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P32471

- EF1B_YEAST

UniProt

P32471 - EF1B_YEAST

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Protein

Elongation factor 1-beta

Gene

EFB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: SGD
  2. translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  1. maintenance of translational fidelity Source: SGD
  2. negative regulation of actin filament bundle assembly Source: SGD
  3. positive regulation of GTPase activity Source: GOC
  4. regulation of translational termination Source: SGD
  5. 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.
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
ProteomesiUP000002311: Chromosome I

Organism-specific databases

SGDiS000000003. EFB1.

Subcellular locationi

GO - Cellular componenti

  1. 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 methioninei1 – 11Removed1 Publication
Chaini2 – 206205Elongation factor 1-betaPRO_0000155042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei31 – 311Phosphoserine1 Publication
Modified residuei86 – 861Phosphoserine3 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP32471.
PaxDbiP32471.
PeptideAtlasiP32471.

2D gel databases

SWISS-2DPAGEP32471.

Expressioni

Gene expression databases

GenevestigatoriP32471.

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. 57 interactions.
DIPiDIP-6445N.
IntActiP32471. 6 interactions.
MINTiMINT-441798.
STRINGi4932.YAL003W.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 10-60, 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

eggNOGiCOG2092.
GeneTreeiENSGT00390000011747.
HOGENOMiHOG000207273.
InParanoidiP32471.
KOiK03232.
OMAiYLECENN.
OrthoDBiEOG7M3J9X.

Family and domain databases

Gene3Di3.30.70.60. 1 hit.
InterProiIPR018940. 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]
PfamiPF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view]
SMARTiSM00888. 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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D14080 Genomic DNA. Translation: BAA03165.1 .
L22015 Genomic DNA. Translation: AAC04954.1 .
BK006935 Genomic DNA. Translation: DAA06983.1 .
PIRi S43445.
RefSeqi NP_009398.1. NM_001178150.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P32471.
SMRi P32471. Positions 10-60, 117-206.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31787. 57 interactions.
DIPi DIP-6445N.
IntActi P32471. 6 interactions.
MINTi MINT-441798.
STRINGi 4932.YAL003W.

2D gel databases

SWISS-2DPAGE P32471.

Proteomic databases

MaxQBi P32471.
PaxDbi P32471.
PeptideAtlasi P32471.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YAL003W ; YAL003W ; YAL003W .
GeneIDi 851260.
KEGGi sce:YAL003W.

Organism-specific databases

SGDi S000000003. EFB1.

Phylogenomic databases

eggNOGi COG2092.
GeneTreei ENSGT00390000011747.
HOGENOMi HOG000207273.
InParanoidi P32471.
KOi K03232.
OMAi YLECENN.
OrthoDBi EOG7M3J9X.

Enzyme and pathway databases

UniPathwayi UPA00345 .
BioCyci YEAST:G3O-28818-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32471.
NextBioi 968216.
PROi P32471.

Gene expression databases

Genevestigatori P32471.

Family and domain databases

Gene3Di 3.30.70.60. 1 hit.
InterProi IPR018940. 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 ]
Pfami PF10587. EF-1_beta_acid. 1 hit.
PF00736. EF1_GNE. 1 hit.
[Graphical view ]
SMARTi SM00888. EF1_GNE. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF54984. SSF54984. 1 hit.
PROSITEi PS00824. EF1BD_1. 1 hit.
PS00825. EF1BD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. 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. 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.

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: October 29, 2014
This is version 139 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

External Data

Dasty 3