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P09914 (IFIT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:IFIT1
Synonyms:G10P1, IFI56, IFNAI1, ISG56
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.13 Ref.18 Ref.21

Subunit structure

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. Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.20

Subcellular location

Cytoplasm Ref.12 Ref.20.

Induction

By type I interferons, dsRNAs and viruses. Ref.1

Domain

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.

Post-translational modification

Phosphorylated. Ref.13

ISGylated. Ref.10

Sequence similarities

Belongs to the IFIT family.

Contains 10 TPR repeats.

Ontologies

Keywords
   Biological processAntiviral defense
Host-virus interaction
Immunity
Innate immunity
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
TPR repeat
   LigandRNA-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to exogenous dsRNA

Inferred from direct assay Ref.12. Source: BHF-UCL

cellular response to type I interferon

Inferred from direct assay Ref.12. Source: BHF-UCL

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular transport of viral protein in host cell

Inferred from direct assay Ref.12. Source: BHF-UCL

negative regulation of defense response to virus by host

Inferred from direct assay Ref.13. Source: BHF-UCL

negative regulation of helicase activity

Inferred from direct assay Ref.12. Source: BHF-UCL

negative regulation of protein binding

Inferred from direct assay Ref.13. Source: BHF-UCL

negative regulation of viral genome replication

Inferred from mutant phenotype Ref.18. Source: UniProtKB

positive regulation of viral genome replication

Inferred from direct assay Ref.13. Source: BHF-UCL

response to virus

Inferred from mutant phenotype Ref.20. Source: UniProtKB

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.20. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

   Molecular_functionRNA binding

Inferred from direct assay Ref.20. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

E1P067898EBI-745117,EBI-7015660From a different organism.
IFIT2P099135EBI-745117,EBI-3507167
IFIT3O148795EBI-745117,EBI-745127

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P09914-1)

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.
Isoform 2 (identifier: P09914-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478Interferon-induced protein with tetratricopeptide repeats 1
PRO_0000106344

Regions

Repeat52 – 8534TPR 1
Repeat95 – 12834TPR 2
Repeat139 – 17436TPR 3
Repeat183 – 21634TPR 4
Repeat218 – 24932TPR 5
Repeat251 – 28434TPR 6
Repeat305 – 33935TPR 7
Repeat340 – 37334TPR 8
Repeat378 – 41235TPR 9
Repeat437 – 47034TPR 10
Region256 – 2627Interaction with the 5'-triphosphate group of PPP-RNA By similarity

Sites

Site341Interaction with PPP-RNA By similarity
Site421Interaction with PPP-RNA By similarity
Site1511Interaction with PPP-RNA By similarity
Site1871Interaction with PPP-RNA By similarity
Site2521Interaction with PPP-RNA By similarity
Site2901Interaction with the 5'-triphosphate group of PPP-RNA By similarity

Natural variations

Alternative sequence1 – 3131Missing in isoform 2.
VSP_054831
Natural variant1311P → H.
Corresponds to variant rs11553019 [ dbSNP | Ensembl ].
VAR_052614

Experimental info

Mutagenesis341D → A: Abolishes PPP-RNA-binding. Ref.21
Mutagenesis381R → M: Abolishes PPP-RNA-binding. Ref.21
Mutagenesis421Q → E: Reduced PPP-RNA-binding. Ref.21
Mutagenesis1511K → M: Abolishes PPP-RNA-binding. Ref.21
Mutagenesis1571Y → F: Reduced PPP-RNA-binding. Ref.21
Mutagenesis1871R → H: Abolishes PPP-RNA-binding. Ref.21
Mutagenesis2551R → M: Abolishes PPP-RNA-binding. Ref.21
Sequence conflict1981H → Y in BAG52612. Ref.3
Sequence conflict3831H → Y in CAA27244. Ref.1
Sequence conflict4011H → R in BAG52612. Ref.3

Secondary structure

................................... 478
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: EF46E652A366E721

FASTA47855,360
        10         20         30         40         50         60 
MSTNGDDHQV KDSLEQLRCH FTWELSIDDD EMPDLENRVL DQIEFLDTKY SVGIHNLLAY 

