Reviewed, UniProtKB/Swiss-Prot P63241 (IF5A1_HUMAN)

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
    eIF-4D
    Rev-binding factor

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	The precise role of eIF-5A in protein biosynthesis is not known but it functions by promoting the formation of the first peptide bond.
Subunit structure	Found in a complex with Ran and XPO4. The hypusine modification increases the interaction with XPO4.
Subcellular location	Nucleus.
Tissue specificity	Expressed in umbilical vein endothelial cells and several cancer cell lines (at protein level).
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).
Sequence similarities	Belongs to the eIF-5A family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Initiation factor
PTM	Acetylation Hypusine
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell proliferation Inferred from mutant phenotype. Source: UniProtKB induction of apoptosis Inferred from direct assay. Source: UniProtKB mRNA export from nucleus Inferred from mutant phenotype. Source: UniProtKB peptidyl-lysine modification to hypusine Inferred from Experiment. Source: Reactome positive regulation of translational initiation Inferred from direct assay. Source: UniProtKB protein export from nucleus Inferred from mutant phenotype. Source: UniProtKB viral genome replication Traceable author statement. Source: ProtInc
Cellular component	annulate lamellae Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome 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. Source: UniProtKB translation initiation factor activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
XRN2	Q9H0D6	1	EBI-373150,EBI-372110

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

Chain

2 – 154

153

Eukaryotic translation initiation factor 5A-1

PRO_0000142451

Amino acid modifications

Modified residue

2

1

Blocked amino end (Ala) Probable

Modified residue

50

1

Hypusine

Modified residue

68

1

N6-acetyllysine

Natural variations

Alternative sequence

1 – 2

2

MA → MCGTGGTDSKTRRPPHRASF LKRLESKPLKMA in isoform 2.

VSP_022020

Experimental info

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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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		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, 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]	"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.
[7]	"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.
[8]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 56-67 AND 87-109, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[9]	"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.
[10]	"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.
[11]	"Differential expression of eIF5A-1 and eIF5A-2 in human cancer cells." Clement P.M., Johansson H.E., Wolff E.C., Park M.H. FEBS J. 273:1102-1114(2006) [PubMed: 16519677] [Abstract] Cited for: TISSUE SPECIFICITY.
[12]	"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: Epithelium.
[13]	"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.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
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.

PIR

FIHUA. B31486.

RefSeq

NP_001961.1.

UniGene

Hs.534314

3D structure databases

PDBMSD

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P63241.

PTM databases

PhosphoSite

P63241.

2-D gel databases

Aarhus/Ghent-2DPAGE

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

DOSAC-COBS-2DPAGE

P63241.

OGP

P63241.

PHCI-2DPAGE

P63241.

Genome annotation databases

Ensembl

ENSG00000132507. Homo sapiens. [Contig view]

GeneID

1984.

KEGG

hsa:1984.

Organism-specific databases

H-InvDB

HIX0013493.

HGNC

HGNC:3300. EIF5A.

HPA

CAB005042.

MIM

600187. gene.

PharmGKB

PA27726.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOGENOM

P63241.

HOVERGEN

P63241.

Gene expression databases

ArrayExpress

P63241.

CleanEx

HS_EIF5A.

GermOnline

ENSG00000132507. Homo sapiens.

Family and domain databases

InterPro

IPR001884. EIF5A_hypusine.
IPR012340. NA-bd_OB-fold.
IPR014722. Transl_SH3_like_sub.
[Graphical view]

Gene3D

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

PANTHER

PTHR11673. EIF5A_hypusine. 1 hit.

Pfam

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

PIRSF

PIRSF003025. eIF5A. 1 hit.

TIGRFAMs

TIGR00037. eIF_5A. 1 hit.

PROSITE

PS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P63241.

NextBio

8037.

SOURCE

Search...

Entry information

Entry name

IF5A1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	January 23, 2007
Last modified:	November 4, 2008
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)