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P09914

- IFIT1_HUMAN

UniProt

P09914 - IFIT1_HUMAN

Protein

Interferon-induced protein with tetratricopeptide repeats 1

Gene

IFIT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Interferon-induced antiviral 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 and inhibiting expression of viral messenger 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. Viruses evolved several ways to evade this restriction system such as encoding their own 2'-O-methylase for their mRNAs or by stealing host cap containing the 2'-O-methylation (cap snatching mechanism). Exhibits antiviral activity against several viruses including human papilloma and hepatitis C viruses.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei34 – 341Interaction with PPP-RNABy similarity
    Sitei42 – 421Interaction with PPP-RNABy similarity
    Sitei151 – 1511Interaction with PPP-RNABy similarity
    Sitei187 – 1871Interaction with PPP-RNABy similarity
    Sitei252 – 2521Interaction with PPP-RNABy similarity
    Sitei290 – 2901Interaction with the 5'-triphosphate group of PPP-RNABy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. RNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to exogenous dsRNA Source: BHF-UCL
    2. cellular response to type I interferon Source: BHF-UCL
    3. cytokine-mediated signaling pathway Source: Reactome
    4. defense response to virus Source: UniProtKB-KW
    5. intracellular transport of viral protein in host cell Source: BHF-UCL
    6. negative regulation of defense response to virus by host Source: BHF-UCL
    7. negative regulation of helicase activity Source: BHF-UCL
    8. negative regulation of protein binding Source: BHF-UCL
    9. negative regulation of viral genome replication Source: UniProtKB
    10. positive regulation of viral genome replication Source: BHF-UCL
    11. response to virus Source: UniProtKB
    12. type I interferon signaling pathway Source: Reactome

    Keywords - Biological processi

    Antiviral defense, Host-virus interaction, Immunity, Innate immunity

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.
    REACT_25162. Interferon alpha/beta signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interferon-induced protein with tetratricopeptide repeats 1
    Short name:
    IFIT-1
    Alternative name(s):
    Interferon-induced 56 kDa protein
    Short name:
    IFI-56K
    Short name:
    P56
    Gene namesi
    Name:IFIT1
    Synonyms:G10P1, IFI56, IFNAI1, ISG56
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:5407. IFIT1.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi34 – 341D → A: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi38 – 381R → M: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi42 – 421Q → E: Reduced PPP-RNA-binding. 1 Publication
    Mutagenesisi151 – 1511K → M: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi157 – 1571Y → F: Reduced PPP-RNA-binding. 1 Publication
    Mutagenesisi187 – 1871R → H: Abolishes PPP-RNA-binding. 1 Publication
    Mutagenesisi255 – 2551R → M: Abolishes PPP-RNA-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA29648.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 478478Interferon-induced protein with tetratricopeptide repeats 1PRO_0000106344Add
    BLAST

    Post-translational modificationi

    Phosphorylated.1 Publication
    ISGylated.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP09914.
    PaxDbiP09914.
    PRIDEiP09914.

    PTM databases

    PhosphoSiteiP09914.

    Expressioni

    Inductioni

    By type I interferons, dsRNAs and viruses.1 Publication

    Gene expression databases

    ArrayExpressiP09914.
    BgeeiP09914.
    CleanExiHS_IFIT1.
    GenevestigatoriP09914.

    Organism-specific databases

    HPAiCAB045980.
    HPA055380.

    Interactioni

    Subunit structurei

    Component of an interferon-dependent multiprotein complex, at least composed of IFIT1, IFIT2 and IFIT3. Interacts (via TPR repeats 4-7) with EEF1A1 By similarity. Interacts with EIF3C By similarity. Interacts with IFIT2 and IFIT3. Interacts (via TPR repeats 1-4) with RPL15. Interacts with TMEM173/MITA and disrupts its interaction with MAVS or TBK1. Interacts with EIF3E. Interacts (via TPR repeat 2) with E1 proteins of HPV types 11, 18 and 3 and this interaction blocks E1 helicase activity and viral replication.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    E1P067898EBI-745117,EBI-7015660From a different organism.
    IFIT2P099135EBI-745117,EBI-3507167
    IFIT3O148795EBI-745117,EBI-745127

    Protein-protein interaction databases

    BioGridi109659. 41 interactions.
    DIPiDIP-37898N.
    IntActiP09914. 36 interactions.
    MINTiMINT-153827.
    STRINGi9606.ENSP00000360869.

