UniProt ID | IF4A3_MOUSE | |
---|---|---|
UniProt AC | Q91VC3 | |
Protein Name | Eukaryotic initiation factor 4A-III | |
Gene Name | Eif4a3 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 411 | |
Subcellular Localization | Nucleus . Nucleus speckle . Cytoplasm . Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments | |
Protein Description | ATP-dependent RNA helicase. Involved in pre-mRNA splicing as component of the spliceosome. Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. The EJC marks the position of the exon-exon junction in the mature mRNA for the gene expression machinery and the core components remain bound to spliced mRNAs throughout all stages of mRNA metabolism thereby influencing downstream processes including nuclear mRNA export, subcellular mRNA localization, translation efficiency and nonsense-mediated mRNA decay (NMD). Its RNA-dependent ATPase and RNA-helicase activities are induced by CASC3, but abolished in presence of the MAGOH-RBM8A heterodimer, thereby trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The inhibition of ATPase activity by the MAGOH-RBM8A heterodimer increases the RNA-binding affinity of the EJC. Involved in translational enhancement of spliced mRNAs after formation of the 80S ribosome complex. Binds spliced mRNA in sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-exon junctions. Shows higher affinity for single-stranded RNA in an ATP-bound core EJC complex than after the ATP is hydrolyzed. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms; the function is different from the established EJC assembly. Involved in craniofacial development.. | |
Protein Sequence | MAANATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSVSVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MAANATMA -------CCCCCCCC | 7.78 | - | |
2 | Acetylation | ------MAANATMAT ------CCCCCCCCC | 14.93 | - | |
6 | Phosphorylation | --MAANATMATSGSA --CCCCCCCCCCHHH | 13.72 | 25367039 | |
9 | Phosphorylation | AANATMATSGSARKR CCCCCCCCCHHHHHH | 23.85 | 29233185 | |
10 | Phosphorylation | ANATMATSGSARKRL CCCCCCCCHHHHHHH | 22.63 | 27566939 | |
12 | Phosphorylation | ATMATSGSARKRLLK CCCCCCHHHHHHHHC | 25.35 | 26824392 | |
24 | Phosphorylation | LLKEEDMTKVEFETS HHCHHHCCCEEEECC | 44.23 | 20469934 | |
54 | Phosphorylation | EDLLRGIYAYGFEKP HHHHHHHHHHCCCCC | 9.15 | 22499769 | |
56 | Phosphorylation | LLRGIYAYGFEKPSA HHHHHHHHCCCCCHH | 12.84 | 22499769 | |
60 | Acetylation | IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH | 41.85 | 22642817 | |
60 | Ubiquitination | IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH | 41.85 | 27667366 | |
124 | Acetylation | ELAVQIQKGLLALGD HHHHHHHHHHHHHCC | 53.83 | - | |
163 | Phosphorylation | GQHVVAGTPGRVFDM CCEEECCCCCHHHHH | 16.91 | 26824392 | |
198 | Acetylation | EMLNKGFKEQIYDVY HHHHHHHHHHHHHHH | 58.33 | 22826441 | |
202 | Phosphorylation | KGFKEQIYDVYRYLP HHHHHHHHHHHHHCC | 10.07 | 18563927 | |
242 | Acetylation | DPIRILVKRDELTLE CCEEEEECCCCCCHH | 51.16 | 23864654 | |
252 | Ubiquitination | ELTLEGIKQFFVAVE CCCHHHHHHHEEEEE | 52.49 | - | |
289 | Acetylation | IFCNTKRKVDWLTEK HHCCCCCCHHHHHHH | 46.21 | 22826441 | |
289 | Ubiquitination | IFCNTKRKVDWLTEK HHCCCCCCHHHHHHH | 46.21 | - | |
296 | Acetylation | KVDWLTEKMREANFT CHHHHHHHHHHCCCE | 37.71 | - | |
321 | Acetylation | KERESIMKEFRSGAS HHHHHHHHHHHHCCC | 52.62 | - | |
374 | Ubiquitination | RSGRYGRKGVAINFV CCCCCCCCCEEEEEE | 54.06 | 27667366 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of IF4A3_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IF4A3_MOUSE !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of IF4A3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
IF4A3_HUMAN | EIF4A3 | physical | 20360068 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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