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Q13325

- IFIT5_HUMAN

UniProt

Q13325 - IFIT5_HUMAN

Protein

Interferon-induced protein with tetratricopeptide repeats 5

Gene

IFIT5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei33 – 331Interaction with PPP-RNA
    Sitei37 – 371Interaction with PPP-RNA
    Sitei41 – 411Interaction with PPP-RNA
    Sitei150 – 1501Interaction with PPP-RNA
    Sitei186 – 1861Interaction with PPP-RNA
    Sitei250 – 2501Interaction with PPP-RNA
    Sitei288 – 2881Interaction with the 5'-triphosphate group of PPP-RNA

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. RNA binding Source: UniProtKB
    3. single-stranded RNA binding Source: UniProtKB
    4. tRNA binding Source: UniProtKB

    GO - Biological processi

    1. defense response to virus Source: UniProtKB
    2. innate immune response Source: UniProtKB-KW

    Keywords - Biological processi

    Antiviral defense, Immunity, Innate immunity

    Keywords - Ligandi

    RNA-binding, tRNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon-induced protein with tetratricopeptide repeats 5
    Short name:
    IFIT-5
    Alternative name(s):
    Interferon-induced 58 kDa protein
    Retinoic acid- and interferon-inducible 58 kDa protein
    Short name:
    P58
    Gene namesi
    Name:IFIT5
    Synonyms:ISG58, RI58
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:13328. IFIT5.

    Subcellular locationi

    Cell projectionruffle membrane 1 Publication
    Note: Colocalized with DDX58/RIG-I at cell surface ruffles. Localizes to actin-rich protrusions from the apical cell surface.

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. apical part of cell Source: UniProtKB
    3. ruffle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi33 – 331E → A: Reduced PPP-RNA-binding. 1 Publication
    Mutagenesisi37 – 371T → V: Abolishes PPP-RNA-binding.
    Mutagenesisi41 – 411Q → E: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi150 – 1501K → M: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi156 – 1561Y → F: Reduced PPP-RNA-binding. 1 Publication
    Mutagenesisi186 – 1861R → H: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi250 – 2501Y → F: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi253 – 2531R → M: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi254 – 2541Y → F: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi260 – 2601R → E: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi287 – 2871H → A: Reduced PPP-RNA-binding. 1 Publication
    Mutagenesisi288 – 2881Q → E: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi291 – 2911L → A: Does not affect RNA-binding. 1 Publication
    Mutagenesisi302 – 3021K → A: Reduced RNA-binding. 1 Publication
    Mutagenesisi307 – 3071R → A: Reduced RNA-binding. 25 fold reduction in tRNA-binding. 1 Publication
    Mutagenesisi309 – 3091K → A: Reduced RNA-binding. 1 Publication
    Mutagenesisi337 – 3371F → A: Abolishes PPP-RNA-binding.
    Mutagenesisi388 – 3892FH → AA: Reduced RNA-binding.
    Mutagenesisi415 – 4151K → A: Reduced RNA-binding. 25 fold reduction in tRNA-binding. 1 Publication
    Mutagenesisi422 – 4221K → A: Reduced RNA-binding. 1 Publication
    Mutagenesisi426 – 4261K → A: Reduced RNA-binding. 5 fold reduction in tRNA-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134988392.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 482482Interferon-induced protein with tetratricopeptide repeats 5PRO_0000106351Add
    BLAST

    Proteomic databases

    MaxQBiQ13325.
    PaxDbiQ13325.
    PeptideAtlasiQ13325.
    PRIDEiQ13325.

    PTM databases

    PhosphoSiteiQ13325.

    Expressioni

    Inductioni

    By interferons (IFNs).

    Gene expression databases

    ArrayExpressiQ13325.
    BgeeiQ13325.
    CleanExiHS_IFIT5.
    GenevestigatoriQ13325.

    Organism-specific databases

    HPAiHPA037957.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi117289. 22 interactions.
    IntActiQ13325. 13 interactions.
    MINTiMINT-1395756.
    STRINGi9606.ENSP00000360860.

    Structurei

    Secondary structure

    1
    482
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1513
    Helixi19 – 213
    Helixi26 – 283
    Helixi31 – 4414
    Beta strandi46 – 483
    Helixi50 – 6314
    Helixi67 – 8418
    Helixi86 – 883
    Helixi91 – 933
    Helixi94 – 10613
    Helixi110 – 12617
    Beta strandi130 – 1334
    Helixi138 – 15013
    Helixi153 – 1553
    Helixi156 – 16914
    Helixi174 – 18916
    Beta strandi193 – 1953
    Helixi201 – 21010
    Helixi215 – 22713
    Helixi231 – 24414
    Helixi249 – 26113
    Helixi265 – 27814
    Helixi283 – 30321
    Turni304 – 3063
    Helixi310 – 33324
    Helixi338 – 35013
    Helixi354 – 36512
    Helixi372 – 38817
    Helixi393 – 40614
    Beta strandi408 – 4103
    Helixi413 – 43018
    Helixi435 – 44713
    Helixi451 – 46414
    Helixi469 – 48012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZGQX-ray2.20A1-482[»]
    4HOQX-ray2.07A1-482[»]
    4HORX-ray1.86A1-482[»]
    4HOSX-ray2.00A1-482[»]
    4HOTX-ray2.50A1-482[»]
    4J0UX-ray1.97A1-482[»]
    ProteinModelPortaliQ13325.
    SMRiQ13325. Positions 1-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati51 – 8434TPR 1Add
    BLAST
    Repeati94 – 12734TPR 2Add
    BLAST
    Repeati138 – 17336TPR 3Add
    BLAST
    Repeati181 – 21434TPR 4Add
    BLAST
    Repeati249 – 28234TPR 5Add
    BLAST
    Repeati338 – 37134TPR 6Add
    BLAST
    Repeati376 – 41035TPR 7Add
    BLAST
    Repeati435 – 46834TPR 8Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni254 – 2607Interaction with the 5'-triphosphate group of PPP-RNA

    Domaini

    RNA recognition is mediated by a convoluted intramolecular fold of the TPR repeats (TPR eddy), which scaffolds unique additional helices that form an RNA binding cleft (PubMed:23317505 and PubMed:23334420). Undergoes a conformational change upon RNA-binding: unliganded exists in a more open conformation, facilitating RNA entry (PubMed:23334420).1 Publication

    Sequence similaritiesi

    Belongs to the IFIT family.Curated
    Contains 8 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiNOG311487.
    HOGENOMiHOG000001558.
    HOVERGENiHBG066330.
    InParanoidiQ13325.
    OMAiNTAIHHY.
    OrthoDBiEOG71K62V.
    PhylomeDBiQ13325.
    TreeFamiTF342671.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR024125. Interferon_induced_IFIT5.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR10271:SF5. PTHR10271:SF5. 1 hit.
    PfamiPF00515. TPR_1. 1 hit.
    PF07719. TPR_2. 2 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 5 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13325-1) [UniParc]FASTAAdd to Basket

    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

    MSEIRKDTLK AILLELECHF TWNLLKEDID LFEVEDTIGQ QLEFLTTKSR    50
    LALYNLLAYV KHLKGQNKDA LECLEQAEEI IQQEHSDKEE VRSLVTWGNY 100
    AWVYYHMDQL EEAQKYTGKI GNVCKKLSSP SNYKLECPET DCEKGWALLK 150
    FGGKYYQKAK AAFEKALEVE PDNPEFNIGY AITVYRLDDS DREGSVKSFS 200
    LGPLRKAVTL NPDNSYIKVF LALKLQDVHA EAEGEKYIEE ILDQISSQPY 250
    VLRYAAKFYR RKNSWNKALE LLKKALEVTP TSSFLHHQMG LCYRAQMIQI 300
    KKATHNRPKG KDKLKVDELI SSAIFHFKAA MERDSMFAFA YTDLANMYAE 350
    GGQYSNAEDI FRKALRLENI TDDHKHQIHY HYGRFQEFHR KSENTAIHHY 400
    LEALKVKDRS PLRTKLTSAL KKLSTKRLCH NALDVQSLSA LGFVYKLEGE 450
    KRQAAEYYEK AQKIDPENAE FLTALCELRL SI 482
    Length:482
    Mass (Da):55,847
    Last modified:November 1, 1996 - v1
    Checksum:i8045BC100384BE05
    GO
    Isoform 2 (identifier: Q13325-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         158-205: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:434
    Mass (Da):50,520
    Checksum:i6CA739D6614569C8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti215 – 2151S → N in CAG33312. 1 PublicationCurated
    Sequence conflicti449 – 4491G → R in BAG35276. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei158 – 20548Missing in isoform 2. 1 PublicationVSP_056412Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34605 mRNA. Translation: AAA84934.1.
    AK293346 mRNA. Translation: BAG56862.1.
    AK312358 mRNA. Translation: BAG35276.1.
    CR457031 mRNA. Translation: CAG33312.1.
    AL353146 Genomic DNA. Translation: CAI12381.1.
    CH471066 Genomic DNA. Translation: EAW50135.1.
    BC025786 mRNA. Translation: AAH25786.1.
    CCDSiCCDS7403.1.
    PIRiG02058.
    RefSeqiNP_036552.1. NM_012420.2.
    UniGeneiHs.252839.