    Structurei

    Secondary structure

    1
    478
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 166
    Helixi20 – 223
    Turni29 – 313
    Helixi32 – 4110
    Helixi48 – 6417
    Helixi68 – 8215
    Helixi92 – 943
    Helixi95 – 10713
    Helixi111 – 12515
    Helixi139 – 15113
    Helixi154 – 1563
    Helixi157 – 17014
    Helixi175 – 19117
    Turni200 – 2034
    Helixi204 – 2129
    Helixi217 – 22913
    Helixi233 – 24614
    Helixi253 – 26412
    Helixi267 – 27711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HOUX-ray1.95A/B7-279[»]
    ProteinModelPortaliP09914.
    SMRiP09914. Positions 10-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati52 – 8534TPR 1Add
    BLAST
    Repeati95 – 12834TPR 2Add
    BLAST
    Repeati139 – 17436TPR 3Add
    BLAST
    Repeati183 – 21634TPR 4Add
    BLAST
    Repeati218 – 24932TPR 5Add
    BLAST
    Repeati251 – 28434TPR 6Add
    BLAST
    Repeati305 – 33935TPR 7Add
    BLAST
    Repeati340 – 37334TPR 8Add
    BLAST
    Repeati378 – 41235TPR 9Add
    BLAST
    Repeati437 – 47034TPR 10Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni256 – 2627Interaction with the 5'-triphosphate group of PPP-RNABy similarity

    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.By similarity

    Sequence similaritiesi

    Belongs to the IFIT family.Curated
    Contains 10 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiNOG311487.
    HOGENOMiHOG000001558.
    HOVERGENiHBG066330.
    InParanoidiP09914.
    KOiK14217.
    OMAiMECPEID.
    OrthoDBiEOG71K62V.
    PhylomeDBiP09914.
    TreeFamiTF342671.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR024121. Interferon-induced_IFIT1.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR10271:SF15. PTHR10271:SF15. 1 hit.
    PfamiPF00515. TPR_1. 2 hits.
    PF07719. TPR_2. 1 hit.
    [Graphical view]
    SMARTiSM00028. TPR. 6 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 6 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: P09914-1) [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

    MSTNGDDHQV KDSLEQLRCH FTWELSIDDD EMPDLENRVL DQIEFLDTKY    50
    SVGIHNLLAY VKHLKGQNEE ALKSLKEAEN LMQEEHDNQA NVRSLVTWGN 100
    FAWMYYHMGR LAEAQTYLDK VENICKKLSN PFRYRMECPE IDCEEGWALL 150
    KCGGKNYERA KACFEKVLEV DPENPESSAG YAISAYRLDG FKLATKNHKP 200
    FSLLPLRQAV RLNPDNGYIK VLLALKLQDE GQEAEGEKYI EEALANMSSQ 250
    TYVFRYAAKF YRRKGSVDKA LELLKKALQE TPTSVLLHHQ IGLCYKAQMI 300
    QIKEATKGQP RGQNREKLDK MIRSAIFHFE SAVEKKPTFE VAHLDLARMY 350
    IEAGNHRKAE ENFQKLLCMK PVVEETMQDI HFHYGRFQEF QKKSDVNAII 400
    HYLKAIKIEQ ASLTRDKSIN SLKKLVLRKL RRKALDLESL SLLGFVYKLE 450
    GNMNEALEYY ERALRLAADF ENSVRQGP 478
    Length:478
    Mass (Da):55,360
    Last modified:October 17, 2006 - v2
    Checksum:iEF46E652A366E721
    GO
    Isoform 2 (identifier: P09914-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-31: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:447
    Mass (Da):51,713
    Checksum:i3CB6ECE609D546E7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti198 – 1981H → Y in BAG52612. (PubMed:14702039)Curated
    Sequence conflicti383 – 3831H → Y in CAA27244. (PubMed:3753936)Curated
    Sequence conflicti401 – 4011H → R in BAG52612. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti131 – 1311P → H.
    Corresponds to variant rs11553019 [ dbSNP | Ensembl ].
    VAR_052614

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3131Missing in isoform 2. 1 PublicationVSP_054831Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03557 mRNA. Translation: CAA27244.1.
    BT006667 mRNA. Translation: AAP35313.1.
    AK092813 mRNA. Translation: BAG52612.1.
    AK314588 mRNA. Translation: BAG37163.1.
    AL353146 Genomic DNA. Translation: CAI12379.1.
    CH471066 Genomic DNA. Translation: EAW50136.1.
    CH471066 Genomic DNA. Translation: EAW50137.1.
    CH471066 Genomic DNA. Translation: EAW50138.1.
    BC007091 mRNA. Translation: AAH07091.1.
    X06559 Genomic DNA. Translation: CAA29802.1.
    CCDSiCCDS31243.1. [P09914-1]
    CCDS59220.1. [P09914-2]
    PIRiA25407.
    RefSeqiNP_001257857.1. NM_001270928.1. [P09914-2]
    NP_001257858.1. NM_001270929.1. [P09914-2]
    NP_001257859.1. NM_001270930.1. [P09914-2]
    NP_001539.3. NM_001548.4. [P09914-1]
    UniGeneiHs.20315.

    Genome annotation databases

    EnsembliENST00000371804; ENSP00000360869; ENSG00000185745. [P09914-1]
    ENST00000546318; ENSP00000441968; ENSG00000185745. [P09914-2]
    GeneIDi3434.
    KEGGihsa:3434.
    UCSCiuc001kgi.4. human. [P09914-1]

    Polymorphism databases

    DMDMi116242522.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03557 mRNA. Translation: CAA27244.1 .
    BT006667 mRNA. Translation: AAP35313.1 .
    AK092813 mRNA. Translation: BAG52612.1 .
    AK314588 mRNA. Translation: BAG37163.1 .
    AL353146 Genomic DNA. Translation: CAI12379.1 .
    CH471066 Genomic DNA. Translation: EAW50136.1 .
    CH471066 Genomic DNA. Translation: EAW50137.1 .
    CH471066 Genomic DNA. Translation: EAW50138.1 .
    BC007091 mRNA. Translation: AAH07091.1 .
    X06559 Genomic DNA. Translation: CAA29802.1 .
    CCDSi CCDS31243.1. [P09914-1 ]
    CCDS59220.1. [P09914-2 ]
    PIRi A25407.
    RefSeqi NP_001257857.1. NM_001270928.1. [P09914-2 ]
    NP_001257858.1. NM_001270929.1. [P09914-2 ]
    NP_001257859.1. NM_001270930.1. [P09914-2 ]
    NP_001539.3. NM_001548.4. [P09914-1 ]
    UniGenei Hs.20315.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HOU X-ray 1.95 A/B 7-279 [» ]
    ProteinModelPortali P09914.
    SMRi P09914. Positions 10-473.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109659. 41 interactions.
    DIPi DIP-37898N.
    IntActi P09914. 36 interactions.
    MINTi MINT-153827.
    STRINGi 9606.ENSP00000360869.

    PTM databases

    PhosphoSitei P09914.

    Polymorphism databases

    DMDMi 116242522.

    Proteomic databases

    MaxQBi P09914.
    PaxDbi P09914.
    PRIDEi P09914.

    Protocols and materials databases

    DNASUi 3434.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371804 ; ENSP00000360869 ; ENSG00000185745 . [P09914-1 ]
    ENST00000546318 ; ENSP00000441968 ; ENSG00000185745 . [P09914-2 ]
    GeneIDi 3434.
    KEGGi hsa:3434.
    UCSCi uc001kgi.4. human. [P09914-1 ]

    Organism-specific databases

    CTDi 3434.
    GeneCardsi GC10P091142.
    HGNCi HGNC:5407. IFIT1.
    HPAi CAB045980.
    HPA055380.
    MIMi 147690. gene.
    neXtProti NX_P09914.
    PharmGKBi PA29648.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311487.
    HOGENOMi HOG000001558.
    HOVERGENi HBG066330.
    InParanoidi P09914.
    KOi K14217.
    OMAi MECPEID.
    OrthoDBi EOG71K62V.
    PhylomeDBi P09914.
    TreeFami TF342671.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_25162. Interferon alpha/beta signaling.

