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Protein

Interferon-induced protein with tetratricopeptide repeats 1

Gene

IFIT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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
Complete GO annotation...

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

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. 44 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 – 166Combined sources
Helixi20 – 223Combined sources
Turni29 – 313Combined sources
Helixi32 – 4110Combined sources
Helixi48 – 6417Combined sources
Helixi68 – 8215Combined sources
Helixi92 – 943Combined sources
Helixi95 – 10713Combined sources
Helixi111 – 12515Combined sources
Helixi139 – 15113Combined sources
Helixi154 – 1563Combined sources
Helixi157 – 17014Combined sources
Helixi175 – 19117Combined sources
Turni200 – 2034Combined sources
Helixi204 – 2129Combined sources
Helixi217 – 22913Combined sources
Helixi233 – 24614Combined sources
Helixi253 – 26412Combined sources
Helixi267 – 27711Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000013876.
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_dom.
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

        10         20         30         40         50
MSTNGDDHQV KDSLEQLRCH FTWELSIDDD EMPDLENRVL DQIEFLDTKY
60 70 80 90 100
SVGIHNLLAY VKHLKGQNEE ALKSLKEAEN LMQEEHDNQA NVRSLVTWGN
110 120 130 140 150
FAWMYYHMGR LAEAQTYLDK VENICKKLSN PFRYRMECPE IDCEEGWALL
160 170 180 190 200
KCGGKNYERA KACFEKVLEV DPENPESSAG YAISAYRLDG FKLATKNHKP
210 220 230 240 250
FSLLPLRQAV RLNPDNGYIK VLLALKLQDE GQEAEGEKYI EEALANMSSQ
260 270 280 290 300
TYVFRYAAKF YRRKGSVDKA LELLKKALQE TPTSVLLHHQ IGLCYKAQMI
310 320 330 340 350
QIKEATKGQP RGQNREKLDK MIRSAIFHFE SAVEKKPTFE VAHLDLARMY
360 370 380 390 400
IEAGNHRKAE ENFQKLLCMK PVVEETMQDI HFHYGRFQEF QKKSDVNAII
410 420 430 440 450
HYLKAIKIEQ ASLTRDKSIN SLKKLVLRKL RRKALDLESL SLLGFVYKLE
460 470
GNMNEALEYY ERALRLAADF ENSVRQGP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi109659. 44 interactions.
DIPiDIP-37898N.
IntActiP09914. 36 interactions.
MINTiMINT-153827.
STRINGi9606.ENSP00000360869.

PTM databases

PhosphoSiteiP09914.

Polymorphism databases

DMDMi116242522.

Proteomic databases

MaxQBiP09914.
PaxDbiP09914.
PRIDEiP09914.

Protocols and materials databases

DNASUi3434.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3434.
GeneCardsiGC10P091142.
HGNCiHGNC:5407. IFIT1.
HPAiCAB045980.
HPA055380.
MIMi147690. gene.
neXtProtiNX_P09914.
PharmGKBiPA29648.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG311487.
GeneTreeiENSGT00390000013876.
HOGENOMiHOG000001558.
HOVERGENiHBG066330.
InParanoidiP09914.
KOiK14217.
OMAiMECPEID.
OrthoDBiEOG71K62V.
PhylomeDBiP09914.
TreeFamiTF342671.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikiiIFIT1.
GenomeRNAii3434.
NextBioi13540.
PROiP09914.
SOURCEiSearch...

Gene expression databases

BgeeiP09914.
CleanExiHS_IFIT1.
GenevestigatoriP09914.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR024121. Interferon-induced_IFIT1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 146 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

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.