    Genome annotation databases

    EnsembliENST00000371795; ENSP00000360860; ENSG00000152778.
    ENST00000416601; ENSP00000414042; ENSG00000152778.
    GeneIDi24138.
    KEGGihsa:24138.
    UCSCiuc010qnh.2. human.

    Polymorphism databases

    DMDMi6831571.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34605 mRNA. Translation: AAA84934.1 .
    AK293346 mRNA. Translation: BAG56862.1 .
    AK312358 mRNA. Translation: BAG35276.1 .
    CR457031 mRNA. Translation: CAG33312.1 .
    AL353146 Genomic DNA. Translation: CAI12381.1 .
    CH471066 Genomic DNA. Translation: EAW50135.1 .
    BC025786 mRNA. Translation: AAH25786.1 .
    CCDSi CCDS7403.1.
    PIRi G02058.
    RefSeqi NP_036552.1. NM_012420.2.
    UniGenei Hs.252839.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZGQ X-ray 2.20 A 1-482 [» ]
    4HOQ X-ray 2.07 A 1-482 [» ]
    4HOR X-ray 1.86 A 1-482 [» ]
    4HOS X-ray 2.00 A 1-482 [» ]
    4HOT X-ray 2.50 A 1-482 [» ]
    4J0U X-ray 1.97 A 1-482 [» ]
    ProteinModelPortali Q13325.
    SMRi Q13325. Positions 1-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117289. 22 interactions.
    IntActi Q13325. 13 interactions.
    MINTi MINT-1395756.
    STRINGi 9606.ENSP00000360860.

    PTM databases

    PhosphoSitei Q13325.

    Polymorphism databases

    DMDMi 6831571.

    Proteomic databases

    MaxQBi Q13325.
    PaxDbi Q13325.
    PeptideAtlasi Q13325.
    PRIDEi Q13325.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371795 ; ENSP00000360860 ; ENSG00000152778 .
    ENST00000416601 ; ENSP00000414042 ; ENSG00000152778 .
    GeneIDi 24138.
    KEGGi hsa:24138.
    UCSCi uc010qnh.2. human.

    Organism-specific databases

    CTDi 24138.
    GeneCardsi GC10P091164.
    HGNCi HGNC:13328. IFIT5.
    HPAi HPA037957.
    neXtProti NX_Q13325.
    PharmGKBi PA134988392.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311487.
    HOGENOMi HOG000001558.
    HOVERGENi HBG066330.
    InParanoidi Q13325.
    OMAi NTAIHHY.
    OrthoDBi EOG71K62V.
    PhylomeDBi Q13325.
    TreeFami TF342671.

    Miscellaneous databases

    GenomeRNAii 24138.
    NextBioi 35467534.
    PROi Q13325.

    Gene expression databases

    ArrayExpressi Q13325.
    Bgeei Q13325.
    CleanExi HS_IFIT5.
    Genevestigatori Q13325.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR024125. Interferon_induced_IFIT5.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR10271:SF5. PTHR10271:SF5. 1 hit.
    Pfami PF00515. TPR_1. 1 hit.
    PF07719. TPR_2. 2 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 5 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel interferon-inducible gene expressed during myeloid differentiation."
      Niikura T., Hirata R., Weil S.C.
      Blood Cells Mol. Dis. 23:337-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Amygdala.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Pancreas and Spleen.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: REVIEW.
    9. Cited for: RNA-BINDING.
    10. "tRNA binding, structure, and localization of the human interferon-induced protein IFIT5."
      Katibah G.E., Lee H.J., Huizar J.P., Vogan J.M., Alber T., Collins K.
      Mol. Cell 49:743-750(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF LEU-291; LYS-302; ARG-307; LYS-309; 388-PHE-HIS-389; LYS-415; LYS-422 AND LYS-426.
    11. "Structural basis for viral 5'-PPP-RNA recognition by human IFIT proteins."
      Abbas Y.M., Pichlmair A., Gorna M.W., Superti-Furga G., Nagar B.
      Nature 494:60-64(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PPP-RNA, FUNCTION, RNA-BINDING, MUTAGENESIS OF GLU-33; GLN-41; LYS-150; TYR-156; ARG-186; TYR-250; ARG-253; TYR-254; ARG-260; HIS-287 AND GLN-288.

    Entry informationi

    Entry nameiIFIT5_HUMAN
    AccessioniPrimary (citable) accession number: Q13325
    Secondary accession number(s): B2R5X9
    , B4DDV1, Q5T7I9, Q6IAX3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 128 of the entry and version 1 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 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3