    Miscellaneous databases

    GeneWikii IFIT1.
    GenomeRNAii 3434.
    NextBioi 13540.
    PROi P09914.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09914.
    Bgeei P09914.
    CleanExi HS_IFIT1.
    Genevestigatori P09914.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR024121. Interferon-induced_IFIT1.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR10271:SF15. PTHR10271:SF15. 1 hit.
    Pfami PF00515. TPR_1. 2 hits.
    PF07719. TPR_2. 1 hit.
    [Graphical view ]
    SMARTi SM00028. TPR. 6 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 6 hits.
    PS50293. TPR_REGION. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, full-length sequence and preliminary characterization of a 56-kDa protein induced by human interferons."
      Wathelet M., Moutschen S., Defilippi P., Cravador A., Collet M., Huez G., Content J.
      Eur. J. Biochem. 155:11-17(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION.
    2. "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] (ISOFORM 1).
    3. "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: Small intestine and Synovium.
    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: Prostate.
    7. "Interferon-induced 56,000 Mr protein and its mRNA in human cells: molecular cloning and partial sequence of the cDNA."
      Chebath J., Merlin G., Metz R., Benech P., Revel M.
      Nucleic Acids Res. 11:1213-1226(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 413-478.
    8. "New inducers revealed by the promoter sequence analysis of two interferon-activated human genes."
      Wathelet M.G., Clauss I.M., Nols C.B., Content J., Huez G.A.
      Eur. J. Biochem. 169:313-321(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2.
    9. "The IFI-56K and IFI-54K interferon-inducible human genes belong to the same gene family."
      Wathelet M.G., Clauss I.M., Content J., Huez G.A.
      FEBS Lett. 231:164-171(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO IFI-54K.
    10. "Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways."
      Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.
      Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION.
    11. "Induction and mode of action of the viral stress-inducible murine proteins, P56 and P54."
      Terenzi F., Pal S., Sen G.C.
      Virology 340:116-124(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3E.
    12. "Interferon-inducible protein, P56, inhibits HPV DNA replication by binding to the viral protein E1."
      Terenzi F., Saikia P., Sen G.C.
      EMBO J. 27:3311-3321(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH E1 PROTEINS OF HPV TYPES 11; 18 AND 31.
    13. "ISG56 is a negative-feedback regulator of virus-triggered signaling and cellular antiviral response."
      Li Y., Li C., Xue P., Zhong B., Mao A.P., Ran Y., Chen H., Wang Y.Y., Yang F., Shu H.B.
      Proc. Natl. Acad. Sci. U.S.A. 106:7945-7950(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TMEM173/MITA, PHOSPHORYLATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "A novel interaction between interferon-inducible protein p56 and ribosomal protein L15 in gastric cancer cells."
      Hsu Y.A., Lin H.J., Sheu J.J., Shieh F.K., Chen S.Y., Lai C.H., Tsai F.J., Wan L., Chen B.H.
      DNA Cell Biol. 30:671-679(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPL15.
    16. "The interferon stimulated gene 54 promotes apoptosis."
      Stawowczyk M., Van Scoy S., Kumar K.P., Reich N.C.
      J. Biol. Chem. 286:7257-7266(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IFIT2.
    17. Cited for: REVIEW.
    18. "ISG56 and IFITM1 proteins inhibit hepatitis C virus replication."
      Raychoudhuri A., Shrivastava S., Steele R., Kim H., Ray R., Ray R.B.
      J. Virol. 85:12881-12889(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Where, in antiviral defense, does IFIT1 fit?"
      Ablasser A., Hornung V.
      Nat. Immunol. 12:588-590(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    20. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH IFIT2 AND IFIT3, RNA-BINDING.
    21. "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 (1.9 ANGSTROMS) OF 7-279, FUNCTION, RNA-BINDING, MUTAGENESIS OF ASP-34; ARG-38; GLN-42; LYS-151; TYR-157; ARG-187 AND ARG-255.

    Entry informationi

    Entry nameiIFIT1_HUMAN
    AccessioniPrimary (citable) accession number: P09914
    Secondary accession number(s): B3KS50
    , D3DR31, Q5T7J1, Q96QM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 143 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 10
      Human chromosome 10: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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