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P63241

- IF5A1_HUMAN

UniProt

P63241 - IF5A1_HUMAN

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Protein

Eukaryotic translation initiation factor 5A-1

Gene
EIF5A
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. protein N-terminus binding Source: UniProtKB
  4. ribosome binding Source: InterPro
  5. RNA binding Source: UniProtKB
  6. translation elongation factor activity Source: UniProtKB
  7. U6 snRNA binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. cellular protein metabolic process Source: Reactome
  3. mRNA export from nucleus Source: UniProtKB
  4. nucleocytoplasmic transport Source: UniProtKB
  5. peptidyl-lysine modification to peptidyl-hypusine Source: Reactome
  6. positive regulation of cell proliferation Source: UniProtKB
  7. positive regulation of translational elongation Source: UniProtKB
  8. positive regulation of translational termination Source: InterPro
  9. post-translational protein modification Source: Reactome
  10. protein export from nucleus Source: UniProtKB
  11. 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: Chromosome 17

Organism-specific databases

HGNCiHGNC:3300. EIF5A.

Subcellular locationi

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.4 Publications

GO - Cellular componenti

  1. annulate lamellae Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. extracellular vesicular exosome Source: UniProt
  6. nuclear pore Source: UniProtKB
  7. 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.

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 – 501Hypusine
Modified residuei121 – 1211N6-acetyllysine By similarity

Post-translational modificationi

Acetylated. Deacetylated by SIRT2.
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

ArrayExpressiP63241.
BgeeiP63241.
CleanExiHS_EIF5A.
GenevestigatoriP63241.

Organism-specific databases

HPAiCAB005042.

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

Protein-protein interaction databases

BioGridi108299. 34 interactions.
IntActiP63241. 11 interactions.
MINTiMINT-1829069.
STRINGi9606.ENSP00000336702.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP63241.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the eIF-5A family.

Phylogenomic databases

eggNOGiCOG0231.
HOVERGENiHBG001104.
InParanoidiP63241.
KOiK03263.
OMAiNDNGDLR.
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. Align

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

MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK    50
HGHAKVHLVG IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS 100
LLQDSGEVRE DLRLPEGDLG KEIEQKYDCG EEILITVLSA MTEEAAVAIK 150
AMAK 154
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22MA → MCGTGGTDSKTRRPPHRASF LKRLESKPLKMA in isoform 2. VSP_022020

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361R → W in AAD14095. 1 Publication
Sequence conflicti45 – 451T → A in AAD14095. 1 Publication
Sequence conflicti85 – 851K → R in AAD14095. 1 Publication
Sequence conflicti109 – 1091R → P in AAD14095. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi54037409.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11099.1. [P63241-1 ]
CCDS45601.1. [P63241-2 ]
PIRi B31486. FIHUA.
RefSeqi NP_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 ]
UniGenei Hs.104825.
Hs.534314.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FH4 model - A 1-154 [» ]
3CPF X-ray 2.50 A/B 15-151 [» ]
ProteinModelPortali P63241.
SMRi P63241. Positions 15-150.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108299. 34 interactions.
IntActi P63241. 11 interactions.
MINTi MINT-1829069.
STRINGi 9606.ENSP00000336702.

PTM databases

PhosphoSitei P63241.

Polymorphism databases

DMDMi 54037409.

2D gel databases

DOSAC-COBS-2DPAGE P63241.
OGPi P63241.

Proteomic databases

MaxQBi P63241.
PaxDbi P63241.
PRIDEi P63241.

Protocols and materials databases

DNASUi 1984.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000336452 ; 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 ]
GeneIDi 1984.
KEGGi hsa:1984.
UCSCi uc002gfr.3. human. [P63241-2 ]
uc002gft.3. human. [P63241-1 ]

Organism-specific databases

CTDi 1984.
GeneCardsi GC17P007210.
HGNCi HGNC:3300. EIF5A.
HPAi CAB005042.
MIMi 600187. gene.
neXtProti NX_P63241.
PharmGKBi PA27726.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0231.
HOVERGENi HBG001104.
InParanoidi P63241.
KOi K03263.
OMAi NDNGDLR.
OrthoDBi EOG7KSXB7.
PhylomeDBi P63241.
TreeFami TF101534.

Enzyme and pathway databases

Reactomei REACT_12469. Hypusine synthesis from eIF5A-lysine.

Miscellaneous databases

ChiTaRSi EIF5A. human.
EvolutionaryTracei P63241.
GeneWikii EIF5A.
GenomeRNAii 1984.
NextBioi 8037.
PMAP-CutDB P63241.
PROi P63241.
SOURCEi Search...

Gene expression databases

ArrayExpressi P63241.
Bgeei P63241.
CleanExi HS_EIF5A.
Genevestigatori P63241.

Family and domain databases

Gene3Di 2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
InterProi IPR012340. 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 ]
PANTHERi PTHR11673. PTHR11673. 1 hit.
Pfami PF01287. eIF-5a. 1 hit.
[Graphical view ]
PIRSFi PIRSF003025. eIF5A. 1 hit.
SUPFAMi SSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00037. eIF_5A. 1 hit.
PROSITEi PS00302. IF5A_HYPUSINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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: September 3, 2014
This is version 111 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

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