKAIEMEG LTWGAHQFIP IGFGIKKLQI NCVVEDDKVS 

       190        200 
LDDLQQSIEE DEDHVQSTDI AAMQKL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the elongation factor EF-1 beta homologue of Saccharomyces cerevisiae. EF-1 beta is essential for growth."
Hiraga K., Suzuki K., Tsuchiya E., Miyakawa T.
FEBS Lett. 316:165-169(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region."
Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B., Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.
Yeast 10:535-541(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
Norbeck J., Blomberg A.
FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 14-22 AND 51-56.
Strain: ATCC 38531 / Y41.
[6]"Protein identifications for a Saccharomyces cerevisiae protein database."
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.
Electrophoresis 15:1466-1486(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 168-178.
Strain: ATCC 204508 / S288c.
[7]"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT ALA-2.
[8]"Mutations in elongation factor 1beta, a guanine nucleotide exchange factor, enhance translational fidelity."
Carr-Schmid A., Valente L., Loik V.I., Williams T., Starita L.M., Kinzy T.G.
Mol. Cell. Biol. 19:5257-5266(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF SER-121.
[9]"A sampling of the yeast proteome."
Futcher B., Latter G.I., Monardo P., McLaughlin C.S., Garrels J.I.
Mol. Cell. Biol. 19:7357-7368(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[10]"Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae."
Shenton D., Grant C.M.
Biochem. J. 374:513-519(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: S-THIOLATION.
[11]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[12]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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].
[16]"Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha."
Andersen G.R., Pedersen L., Valente L., Chatterjee I., Kinzy T.G., Kjeldgaard M., Nyborg J.
Mol. Cell 6:1261-1266(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 113-206 IN COMPLEX WITH EEF1A, MUTAGENESIS OF PHE-163.
[17]"Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex."
Andersen G.R., Valente L., Pedersen L., Kinzy T.G., Nyborg J.
Nat. Struct. Biol. 8:531-534(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 113-206 IN COMPLEX WITH EEF1A, MUTAGENESIS OF LYS-205.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14080 Genomic DNA. Translation: BAA03165.1.
L22015 Genomic DNA. Translation: AAC04954.1.
BK006935 Genomic DNA. Translation: DAA06983.1.
PIRS43445.
RefSeqNP_009398.1. NM_001178150.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F60X-ray1.67B113-206[»]
1G7CX-ray2.05B113-206[»]
1IJEX-ray2.40B117-206[»]
1IJFX-ray3.00B117-206[»]
2B7BX-ray2.60B113-204[»]
2B7CX-ray1.80B113-204[»]
ProteinModelPortalP32471.
SMRP32471. Positions 10-66, 117-206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31787. 56 interactions.
DIPDIP-6445N.
IntActP32471. 6 interactions.
MINTMINT-441798.
STRING4932.YAL003W.

2D gel databases

SWISS-2DPAGEP32471.

Proteomic databases

PaxDbP32471.
PeptideAtlasP32471.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL003W; YAL003W; YAL003W.
GeneID851260.
KEGGsce:YAL003W.

Organism-specific databases

SGDS000000003. EFB1.

Phylogenomic databases

eggNOGCOG2092.
GeneTreeENSGT00390000011747.
HOGENOMHOG000207273.
KOK03232.
OMAFADETED.
OrthoDBEOG7M3J9X.

Enzyme and pathway databases

BioCycYEAST:G3O-28818-MONOMER.
UniPathwayUPA00345.

Gene expression databases

GenevestigatorP32471.

Family and domain databases

Gene3D3.30.70.60. 1 hit.
InterProIPR018940. EF-1_beta_acid_region_euk.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
[Graphical view]
PfamPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTSM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF54984. SSF54984. 1 hit.
PROSITEPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP32471.
NextBio968216.
PROP32471.

Entry information

Entry nameEF1B_YEAST
AccessionPrimary (citable) accession number: P32471
Secondary accession number(s): D6VPL3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways