IF4A3_MOUSE - dbPTM
IF4A3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MAANATMA
-------CCCCCCCC
7.78-
2Acetylation------MAANATMAT
------CCCCCCCCC
14.93-
6Phosphorylation--MAANATMATSGSA
--CCCCCCCCCCHHH
13.7225367039
9PhosphorylationAANATMATSGSARKR
CCCCCCCCCHHHHHH
23.8529233185
10PhosphorylationANATMATSGSARKRL
CCCCCCCCHHHHHHH
22.6327566939
12PhosphorylationATMATSGSARKRLLK
CCCCCCHHHHHHHHC
25.3526824392
24PhosphorylationLLKEEDMTKVEFETS
HHCHHHCCCEEEECC
44.2320469934
54PhosphorylationEDLLRGIYAYGFEKP
HHHHHHHHHHCCCCC
9.1522499769
56PhosphorylationLLRGIYAYGFEKPSA
HHHHHHHHCCCCCHH
12.8422499769
60AcetylationIYAYGFEKPSAIQQR
HHHHCCCCCHHHHHH
41.8522642817
60UbiquitinationIYAYGFEKPSAIQQR
HHHHCCCCCHHHHHH
41.8527667366
124AcetylationELAVQIQKGLLALGD
HHHHHHHHHHHHHCC
53.83-
163PhosphorylationGQHVVAGTPGRVFDM
CCEEECCCCCHHHHH
16.9126824392
198AcetylationEMLNKGFKEQIYDVY
HHHHHHHHHHHHHHH
58.3322826441
202PhosphorylationKGFKEQIYDVYRYLP
HHHHHHHHHHHHHCC
10.0718563927
242AcetylationDPIRILVKRDELTLE
CCEEEEECCCCCCHH
51.1623864654
252UbiquitinationELTLEGIKQFFVAVE
CCCHHHHHHHEEEEE
52.49-
289AcetylationIFCNTKRKVDWLTEK
HHCCCCCCHHHHHHH
46.2122826441
289UbiquitinationIFCNTKRKVDWLTEK
HHCCCCCCHHHHHHH
46.21-
296AcetylationKVDWLTEKMREANFT
CHHHHHHHHHHCCCE
37.71-
321AcetylationKERESIMKEFRSGAS
HHHHHHHHHHHHCCC
52.62-
374UbiquitinationRSGRYGRKGVAINFV
CCCCCCCCCEEEEEE
54.0627667366

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF4A3_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF4A3_HUMANEIF4A3physical
20360068

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF4A3_MOUSE

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Related Literatures of Post-Translational Modification

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