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Q8R5F7 (IFIH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-induced helicase C domain-containing protein 1

EC=3.6.4.13
Alternative name(s):
Helicase with 2 CARD domains
Short name=Helicard
Interferon induced with helicase C domain protein 1
Melanoma differentiation-associated protein 5
Short name=MDA-5
RIG-I-like receptor 2
Short name=RLR-2
Gene names
Name:Ifih1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and theiler's murine encephalomyelitis virus (TMEV). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines. Ref.1 Ref.7 Ref.9 Ref.11 Ref.16

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Zinc By similarity.

Subunit structure

Monomer in the absence of ligands and homodimerizes in the presence of dsRNA ligands. Can assemble into helical or linear polymeric filaments on long dsRNA. Interacts with MAVS/IPS1. Interacts with V protein of Sendai virus. Binding to paramyxoviruses V proteins prevents IFN-beta induction, and the further establishment of an antiviral state By similarity. Interacts with PCBP2 By similarity. Interacts with NLRC5 By similarity. Interacts with PIAS2-beta By similarity. Interacts with DDX60 By similarity. Ref.17

Subcellular location

Cytoplasm. Nucleus Potential. Note: May be found in the nucleus, during apoptosis. Ref.1

Tissue specificity

Expression is prominent in lung, liver, kidney, heart and spleen (at protein level). Widely expressed at low level. Ref.1

Induction

By interferon (IFN).

Post-translational modification

During apoptosis, processed into 3 cleavage products. The helicase-containing fragment, once liberated from the CARD domains, translocate from the cytoplasm to the nucleus. The processed protein significantly sensitizes cells to DNA degradation.

Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta By similarity.

Ubiquitinated. USP17L2/USP17-dependent deubiquitination positively regulates the receptor By similarity.

Sequence similarities

Belongs to the helicase family. RLR subfamily.

Contains 2 CARD domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence AAH25508.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Inferred from mutant phenotype Ref.9. Source: UniProtKB

positive regulation of interferon-alpha production

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of interferon-beta production

Inferred from sequence or structural similarity. Source: UniProtKB

protein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

response to virus

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: InterPro

double-stranded RNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 21791617. Source: MGI

ribonucleoprotein complex binding

Inferred from electronic annotation. Source: Ensembl

single-stranded RNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8R5F7-1)

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: Q8R5F7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     207-255: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10251025Interferon-induced helicase C domain-containing protein 1
PRO_0000102013

Regions

Domain7 – 9791CARD 1
Domain110 – 19081CARD 2
Domain317 – 510194Helicase ATP-binding
Domain700 – 872173Helicase C-terminal

Sites

Metal binding9071Zinc By similarity
Metal binding9101Zinc By similarity
Metal binding9621Zinc By similarity
Metal binding9641Zinc By similarity
Site208 – 2092Cleavage
Site216 – 2172Cleavage
Site251 – 2522Cleavage

Amino acid modifications

Modified residue6451Phosphoserine Ref.8
Modified residue6481Phosphoserine Ref.8

Natural variations

Alternative sequence207 – 25549Missing in isoform 2.
VSP_013339

Experimental info

Sequence conflict1001T → I in AAH80200. Ref.6
Sequence conflict3391V → E in BAE31652. Ref.4
Sequence conflict412 – 4143IST → TRP in AAH25508. Ref.6
Sequence conflict6241Y → H in AAH25508. Ref.6
Sequence conflict6291T → A in AAM21359. Ref.3
Sequence conflict6471K → E in AAH25508. Ref.6
Sequence conflict6471K → E in AAH04031. Ref.6
Sequence conflict6471K → E in AAH80200. Ref.6
Sequence conflict8891K → E in BAB31303. Ref.4

Secondary structure

............. 1025
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2002. Version 1.
Checksum: 708FCAC690C9F6D8

FASTA1,025115,971
        10         20         30         40         50         60 
MSIVCSAEDS FRNLILFFRP RLKMYIQVEP VLDHLIFLSA ETKEQILKKI NTCGNTSAAE 

        70         80         90        100        110        120 
LLLSTLEQGQ WPLGWTQMFV EALEHSGNPL AARYVKPTLT DLPSPSSETA HDECLHLLTL 

