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P47813

- IF1AX_HUMAN

UniProt

P47813 - IF1AX_HUMAN

Protein

Eukaryotic translation initiation factor 1A, X-chromosomal

Gene

EIF1AX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. translation factor activity, nucleic acid binding Source: ProtInc
    3. translation initiation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. translation Source: Reactome
    4. translational initiation Source: Reactome

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 1A, X-chromosomal
    Short name:
    eIF-1A X isoform
    Alternative name(s):
    Eukaryotic translation initiation factor 4C
    Short name:
    eIF-4C
    Gene namesi
    Name:EIF1AX
    Synonyms:EIF1A, EIF4C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:3250. EIF1AX.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27684.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 144144Eukaryotic translation initiation factor 1A, X-chromosomalPRO_0000145101Add
    BLAST

    Proteomic databases

    MaxQBiP47813.
    PaxDbiP47813.
    PRIDEiP47813.

    Expressioni

    Gene expression databases

    BgeeiP47813.
    CleanExiHS_EIF1AX.
    GenevestigatoriP47813.

    Organism-specific databases

    HPAiHPA002561.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IPO13O9482914EBI-1045377,EBI-747310

    Protein-protein interaction databases

    BioGridi108284. 9 interactions.
    DIPiDIP-40995N.
    IntActiP47813. 3 interactions.
    MINTiMINT-144981.
    STRINGi9606.ENSP00000368927.

    Structurei

    Secondary structure

    1
    144
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 126
    Beta strandi33 – 419
    Beta strandi43 – 519
    Turni52 – 543
    Beta strandi55 – 606
    Helixi64 – 674
    Beta strandi76 – 805
    Beta strandi82 – 876
    Beta strandi90 – 956
    Turni97 – 993
    Helixi100 – 1067
    Beta strandi120 – 1223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D7QNMR-A2-144[»]
    3ZJYX-ray3.60C1-112[»]
    4KZYX-ray7.01n1-144[»]
    4KZZX-ray7.03n1-144[»]
    ProteinModelPortaliP47813.
    SMRiP47813. Positions 2-131.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP47813.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 9675S1-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the eIF-1A family.Curated
    Contains 1 S1-like domain.Curated

    Phylogenomic databases

    eggNOGiCOG0361.
    HOGENOMiHOG000223675.
    HOVERGENiHBG001131.
    InParanoidiP47813.
    KOiK03236.
    OMAiWNEYATI.
    OrthoDBiEOG7VHT0G.
    PhylomeDBiP47813.
    TreeFamiTF350394.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    HAMAPiMF_00216. aIF_1A.
    InterProiIPR012340. NA-bd_OB-fold.
    IPR006196. RNA-binding_domain_S1_IF1.
    IPR001253. TIF_eIF-1A.
    IPR018104. TIF_eIF-1A_CS.
    [Graphical view]
    PANTHERiPTHR21668. PTHR21668. 1 hit.
    PfamiPF01176. eIF-1a. 1 hit.
    [Graphical view]
    ProDomiPD005579. TIF_eIF-1A. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00652. eIF1a. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00523. eIF-1A. 1 hit.
    PROSITEiPS01262. IF1A. 1 hit.
    PS50832. S1_IF1_TYPE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P47813-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKNKGKGGK NRRRGKNENE SEKRELVFKE DGQEYAQVIK MLGNGRLEAM    50
    CFDGVKRLCH IRGKLRKKVW INTSDIILVG LRDYQDNKAD VILKYNADEA 100
    RSLKAYGELP EHAKINETDT FGPGDDDEIQ FDDIGDDDED IDDI 144
    Length:144
    Mass (Da):16,460
    Last modified:January 23, 2007 - v2
    Checksum:i1C4209855B21BFD4
    GO

    Sequence cautioni

    The sequence CAI40551.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18960 mRNA. Translation: AAA19812.1.
    AK312320 mRNA. Translation: BAG35242.1.
    BT007064 mRNA. Translation: AAP35727.1.
    AL732366 Genomic DNA. Translation: CAI40550.1.
    AL732366 Genomic DNA. Translation: CAI40551.1. Sequence problems.
    BC000793 mRNA. Translation: AAH00793.1.
    BC067851 mRNA. Translation: AAH67851.1.
    CCDSiCCDS14196.1.
    PIRiC53045.
    RefSeqiNP_001403.1. NM_001412.3.
    UniGeneiHs.522590.

    Genome annotation databases

    EnsembliENST00000379607; ENSP00000368927; ENSG00000173674.
    GeneIDi1964.
    KEGGihsa:1964.
    UCSCiuc004czt.3. human.

    Polymorphism databases

    DMDMi1352425.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18960 mRNA. Translation: AAA19812.1 .
    AK312320 mRNA. Translation: BAG35242.1 .
    BT007064 mRNA. Translation: AAP35727.1 .
    AL732366 Genomic DNA. Translation: CAI40550.1 .
    AL732366 Genomic DNA. Translation: CAI40551.1 . Sequence problems.
    BC000793 mRNA. Translation: AAH00793.1 .
    BC067851 mRNA. Translation: AAH67851.1 .
    CCDSi CCDS14196.1.
    PIRi C53045.
    RefSeqi NP_001403.1. NM_001412.3.
    UniGenei Hs.522590.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D7Q NMR - A 2-144 [» ]
    3ZJY X-ray 3.60 C 1-112 [» ]
    4KZY X-ray 7.01 n 1-144 [» ]
    4KZZ X-ray 7.03 n 1-144 [» ]
    ProteinModelPortali P47813.
    SMRi P47813. Positions 2-131.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108284. 9 interactions.
    DIPi DIP-40995N.
    IntActi P47813. 3 interactions.
    MINTi MINT-144981.
    STRINGi 9606.ENSP00000368927.

    Polymorphism databases

    DMDMi 1352425.

    Proteomic databases

    MaxQBi P47813.
    PaxDbi P47813.
    PRIDEi P47813.

    Protocols and materials databases

    DNASUi 1964.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379607 ; ENSP00000368927 ; ENSG00000173674 .
    GeneIDi 1964.
    KEGGi hsa:1964.
    UCSCi uc004czt.3. human.

    Organism-specific databases

    CTDi 1964.
    GeneCardsi GC0XM020052.
    H-InvDB HIX0028844.
    HGNCi HGNC:3250. EIF1AX.
    HPAi HPA002561.
    MIMi 300186. gene.
    neXtProti NX_P47813.
    PharmGKBi PA27684.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0361.
    HOGENOMi HOG000223675.
    HOVERGENi HBG001131.
    InParanoidi P47813.
    KOi K03236.
    OMAi WNEYATI.
    OrthoDBi EOG7VHT0G.
    PhylomeDBi P47813.
    TreeFami TF350394.

    Enzyme and pathway databases

    Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Miscellaneous databases

    ChiTaRSi EIF1AX. human.
    EvolutionaryTracei P47813.
    GeneWikii EIF1AX.
    NextBioi 7965.
    PROi P47813.
    SOURCEi Search...

    Gene expression databases

    Bgeei P47813.
    CleanExi HS_EIF1AX.
    Genevestigatori P47813.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    HAMAPi MF_00216. aIF_1A.
    InterProi IPR012340. NA-bd_OB-fold.
    IPR006196. RNA-binding_domain_S1_IF1.
    IPR001253. TIF_eIF-1A.
    IPR018104. TIF_eIF-1A_CS.
    [Graphical view ]
    PANTHERi PTHR21668. PTHR21668. 1 hit.
    Pfami PF01176. eIF-1a. 1 hit.
    [Graphical view ]
    ProDomi PD005579. TIF_eIF-1A. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00652. eIF1a. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00523. eIF-1A. 1 hit.
    PROSITEi PS01262. IF1A. 1 hit.
    PS50832. S1_IF1_TYPE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Determination of the amino acid sequence of rabbit, human, and wheat germ protein synthesis factor eIF-4C by cloning and chemical sequencing."
      Dever T.E., Wei C.-L., Benkowski L.A., Browning K., Merrick W.C., Hershey J.W.B.
      J. Biol. Chem. 269:3212-3218(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Cerebellum.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Hypothalamus and Placenta.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "The eIF1A solution structure reveals a large RNA-binding surface important for scanning function."
      Battiste J.L., Pestova T.V., Hellen C.U., Wagner G.
      Mol. Cell 5:109-119(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.

    Entry informationi

    Entry nameiIF1AX_HUMAN
    AccessioniPrimary (citable) accession number: P47813
    Secondary accession number(s): B2R5U5
    , Q0VGC2, Q5JPS5, Q5JPS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 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, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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