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Eukaryotic translation initiation factor 5A-1 (eIF-5A-1) (eIF-5A1) (Eukaryotic initiation factor 5A isoform 1) (eIF-5A) (Rev-binding factor) (eIF-4D)

 IF5A1_HUMAN             Reviewed;         154 AA.
P63241; A8K9A0; D3DTP2; P10159; Q16182; Q7L7L3; Q7Z4L1; Q9D0G2;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
18-JUL-2018, entry version 152.
RecName: Full=Eukaryotic translation initiation factor 5A-1;
Short=eIF-5A-1;
Short=eIF-5A1;
AltName: Full=Eukaryotic initiation factor 5A isoform 1;
Short=eIF-5A;
AltName: Full=Rev-binding factor;
AltName: Full=eIF-4D;
Name=EIF5A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2492279;
Smit-Mcbride Z., Dever T.E., Hershey J.W.B., Merrick W.C.;
"Sequence determination and cDNA cloning of eukaryotic initiation
factor 4D, the hypusine-containing protein.";
J. Biol. Chem. 264:1578-1583(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-154, INTERACTION
WITH HIV-1 REV, AND SUBCELLULAR LOCATION.
PubMed=8253832; DOI=10.1083/jcb.123.6.1309;
Ruhl M., Himmelspach M., Bahr G.M., Hammerschmid F., Jaksche H.,
Wolff B., Aschauer H., Farrington G.K., Probst H., Bevec D.,
Hauber J.;
"Eukaryotic initiation factor 5A is a cellular target of the human
immunodeficiency virus type 1 Rev activation domain mediating trans-
activation.";
J. Cell Biol. 123:1309-1320(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=7545941; DOI=10.1016/0378-1119(94)90385-9;
Koettnitz K., Kappel B., Baumruker T., Hauber J., Bevec D.;
"The genomic structure encoding human initiation factor eIF-5A.";
Gene 144:249-252(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=7622067; DOI=10.1016/0378-1119(95)00136-T;
Koettnitz K., Woehl T., Kappel B., Lottspeich F., Hauber J., Bevec D.;
"Identification of a new member of the human eIF-5A gene family.";
Gene 159:283-284(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Johansson H.E., Jenkins Z.A.;
"Differential expression of eIF5AI-mRNAs.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, Prostate, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-6, AND INTERACTION WITH DHPS.
PubMed=10229683; DOI=10.1042/bj3400273;
Lee Y.B., Joe Y.A., Wolff E.C., Dimitriadis E.K., Park M.H.;
"Complex formation between deoxyhypusine synthase and its protein
substrate, the eukaryotic translation initiation factor 5A (eIF5A)
precursor.";
Biochem. J. 340:273-281(1999).
[10]
PROTEIN SEQUENCE OF 2-26; 56-67; 69-85 AND 110-121, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Waridel P., Quadroni M.;
Submitted (MAR-2009) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 48-55, AND HYPUSINE AT LYS-50.
PubMed=3095320;
Park M.H., Liu T.-Y., Neece S.H., Swiggard W.J.;
"Eukaryotic initiation factor 4D. Purification from human red blood
cells and the sequence of amino acids around its single hypusine
residue.";
J. Biol. Chem. 261:14515-14519(1986).
[12]
PROTEIN SEQUENCE OF 56-121, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
PROTEIN SEQUENCE OF 68-84 AND 114-121.
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[14]
SUBCELLULAR LOCATION.
PubMed=8660923; DOI=10.1006/excr.1996.0185;
Shi X.-P., Yin K.-C., Zimolo Z.A., Stern A.M., Waxman L.;
"The subcellular distribution of eukaryotic translation initiation
factor, eIF-5A, in cultured cells.";
Exp. Cell Res. 225:348-356(1996).
[15]
IDENTIFICATION IN A COMPLEX WITH RAN AND XPO4.
PubMed=10944119; DOI=10.1093/emboj/19.16.4362;
Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S.,
Hartmann E., Kutay U., Goerlich D.;
"Exportin 4: a mediator of a novel nuclear export pathway in higher
eukaryotes.";
EMBO J. 19:4362-4371(2000).
[16]
MRNA-BINDING.
PubMed=15303967; DOI=10.1042/BJ20041232;
Xu A., Jao D.L., Chen K.Y.;
"Identification of mRNA that binds to eukaryotic initiation factor 5A
by affinity co-purification and differential display.";
Biochem. J. 384:585-590(2004).