        70         80         90        100        110        120 
VKHLKGQNEE ALKSLKEAEN LMQEEHDNQA NVRSLVTWGN FAWMYYHMGR LAEAQTYLDK 

       130        140        150        160        170        180 
VENICKKLSN PFRYRMECPE IDCEEGWALL KCGGKNYERA KACFEKVLEV DPENPESSAG 

       190        200        210        220        230        240 
YAISAYRLDG FKLATKNHKP FSLLPLRQAV RLNPDNGYIK VLLALKLQDE GQEAEGEKYI 

       250        260        270        280        290        300 
EEALANMSSQ TYVFRYAAKF YRRKGSVDKA LELLKKALQE TPTSVLLHHQ IGLCYKAQMI 

       310        320        330        340        350        360 
QIKEATKGQP RGQNREKLDK MIRSAIFHFE SAVEKKPTFE VAHLDLARMY IEAGNHRKAE 

       370        380        390        400        410        420 
ENFQKLLCMK PVVEETMQDI HFHYGRFQEF QKKSDVNAII HYLKAIKIEQ ASLTRDKSIN 

       430        440        450        460        470 
SLKKLVLRKL RRKALDLESL SLLGFVYKLE GNMNEALEYY ERALRLAADF ENSVRQGP 

« Hide

Isoform 2 [UniParc].

Checksum: 3CB6ECE609D546E7
Show »

FASTA44751,713

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The ISG56/IFIT1 gene family."
Fensterl V., Sen G.C.
J. Interferon Cytokine Res. 31:71-78(2011) [PubMed] [Europe PMC] [Abstract]
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]"IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA."
Pichlmair A., Lassnig C., Eberle C.A., Gorna M.W., Baumann C.L., Burkard T.R., Buerckstuemmer T., Stefanovic A., Krieger S., Bennett K.L., Ruelicke T., Weber F., Colinge J., Mueller M., Superti-Furga G.
Nat. Immunol. 12:624-630(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS31243.1.
PIRA25407.
RefSeqNP_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]
UniGeneHs.20315.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HOUX-ray1.95A/B7-279[»]
ProteinModelPortalP09914.
SMRP09914. Positions 10-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109659. 39 interactions.
DIPDIP-37898N.
IntActP09914. 36 interactions.
MINTMINT-153827.
STRING9606.ENSP00000360869.

PTM databases

PhosphoSiteP09914.

Polymorphism databases

DMDM116242522.

Proteomic databases

MaxQBP09914.
PaxDbP09914.
PRIDEP09914.

Protocols and materials databases

DNASU3434.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371804; ENSP00000360869; ENSG00000185745.
ENST00000546318; ENSP00000441968; ENSG00000185745.
GeneID3434.
KEGGhsa:3434.
UCSCuc001kgi.4. human. [P09914-1]

Organism-specific databases

CTD3434.
GeneCardsGC10P091142.
HGNCHGNC:5407. IFIT1.
HPACAB045980.
HPA055380.
MIM147690. gene.
neXtProtNX_P09914.
PharmGKBPA29648.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG311487.
HOGENOMHOG000001558.
HOVERGENHBG066330.
InParanoidP09914.
KOK14217.
OMAMECPEID.
OrthoDBEOG71K62V.
PhylomeDBP09914.
TreeFamTF342671.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP09914.
BgeeP09914.
CleanExHS_IFIT1.
GenevestigatorP09914.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR024121. Interferon-induced_IFIT1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10271:SF15. PTHR10271:SF15. 1 hit.
PfamPF00515. TPR_1. 2 hits.
PF07719. TPR_2. 1 hit.
[Graphical view]
SMARTSM00028. TPR. 6 hits.
[Graphical view]
PROSITEPS50005. TPR. 6 hits.
PS50293. TPR_REGION. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiIFIT1.
GenomeRNAi3434.
NextBio13540.
PROP09914.
SOURCESearch...

Entry information

Entry nameIFIT1_HUMAN
AccessionPrimary (citable) accession number: P09914
Secondary accession number(s): B3KS50 expand/collapse secondary AC list , D3DR31, Q5T7J1, Q96QM5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM