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P63241 (IF5A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.22 Ref.24

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.15 Ref.18 Ref.23

Subcellular location

Cytoplasm. Nucleus. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Nucleusnuclear 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.22 Ref.26

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 a 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 processmRNA transport
Protein biosynthesis
Protein transport
Translocation
Transport
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Nuclear pore complex
Nucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   Molecular functionElongation factor
   PTMAcetylation
Hypusine
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from direct assay Ref.18Ref.22. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

mRNA export from nucleus

Inferred from mutant phenotype PubMed 9465063. Source: UniProtKB

nucleocytoplasmic transport

Inferred from mutant phenotype PubMed 10381392. Source: UniProtKB

peptidyl-lysine modification to hypusine

Traceable author statement. Source: Reactome

positive regulation of cell proliferation

Inferred from genetic interaction PubMed 14622290. 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 PubMed 8596953. Source: UniProtKB

translational frameshifting

Inferred from electronic annotation. Source: InterPro

   Cellular_componentannulate lamellae

Inferred from direct assay PubMed 12210765. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 12210765Ref.22. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear pore

Inferred from direct assay PubMed 10381392. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 12210765Ref.22. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from direct assay Ref.16. Source: UniProtKB

U6 snRNA binding

Inferred from direct assay PubMed 9285100. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9 Ref.10
Chain2 – 154153Eukaryotic translation initiation factor 5A-1
PRO_0000142451

Regions

Region20 – 9071DOHH-binding

Amino acid modifications

Modified residue21N-acetylalanine Ref.10
Modified residue471N6-acetyllysine Ref.26
Modified residue501Hypusine
Modified residue1211N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 22MA → MCGTGGTDSKTRRPPHRASF LKRLESKPLKMA in isoform 2.
VSP_022020

Experimental info

Mutagenesis471K → A or R: Abolishes acetylation. Ref.25 Ref.26
Mutagenesis471K → D: Causes total inactivation of eIF5A in supporting yeast growth. Ref.25 Ref.26
Mutagenesis491G → A: Causes total inactivation of eIF5A in supporting yeast growth. Ref.25
Mutagenesis501K → A: Decreases significantly the acetylation at position K-47 and causes total inactivation of eIF5A in supporting yeast growth. Ref.22 Ref.25 Ref.26
Mutagenesis501K → I, D or R: Causes total inactivation of eIF5A in supporting yeast growth. Ref.22 Ref.25 Ref.26
Mutagenesis521G → A: Causes total inactivation of eIF5A in supporting yeast growth. Ref.25
Mutagenesis551K → A: Causes total inactivation of eIF5A in supporting yeast growth. Ref.25
Mutagenesis811V → G: Leads to temperature sensitivity when expressed in yeast cells. Ref.21
Sequence conflict361R → W in AAD14095. Ref.3
Sequence conflict451T → A in AAD14095. Ref.3
Sequence conflict851K → R in AAD14095. Ref.3
Sequence conflict1091R → P in AAD14095. Ref.3

Secondary structure

......................... 154
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (B) (C) (D) [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 07EF043C7DEA3091

FASTA15416,832
        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 

« Hide

Isoform 2 (A) [UniParc].

Checksum: 9E2A400E66540B74
Show »

FASTA18420,170

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF VAL-81.
[22]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF LYS-50.
[23]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOHH.
[24]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-47; GLY-49; LYS-50; GLY-52 AND LYS-55.
[26]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-47, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-47 AND LYS-50.
[27]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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] [Europe PMC] [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.
PIRFIHUA. B31486.
RefSeqNP_001137232.1. NM_001143760.1.
NP_001137233.1. NM_001143761.1.
NP_001137234.1. NM_001143762.1.
NP_001961.1. NM_001970.4.
XP_005256566.1. XM_005256509.1.
UniGeneHs.104825.
Hs.534314.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FH4model-A1-154[»]
3CPFX-ray2.50A/B15-151[»]
ProteinModelPortalP63241.
SMRP63241. Positions 15-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108299. 32 interactions.
IntActP63241. 11 interactions.
MINTMINT-1829069.
STRING9606.ENSP00000336702.

PTM databases

PhosphoSiteP63241.

Polymorphism databases

DMDM54037409.

2D gel databases

DOSAC-COBS-2DPAGEP63241.
OGPP63241.

Proteomic databases

PaxDbP63241.
PRIDEP63241.

Protocols and materials databases

DNASU1984.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336452; ENSP00000336702; ENSG00000132507. [P63241-2]
ENST00000336458; ENSP00000336776; ENSG00000132507. [P63241-1]
ENST00000416016; ENSP00000396073; ENSG00000132507. [P63241-1]
ENST00000419711; ENSP00000390677; ENSG00000132507. [P63241-1]
ENST00000571955; ENSP00000458269; ENSG00000132507. [P63241-1]
ENST00000573542; ENSP00000459611; ENSG00000132507. [P63241-1]
ENST00000576930; ENSP00000459196; ENSG00000132507. [P63241-1]
GeneID1984.
KEGGhsa:1984.
UCSCuc002gfr.3. human. [P63241-2]
uc002gft.3. human. [P63241-1]

Organism-specific databases

CTD1984.
GeneCardsGC17P007210.
HGNCHGNC:3300. EIF5A.
HPACAB005042.
MIM600187. gene.
neXtProtNX_P63241.
PharmGKBPA27726.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0231.
HOVERGENHBG001104.
InParanoidP63241.
KOK03263.
OMAIPDGDLG.
OrthoDBEOG7KSXB7.
PhylomeDBP63241.
TreeFamTF101534.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP63241.
BgeeP63241.
CleanExHS_EIF5A.
GenevestigatorP63241.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
InterProIPR012340. NA-bd_OB-fold.
IPR014722. Rib_L2_dom2.
IPR019769. Trans_elong_IF5A_hypusine_site.
IPR001884. Transl_elong_IF5A.
IPR020189. Transl_elong_IF5A_C.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERPTHR11673. PTHR11673. 1 hit.
PfamPF01287. eIF-5a. 1 hit.
[Graphical view]
PIRSFPIRSF003025. eIF5A. 1 hit.
SUPFAMSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsTIGR00037. eIF_5A. 1 hit.
PROSITEPS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF5A. human.
EvolutionaryTraceP63241.
GeneWikiEIF5A.
GenomeRNAi1984.
NextBio8037.
PMAP-CutDBP63241.
PROP63241.
SOURCESearch...

Entry information

Entry nameIF5A1_HUMAN
AccessionPrimary (citable) accession number: P63241
Secondary accession number(s): A8K9A0 expand/collapse secondary AC list , D3DTP2, P10159, Q16182, Q7L7L3, Q7Z4L1, Q9D0G2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM