Version 5.4
Homo sapiens Protein: EIF1AX
Summary
InnateDB Protein IDBP-50662.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol EIF1AX
Protein Name eukaryotic translation initiation factor 1A, X-linked
Synonyms eIF-1A; eIF-4C; EIF1A; EIF1AP1; EIF4C;
Species Homo sapiens
Ensembl Protein ENSP00000368912
InnateDB Gene IDBG-50658 (EIF1AX)
Protein Structure
UniProt Annotation
Function Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 17 experimentally validated interaction(s) in this database.
Experimentally validated
Total 17 [view]
Protein-Protein 16 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003723 RNA binding
GO:0003743 translation initiation factor activity
Biological Process
GO:0006413 translational initiation
Cellular Component
Protein Structure and Domains
PDB ID
InterPro IPR001253 Translation initiation factor 1A (eIF-1A)
IPR006196 RNA-binding domain, S1, IF1 type
IPR012340 Nucleic acid-binding, OB-fold
PFAM PF01176
PRINTS
PIRSF
SMART SM00652
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-P47813
TrEMBL X6RAC9
UniProt Splice Variant
Entrez Gene 1964
UniGene Hs.737196
RefSeq
HUGO HGNC:3250
OMIM 300186
CCDS
HPRD 02174
IMGT
EMBL AL732366
GenPept

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca