Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
50114 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Protein Name
Elongation factor 1-alpha 1 
Protein Synonyms/Alias
EF-1-alpha-1 Elongation factor Tu;EF-Tu Eukaryotic elongation factor 1 A-1;eEF1A-1 
Mus musculus (Mouse) 
NCBI Taxonomy ID
Chromosome Location
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Probability (GAS) of Function in Spermatogenesis
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Temporarily unavailable 
Abstract of related literatures
1. Eukaryotic protein synthesis initiation factor 4A (eIF-4A), a 46-kDa polypeptide, is involved both in mRNA cap recognition and in the binding of mRNA to 40S ribosomal subunits. A 41-mer oligodeoxynucleotide probe was synthesized complementary to a portion of the published coding sequence of eIF-4A mRNA [Nielsen et al., Nucleic Acids Res. 13 (1985) 6867-6870] and used to screen a mouse genomic library. We have isolated and characterized a full-length clone from that library. The eIF-4A sequence is contained in eleven exons. The eleventh exon also has the 3'-nontranslated sequence and two separate polyadenylation sites. Northern-blot analysis of mouse poly(A)+RNA indicates that there are several distinct mRNA species coding for eIF-4A. Two of these contain the same coding sequence and differ only in the length of the 3'-nontranslated region. Two of the eIF-4A mRNAs are therefore likely to be the result of differential processing at the 3'-end. We have used a fragment of the genomic clone to measure the steady-state levels of eIF-4A mRNA during the induced differentiation of murine erythroleukemia cells. S1 nuclease protection experiments demonstrated that by the fourth day after induction eIF-4A mRNA declined to 25% of its steady-state level in uninduced cells. In contrast, the steady-state level of beta-globin mRNA increased dramatically during differentiation. In vitro transcription assays using nuclei isolated from uninduced and induced cells show that the rate of transcription of eIF-4A mRNA was 40% greater in differentiated cells, indicating a posttranscriptional component is involved in the regulation of the steady-state mRNA level. PMID: [3215517] 

3. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

4. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

5. The eucaryotic elongation factor Tu (eEF-Tu) is a single polypeptide with an approximate Mr of 53,000. During protein synthesis eEF-Tu promotes the binding of aminoacyl-tRNA to the ribosome. To study the expression of the gene(s) for this factor, a genomic clone was isolated that contains a mouse eEF-Tu gene. We screened a phage genomic library with a synthetic oligonucleotide probe complementary to a region of the Saccharomyces cerevisiae and Artemia sp. eEF-Tu genes which codes for an area that is highly conserved between both yeast and Artemia sp. eEF-Tu. From approximately 75,000 phage plaques we obtained five isolates with apparently identical inserts. All five clones contained a 3.8-kilobase EcoRI fragment that hybridized to additional oligonucleotide probes corresponding to different conserved regions of eEF-Tu. We sequenced the 5' end of one genomic clone and determined the length of the cloned fragment that was protected by eEF-Tu mRNA in S1 nuclease protection assays. A quantitative S1 nuclease protection assay was used to compare the relative steady-state levels of eEF-Tu mRNA in total mRNA in total RNA isolated from hexamethylene-bisacetamide-induced murine erythroleukemia cells. The results show a dramatic reduction in the steady-state level of eEF-Tu mRNA as differentiation proceeds. A similar reduction in transcription of eEF-Tu mRNA was observed in isolated nuclei. Finally, we examined the in vivo synthesis of eEF-Tu during differentiation and found that it declined in a manner parallel to the decline in the steady-state level of eEF-Tu mRNA. In addition, we have isolated and sequenced a cDNA clone for mouse eEF-Tu. The derived amino acid sequence is compared with sequences from other eucaryotes. PMID: [3481036] 

7. Elongation Factor 1 alpha (EF-1 alpha), an important eukaryotic translation factor, transports charged aminoacyl-tRNA from the cytosol to the ribosomes during poly-peptide synthesis. Metabolic radiolabeling with [3H] ethanolamine shows that, in all cells examined, EF-1 alpha is the major radiolabeled protein. Radiolabeled EF-1 alpha has an apparent Mr = 53,000 and a basic isoelectric point. It is cytosolic and does not contain N-linked oligosaccharides. Trypsin digestion of murine EF-1 alpha generated two major [3H]ethanolamine-labeled peptides. Three peptides were sequenced and were identical to two distinct regions of the human EF-1 alpha protein. Blank sequencing cycles coinciding with glutamic acid in the human cDNA-derived sequence were also found to release [3H]ethanolamine, and compositional analysis of these peptides confirmed the presence of glutamic acid. Dansylation analysis demonstrates that the amine group of the ethanolamine is blocked. These results indicate that EF-1 alpha is posttranslationally modified by the covalent attachment of ethanolamine via an amide bond to at least two specific glutamic acid residues (Glu-301 and Glu-374). The hydroxyl group of the attached ethanolamine was shown by mass spectrometry and compositional analysis, to be further modified by the addition of a phosphoglycerol unit. This novel posttranslational modification may represent an important alteration of EF-1 alpha, comparable to the regulatory effects of posttranslational methylation of EF-1 alpha lysine residues. PMID: [2569467] 

