EIF5A

EIF5A (Eukaryotic Translation Initiation Factor 5A) is a Protein Coding gene. Diseases associated with EIF5A include Human Immunodeficiency Virus Type 1 and Retinitis Pigmentosa 14. Among its related pathways are Metabolism of proteins and Translation Factors. Gene Ontology (GO) annotations related to this gene include protein N-terminus binding. An important paralog of this gene is EIF5AL1.

Eukaryotic Translation Initiation Factor 5A

mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. 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. Regulates also TNF-alpha-mediated apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation. 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.

Cellular response to virus Source: UniProtKB
mRNA transport Source: UniProtKB-KW
Positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
Positive regulation of transcription by RNA polymerase II Source: UniProtKB
Positive regulation of translational elongation Source: UniProtKB
Positive regulation of translational termination Source: InterPro
Protein transport Source: UniProtKB-KW
Tumor necrosis factor-mediated signaling pathway Source: UniProtKB

Endoplasmic reticulum membrane; Nucleus; Nuclear pore complex; Cytoplasm. 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.

Acetylated. Deacetylated by SIRT2.
eIF-5A seems to be the only eukaryotic protein to have a hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine).