EIF5A

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)
End	7,312,463 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	69,812,784 bp
RNA expression pattern
	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
	; ; ; ;
	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
	1984
	276770
	ENSG00000132507; ENSG00000288145
	ENSMUSG00000078812
	P63241
	P63242
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
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
	Wikidata
View/Edit Human	View/Edit Mouse

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

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]

^ ^a ^b ^c ENSG00000288145 GRCh38: Ensembl release 89: ENSG00000132507, ENSG00000288145 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000078812 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Steinkasserer A, Jones T, Sheer D, Koettnitz K, Hauber J, Bevec D (February 1995). "The eukaryotic cofactor for the human immunodeficiency virus type 1 (HIV-1) rev protein, eIF-5A, maps to chromosome 17p12-p13: three eIF-5A pseudogenes map to 10q23.3, 17q25, and 19q13.2". Genomics. 25 (3): 749–752. doi:10.1016/0888-7543(95)80025-H. PMID 7759117.
^ Wolff EC, Kang KR, Kim YS, Park MH (August 2007). "Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification". Amino Acids. 33 (2): 341–350. doi:10.1007/s00726-007-0525-0. PMC 2572820. PMID 17476569.
^ Park JH, Johansson HE, Aoki H, Huang BX, Kim HY, Ganoza MC, Park MH (January 2012). "Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)". The Journal of Biological Chemistry. 287 (4): 2579–2590. doi:10.1074/jbc.M111.309633. PMC 3268417. PMID 22128152.
^ Peil L, Starosta AL, Virumäe K, Atkinson GC, Tenson T, Remme J, Wilson DN (August 2012). "Lys34 of translation elongation factor EF-P is hydroxylated by YfcM". Nature Chemical Biology. 8 (8): 695–697. doi:10.1038/nchembio.1001. PMID 22706199.
^ Rossi D, Kuroshu R, Zanelli CF, Valentini SR (2013). "eIF5A and EF-P: two unique translation factors are now traveling the same road". Wiley Interdisciplinary Reviews. RNA. 5 (2): 209–222. doi:10.1002/wrna.1211. PMID 24402910. S2CID 25447826.

[refGRCh38Ensembl-1] ENSG00000288145 GRCh38: Ensembl release 89: ENSG00000132507, ENSG00000288145 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000078812 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7759117-5] Steinkasserer A, Jones T, Sheer D, Koettnitz K, Hauber J, Bevec D (February 1995). "The eukaryotic cofactor for the human immunodeficiency virus type 1 (HIV-1) rev protein, eIF-5A, maps to chromosome 17p12-p13: three eIF-5A pseudogenes map to 10q23.3, 17q25, and 19q13.2". Genomics. 25 (3): 749–752. doi:10.1016/0888-7543(95)80025-H. PMID 7759117.

[pmid17476569-6] Wolff EC, Kang KR, Kim YS, Park MH (August 2007). "Posttranslational synthesis of hypusine: evolutionary progression and specificity of the hypusine modification". Amino Acids. 33 (2): 341–350. doi:10.1007/s00726-007-0525-0. PMC 2572820. PMID 17476569.

[pmid22128152-7] Park JH, Johansson HE, Aoki H, Huang BX, Kim HY, Ganoza MC, Park MH (January 2012). "Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)". The Journal of Biological Chemistry. 287 (4): 2579–2590. doi:10.1074/jbc.M111.309633. PMC 3268417. PMID 22128152.

[pmid22706199-8] Peil L, Starosta AL, Virumäe K, Atkinson GC, Tenson T, Remme J, Wilson DN (August 2012). "Lys34 of translation elongation factor EF-P is hydroxylated by YfcM". Nature Chemical Biology. 8 (8): 695–697. doi:10.1038/nchembio.1001. PMID 22706199.

[pmid24402910-9] Rossi D, Kuroshu R, Zanelli CF, Valentini SR (2013). "eIF5A and EF-P: two unique translation factors are now traveling the same road". Wiley Interdisciplinary Reviews. RNA. 5 (2): 209–222. doi:10.1002/wrna.1211. PMID 24402910. S2CID 25447826.

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