EIF5A
entrez
1984
canonical
uniprot
P63241
canonical
ensembl
ENSG00000132507
resolver
ensembl
ENSG00000288145
resolver
ensp
ENSP00000336702
resolver
ensp
ENSP00000336776
resolver
ensp
ENSP00000390677
resolver
ensp
ENSP00000396073
resolver
ensp
ENSP00000460284
resolver
ensp
ENSP00000564354
resolver
ensp
ENSP00000564368
resolver
genesymbol
EIF5A
resolver
hgnc
HGNC:3300
resolver
uniprot
A8K9A0
resolver
uniprot
D3DTP2
resolver
uniprot
P10159
resolver
uniprot
Q16182
resolver
uniprot
Q7L7L3
resolver
uniprot
Q7Z4L1
resolver
uniprot
Q9D0G2
resolver
uniprot_entry
IF5A1_HUMAN
resolver
uniprot_sec
A8K9A0
resolver
uniprot_sec
D3DTP2
resolver
uniprot_sec
P10159
resolver
uniprot_sec
Q16182
resolver
uniprot_sec
Q7L7L3
resolver
uniprot_sec
Q7Z4L1
resolver
uniprot_sec
Q9D0G2
resolver
amino_acid_sequence
MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVREDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK
uniprot
proteins
disease_involvement
DISEASE: Faundes-Banka syndrome (FABAS) [MIM:619376]: An autosomal dominant disorder characterized by variable combinations of developmental delay, microcephaly, micrognathia and dysmorphic features. {ECO:0000269|PubMed:33547280}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:33547280). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of polyproline-containing peptides as well as other motifs that stall the ribosome (By similarity). Acts as a ribosome quality control (RQC) cofactor by joining the RQC complex to facilitate peptidyl transfer during CAT tailing step (By similarity). Also 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 (PubMed:16987817). With syntenin SDCBP, functions as a regulator of p53/TP53 and p53/TP53-dependent apoptosis (PubMed:15371445). Also regulates TNF-mediated apoptosis (PubMed:15452064, PubMed:17187778). Mediates effects of polyamines on neuronal process extension and survival (PubMed:17360499). Is required for autophagy by assisting the ribosome in translating the ATG3 protein at a specific amino acid sequence, the 'ASP-ASP-Gly' motif, leading to the increase of the efficiency of ATG3 translation and facilitation of LC3B lipidation and autophagosome formation (PubMed:29712776). {ECO:0000250|UniProtKB:P23301, ECO:0000269|PubMed:15371445, ECO:0000269|PubMed:15452064, ECO:0000269|PubMed:16987817, ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:17360499, ECO:0000269|PubMed:29712776, ECO:0000269|PubMed:33547280}.; FUNCTION: (Microbial infection) 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. {ECO:0000269|PubMed:8253832}.
uniprot
proteins
mass_dalton
16832
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="K->A,R: Abolishes acetylation."; /evidence="ECO:0000269|PubMed:18067580, ECO:0000269|PubMed:19379712"; MUTAGEN 47; /note="K->D: Causes total inactivation of eIF5A in supporting yeast growth."; /evidence="ECO:0000269|PubMed:18067580, ECO:0000269|PubMed:19379712"; MUTAGEN 49; /note="G->A: Causes total inactivation of eIF5A in supporting yeast growth."; /evidence="ECO:0000269|PubMed:18067580"; MUTAGEN 50; /note="K->A: Decreases significantly the acetylation at position K-47 and causes total inactivation of eIF5A in supporting yeast growth."; /evidence="ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:18067580, ECO:0000269|PubMed:19379712"; MUTAGEN 50; /note="K->I,D,R: Causes total inactivation of eIF5A in supporting yeast growth."; /evidence="ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:18067580, ECO:0000269|PubMed:19379712"; MUTAGEN 52; /note="G->A: Causes total inactivation of eIF5A in supporting yeast growth."; /evidence="ECO:0000269|PubMed:18067580"; MUTAGEN 55; /note="K->A: Causes total inactivation of eIF5A in supporting yeast growth."; /evidence="ECO:0000269|PubMed:18067580"; MUTAGEN 81; /note="V->G: Leads to temperature sensitivity when expressed in yeast cells."; /evidence="ECO:0000269|PubMed:16987817
uniprot
proteins
post_translational_modification
PTM: Acetylated by PCAF/KAT2B, regulating its subcellular localization (PubMed:19379712, PubMed:22771473). Deacetylated by SIRT2 (PubMed:22771473). {ECO:0000269|PubMed:19379712, ECO:0000269|PubMed:22771473}.; PTM: Lys-50 undergoes hypusination, a unique post-translational modification that consists in the addition of a butylamino group from spermidine to lysine side chain, leading to the formation of the unusual amino acid hypusine. eIF-5As are the only known proteins to undergo this modification, which is essential for their function. {ECO:0000269|PubMed:10229683, ECO:0000269|PubMed:17213197, ECO:0000269|PubMed:18067580, ECO:0000269|PubMed:2492279, ECO:0000269|PubMed:27306458, ECO:0000269|PubMed:3095320}.
uniprot
proteins
protein_family
EIF-5A family
uniprot
proteins
pubmed
10229683
uniprot
proteins
pubmed
10944119
uniprot
proteins
pubmed
11742107
uniprot
proteins
pubmed
1286667
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15262146
uniprot
proteins
pubmed
15303967
uniprot
proteins
pubmed
15371445
uniprot
proteins
pubmed
15452064
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16519677
uniprot
proteins
pubmed
16987817
uniprot
proteins
pubmed
17187778
uniprot
proteins
pubmed
17213197
uniprot
proteins
pubmed
17360499
uniprot
proteins
pubmed
18067580
uniprot
proteins
pubmed
19280598
uniprot
proteins
pubmed
19379712
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22771473
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2492279
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27115996
uniprot
proteins
pubmed
27306458
uniprot
proteins
pubmed
29712776
uniprot
proteins
pubmed
3095320
uniprot
proteins
pubmed
33547280
uniprot
proteins
pubmed
7545941
uniprot
proteins
pubmed
7622067
uniprot
proteins
pubmed
8253832
uniprot
proteins
pubmed
8660923
uniprot
proteins
sequence_length
154
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:19379712, ECO:0000269|PubMed:27306458, ECO:0000269|PubMed:8660923}. Nucleus {ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:17187778, ECO:0000269|PubMed:19379712, ECO:0000269|PubMed:27306458, ECO:0000269|PubMed:8253832}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:8660923}; Peripheral membrane protein {ECO:0000269|PubMed:8660923}; Cytoplasmic side {ECO:0000269|PubMed:8660923}. 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 (PubMed:19379712, PubMed:27306458). Nuclear export of hypusinated protein is mediated by XPO4 (PubMed:10944119, PubMed:27306458). {ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:19379712, ECO:0000269|PubMed:27306458}.
uniprot
proteins