Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Elongation factor 1-beta  

UniProtKB / Swiss-Prot ID :  EF1B_YEAST

Gene Name (Synonyms) : 
EFB1, TEF5 YAL003W  

Species :  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 

Subcellular Localization :   

Protein 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. 

Protein Sequence MASTDFSKIETLKQLNASLADKSYIEGTAVSQADVTVFKAFQSAYPEFSRWFNHIASKADEFDSFPAASA...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHCCCEECCCCCCHHHHHHHHHCCCCCCHHHHHHHHHHHHHHHHCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASTDF
---CCCCCC
22.57UniProtKB
Link-
4Phosphothreonine-MASTDFSK
-CCCCCCCH
31.37SysPTM
Link-
4Phosphothreonine.-MASTDFSK
-CCCCCCCH
31.37UniProtKB
Link-
31PhosphoserineGTAVSQADV
CCCCCHHHH
19.72SysPTM
Link-
31Phosphoserine.GTAVSQADV
CCCCCHHHH
19.72UniProtKB
Link-
43PhosphoserineKAFQSAYPE
HHCCCCCCH
24.26SysPTM
Link-
43Phosphoserine.KAFQSAYPE
HHCCCCCCH
24.26UniProtKB
Link-
86PhosphoserineDLFGSDDEE
CCCCCCCCC
34.26SysPTM
Link-
86Phosphoserine.DLFGSDDEE
CCCCCCCCC
34.26UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization 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).
Cited for: ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-86, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-43 AND SER-86,AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures