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Protein

Eukaryotic translation initiation factor 5A-1

Gene

EIF5A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • ribosome binding Source: InterPro
  • RNA binding Source: UniProtKB
  • translation elongation factor activity Source: UniProtKB
  • U6 snRNA binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB
  • cellular protein metabolic process Source: Reactome
  • mRNA export from nucleus Source: UniProtKB
  • nucleocytoplasmic transport Source: UniProtKB
  • peptidyl-lysine modification to peptidyl-hypusine Source: Reactome
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of translational elongation Source: UniProtKB
  • positive regulation of translational termination Source: InterPro
  • post-translational protein modification Source: Reactome
  • protein export from nucleus Source: UniProtKB
  • translational frameshifting Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

mRNA transport, Protein biosynthesis, Protein transport, Translocation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_12469. Hypusine synthesis from eIF5A-lysine.

Names & Taxonomyi

Protein namesi
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 namesi
Name:EIF5A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3300. EIF5A.

Subcellular locationi

GO - Cellular componenti

  • annulate lamellae Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear pore Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nuclear pore complex, Nucleus

Pathology & Biotechi

Biotechnological usei

Mature eIF5A-1 may be used as an in situ diagnostic marker for aberrant proliferation in intraepithelial neoplasia of the vulva.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi47 – 471K → A or R: Abolishes acetylation. 2 Publications
Mutagenesisi47 – 471K → D: Causes total inactivation of eIF5A in supporting yeast growth. 2 Publications
Mutagenesisi49 – 491G → A: Causes total inactivation of eIF5A in supporting yeast growth. 1 Publication
Mutagenesisi50 – 501K → A: Decreases significantly the acetylation at position K-47 and causes total inactivation of eIF5A in supporting yeast growth. 3 Publications
Mutagenesisi50 – 501K → I, D or R: Causes total inactivation of eIF5A in supporting yeast growth. 3 Publications
Mutagenesisi52 – 521G → A: Causes total inactivation of eIF5A in supporting yeast growth. 1 Publication
Mutagenesisi55 – 551K → A: Causes total inactivation of eIF5A in supporting yeast growth. 1 Publication
Mutagenesisi81 – 811V → G: Leads to temperature sensitivity when expressed in yeast cells. 1 Publication

Organism-specific databases

PharmGKBiPA27726.

Polymorphism and mutation databases

BioMutaiEIF5A.
DMDMi54037409.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 154153Eukaryotic translation initiation factor 5A-1PRO_0000142451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei47 – 471N6-acetyllysine1 Publication
Modified residuei50 – 501Hypusine1 Publication
Modified residuei121 – 1211N6-acetyllysineBy similarity

Post-translational modificationi

Acetylated. Deacetylated by SIRT2.3 Publications
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).

Keywords - PTMi

Acetylation, Hypusine

Proteomic databases

MaxQBiP63241.
PaxDbiP63241.
PRIDEiP63241.

2D gel databases

DOSAC-COBS-2DPAGEP63241.
OGPiP63241.

PTM databases

PhosphoSiteiP63241.

Miscellaneous databases

PMAP-CutDBP63241.

Expressioni

Tissue specificityi

Expressed in umbilical vein endothelial cells and several cancer cell lines (at protein level).1 Publication

Gene expression databases

BgeeiP63241.
CleanExiHS_EIF5A.
ExpressionAtlasiP63241. baseline and differential.
GenevisibleiP63241. HS.

Organism-specific databases

HPAiCAB005042.
HPA061298.

Interactioni

Subunit structurei

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 XPO4.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRXO431863EBI-373150,EBI-748171
DHPSP493663EBI-373150,EBI-741925
MEOX2A4D1273EBI-373150,EBI-10172134
RELQ048643EBI-373150,EBI-307352

Protein-protein interaction databases

BioGridi108299. 40 interactions.
IntActiP63241. 16 interactions.
MINTiMINT-1829069.
STRINGi9606.ENSP00000336702.

Structurei

Secondary structure

1
154
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 215Combined sources
Helixi22 – 243Combined sources
Beta strandi29 – 335Combined sources
Beta strandi36 – 4611Combined sources
Beta strandi55 – 628Combined sources
Turni63 – 653Combined sources
Beta strandi68 – 747Combined sources
Beta strandi77 – 826Combined sources
Beta strandi85 – 9511Combined sources
Beta strandi98 – 1025Combined sources
Helixi117 – 12913Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi143 – 1508Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FH4model-A1-154[»]
3CPFX-ray2.50A/B15-151[»]
ProteinModelPortaliP63241.
SMRiP63241. Positions 15-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63241.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 9071DOHH-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-5A family.Curated

Phylogenomic databases

eggNOGiCOG0231.
GeneTreeiENSGT00390000003738.
HOVERGENiHBG001104.
InParanoidiP63241.
KOiK03263.
OMAiGHAKANI.
OrthoDBiEOG7KSXB7.
PhylomeDBiP63241.
TreeFamiTF101534.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR012340. 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]
PANTHERiPTHR11673. PTHR11673. 1 hit.
PfamiPF01287. eIF-5a. 1 hit.
[Graphical view]
PIRSFiPIRSF003025. eIF5A. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00037. eIF_5A. 1 hit.
PROSITEiPS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P63241-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK
60 70 80 90 100
HGHAKVHLVG IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS
110 120 130 140 150
LLQDSGEVRE DLRLPEGDLG KEIEQKYDCG EEILITVLSA MTEEAAVAIK

AMAK
Length:154
Mass (Da):16,832
Last modified:January 23, 2007 - v2
Checksum:i07EF043C7DEA3091
GO
Isoform 2 (identifier: P63241-2) [UniParc]FASTAAdd to basket

Also known as: A

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

Show »
Length:184
Mass (Da):20,170
Checksum:i9E2A400E66540B74
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361R → W in AAD14095 (PubMed:7545941).Curated
Sequence conflicti45 – 451T → A in AAD14095 (PubMed:7545941).Curated
Sequence conflicti85 – 851K → R in AAD14095 (PubMed:7545941).Curated
Sequence conflicti109 – 1091R → P in AAD14095 (PubMed:7545941).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22MA → MCGTGGTDSKTRRPPHRASF LKRLESKPLKMA in isoform 2. 1 PublicationVSP_022020

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11099.1. [P63241-1]
CCDS45601.1. [P63241-2]
PIRiB31486. FIHUA.
RefSeqiNP_001137232.1. NM_001143760.1. [P63241-2]
NP_001137233.1. NM_001143761.1. [P63241-1]
NP_001137234.1. NM_001143762.1. [P63241-1]
NP_001961.1. NM_001970.4. [P63241-1]
XP_005256566.1. XM_005256509.1. [P63241-1]
UniGeneiHs.104825.
Hs.534314.

Genome annotation databases

EnsembliENST00000336452; 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]
GeneIDi1984.
KEGGihsa:1984.
UCSCiuc002gfr.3. human. [P63241-2]
uc002gft.3. human. [P63241-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11099.1. [P63241-1]
CCDS45601.1. [P63241-2]
PIRiB31486. FIHUA.
RefSeqiNP_001137232.1. NM_001143760.1. [P63241-2]
NP_001137233.1. NM_001143761.1. [P63241-1]
NP_001137234.1. NM_001143762.1. [P63241-1]
NP_001961.1. NM_001970.4. [P63241-1]
XP_005256566.1. XM_005256509.1. [P63241-1]
UniGeneiHs.104825.
Hs.534314.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FH4model-A1-154[»]
3CPFX-ray2.50A/B15-151[»]
ProteinModelPortaliP63241.
SMRiP63241. Positions 15-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108299. 40 interactions.
IntActiP63241. 16 interactions.
MINTiMINT-1829069.
STRINGi9606.ENSP00000336702.

PTM databases

PhosphoSiteiP63241.

Polymorphism and mutation databases

BioMutaiEIF5A.
DMDMi54037409.

2D gel databases

DOSAC-COBS-2DPAGEP63241.
OGPiP63241.

Proteomic databases

MaxQBiP63241.
PaxDbiP63241.
PRIDEiP63241.

Protocols and materials databases

DNASUi1984.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336452; 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]
GeneIDi1984.
KEGGihsa:1984.
UCSCiuc002gfr.3. human. [P63241-2]
uc002gft.3. human. [P63241-1]

Organism-specific databases

CTDi1984.
GeneCardsiGC17P007210.
HGNCiHGNC:3300. EIF5A.
HPAiCAB005042.
HPA061298.
MIMi600187. gene.
neXtProtiNX_P63241.
PharmGKBiPA27726.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0231.
GeneTreeiENSGT00390000003738.
HOVERGENiHBG001104.
InParanoidiP63241.
KOiK03263.
OMAiGHAKANI.
OrthoDBiEOG7KSXB7.
PhylomeDBiP63241.
TreeFamiTF101534.

Enzyme and pathway databases

ReactomeiREACT_12469. Hypusine synthesis from eIF5A-lysine.

Miscellaneous databases

ChiTaRSiEIF5A. human.
EvolutionaryTraceiP63241.
GeneWikiiEIF5A.
GenomeRNAii1984.
NextBioi8037.
PMAP-CutDBP63241.
PROiP63241.
SOURCEiSearch...

Gene expression databases

BgeeiP63241.
CleanExiHS_EIF5A.
ExpressionAtlasiP63241. baseline and differential.
GenevisibleiP63241. HS.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR012340. 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]
PANTHERiPTHR11673. PTHR11673. 1 hit.
PfamiPF01287. eIF-5a. 1 hit.
[Graphical view]
PIRSFiPIRSF003025. eIF5A. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00037. eIF_5A. 1 hit.
PROSITEiPS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Acetylation regulates subcellular localization of eukaryotic translation initiation factor 5A (eIF5A)."
    Ishfaq M., Maeta K., Maeda S., Natsume T., Ito A., Yoshida M.
    FEBS Lett. 586:3236-3241(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, DEACETYLATION BY SIRT2.
  29. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiIF5A1_HUMAN
AccessioniPrimary (citable) accession number: P63241
Secondary accession number(s): A8K9A0
, D3DTP2, P10159, Q16182, Q7L7L3, Q7Z4L1, Q9D0G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Translation initiation factors
    List of translation initiation factor entries
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.