8. Though the interferon-inducible protein ISG15 was one of the first ubiquitin-like modifiers to be discovered, much remains unknown about the identity of proteins conjugated to ISG15 or the biologic consequences of modification. To gain a better understanding of the cellular pathways affected by ISG15, we identified proteins targeted for ISGylation using a proteomic approach. Mass spectrometric analysis identified 76 candidate ISGylation targets in anti-ISG15 immunoprecipitates from interferon-treated mouse or human cells. Twenty-one proteins were found in both mouse and human samples, including STAT1, a known target of ISGylation. Candidates identified in both species were tested for ISGylation in a transfection system: 18 of 19 proteins tested were ISGylated in this system. Two candidates, EF-2 and VCP, were also shown to be ISGylated in an interferon-dependent manner in the absence of exogenous over-expression. Seven proteins identified from a single species, but functionally related to candidates found in both species, were also ISGylated in the over-expression system. Proteins that can be ISGylated play important roles in translation, glycolysis, stress responses, and cell motility. These data indicate that ISGylation targets proteins found in several fundamentally important cellular pathways and will contribute to understanding the physiologic role of interferon-induced ISG15 and ISG15 conjugation. PMID: [16139798] 

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This protein promotes the GTP-dependent binding ofaminoacyl-tRNA to the A-site of ribosomes during proteinbiosynthesis. With PARP1 and TXK, forms a complex that acts as a Thelper 1 (Th1) cell-specific transcription factor and binds thepromoter of IFN-gamma to directly regulate its transcription, andis thus involved importantly in Th1 cytokine production (Bysimilarity). 
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Subcellular Location
Cytoplasm. Nucleus (By similarity). 
Tissue Specificity
Gene Ontology
GO IDGO termEvidence
GO:0005737 C:cytoplasm IDA:UniProtKB.
GO:0005634 C:nucleus IEA:UniProtKB-SubCell.
GO:0005525 F:GTP binding IEA:UniProtKB-KW.
GO:0003924 F:GTPase activity IEA:InterPro.
GO:0003746 F:translation elongation factor activity IEA:UniProtKB-KW.
GO:0006184 P:GTP catabolic process IEA:GOC.
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IPR000795;    ProtSyn_GTP-bd.
IPR009001;    Transl_elong_EF1A/Init_IF2_C.
IPR004539;    Transl_elong_EF1A_euk/arc.
IPR004161;    Transl_elong_EFTu/EF1A_2.
IPR004160;    Transl_elong_EFTu/EF1A_C.
IPR009000;    Transl_elong_init/rib_B-barrel.
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PF00009;    GTP_EFTU;    1.
PF03144;    GTP_EFTU_D2;    1.
PF03143;    GTP_EFTU_D3;    1.
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PS00301;    EFACTOR_GTP;    1.
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PR00315;    ELONGATNFCT.;   
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Created Date
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    462       Elongation factor 1-alpha 1.
NP_BIND      14     21       GTP (By similarity).
NP_BIND      91     95       GTP (By similarity).
NP_BIND     153    156       GTP (By similarity).
MOD_RES      29     29       Phosphotyrosine (By similarity).
MOD_RES      36     36       N6,N6,N6-trimethyllysine (By similarity).
MOD_RES      41     41       N6-acetyllysine (By similarity).
MOD_RES      44     44       N6-acetyllysine (By similarity).
MOD_RES      55     55       N6,N6-dimethyllysine (By similarity).
MOD_RES      55     55       N6-acetyllysine (By similarity).
MOD_RES      79     79       N6,N6,N6-trimethyllysine (By similarity).
MOD_RES      86     86       Phosphotyrosine (By similarity).
MOD_RES     141    141       Phosphotyrosine (By similarity).
MOD_RES     146    146       N6-acetyllysine (By similarity).
MOD_RES     162    162       Phosphotyrosine (By similarity).
MOD_RES     165    165       N6,N6-dimethyllysine (By similarity).
MOD_RES     172    172       N6-acetyllysine (By similarity).
MOD_RES     179    179       N6-acetyllysine (By similarity).
MOD_RES     255    255       N6-acetyllysine (By similarity).
MOD_RES     300    300       Phosphoserine; by TGFBR1 (By similarity).
MOD_RES     301    301       5-glutamyl
MOD_RES     318    318       N6,N6,N6-trimethyllysine; alternate (By
MOD_RES     318    318       N6-acetyllysine; alternate (By
MOD_RES     374    374       5-glutamyl
MOD_RES     392    392       N6-acetyllysine (By similarity).
MOD_RES     395    395       N6-acetyllysine (By similarity).
MOD_RES     432    432       Phosphothreonine; by PASK (By
MOD_RES     439    439       N6-acetyllysine (By similarity).
CONFLICT      7      7       H -> R (in Ref. 5; AAA37538).
CONFLICT     15     15       H -> L (in Ref. 5; AAA37538).
CONFLICT     23     23       T -> S (in Ref. 5; AAA37538).
CONFLICT     77     78       LW -> QR (in Ref. 2; CAA31957).
CONFLICT     83     83       S -> A (in Ref. 6; CAA27324).
CONFLICT     91     92       DA -> ES (in Ref. 2; CAA31957).
CONFLICT    108    108       Q -> R (in Ref. 5; AAA37538).
CONFLICT    156    156       D -> G (in Ref. 3; BAC28085).
CONFLICT    222    222       S -> H (in Ref. 1; AAA50406).
CONFLICT    224    226       SGT -> VAP (in Ref. 2; CAA31957).
CONFLICT    225    225       G -> D (in Ref. 4; AAH04005).
CONFLICT    239    239       Missing (in Ref. 2; CAA31957).
CONFLICT    350    350       P -> T (in Ref. 3; BAC36446).
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Nucleotide Sequence
Length: 1722 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 462 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Other Protein-Protein interaction resources
String database  
View Microarray data