       130        140        150        160        170        180 
LQPTLVDKLL INDVLDTCFE KGLLTVEDRN RISAAGNSGN ESGVRELLRR IVQKENWFST 

       190        200        210        220        230        240 
FLDVLRQTGN DALFQELTGG GCPEDNTDLA NSSHRDGPAA NECLLPAVDE SSLETEAWNV 

       250        260        270        280        290        300 
DDILPEASCT DSSVTTESDT SLAEGSVSCF DESLGHNSNM GRDSGTMGSD SDESVIQTKR 

       310        320        330        340        350        360 
VSPEPELQLR PYQMEVAQPA LDGKNIIICL PTGSGKTRVA VYITKDHLDK KKQASESGKV 

       370        380        390        400        410        420 
IVLVNKVMLA EQLFRKEFNP YLKKWYRIIG LSGDTQLKIS FPEVVKSYDV IISTAQILEN 

       430        440        450        460        470        480 
SLLNLESGDD DGVQLSDFSL IIIDECHHTN KEAVYNNIMR RYLKQKLRNN DLKKQNKPAI 

       490        500        510        520        530        540 
PLPQILGLTA SPGVGAAKKQ SEAEKHILNI CANLDAFTIK TVKENLGQLK HQIKEPCKKF 

       550        560        570        580        590        600 
VIADDTRENP FKEKLLEIMA SIQTYCQKSP MSDFGTQHYE QWAIQMEKKA AKDGNRKDRV 

       610        620        630        640        650        660 
CAEHLRKYNE ALQINDTIRM IDAYSHLETF YTDEKEKKFA VLNDSDKSDD EASSCNDQLK 

       670        680        690        700        710        720 
GDVKKSLKLD ETDEFLMNLF FDNKKMLKKL AENPKYENEK LIKLRNTILE QFTRSEESSR 

       730        740        750        760        770        780 
GIIFTKTRQS TYALSQWIME NAKFAEVGVK AHHLIGAGHS SEVKPMTQTE QKEVISKFRT 

       790        800        810        820        830        840 
GEINLLIATT VAEEGLDIKE CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVTSSGSGV 

       850        860        870        880        890        900 
TEREIVNDFR EKMMYKAINR VQNMKPEEYA HKILELQVQS ILEKKMKVKR SIAKQYNDNP 

       910        920        930        940        950        960 
SLITLLCKNC SMLVCSGENI HVIEKMHHVN MTPEFKGLYI VRENKALQKK FADYQTNGEI 

       970        980        990       1000       1010       1020 
ICKCGQAWGT MMVHKGLDLP CLKIRNFVVN FKNNSPKKQY KKWVELPIRF PDLDYSEYCL 


YSDED 

« Hide

Isoform 2 [UniParc].

Checksum: B9F6D84C207F1031
Show »

