Tag Content
SG ID
SG00021960 
UniProt Accession
Theoretical PI
5.08  
Molecular Weight
16832 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Eif5a 
Gene Synonyms/Alias
 
Protein Name
Eukaryotic translation initiation factor 5A-1 
Protein Synonyms/Alias
eIF-5A-1eIF-5A1 Eukaryotic initiation factor 5A isoform 1;eIF-5A eIF-4D; 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:11;69730216-69735460;-1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.966285114 
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.
Description
Temporarily unavailable 
Abstract of related literatures
1. 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] 

2. The mouse (Mus musculus) is the premier animal model for understanding human disease and development. Here we show that a comprehensive understanding of mouse biology is only possible with the availability of a finished, high-quality genome assembly. The finished clone-based assembly of the mouse strain C57BL/6J reported here has over 175,000 fewer gaps and over 139 Mb more of novel sequence, compared with the earlier MGSCv3 draft genome assembly. In a comprehensive analysis of this revised genome sequence, we are now able to define 20,210 protein-coding genes, over a thousand more than predicted in the human genome (19,042 genes). In addition, we identified 439 long, non-protein-coding RNAs with evidence for transcribed orthologs in human. We analyzed the complex and repetitive landscape of 267 Mb of sequence that was missing or misassembled in the previously published assembly, and we provide insights into the reasons for its resistance to sequencing and assembly by whole-genome shotgun approaches. Duplicated regions within newly assembled sequence tend to be of more recent ancestry than duplicates in the published draft, correcting our initial understanding of recent evolution on the mouse lineage. These duplicates appear to be largely composed of sequence regions containing transposable elements and duplicated protein-coding genes; of these, some may be fixed in the mouse population, but at least 40% of segmentally duplicated sequences are copy number variable even among laboratory mouse strains. Mouse lineage-specific regions contain 3,767 genes drawn mainly from rapidly-changing gene families associated with reproductive functions. The finished mouse genome assembly, therefore, greatly improves our understanding of rodent-specific biology and allows the delineation of ancestral biological functions that are shared with human from derived functions that are not. PMID: [19468303] 

3. 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] 

4. To examine the roles of active hypusinated eIF5A (eukaryotic translation initiation factor 5A) and polyamines in cell proliferation, mouse mammary carcinoma FM3A cells were treated with an inhibitor of deoxyhypusine synthase, GC7 (N1-guanyl-1, 7-diaminoheptane), or with an inhibitor of ornithine decarboxylase, DFMO (a-difluoromethylornithine), or with DFMO plus an inhibitor of spermine synthase, APCHA [N1-(3-aminopropyl)-cyclohexylamine]. Treatment with GC7 decreased the level of active eIF5A on day 1 without affecting cellular polyamine content, and inhibition of cell growth occurred from day 2. This delay reflects the fact that eIF5A was present in excess and was very stable in these cells. Treatment with DFMO or with DFMO plus APCHA inhibited cell growth on day 1. DFMO considerably decreased the levels of putrescine and spermidine, and the formation of active eIF5A began to decrease when the level of spermidine fell below 8 nmol/mg of protein after 12 h of incubation with DFMO. The combination of DFMO and APCHA markedly decreased the levels of putrescine and spermine and significantly decreased the level of spermidine, but did not affect the level of active eIF5A until day 3 when spermidine level decreased to 7 nmol/mg of protein. The results show that a decrease in either active eIF5A or polyamines inhibits cell growth, indicating that eIF5A and polyamines are independently involved in cell growth PMID: [15377278] 

