- EGFR Signaling Pathway
- TGF-beta Signaling
- Canonical Wnt Signaling
- non-Canonical Wnt Signaling
- Notch Signaling
- p53 Pathway
- NF-kB Pathway
- Cytokine Signaling
EIF-5A, also known as EIF5, functions in start site selection as a GTPase accelerating protein (GAP) for the eukaryotic translation initiation factor (eIF) 2•GTP•tRNA ternary complex within the ribosome-bound pre-initiation complex. In protein synthesis initiation, eIF2 functions in its GTP-bound state to deliver initiator methionyl-tRNA to the small ribosomal subunit and is necessary for protein synthesis in all cells. EIF-5A stabilizes the binding of GDP to eIF2 and is therefore a bi-functional protein that acts as a GDP dissociation inhibitor (GDI). EIF-5A also interacts with eIF1 and eIF3 and binds the eIF2-GTP/Met-tRNA ternary complex along with the 40S ribosome subunit.
EIF-5A ELISA Pair sets
EIF-5A cDNA Clones
EIF-5, EIF-5A [Homo sapiens]
2810011H21Rik, D12Ertd549e, eIF-5 [Mus musculus]
Wikipedia summary for EIF-5A:
Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene.
It is the only known protein to contain the unusual amino acid hypusine [N (ε)- (4-amino-2-hydroxybutyl)-lysine], which is synthesized on eIF-5A at a specific lysine residue from the polyamine spermidine by two catalytic steps.
EF-P is the prokaryotic homolog of eIF-5A, which is also modified post-translationally in a similar but distinct way
Eukaryotic initiation factor 5A isoform 1, Short name=eIF-5A
eIF-5A belongs to the eIF-5A family.
eIF-5A seems to be the only eukaryotic protein to have an hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine).
eIF-5A interacts with DHPS, with SDCBP and DOHH. Interacts with HIV-1 protein Rev. eIF-5A is found in a complex with Ran and XPO4. The hypusine modification increases the interaction with XPO4.
|Subcellular location:||Cytoplasm. Nucleus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus › nuclear pore complex. Note: Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions.|
eIF-5A is expressed in umbilical vein endothelial cells and several cancer cell lines (at protein level).
|Biotechnological use:||Mature eIF5A-1 may be used as an in situ diagnostic marker for aberrant proliferation in intraepithelial neoplasia of the vulva.|
General information above from UniProt
EIF-5A is mRNA-binding protein involved in translation elongation. EIF-5A has an important function at the level of mRNA turnover, probably acting downstream of decapping. EIF-5A is involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis. EIF-5A regulates also TNF-alpha-mediated apoptosis. EIF-5A mediates effects of polyamines on neuronal process extension and survival. EIF-5A may play an important role in brain development and function, and in skeletal muscle stem cell differentiation. EIF-5A is also described as a cellular cofactor of human T-cell leukemia virus type I (HTLV-1) Rex protein and of human immunodeficiency virus type 1 (HIV-1) Rev protein, essential for mRNA export of retroviral transcripts.
- EIF-5A is involved in the regulation of apoptosis and cell proliferation
- EIF-5A is only cellular protein that contains the unique polyamine-derived amino acid, hypusine (Park 2006)
- EIF5A protein and deoxyhypusine/hypusine modification are essential for eukaryotic cell proliferation (Park 2006)
- EIF-5A contributes to the production of proinflammatory cytokines (Maier 2010)
- role for EIF-5A, relating it to embryogenesis, development and cell differentiation (Parreiras-E-Silv 2010)
- EIF-5A is required for the rapid onset of stress-induced translational repression (Li 2010)
- unhypusinated EIF5A plays a central role in the regulation of apoptosis (Sun 2010)