Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Elongation factor 1-beta

Gene

EFB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Pathwayi: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.
View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein biosynthesis.

GO - Molecular functioni

GO - Biological processi

  • maintenance of translational fidelity Source: SGD
  • negative regulation of actin filament bundle assembly Source: SGD
  • regulation of translational termination Source: SGD
  • translational elongation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciYEAST:G3O-28818-MONOMER.
ReactomeiR-SCE-156842. Eukaryotic Translation Elongation.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
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 namesi
Name:EFB1
Synonyms:TEF5
Ordered Locus Names:YAL003W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL003W.
SGDiS000000003. EFB1.

Subcellular locationi

GO - Cellular componenti

  • eukaryotic translation elongation factor 1 complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1223KSI → R in TEF5-7; reduces translation efficiency and enhances translation fidelity.
Mutagenesisi121 – 1211S → I, L or N: Reduces translation efficiency and enhances translation fidelity. 1 Publication
Mutagenesisi163 – 1631F → A: Temperature-sensitive. 1 Publication
Mutagenesisi205 – 2051K → A: Loss of catalytic activity, but still binds to eEF1A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 206205Elongation factor 1-betaPRO_0000155042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Cross-linki13 – 13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei86 – 861PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP32471.
TopDownProteomicsiP32471.

2D gel databases

SWISS-2DPAGEP32471.

PTM databases

iPTMnetiP32471.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

BioGridi31787. 56 interactions.
DIPiDIP-6445N.
IntActiP32471. 6 interactions.
MINTiMINT-441798.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi120 – 13112Combined sources
Helixi136 – 1449Combined sources
Beta strandi151 – 16212Combined sources
Beta strandi165 – 17511Combined sources
Turni176 – 1783Combined sources
Helixi181 – 1899Combined sources
Turni192 – 1943Combined sources
Beta strandi195 – 20511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP32471.
SMRiP32471. Positions 117-206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32471.

Family & Domainsi

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207273.
InParanoidiP32471.
KOiK03232.
OMAiQSAYPEF.
OrthoDBiEOG092C48AL.

Family and domain databases

CDDicd00292. EF1B. 1 hit.
Gene3Di3.30.70.60. 1 hit.
InterProiIPR018940. EF-1_beta_acid_region_euk.
IPR014038. EF1B_bsu/dsu_GNE.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
[Graphical view]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM01182. EF-1_beta_acid. 1 hit.
SM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P32471-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTDFSKIE TLKQLNASLA DKSYIEGTAV SQADVTVFKA FQSAYPEFSR
60 70 80 90 100
WFNHIASKAD EFDSFPAASA AAAEEEEDDD VDLFGSDDEE ADAEAEKLKA
110 120 130 140 150
ERIAAYNAKK AAKPAKPAAK SIVTLDVKPW DDETNLEEMV ANVKAIEMEG
160 170 180 190 200
LTWGAHQFIP IGFGIKKLQI NCVVEDDKVS LDDLQQSIEE DEDHVQSTDI

AAMQKL
Length:206
Mass (Da):22,627
Last modified:January 23, 2007 - v4
Checksum:iBEA764852CE125F7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491S → F in BAA03165 (PubMed:8420802).Curated
Sequence conflicti57 – 571S → F in BAA03165 (PubMed:8420802).Curated
Sequence conflicti98 – 981L → W in BAA03165 (PubMed:8420802).Curated
Sequence conflicti168 – 1681L → E AA sequence (PubMed:7895733).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14080 Genomic DNA. Translation: BAA03165.1.
L22015 Genomic DNA. Translation: AAC04954.1.
BK006935 Genomic DNA. Translation: DAA06983.1.
PIRiS43445.
RefSeqiNP_009398.1. NM_001178150.1.

Genome annotation databases

EnsemblFungiiYAL003W; YAL003W; YAL003W.
GeneIDi851260.
KEGGisce:YAL003W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14080 Genomic DNA. Translation: BAA03165.1.
L22015 Genomic DNA. Translation: AAC04954.1.
BK006935 Genomic DNA. Translation: DAA06983.1.
PIRiS43445.
RefSeqiNP_009398.1. NM_001178150.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP32471.
SMRiP32471. Positions 117-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31787. 56 interactions.
DIPiDIP-6445N.
IntActiP32471. 6 interactions.
MINTiMINT-441798.

PTM databases

iPTMnetiP32471.

2D gel databases

SWISS-2DPAGEP32471.

Proteomic databases

MaxQBiP32471.
TopDownProteomicsiP32471.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL003W; YAL003W; YAL003W.
GeneIDi851260.
KEGGisce:YAL003W.

Organism-specific databases

EuPathDBiFungiDB:YAL003W.
SGDiS000000003. EFB1.

Phylogenomic databases

GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207273.
InParanoidiP32471.
KOiK03232.
OMAiQSAYPEF.
OrthoDBiEOG092C48AL.

Enzyme and pathway databases

UniPathwayiUPA00345.
BioCyciYEAST:G3O-28818-MONOMER.
ReactomeiR-SCE-156842. Eukaryotic Translation Elongation.

Miscellaneous databases

EvolutionaryTraceiP32471.
PROiP32471.

Family and domain databases

CDDicd00292. EF1B. 1 hit.
Gene3Di3.30.70.60. 1 hit.
InterProiIPR018940. EF-1_beta_acid_region_euk.
IPR014038. EF1B_bsu/dsu_GNE.
IPR010987. Glutathione-S-Trfase_C-like.
IPR014717. Transl_elong_EF1B/ribosomal_S6.
IPR001326. Transl_elong_EF1B_B/D_CS.
[Graphical view]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM01182. EF-1_beta_acid. 1 hit.
SM00888. EF1_GNE. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF54984. SSF54984. 1 hit.
PROSITEiPS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEF1B_YEAST
AccessioniPrimary (citable) accession number: P32471
Secondary accession number(s): D6VPL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.