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P63241

- IF5A1_HUMAN

UniProt

P63241 - IF5A1_HUMAN

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
  1. 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

    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.

    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. membrane Source: UniProtKB
    7. nuclear pore Source: UniProtKB
    8. nucleus Source: UniProtKB

    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-acetylalanine2 Publications
    Modified residuei47 – 471N6-acetyllysine2 Publications
    Modified residuei50 – 501Hypusine
    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

    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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 112 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