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-alpha  

UniProtKB / Swiss-Prot ID :  EF1A_YEAST

Gene Name (Synonyms) : 
TEF1 YPR080W P9513.7
TEF2 YBR118W YBR0913  

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

Subcellular Localization :  Cytoplasm. Cytoplasm, cytoskeleton. 

Protein Function :  GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. 

Protein Sequence MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERG...
Predicted Secondary Structure CCCCCCEEEEEEEEEECCCHHHHHHHHHHHHCCCCHHHHHHHHHHHHHCCCCCCHHHHHHCCCCHHHHCC...
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
1Blocked amino end (Met).----MGKEK
----CCCCC
18.26UniProtKB
Link
6PhosphoserineGKEKSHINV
CCCCCEEEE
30.59SysPTM
Link
6Phosphoserine.GKEKSHINV
CCCCCEEEE
30.59UniProtKB
Link
18Phosphoserine.GHVDSGKST
EEECCCHHH
47.21UniProtKB
Link
30N6-methyllysineHLIYKCGGI
HHHHHHCCC
21.29MeMo
Link
53PhosphoserineLGKGSFKYA
CCCCCCHHH
23.27SysPTM
Link
53Phosphoserine.LGKGSFKYA
CCCCCCHHH
23.27UniProtKB
Link
72Phosphothreonine.ERGITIDIA
HCCEEEEEE
18.54UniProtKB
Link
79N6,N6,N6-trimethyllysineIALWKFETP
EEEEEEECC
33.89MeMo
Link
79N6,N6,N6-trimethyllysine.IALWKFETP
EEEEEEECC
33.89UniProtKB
Link
163Phosphoserine.KWDESRFQE
CCCHHHHHH
35.60UniProtKB
Link
259PhosphothreonineGGIGTVPVG
CCCEEEEEE
21.51SysPTM
Link
259Phosphothreonine.GGIGTVPVG
CCCEEEEEE
21.51UniProtKB
Link
316N6,N6-dimethyllysineNVSVKEIRR
CCCHHHEEE
39.66MeMo
Link
355PhosphotyrosineISAGYSPVL
ECCCCCEEE
14.98SysPTM
Link
355Phosphotyrosine.ISAGYSPVL
ECCCCCEEE
14.98UniProtKB
Link
356PhosphoserineSAGYSPVLD
CCCCCEEEE
13.96SysPTM
Link
356Phosphoserine.SAGYSPVLD
CCCCCEEEE
13.96UniProtKB
Link
390N6-methyllysineEDHPKFLKS
CCCCCEECC
60.97MeMo
Link
394PhosphoserineKFLKSGDAA
CEECCCCEE
44.01SysPTM
Link
394Phosphoserine.KFLKSGDAA
CEECCCCEE
44.01UniProtKB
Link
414PhosphoserineVEAFSEYPP
ECCCCCCCC
43.18SysPTM
Link
414Phosphoserine.VEAFSEYPP
ECCCCCCCC
43.18UniProtKB
Link
430Phosphothreonine.DMRQTVAVG
ECCEEEEEE
10.48UniProtKB
Link
458Lysine methyl ester.KAAKK
CCCCC
61.93UniProtKB
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
Methylation
ReferencePubMed
"Characterization of yeast EF-1 alpha: non-conservation of post-translational modifications.";
Cavallius J., Zoll W., Chakraburtty K., Merrick W.C.;
Biochim. Biophys. Acta 1163:75-80(1993).
Cited for: PARTIAL PROTEIN SEQUENCE, AND METHYLATION AT LYS-30; LYS-79; LYS-316AND LYS-390.
"A novel post-translational modification of yeast elongation factor1A. Methylesterification at the C-terminus.";
Zobel-Thropp P., Yang M.C., Machado L., Clarke S.;
J. Biol. Chem. 275:37150-37158(2000).
Cited for: METHYLATION AT LYS-458.
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 SER-394, 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-6; SER-18; THR-72;SER-163; SER-414 AND THR-430, AND MASS SPECTROMETRY.
"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-53; THR-259; TYR-355;SER-356; SER-394 AND SER-414, 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