SpermatogenesisOnline 1.0

Tag Content
SG ID
SG00005308 
UniProt Accession
Theoretical PI
5.36  
Molecular Weight
48968 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Eif5 
Gene Synonyms/Alias
 
Protein Name
Eukaryotic translation initiation factor 5 
Protein Synonyms/Alias
eIF-5 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:12;112776312-112794270;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.752404579 
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. 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] 

2. Protein phosphorylation is a complex network of signaling and regulatory events that affects virtually every cellular process. Our understanding of the nature of this network as a whole remains limited, largely because of an array of technical challenges in the isolation and high-throughput sequencing of phosphorylated species. In the present work, we demonstrate that a combination of tandem phosphopeptide enrichment methods, high performance MS, and optimized database search/data filtering strategies is a powerful tool for surveying the phosphoproteome. Using our integrated analytical platform, we report the identification of 5,635 nonredundant phosphorylation sites from 2,328 proteins from mouse liver. From this list of sites, we extracted both novel and known motifs for specific Ser/Thr kinases including a "dipolar" motif. We also found that C-terminal phosphorylation was more frequent than at any other location and that the distribution of potential kinases for these sites was unique. Finally, we identified double phosphorylation motifs that may be involved in ordered phosphorylation. PMID: [17242355] 

3. Kinases play a prominent role in tumor development, pointing to the presence of specific phosphorylation patterns in tumor tissues. Here, we investigate whether recently developed high resolution mass spectrometric (MS) methods for proteome and phosphoproteome analysis can also be applied to solid tumors. As tumor model, we used TG3 mutant mice carrying skin melanomas. At total of 100 microg of solid tumor lysate yielded a melanoma proteome of 4443 identified proteins, including at least 88 putative melanoma markers previously found by cDNA microarray technology. Analysis of 2 mg of lysate from dissected melanoma with titansphere chromatography and 8 mg with strong cation exchange together resulted in the identification of more than 5600 phosphorylation sites on 2250 proteins. The phosphoproteome included many hits from pathways important in melanoma. One-month storage at -80 degrees C did not significantly decrease the number of identified phosphorylation sites. Thus, solid tumor can be analyzed by MS-based proteomics with similar efficiency as cell culture models and in amounts compatible with biopsies. PMID: [19367708] 

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Function
Catalyzes the hydrolysis of GTP bound to the 40Sribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) withthe subsequent joining of a 60S ribosomal subunit resulting in therelease of eIF-2 and the guanine nucleotide. The subsequentjoining of a 60S ribosomal subunit results in the formation of afunctional 80S initiation complex (80S.mRNA.Met-tRNA[F]). 
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Subcellular Location
 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0005525 F:GTP binding IEA:UniProtKB-KW.
GO:0003743 F:translation initiation factor activity IEA:UniProtKB-KW.
GO:0016070 P:RNA metabolic process IEA:InterPro.
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Interpro
IPR016024;    ARM-type_fold.
IPR016021;    MIF4-like_typ_1/2/3.
IPR002735;    Transl_init_fac_IF2/IF5.
IPR016189;    Transl_init_fac_IF2/IF5_N.
IPR016190;    Transl_init_fac_IF2/IF5_Zn-bd.
IPR003307;    W2_domain.
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Pfam
PF01873;    eIF-5_eIF-2B;    1.
PF02020;    W2;    1.
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SMART
SM00653;    eIF2B_5;    1.
SM00515;    eIF5C;    1.
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PROSITE
PS51363;    W2;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
CHAIN         1    429       Eukaryotic translation initiation factor
                             5.
                             /FTId=PRO_0000212517.
DOMAIN      231    390       W2.
NP_BIND      27     34       GTP (Potential).
COMPBIAS    194    200       Asp/Glu-rich (highly acidic).
COMPBIAS    382    400       Asp/Glu-rich (highly acidic).
COMPBIAS    421    427       Asp-rich (acidic).
MOD_RES      10     10       Phosphoserine (By similarity).
MOD_RES     149    149       Phosphoserine (By similarity).
MOD_RES     227    227       Phosphoserine (By similarity).
MOD_RES     387    387       Phosphoserine.
MOD_RES     388    388       Phosphoserine.
MOD_RES     403    403       Phosphotyrosine (By similarity).
MOD_RES     408    408       Phosphoserine (By similarity).
MOD_RES     417    417       Phosphoserine (By similarity).
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Nucleotide Sequence
Length: 3711 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 429 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
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