FASTA976110,842

References

« Hide 'large scale' references
[1]"Overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation."
Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J.
Curr. Biol. 12:838-843(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CLEAVAGE SITES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]Erratum
Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J.
Curr. Biol. 12:1633-1633(2002)
[3]"mda-5: an interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties."
Kang D.-C., Gopalkrishnan R.V., Wu Q., Jankowsky E., Pyle A.M., Fisher P.B.
Proc. Natl. Acad. Sci. U.S.A. 99:637-642(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone marrow, Cecum, Thymus and Vagina.
[5]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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 2).
Strain: FVB/N.
Tissue: Mammary gland.
[7]"Differential roles of MDA5 and RIG-I helicases in the recognition of RNA viruses."
Kato H., Takeuchi O., Sato S., Yoneyama M., Yamamoto M., Matsui K., Uematsu S., Jung A., Kawai T., Ishii K.J., Yamaguchi O., Otsu K., Tsujimura T., Koh C.S., Reis e Sousa C., Matsuura Y., Fujita T., Akira S.
Nature 441:101-105(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Distinct RIG-I and MDA5 signaling by RNA viruses in innate immunity."
Loo Y.M., Fornek J., Crochet N., Bajwa G., Perwitasari O., Martinez-Sobrido L., Akira S., Gill M.A., Garcia-Sastre A., Katze M.G., Gale M. Jr.
J. Virol. 82:335-345(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Activation of MDA5 requires higher-order RNA structures generated during virus infection."
Pichlmair A., Schulz O., Tan C.P., Rehwinkel J., Kato H., Takeuchi O., Akira S., Way M., Schiavo G., Reis e Sousa C.
J. Virol. 83:10761-10769(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Immune signaling by RIG-I-like receptors."
Loo Y.M., Gale M. Jr.
Immunity 34:680-692(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[13]"RIG-I-like receptors: cytoplasmic sensors for non-self RNA."
Kato H., Takahasi K., Fujita T.
Immunol. Rev. 243:91-98(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[14]"Retinoic acid-inducible gene-I-like receptors."
Onoguchi K., Yoneyama M., Fujita T.
J. Interferon Cytokine Res. 31:27-31(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[15]"2 methylate or not 2 methylate: viral evasion of the type I interferon response."
Garcia-Sastre A.
Nat. Immunol. 12:114-115(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[16]"Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5."
Zuest R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W., Ziebuhr J., Szretter K.J., Baker S.C., Barchet W., Diamond M.S., Siddell S.G., Ludewig B., Thiel V.
Nat. Immunol. 12:137-143(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA."
Berke I.C., Modis Y.
EMBO J. 31:1714-1726(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 545-697, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY075132 mRNA. Translation: AAL77205.1.
AF374384 mRNA. Translation: AAM21359.1.
AK018602 mRNA. Translation: BAB31303.2.
AK037057 mRNA. Translation: BAC29687.2.
AK040519 mRNA. Translation: BAC30614.1.
AK153018 mRNA. Translation: BAE31652.1.
AL929246 Genomic DNA. Translation: CAM21790.1.
BC004031 mRNA. Translation: AAH04031.1.
BC019605 mRNA. Translation: AAH19605.1.
BC025508 mRNA. Translation: AAH25508.1. Different initiation.
BC080200 mRNA. Translation: AAH80200.1.
CCDSCCDS16068.1. [Q8R5F7-1]
CCDS50594.1. [Q8R5F7-2]
RefSeqNP_001157949.1. NM_001164477.1. [Q8R5F7-2]
NP_082111.2. NM_027835.3. [Q8R5F7-1]
UniGeneMm.136224.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3TS9X-ray2.00A545-697[»]
ProteinModelPortalQ8R5F7.
SMRQ8R5F7. Positions 8-199, 300-1025.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid214799. 1 interaction.
DIPDIP-60085N.
IntActQ8R5F7. 1 interaction.
MINTMINT-4118007.

PTM databases

PhosphoSiteQ8R5F7.

Proteomic databases

MaxQBQ8R5F7.
PaxDbQ8R5F7.
PRIDEQ8R5F7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028259; ENSMUSP00000028259; ENSMUSG00000026896. [Q8R5F7-1]
ENSMUST00000112459; ENSMUSP00000108078; ENSMUSG00000026896. [Q8R5F7-2]
GeneID71586.
KEGGmmu:71586.
UCSCuc008jvm.2. mouse. [Q8R5F7-1]
uc012bvy.1. mouse. [Q8R5F7-2]

Organism-specific databases

CTD64135.
MGIMGI:1918836. Ifih1.

Phylogenomic databases

eggNOGCOG1111.
GeneTreeENSGT00510000046789.
HOVERGENHBG106019.
InParanoidA2AUY7.
KOK12647.
OMAKCGQAWG.
OrthoDBEOG7RV9FC.
PhylomeDBQ8R5F7.
TreeFamTF330258.

Gene expression databases

ArrayExpressQ8R5F7.
BgeeQ8R5F7.
CleanExMM_IFIH1.
GenevestigatorQ8R5F7.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR021673. RIG-I_C-RD.
[Graphical view]
PfamPF00619. CARD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio334053.
PROQ8R5F7.
SOURCESearch...

Entry information

Entry nameIFIH1_MOUSE
AccessionPrimary (citable) accession number: Q8R5F7
Secondary accession number(s): A2AUY7 expand/collapse secondary AC list , Q3U6S2, Q68EM4, Q8BYC9, Q8BZ01, Q8K5C7, Q8R144, Q8VE79, Q99KS4, Q9D2Z5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot