P63241 (IF5A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Eukaryotic translation initiation factor 5A-1
Short name=eIF-5A-1
Short name=eIF-5A1

Alternative name(s):
Eukaryotic initiation factor 5A isoform 1
Short name=eIF-5A
Rev-binding factor
eIF-4D

Gene names

Name:

EIF5A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	154 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.18 Ref.19 Ref.21 Ref.23 Ref.25
Subunit structure	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. Ref.2 Ref.9 Ref.18 Ref.24
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. Ref.2 Ref.14 Ref.23 Ref.28
Tissue specificity	Expressed in umbilical vein endothelial cells and several cancer cell lines (at protein level). Ref.20
Post-translational modification	eIF-5A seems to be the only eukaryotic protein to have an hypusine residue which is a post-translational modification of a lysine by the addition of a butylamino group (from spermidine).
Biotechnological use	Mature eIF5A-1 may be used as an in situ diagnostic marker for aberrant proliferation in intraepithelial neoplasia of the vulva. Ref.17
Sequence similarities	Belongs to the eIF-5A family.

Ontologies

Keywords
Biological process	Protein biosynthesis Protein transport Translocation Transport mRNA transport
Cellular component	Cytoplasm Endoplasmic reticulum Membrane Nuclear pore complex Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
Molecular function	Elongation factor
PTM	Acetylation Hypusine Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	induction of apoptosis Inferred from direct assay Ref.18Ref.23. Source: UniProtKB mRNA export from nucleus Inferred from mutant phenotype. Source: UniProtKB peptidyl-lysine modification to hypusine Traceable author statement. Source: Reactome positive regulation of cell proliferation Inferred from genetic interaction. Source: UniProtKB positive regulation of translational elongation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of translational termination Inferred from electronic annotation. Source: InterPro post-translational protein modification Traceable author statement. Source: Reactome protein export from nucleus Inferred from mutant phenotype. Source: UniProtKB translational frameshifting Inferred from electronic annotation. Source: InterPro
Cellular component	annulate lamellae Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear pore Inferred from direct assay. Source: UniProtKB
Molecular function	U6 snRNA binding Inferred from direct assay. Source: UniProtKB protein N-terminus binding Inferred from physical interaction Ref.18. Source: UniProtKB ribosome binding Inferred from electronic annotation. Source: InterPro translation elongation factor activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P63241-1)

Also known as: B; C; D;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P63241-2)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MA → MCGTGGTDSKTRRPPHRASFLKRLESKPLKMA

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9 Ref.10

Chain

2 – 154

153

Eukaryotic translation initiation factor 5A-1

PRO_0000142451

Regions

Region

20 – 90

71

DOHH-binding

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10 Ref.27

Modified residue

46

1

Phosphoserine Ref.27

Modified residue

47

1

N6-acetyllysine Ref.28

Modified residue

50

1

Hypusine

Modified residue

68

1

N6-acetyllysine Ref.22

Natural variations

Alternative sequence

1 – 2

2

MA → MCGTGGTDSKTRRPPHRASF LKRLESKPLKMA in isoform 2.

VSP_022020

Experimental info

Mutagenesis

47

1

K → A or R: Abolishes acetylation. Ref.26 Ref.28

Mutagenesis

47

1

K → D: Causes total inactivation of eIF5A in supporting yeast growth. Ref.26 Ref.28

Mutagenesis

49

1

G → A: Causes total inactivation of eIF5A in supporting yeast growth. Ref.26

Mutagenesis

50

1

K → A: Decreases significantly the acetylation at position K-47 and causes total inactivation of eIF5A in supporting yeast growth. Ref.23 Ref.26 Ref.28

Mutagenesis

50

1

K → I, D or R: Causes total inactivation of eIF5A in supporting yeast growth. Ref.23 Ref.26 Ref.28

Mutagenesis

52

1

G → A: Causes total inactivation of eIF5A in supporting yeast growth. Ref.26

Mutagenesis

55

1

K → A: Causes total inactivation of eIF5A in supporting yeast growth. Ref.26

Mutagenesis

81

1

V → G: Leads to temperature sensitivity when expressed in yeast cells. Ref.21

Sequence conflict

36

1

R → W in AAD14095. Ref.3

Sequence conflict

45

1

T → A in AAD14095. Ref.3

Sequence conflict

85

1

K → R in AAD14095. Ref.3

Sequence conflict

109

1

R → P in AAD14095. Ref.3

Secondary structure

1

.

.

.

.

.

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.

.

.

.

.

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.

.

.

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.

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154

Helix Strand Turn

Details...

Beta strand

17 – 21

5

Helix

22 – 24

3

Beta strand

29 – 33

5

Beta strand

36 – 46

11

Beta strand

55 – 62

8

Turn

63 – 65

3

Beta strand

68 – 74

7

Beta strand

77 – 82

6

Beta strand

85 – 95

11

Beta strand

98 – 102

5

Helix

117 – 129

13

Beta strand

134 – 140

7

Beta strand

143 – 150

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (B) (C) (D) [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 07EF043C7DEA3091	FASTA	154	16,832
	10 20 30 40 50 60 MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG 70 80 90 100 110 120 IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG 130 140 150 KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK
	Isoform 2 (A) [UniParc]. Checksum: 9E2A400E66540B74	FASTA	184	20,170
	10 20 30 40 50 60 MCGTGGTDSK TRRPPHRASF LKRLESKPLK MADDLDFETG DAGASATFPM QCSALRKNGF 70 80 90 100 110 120 VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ 130 140 150 160 170 180 LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence determination and cDNA cloning of eukaryotic initiation factor 4D, the hypusine-containing protein." Smit-Mcbride Z., Dever T.E., Hershey J.W.B., Merrick W.C. J. Biol. Chem. 264:1578-1583(1989) [PubMed: 2492279] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Eukaryotic initiation factor 5A is a cellular target of the human immunodeficiency virus type 1 Rev activation domain mediating trans-activation." Ruhl M., Himmelspach M., Bahr G.M., Hammerschmid F., Jaksche H., Wolff B., Aschauer H., Farrington G.K., Probst H., Bevec D., Hauber J. J. Cell Biol. 123:1309-1320(1993) [PubMed: 8253832] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-154, INTERACTION WITH HIV-1 REV, SUBCELLULAR LOCATION.
[3]	"The genomic structure encoding human initiation factor eIF-5A." Koettnitz K., Kappel B., Baumruker T., Hauber J., Bevec D. Gene 144:249-252(1994) [PubMed: 7545941] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[4]	"Identification of a new member of the human eIF-5A gene family." Koettnitz K., Woehl T., Kappel B., Lottspeich F., Hauber J., Bevec D. Gene 159:283-284(1995) [PubMed: 7622067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
[5]	"Differential expression of eIF5AI-mRNAs." Johansson H.E., Jenkins Z.A. Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Thymus.
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Muscle, Prostate and Uterus.
[9]	"Complex formation between deoxyhypusine synthase and its protein substrate, the eukaryotic translation initiation factor 5A (eIF5A) precursor." Lee Y.B., Joe Y.A., Wolff E.C., Dimitriadis E.K., Park M.H. Biochem. J. 340:273-281(1999) [PubMed: 10229683] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-6, INTERACTION WITH DHPS.
[10]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-26; 56-67; 69-85 AND 110-121, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Eukaryotic initiation factor 4D. Purification from human red blood cells and the sequence of amino acids around its single hypusine residue." Park M.H., Liu T.-Y., Neece S.H., Swiggard W.J. J. Biol. Chem. 261:14515-14519(1986) [PubMed: 3095320] [Abstract] Cited for: PROTEIN SEQUENCE OF 48-55, HYPUSINE AT LYS-50.
[12]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 56-121, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[13]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 68-84 AND 114-121.
[14]	"The subcellular distribution of eukaryotic translation initiation factor, eIF-5A, in cultured cells." Shi X.-P., Yin K.-C., Zimolo Z.A., Stern A.M., Waxman L. Exp. Cell Res. 225:348-356(1996) [PubMed: 8660923] [Abstract] Cited for: SUBCELLULAR LOCATION.
[15]	"Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes." Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S., Hartmann E., Kutay U., Goerlich D. EMBO J. 19:4362-4371(2000) [PubMed: 10944119] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH RAN AND XPO4.
[16]	"Identification of mRNA that binds to eukaryotic initiation factor 5A by affinity co-purification and differential display." Xu A., Jao D.L., Chen K.Y. Biochem. J. 384:585-590(2004) [PubMed: 15303967] [Abstract] Cited for: MRNA-BINDING.
[17]	"Eukaryotic initiation factor 5A-1 (eIF5A-1) as a diagnostic marker for aberrant proliferation in intraepithelial neoplasia of the vulva." Cracchiolo B.M., Heller D.S., Clement P.M.J., Wolff E.C., Park M.H., Hanauske-Abel H.M. Gynecol. Oncol. 94:217-222(2004) [PubMed: 15262146] [Abstract] Cited for: BIOTECHNOLOGY.
[18]	"A novel eIF5A complex functions as a regulator of p53 and p53-dependent apoptosis." 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. J. Biol. Chem. 279:49251-49258(2004) [PubMed: 15371445] [Abstract] Cited for: FUNCTION, INTERACTION WITH SDCBP.
[19]	"Role of eIF5A in TNF-alpha-mediated apoptosis of lamina cribrosa cells." Taylor C.A., Senchyna M., Flanagan J., Joyce E.M., Cliche D.O., Boone A.N., Culp-Stewart S., Thompson J.E. Invest. Ophthalmol. Vis. Sci. 45:3568-3576(2004) [PubMed: 15452064] [Abstract] Cited for: FUNCTION.
[20]	"Differential expression of eIF5A-1 and eIF5A-2 in human cancer cells." Clement P.M.J., Johansson H.E., Wolff E.C., Park M.H. FEBS J. 273:1102-1114(2006) [PubMed: 16519677] [Abstract] Cited for: TISSUE SPECIFICITY.
[21]	"Temperature-sensitive eIF5A mutant accumulates transcripts targeted to the nonsense-mediated decay pathway." Schrader R., Young C., Kozian D., Hoffmann R., Lottspeich F. J. Biol. Chem. 281:35336-35346(2006) [PubMed: 16987817] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF VAL-81.
[22]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Eukaryotic translation initiation factor 5A induces apoptosis in colon cancer cells and associates with the nucleus in response to tumour necrosis factor alpha signalling." Taylor C.A., Sun Z., Cliche D.O., Ming H., Eshaque B., Jin S., Hopkins M.T., Thai B., Thompson J.E. Exp. Cell Res. 313:437-449(2007) [PubMed: 17187778] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-50.
[24]	"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." Kang K.R., Kim Y.S., Wolff E.C., Park M.H. J. Biol. Chem. 282:8300-8308(2007) [PubMed: 17213197] [Abstract] Cited for: INTERACTION WITH DOHH.
[25]	"Neuronal growth and survival mediated by eIF5A, a polyamine-modified translation initiation factor." Huang Y., Higginson D.S., Hester L., Park M.H., Snyder S.H. Proc. Natl. Acad. Sci. U.S.A. 104:4194-4199(2007) [PubMed: 17360499] [Abstract] Cited for: FUNCTION.
[26]	"Mutational analyses of human eIF5A-1: identification of amino acid residues critical for eIF5A activity and hypusine modification." 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. FEBS J. 275:44-58(2008) [PubMed: 18067580] [Abstract] Cited for: MUTAGENESIS OF LYS-47; GLY-49; LYS-50; GLY-52 AND LYS-55.
[27]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[28]	"The effect of hypusine modification on the intracellular localization of eIF5A." Lee S.B., Park J.-H., Kaevel J., Sramkova M., Weigert R., Park M.H. Biochem. Biophys. Res. Commun. 383:497-502(2009) [PubMed: 19379712] [Abstract] Cited for: ACETYLATION AT LYS-47, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-47 AND LYS-50.
[29]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]	"Homology modelling of the human eukaryotic initiation factor 5A (eIF-5A)." Facchiano A.M., Stiuso P., Chiusano M.L., Caraglia M., Giuberti G., Marra M., Abbruzzese A., Colonna G. Protein Eng. 14:881-890(2001) [PubMed: 11742107] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M23419 mRNA. Translation: AAA58453.1.
S72024 Genomic DNA. Translation: AAD14095.1.
U17969 Genomic DNA. Translation: AAA86989.1.
AY129319 mRNA. Translation: AAN17514.1.
AY129320 mRNA. Translation: AAN17515.1.
AY129321 mRNA. Translation: AAN17516.1.
AY129322 mRNA. Translation: AAN17518.1.
AK292615 mRNA. Translation: BAF85304.1.
CH471108 Genomic DNA. Translation: EAW90219.1.
CH471108 Genomic DNA. Translation: EAW90220.1.
CH471108 Genomic DNA. Translation: EAW90221.1.
CH471108 Genomic DNA. Translation: EAW90222.1.
BC000751 mRNA. Translation: AAH00751.1.
BC001832 mRNA. Translation: AAH01832.1.
BC030160 mRNA. Translation: AAH30160.1.
BC080196 mRNA. Translation: AAH80196.1.
BC085015 mRNA. Translation: AAH85015.1.
BC107779 mRNA. Translation: AAI07780.1.

IPI

IPI00376005.
IPI00411704.

PIR

FIHUA. B31486.

RefSeq

NP_001137232.1. NM_001143760.1.
NP_001137233.1. NM_001143761.1.
NP_001137234.1. NM_001143762.1.
NP_001961.1. NM_001970.4.

UniGene

Hs.534314.
Hs.729454.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FH4	model	-	A	1-154	[»]
3CPF	X-ray	2.50	A/B	15-151	[»]

ProteinModelPortal

P63241.

SMR

P63241. Positions 15-150.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63241. 8 interactions.

STRING

P63241.

PTM databases

PhosphoSite

P63241.

Polymorphism databases

DMDM

54037409.

2D gel databases

Aarhus/Ghent-2DPAGE

8009. IEF.
8010. IEF.
8016. IEF.

DOSAC-COBS-2DPAGE

P63241.

OGP

P63241.

PHCI-2DPAGE

P63241.

Proteomic databases

PRIDE

P63241.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000336452; ENSP00000336702; ENSG00000132507.
ENST00000336458; ENSP00000336776; ENSG00000132507.
ENST00000416016; ENSP00000396073; ENSG00000132507.
ENST00000419711; ENSP00000390677; ENSG00000132507.

GeneID

1984.

KEGG

hsa:1984.

UCSC

uc002gfs.1. human.

Organism-specific databases

CTD

1984.

GeneCards

GC17P007210.

H-InvDB

HIX0013493.
HIX0035654.

HGNC

HGNC:3300. EIF5A.

HPA

CAB005042.

MIM

600187. gene.

neXtProt

NX_P63241.

PharmGKB

PA27726.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06490.

HOGENOM

HBG526951.

HOVERGEN

HBG001104.

InParanoid

P63241.

OMA

NGDLRED.

OrthoDB

EOG41JZDF.

PhylomeDB

P63241.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpress

P63241.

Bgee

P63241.

CleanEx

HS_EIF5A.

Genevestigator

P63241.

GermOnline

ENSG00000132507. Homo sapiens.

Family and domain databases

InterPro

IPR005824. KOW.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR019769. Trans_elong_IF5A_hypusine_site.
IPR001884. Transl_elong_IF5A.
IPR020189. Transl_elong_IF5A_C.
IPR014722. Transl_SH3-like_sub.
IPR008991. Translation_prot_SH3-like.
[Graphical view]

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:2.30.30.30. Ribosomal_L2. 1 hit.

KO

K03263.

PANTHER

PTHR11673. EIF5A_hypusine. 1 hit.

Pfam

PF01287. eIF-5a. 1 hit.
PF00467. KOW. 1 hit.
[Graphical view]

PIRSF

PIRSF003025. eIF5A. 1 hit.

SUPFAM

SSF50249. Nucleic_acid_OB. 1 hit.
SSF50104. Transl_SH3_like. 1 hit.

TIGRFAMs

TIGR00037. EIF_5A. 1 hit.

PROSITE

PS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

8037.

PMAP-CutDB

P63241.

SOURCE

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Entry information

Entry name

IF5A1_HUMAN

Accession

Primary (citable) accession number: P63241
Secondary accession number(s): A8K9A0 , D3DTP2, P10159, Q16182, Q7L7L3, Q7Z4L1, Q9D0G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.