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Q9GZV4

- IF5A2_HUMAN

UniProt

Q9GZV4 - IF5A2_HUMAN

Protein

Eukaryotic translation initiation factor 5A-2

Gene

EIF5A2

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. Functions as a regulator of 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 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. ribosome binding Source: InterPro
    3. translation elongation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. mRNA transport Source: UniProtKB-KW
    3. peptidyl-lysine modification to peptidyl-hypusine Source: Reactome
    4. polyamine homeostasis Source: UniProtKB
    5. positive regulation of cell proliferation Source: UniProtKB
    6. positive regulation of translational elongation Source: InterPro
    7. positive regulation of translational termination Source: InterPro
    8. post-translational protein modification Source: Reactome
    9. protein transport Source: UniProtKB-KW
    10. spermatogenesis 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-2
    Short name:
    eIF-5A-2
    Short name:
    eIF-5A2
    Alternative name(s):
    Eukaryotic initiation factor 5A isoform 2
    Gene namesi
    Name:EIF5A2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3301. EIF5A2.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Nucleusnuclear pore complex By similarity
    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.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. nuclear pore Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27727.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 153152Eukaryotic translation initiation factor 5A-2PRO_0000229764Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei50 – 501Hypusine

    Post-translational modificationi

    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

    MaxQBiQ9GZV4.
    PaxDbiQ9GZV4.
    PRIDEiQ9GZV4.

    PTM databases

    PhosphoSiteiQ9GZV4.

    Expressioni

    Tissue specificityi

    Expressed in ovarian and colorectal cancer cell lines (at protein level). Highly expressed in testis. Overexpressed in some cancer cells.2 Publications

    Gene expression databases

    ArrayExpressiQ9GZV4.
    BgeeiQ9GZV4.
    CleanExiHS_EIF5A2.
    GenevestigatoriQ9GZV4.

    Organism-specific databases

    HPAiHPA029090.

    Interactioni

    Protein-protein interaction databases

    BioGridi121162. 11 interactions.
    IntActiQ9GZV4. 8 interactions.
    MINTiMINT-1453868.
    STRINGi9606.ENSP00000295822.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9GZV4.
    SMRiQ9GZV4. Positions 15-150.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the eIF-5A family.Curated

    Phylogenomic databases

    eggNOGiCOG0231.
    HOGENOMiHOG000106270.
    HOVERGENiHBG001104.
    InParanoidiQ9GZV4.
    KOiK03263.
    OMAiCAMSEEC.
    OrthoDBiEOG7KSXB7.
    PhylomeDBiQ9GZV4.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q9GZV4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADEIDFTTG DAGASSTYPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK    50
    HGHAKVHLVG IDIFTGKKYE DICPSTHNMD VPNIKRNDYQ LICIQDGYLS 100
    LLTETGEVRE DLKLPEGELG KEIEGKYNAG EDVQVSVMCA MSEEYAVAIK 150
    PCK 153
    Length:153
    Mass (Da):16,793
    Last modified:January 23, 2007 - v3
    Checksum:i632BFE7F6DB073BD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421E → D.1 Publication
    VAR_027943

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF262027 mRNA. Translation: AAF98810.1.
    AF293387, AF293386 Genomic DNA. Translation: AAG23176.1.
    AY205258 mRNA. Translation: AAO18676.1.
    AY205259 mRNA. Translation: AAO18677.1.
    AY205260 mRNA. Translation: AAO18678.1.
    AY205261 mRNA. Translation: AAO18679.1.
    AK311962 mRNA. Translation: BAG34902.1.
    CH471052 Genomic DNA. Translation: EAW78501.1.
    BC036072 mRNA. Translation: AAH36072.1.
    CCDSiCCDS3214.1.
    RefSeqiNP_065123.1. NM_020390.5.
    UniGeneiHs.164144.

    Genome annotation databases

    EnsembliENST00000295822; ENSP00000295822; ENSG00000163577.
    GeneIDi56648.
    KEGGihsa:56648.
    UCSCiuc003fhd.3. human.

    Polymorphism databases

    DMDMi74762725.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF262027 mRNA. Translation: AAF98810.1 .
    AF293387 , AF293386 Genomic DNA. Translation: AAG23176.1 .
    AY205258 mRNA. Translation: AAO18676.1 .
    AY205259 mRNA. Translation: AAO18677.1 .
    AY205260 mRNA. Translation: AAO18678.1 .
    AY205261 mRNA. Translation: AAO18679.1 .
    AK311962 mRNA. Translation: BAG34902.1 .
    CH471052 Genomic DNA. Translation: EAW78501.1 .
    BC036072 mRNA. Translation: AAH36072.1 .
    CCDSi CCDS3214.1.
    RefSeqi NP_065123.1. NM_020390.5.
    UniGenei Hs.164144.

    3D structure databases

    ProteinModelPortali Q9GZV4.
    SMRi Q9GZV4. Positions 15-150.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121162. 11 interactions.
    IntActi Q9GZV4. 8 interactions.
    MINTi MINT-1453868.
    STRINGi 9606.ENSP00000295822.

    PTM databases

    PhosphoSitei Q9GZV4.

    Polymorphism databases

    DMDMi 74762725.

    Proteomic databases

    MaxQBi Q9GZV4.
    PaxDbi Q9GZV4.
    PRIDEi Q9GZV4.

    Protocols and materials databases

    DNASUi 56648.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295822 ; ENSP00000295822 ; ENSG00000163577 .
    GeneIDi 56648.
    KEGGi hsa:56648.
    UCSCi uc003fhd.3. human.

    Organism-specific databases

    CTDi 56648.
    GeneCardsi GC03M170607.
    HGNCi HGNC:3301. EIF5A2.
    HPAi HPA029090.
    MIMi 605782. gene.
    neXtProti NX_Q9GZV4.
    PharmGKBi PA27727.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0231.
    HOGENOMi HOG000106270.
    HOVERGENi HBG001104.
    InParanoidi Q9GZV4.
    KOi K03263.
    OMAi CAMSEEC.
    OrthoDBi EOG7KSXB7.
    PhylomeDBi Q9GZV4.
    TreeFami TF101534.

    Enzyme and pathway databases

    Reactomei REACT_12469. Hypusine synthesis from eIF5A-lysine.

    Miscellaneous databases

    ChiTaRSi EIF5A2. human.
    GeneWikii EIF5A2.
    GenomeRNAii 56648.
    NextBioi 62085.
    PROi Q9GZV4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9GZV4.
    Bgeei Q9GZV4.
    CleanExi HS_EIF5A2.
    Genevestigatori Q9GZV4.

    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. "Isolation of a novel candidate oncogene within a frequently amplified region at 3q26 in ovarian cancer."
      Guan X.-Y.Y., Sham J.S.T., Tang T.C.-M., Fang Y., Huo K.-K., Yang J.-M.
      Cancer Res. 61:3806-3809(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Ovarian carcinoma.
    2. "Human eIF5A2 on chromosome 3q25-q27 is a phylogenetically conserved vertebrate variant of eukaryotic translation initiation factor 5A with tissue-specific expression."
      Jenkins Z.A., Haag P.G., Johansson H.E.
      Genomics 71:101-109(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
    3. "Expression of eIF5A genes in human cancer cells."
      Clement P.M.J., Jenkins Z.A., Park M.H., Johansson H.E.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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].
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    7. Cited for: FUNCTION, HYPUSINE AT LYS-50.
    8. "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.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "Screening the SPO11 and EIF5A2 genes in a population of infertile men."
      Christensen G.L., Ivanov I.P., Atkins J.F., Mielnik A., Schlegel P.N., Carrell D.T.
      Fertil. Steril. 84:758-760(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-42.

    Entry informationi

    Entry nameiIF5A2_HUMAN
    AccessioniPrimary (citable) accession number: Q9GZV4
    Secondary accession number(s): B2R4V5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 of the entry and version 3 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. Translation initiation factors
      List of translation initiation factor entries
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3