[17]
BIOTECHNOLOGY.
PubMed=15262146; DOI=10.1016/j.ygyno.2004.03.018;
Cracchiolo B.M., Heller D.S., Clement P.M.J., Wolff E.C., Park M.H.,
Hanauske-Abel H.M.;
"Eukaryotic initiation factor 5A-1 (eIF5A-1) as a diagnostic marker
for aberrant proliferation in intraepithelial neoplasia of the
vulva.";
Gynecol. Oncol. 94:217-222(2004).
[18]
FUNCTION, AND INTERACTION WITH SDCBP.
PubMed=15371445; DOI=10.1074/jbc.M407165200;
Li A.-L., Li H.-Y., Jin B.-F., Ye Q.-N., Zhou T., Yu X.-D., Pan X.,
Man J.-H., He K., Yu M., Hu M.-R., Wang J., Yang S.-C., Shen B.-F.,
Zhang X.-M.;
"A novel eIF5A complex functions as a regulator of p53 and p53-
dependent apoptosis.";
J. Biol. Chem. 279:49251-49258(2004).
[19]
FUNCTION.
PubMed=15452064; DOI=10.1167/iovs.03-1367;
Taylor C.A., Senchyna M., Flanagan J., Joyce E.M., Cliche D.O.,
Boone A.N., Culp-Stewart S., Thompson J.E.;
"Role of eIF5A in TNF-alpha-mediated apoptosis of lamina cribrosa
cells.";
Invest. Ophthalmol. Vis. Sci. 45:3568-3576(2004).
[20]
TISSUE SPECIFICITY.
PubMed=16519677; DOI=10.1111/j.1742-4658.2006.05135.x;
Clement P.M.J., Johansson H.E., Wolff E.C., Park M.H.;
"Differential expression of eIF5A-1 and eIF5A-2 in human cancer
cells.";
FEBS J. 273:1102-1114(2006).
[21]
FUNCTION, AND MUTAGENESIS OF VAL-81.
PubMed=16987817; DOI=10.1074/jbc.M601460200;
Schrader R., Young C., Kozian D., Hoffmann R., Lottspeich F.;
"Temperature-sensitive eIF5A mutant accumulates transcripts targeted
to the nonsense-mediated decay pathway.";
J. Biol. Chem. 281:35336-35346(2006).
[22]
SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF LYS-50.
PubMed=17187778; DOI=10.1016/j.yexcr.2006.09.030;
Taylor C.A., Sun Z., Cliche D.O., Ming H., Eshaque B., Jin S.,
Hopkins M.T., Thai B., Thompson J.E.;
"Eukaryotic translation initiation factor 5A induces apoptosis in
colon cancer cells and associates with the nucleus in response to
tumour necrosis factor alpha signalling.";
Exp. Cell Res. 313:437-449(2007).
[23]
INTERACTION WITH DOHH.
PubMed=17213197; DOI=10.1074/jbc.M607495200;
Kang K.R., Kim Y.S., Wolff E.C., Park M.H.;
"Specificity of the deoxyhypusine hydroxylase-eukaryotic translation
initiation factor (eIF5A) interaction: identification of amino acid
residues of the enzyme required for binding of its substrate,
deoxyhypusine-containing eIF5A.";
J. Biol. Chem. 282:8300-8308(2007).
[24]
FUNCTION.
PubMed=17360499; DOI=10.1073/pnas.0611609104;
Huang Y., Higginson D.S., Hester L., Park M.H., Snyder S.H.;
"Neuronal growth and survival mediated by eIF5A, a polyamine-modified
translation initiation factor.";
Proc. Natl. Acad. Sci. U.S.A. 104:4194-4199(2007).
[25]
MUTAGENESIS OF LYS-47; GLY-49; LYS-50; GLY-52 AND LYS-55.
PubMed=18067580; DOI=10.1111/j.1742-4658.2007.06172.x;
Cano V.S.P., Jeon G.A., Johansson H.E., Henderson C.A., Park J.-H.,
Valentini S.R., Hershey J.W.B., Park M.H.;
"Mutational analyses of human eIF5A-1: identification of amino acid
residues critical for eIF5A activity and hypusine modification.";
FEBS J. 275:44-58(2008).
[26]
ACETYLATION AT LYS-47, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-47
AND LYS-50.
PubMed=19379712; DOI=10.1016/j.bbrc.2009.04.049;
Lee S.B., Park J.-H., Kaevel J., Sramkova M., Weigert R., Park M.H.;
"The effect of hypusine modification on the intracellular localization
of eIF5A.";
Biochem. Biophys. Res. Commun. 383:497-502(2009).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
ACETYLATION, AND DEACETYLATION BY SIRT2.
PubMed=22771473; DOI=10.1016/j.febslet.2012.06.042;
Ishfaq M., Maeta K., Maeda S., Natsume T., Ito A., Yoshida M.;
"Acetylation regulates subcellular localization of eukaryotic
translation initiation factor 5A (eIF5A).";
FEBS Lett. 586:3236-3241(2012).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[31]
3D-STRUCTURE MODELING.
PubMed=11742107; DOI=10.1093/protein/14.11.881;
Facchiano A.M., Stiuso P., Chiusano M.L., Caraglia M., Giuberti G.,
Marra M., Abbruzzese A., Colonna G.;
"Homology modelling of the human eukaryotic initiation factor 5A (eIF-
5A).";
Protein Eng. 14:881-890(2001).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:15371445, ECO:0000269|PubMed:15452064,
ECO:0000269|PubMed:16987817, ECO:0000269|PubMed:17187778,
ECO:0000269|PubMed:17360499}.
-!- SUBUNIT: Interacts with DHPS, with SDCBP and DOHH. Interacts with
HIV-1 protein Rev. Found in a complex with Ran and XPO4. The
hypusine modification increases the interaction with XPO4.
{ECO:0000269|PubMed:10229683, ECO:0000269|PubMed:10944119,
ECO:0000269|PubMed:15371445, ECO:0000269|PubMed:17213197,
ECO:0000269|PubMed:8253832}.
-!- INTERACTION:
O43186:CRX; NbExp=3; IntAct=EBI-373150, EBI-748171;
P49366:DHPS; NbExp=5; IntAct=EBI-373150, EBI-741925;
P50222:MEOX2; NbExp=3; IntAct=EBI-373150, EBI-748397;
Q04864:REL; NbExp=3; IntAct=EBI-373150, EBI-307352;
Q05086-3:UBE3A; NbExp=4; IntAct=EBI-373150, EBI-11026619;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=B, C, D;
IsoId=P63241-1; Sequence=Displayed;
Name=2; Synonyms=A;
IsoId=P63241-2; Sequence=VSP_022020;
-!- TISSUE SPECIFICITY: Expressed in umbilical vein endothelial cells
and several cancer cell lines (at protein level).
{ECO:0000269|PubMed:16519677}.
-!- PTM: Acetylated. Deacetylated by SIRT2.
{ECO:0000269|PubMed:19379712, ECO:0000269|PubMed:22771473,
ECO:0000269|Ref.10}.
-!- PTM: 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).
-!- BIOTECHNOLOGY: Mature eIF5A-1 may be used as an in situ diagnostic
marker for aberrant proliferation in intraepithelial neoplasia of
the vulva. {ECO:0000269|PubMed:15262146}.
-!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}.
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EMBL; M23419; AAA58453.1; -; mRNA.
EMBL; S72024; AAD14095.1; -; Genomic_DNA.
EMBL; U17969; AAA86989.1; -; Genomic_DNA.
EMBL; AY129319; AAN17514.1; -; mRNA.
EMBL; AY129320; AAN17515.1; -; mRNA.
EMBL; AY129321; AAN17516.1; -; mRNA.
EMBL; AY129322; AAN17518.1; -; mRNA.
EMBL; AK292615; BAF85304.1; -; mRNA.
EMBL; CH471108; EAW90219.1; -; Genomic_DNA.
EMBL; CH471108; EAW90220.1; -; Genomic_DNA.
EMBL; CH471108; EAW90221.1; -; Genomic_DNA.
EMBL; CH471108; EAW90222.1; -; Genomic_DNA.
EMBL; BC000751; AAH00751.1; -; mRNA.
EMBL; BC001832; AAH01832.1; -; mRNA.
EMBL; BC030160; AAH30160.1; -; mRNA.
EMBL; BC080196; AAH80196.1; -; mRNA.
EMBL; BC085015; AAH85015.1; -; mRNA.
EMBL; BC107779; AAI07780.1; -; mRNA.
CCDS; CCDS11099.1; -. [P63241-1]
CCDS; CCDS45601.1; -. [P63241-2]
PIR; B31486; FIHUA.
RefSeq; NP_001137232.1; NM_001143760.1. [P63241-2]
RefSeq; NP_001137233.1; NM_001143761.1. [P63241-1]
RefSeq; NP_001137234.1; NM_001143762.1. [P63241-1]
RefSeq; NP_001961.1; NM_001970.4. [P63241-1]
RefSeq; XP_005256566.1; XM_005256509.2. [P63241-1]
UniGene; Hs.104825; -.
UniGene; Hs.534314; -.
PDB; 1FH4; Model; -; A=1-154.
PDB; 3CPF; X-ray; 2.50 A; A/B=15-151.
PDB; 5DLQ; X-ray; 3.20 A; E/F=15-154.
PDBsum; 1FH4; -.
PDBsum; 3CPF; -.
PDBsum; 5DLQ; -.
ProteinModelPortal; P63241; -.
SMR; P63241; -.
BioGrid; 108299; 61.
IntAct; P63241; 37.
MINT; P63241; -.
STRING; 9606.ENSP00000336702; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P63241; -.
PhosphoSitePlus; P63241; -.
SwissPalm; P63241; -.
BioMuta; EIF5A; -.
DMDM; 54037409; -.
DOSAC-COBS-2DPAGE; P63241; -.
OGP; P63241; -.
EPD; P63241; -.
MaxQB; P63241; -.
PaxDb; P63241; -.
PeptideAtlas; P63241; -.
PRIDE; P63241; -.
ProteomicsDB; 57510; -.
ProteomicsDB; 57511; -. [P63241-2]
TopDownProteomics; P63241-1; -. [P63241-1]
TopDownProteomics; P63241-2; -. [P63241-2]
DNASU; 1984; -.
Ensembl; ENST00000336452; ENSP00000336702; ENSG00000132507. [P63241-2]
Ensembl; ENST00000336458; ENSP00000336776; ENSG00000132507. [P63241-1]
Ensembl; ENST00000416016; ENSP00000396073; ENSG00000132507. [P63241-1]
Ensembl; ENST00000419711; ENSP00000390677; ENSG00000132507. [P63241-1]
Ensembl; ENST00000571955; ENSP00000458269; ENSG00000132507. [P63241-1]
Ensembl; ENST00000573542; ENSP00000459611; ENSG00000132507. [P63241-1]
Ensembl; ENST00000576930; ENSP00000459196; ENSG00000132507. [P63241-1]
GeneID; 1984; -.
KEGG; hsa:1984; -.
UCSC; uc002gfr.3; human. [P63241-1]
CTD; 1984; -.
DisGeNET; 1984; -.
EuPathDB; HostDB:ENSG00000132507.17; -.
GeneCards; EIF5A; -.
HGNC; HGNC:3300; EIF5A.
HPA; CAB005042; -.
HPA; HPA061298; -.
MIM; 600187; gene.
neXtProt; NX_P63241; -.
OpenTargets; ENSG00000132507; -.
PharmGKB; PA27726; -.
eggNOG; KOG3271; Eukaryota.
eggNOG; COG0231; LUCA.
GeneTree; ENSGT00390000003738; -.
HOVERGEN; HBG001104; -.
InParanoid; P63241; -.
KO; K03263; -.
OMA; CVIAIKT; -.
PhylomeDB; P63241; -.
TreeFam; TF101534; -.
Reactome; R-HSA-204626; Hypusine synthesis from eIF5A-lysine.
ChiTaRS; EIF5A; human.
EvolutionaryTrace; P63241; -.
GeneWiki; EIF5A; -.
GenomeRNAi; 1984; -.
PMAP-CutDB; P63241; -.
PRO; PR:P63241; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000132507; -.
CleanEx; HS_EIF5A; -.
ExpressionAtlas; P63241; baseline and differential.
Genevisible; P63241; HS.
GO; GO:0005642; C:annulate lamellae; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0043022; F:ribosome binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003746; F:translation elongation factor activity; ISS:UniProtKB.
GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; IMP:UniProtKB.
GO; GO:0006913; P:nucleocytoplasmic transport; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IGI:UniProtKB.
GO; GO:0045901; P:positive regulation of translational elongation; ISS:UniProtKB.
GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
GO; GO:0006611; P:protein export from nucleus; IMP:UniProtKB.
GO; GO:0006452; P:translational frameshifting; IEA:InterPro.
Gene3D; 2.30.30.30; -; 1.
InterPro; IPR001884; IF5A-like.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR014722; Rib_L2_dom2.
InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
InterPro; IPR020189; Transl_elong_IF5A_C.
InterPro; IPR008991; Translation_prot_SH3-like_sf.
