Elongation factor 1-beta - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P32471 (EF1B_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Molecular function	Elongation factor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	eukaryotic translation elongation factor 1 complex Inferred from mutant phenotype Ref.1. Source: SGD ribosome Traceable author statement PubMed 9841679. Source: SGD
Molecular_function	guanyl-nucleotide exchange factor activity Inferred from direct assay PubMed 17925388. Source: SGD translation elongation factor activity Traceable author statement PubMed 9841679. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 206

205

Elongation factor 1-beta

PRO_0000155042

Amino acid modifications

Modified residue

N-acetylalanine Ref.7

Modified residue

Phosphothreonine Ref.11

Modified residue

Phosphoserine Ref.14

Modified residue

Phosphoserine Ref.14

Modified residue

Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14

Experimental info

Mutagenesis

120 – 122

KSI → R in TEF5-7; reduces translation efficiency and enhances translation fidelity.

Mutagenesis

121

S → I, L or N: Reduces translation efficiency and enhances translation fidelity. Ref.8

Mutagenesis

163

F → A: Temperature-sensitive. Ref.15

Mutagenesis

205

K → A: Loss of catalytic activity, but still binds to eEF1A. Ref.16

Sequence conflict

S → F in BAA03165. Ref.1

Sequence conflict

S → F in BAA03165. Ref.1

Sequence conflict

L → W in BAA03165. Ref.1

Sequence conflict

168

L → E AA sequence Ref.6

Secondary structure

206

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P32471 [UniParc].

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

206

22,627

        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' referencesShow '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 [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"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 204511 / S288c / AB972.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-86, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Strain: ADR376.
[13]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, MASS SPECTROMETRY.
[14]	"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; SER-43 AND SER-86, MASS SPECTROMETRY.
[15]	"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.
[16]	"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.

PIR

S43445.

RefSeq

NP_009398.1. NM_001178150.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F60	X-ray	1.67	B	113-206	[»]
1G7C	X-ray	2.05	B	113-206	[»]
1IJE	X-ray	2.40	B	117-206	[»]
1IJF	X-ray	3.00	B	117-206	[»]
2B7B	X-ray	2.60	B	113-204	[»]
2B7C	X-ray	1.80	B	113-204	[»]

ProteinModelPortal

P32471.

SMR

P32471. Positions 10-60, 117-206.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6445N.

IntAct

P32471. 5 interactions.

MINT

MINT-441798.

STRING

4932.YAL003W.

2D gel databases

SWISS-2DPAGE

P32471.

Proteomic databases

PaxDb

P32471.

PeptideAtlas

P32471.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YAL003W; YAL003W; YAL003W.

GeneID

851260.

KEGG

sce:YAL003W.

Organism-specific databases

SGD

S000000003. EFB1.

Phylogenomic databases

eggNOG

COG2092.

GeneTree

ENSGT00390000011747.

HOGENOM

HOG000207273.

K03232.

OMA

EDEERTC.

OrthoDB

EOG441TMN.

Enzyme and pathway databases

UniPathway

UPA00345.

Gene expression databases

Genevestigator

P32471.

GermOnline

YAL003W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.70.60. 1 hit.

InterPro

IPR018940. EF-1_beta_acid_region_euk.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
IPR014038. Transl_elong_fac_EF1B_bsu/dsu.
[Graphical view]

Pfam

PF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]

SMART

SM00888. EF1_GNE. 1 hit.
[Graphical view]

SUPFAM

SSF54984. Transl_elong_EF1B_B/D_G_exch. 1 hit.

PROSITE

PS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P32471.

NextBio

968216.

Entry information

Entry name

EF1B_YEAST

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome I

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents