EIF5A

Eukaryotic translation initiation factor 5A-1 is a protein that in humans is encoded by the EIF5A gene.^[5]

PDBOrtholog search: I3L397 PDBe I3L397 RCSB

AliasesEIF5A, EIF-5A, EIF5A1, eIF5AI, eukaryotic translation initiation factor 5A, eIF-4D, FABAS

External IDsOMIM: 600187; MGI: 106248; HomoloGene: 133803; GeneCards: EIF5A; OMA:EIF5A - orthologs

Chr.Chromosome 17 (human)^[1]

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EIF5A
Available structures PDB Ortholog search: I3L397 PDBe I3L397 RCSB List of PDB id codes 3CPF, 5DLQ
Identifiers
Aliases	EIF5A, EIF-5A, EIF5A1, eIF5AI, eukaryotic translation initiation factor 5A, eIF-4D, FABAS
External IDs	OMIM: 600187; MGI: 106248; HomoloGene: 133803; GeneCards: EIF5A; OMA:EIF5A - orthologs
Gene location (Human) Chr. Chromosome 17 (human)[1] Band 17p13.1 Start 7,306,999 bp[1] End 7,312,463 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11|11 B3 Start 69,807,540 bp[2] End 69,812,784 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in skin of abdomen skin of leg stromal cell of endometrium mucosa of transverse colon right testis appendix left testis gastrocnemius muscle islet of Langerhans right adrenal gland Top expressed in somite primitive streak hand mandibular prominence dermis maxillary prominence human fetus abdominal wall Gonadal ridge migratory enteric neural crest cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein N-terminus binding ribosome binding translation elongation factor activity protein binding RNA binding U6 snRNA binding Cellular component cytoplasm cytosol endoplasmic reticulum membrane membrane nuclear pore lamellae anulatae endoplasmic reticulum extracellular exosome nucleus dendrite soma Biological process mRNA transport protein biosynthesis positive regulation of translational elongation translational elongation mRNA export from nucleus peptidyl-lysine modification to peptidyl-hypusine nucleocytoplasmic transport protein export from nucleus positive regulation of cell population proliferation protein transport translational frameshifting positive regulation of translational termination apoptotic process positive regulation of cytosolic calcium ion concentration ageing positive regulation of cardiac muscle cell apoptotic process positive regulation of apoptotic process negative regulation of apoptotic process positive regulation of muscle cell differentiation cellular response to thyroid hormone stimulus positive regulation of reactive oxygen species metabolic process transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1984 276770 Ensembl ENSG00000132507 ENSG00000288145 ENSMUSG00000078812 UniProt P63241 P63242 RefSeq (mRNA) NM_001143760 NM_001143761 NM_001143762 NM_001970 NM_001370420 NM_001370421 NM_001166589 NM_001166590 NM_001166591 NM_001166592 NM_001166593 NM_001166594 NM_001166595 NM_001166596 NM_181582 RefSeq (protein) NP_001137232 NP_001137233 NP_001137234 NP_001961 NP_001357349 NP_001357350 NP_001160061 NP_001160062 NP_001160063 NP_001160064 NP_001160065 NP_001160066 NP_001160067 NP_001160068 NP_853613 Location (UCSC) Chr 17: 7.31 – 7.31 Mb Chr 11: 69.81 – 69.81 Mb PubMed search [3] [4]
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It is the only known protein to contain the unusual amino acid hypusine [N^ε-(4-amino-2-hydroxybutyl)-lysine], which is synthesized on eIF5A at a specific lysine residue from the polyamine spermidine by two catalytic steps.^[6]

EF-P is the bacterial homolog of eIF5A, which is modified post-translationally in a similar but distinct way.^[7][8] Both proteins are believed to catalyze peptide bond formation and help resolve ribosomal stalls, making them elongation factors despite the "initiation factor" name originally assigned.^[9]