PANTHER; PTHR11673; PTHR11673; 1.
Pfam; PF01287; eIF-5a; 1.
PIRSF; PIRSF003025; eIF5A; 1.
SMART; SM01376; eIF-5a; 1.
SUPFAM; SSF50104; SSF50104; 1.
SUPFAM; SSF50249; SSF50249; 1.
TIGRFAMs; TIGR00037; eIF_5A; 1.
PROSITE; PS00302; IF5A_HYPUSINE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Elongation factor;
Endoplasmic reticulum; Hypusine; Membrane; mRNA transport;
Nuclear pore complex; Nucleus; Protein biosynthesis;
Protein transport; Reference proteome; RNA-binding; Translocation;
Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10229683,
ECO:0000269|Ref.10}.
CHAIN 2 154 Eukaryotic translation initiation factor
5A-1.
/FTId=PRO_0000142451.
REGION 20 90 DOHH-binding.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.10}.
MOD_RES 47 47 N6-acetyllysine.
{ECO:0000269|PubMed:19379712}.
MOD_RES 50 50 Hypusine. {ECO:0000269|PubMed:3095320}.
MOD_RES 121 121 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63242}.
VAR_SEQ 1 2 MA -> MCGTGGTDSKTRRPPHRASFLKRLESKPLKMA
(in isoform 2). {ECO:0000303|Ref.5}.
/FTId=VSP_022020.
MUTAGEN 47 47 K->A,R: Abolishes acetylation.
{ECO:0000269|PubMed:18067580,
ECO:0000269|PubMed:19379712}.
MUTAGEN 47 47 K->D: Causes total inactivation of eIF5A
in supporting yeast growth.
{ECO:0000269|PubMed:18067580,
ECO:0000269|PubMed:19379712}.
MUTAGEN 49 49 G->A: Causes total inactivation of eIF5A
in supporting yeast growth.
{ECO:0000269|PubMed:18067580}.
MUTAGEN 50 50 K->A: Decreases significantly the
acetylation at position K-47 and causes
total inactivation of eIF5A in supporting
yeast growth.
{ECO:0000269|PubMed:17187778,
ECO:0000269|PubMed:18067580,
ECO:0000269|PubMed:19379712}.
MUTAGEN 50 50 K->I,D,R: Causes total inactivation of
eIF5A in supporting yeast growth.
{ECO:0000269|PubMed:17187778,
ECO:0000269|PubMed:18067580,
ECO:0000269|PubMed:19379712}.
MUTAGEN 52 52 G->A: Causes total inactivation of eIF5A
in supporting yeast growth.
{ECO:0000269|PubMed:18067580}.
MUTAGEN 55 55 K->A: Causes total inactivation of eIF5A
in supporting yeast growth.
{ECO:0000269|PubMed:18067580}.
MUTAGEN 81 81 V->G: Leads to temperature sensitivity
when expressed in yeast cells.
{ECO:0000269|PubMed:16987817}.
CONFLICT 36 36 R -> W (in Ref. 3; AAD14095).
{ECO:0000305}.
CONFLICT 45 45 T -> A (in Ref. 3; AAD14095).
{ECO:0000305}.
CONFLICT 85 85 K -> R (in Ref. 3; AAD14095).
{ECO:0000305}.
CONFLICT 109 109 R -> P (in Ref. 3; AAD14095).
{ECO:0000305}.
STRAND 17 21 {ECO:0000244|PDB:3CPF}.
HELIX 22 24 {ECO:0000244|PDB:3CPF}.
STRAND 29 33 {ECO:0000244|PDB:3CPF}.
STRAND 36 46 {ECO:0000244|PDB:3CPF}.
STRAND 55 62 {ECO:0000244|PDB:3CPF}.
TURN 63 65 {ECO:0000244|PDB:3CPF}.
STRAND 68 74 {ECO:0000244|PDB:3CPF}.
STRAND 77 82 {ECO:0000244|PDB:3CPF}.
STRAND 85 95 {ECO:0000244|PDB:3CPF}.
STRAND 98 102 {ECO:0000244|PDB:3CPF}.
HELIX 117 129 {ECO:0000244|PDB:3CPF}.
STRAND 134 140 {ECO:0000244|PDB:3CPF}.
STRAND 143 150 {ECO:0000244|PDB:3CPF}.
SEQUENCE 154 AA; 16832 MW; 07EF043C7DEA3091 CRC64;
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG
IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG
KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK


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