5. The eukaryotic translation initiation factor 5A (eIF5A) is a ubiquitous protein of eukaryotic and archaeal organisms which undergoes hypusination, a unique post-translational modification. We have generated a polyclonal antibody against murine eIF5A, which in immunocytochemical assays in B16-F10 cells revealed that the endogenous protein is preferentially localized to the nuclear region. We therefore analyzed possible structural features present in eIF5A proteins that could be responsible for that characteristic. Multiple sequence alignment analysis of eIF5A proteins from different eukaryotic and archaeal organisms showed that the former sequences have an extended N-terminal segment. We have then performed in silico prediction analyses and constructed different truncated forms of murine eIF5A to verify any possible role that the N-terminal extension might have in determining the subcellular localization of the eIF5A in eukaryotic organisms. Our results indicate that the N-terminal extension of the eukaryotic eIF5A contributes in signaling this protein to nuclear localization, despite of bearing no structural similarity with classical nuclear localization signals. PMID: [17707773] 

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Function
mRNA-binding protein involved in translation elongation.Has an important function at the level of mRNA turnover, probablyacting downstream of decapping. Involved in actin dynamics andcell cycle progression, mRNA decay and probably in a pathwayinvolved in stress response and maintenance of cell wallintegrity. With syntenin SDCBP, functions as a regulator ofp53/TP53 and p53/TP53-dependent apoptosis. Regulates also TNF-alpha-mediated apoptosis. Mediates effects of polyamines onneuronal process extension and survival. May play an importantrole in brain development and function, and in skeletal musclestem cell differentiation (By similarity). 
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Subcellular Location
Cytoplasm. Nucleus. Endoplasmic reticulummembrane; Peripheral membrane protein; Cytoplasmic side (Bysimilarity). Nucleus, nuclear pore complex (By similarity).Note=The N-terminal extension contributes in signaling thisprotein to nuclear localization. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0005737 C:cytoplasm IDA:MGI.
GO:0005789 C:endoplasmic reticulum membrane IEA:UniProtKB-SubCell.
GO:0005643 C:nuclear pore IEA:UniProtKB-SubCell.
GO:0005634 C:nucleus IDA:MGI.
GO:0043022 F:ribosome binding IEA:InterPro.
GO:0003746 F:translation elongation factor activity IEA:UniProtKB-KW.
GO:0006915 P:apoptotic process IDA:MGI.
GO:0051028 P:mRNA transport IEA:UniProtKB-KW.
GO:0008612 P:peptidyl-lysine modification to hypusine IEA:InterPro.
GO:0045901 P:positive regulation of translational elongation IEA:InterPro.
GO:0045905 P:positive regulation of translational termination IEA:InterPro.
GO:0015031 P:protein transport IEA:UniProtKB-KW.
GO:0006452 P:translational frameshifting IEA:InterPro.
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Interpro
IPR005824;    KOW.
IPR012340;    NA-bd_OB-fold.
IPR016027;    NA-bd_OB-fold-like.
IPR019769;    Trans_elong_IF5A_hypusine_site.
IPR001884;    Transl_elong_IF5A.
IPR020189;    Transl_elong_IF5A_C.
IPR014722;    Transl_SH3-like_sub.
IPR008991;    Translation_prot_SH3-like.
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Pfam
PF01287;    eIF-5a;    1.
PF00467;    KOW;    1.
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SMART
PROSITE
PS00302;    IF5A_HYPUSINE;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed (By similarity).
CHAIN         2    154       Eukaryotic translation initiation factor
                             5A-1.
                             /FTId=PRO_0000142452.
REGION        2     19       Nuclear localization regulation.
MOD_RES       2      2       N-acetylalanine (By similarity).
MOD_RES      46     46       Phosphoserine (By similarity).
MOD_RES      50     50       Hypusine (By similarity).
MOD_RES      68     68       N6-acetyllysine (By similarity).
CONFLICT      8      8       E -> Y (in Ref. 2; BAB27641).
CONFLICT     16     16       A -> S (in Ref. 2; BAB27641).
CONFLICT    139    139       S -> F (in Ref. 2; BAB27641).
CONFLICT    143    143       E -> K (in Ref. 2; BAB27641).
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Nucleotide Sequence
Length: 1290 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 154 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
YwhazIntAct 
Other Protein-Protein interaction resources
String database  
View Microarray data
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