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Q9BYX4 (IFIH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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 helicase C domain-containing protein 1

EC=3.6.4.13
Alternative name(s):
Clinically amyopathic dermatomyositis autoantigen 140 kDa
Short name=CADM-140 autoantigen
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
Murabutide down-regulated protein
RIG-I-like receptor 2
Short name=RLR-2
RNA helicase-DEAD box protein 116
Gene names
Name:IFIH1
Synonyms:MDA5, RH116
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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) and mengo encephalomyocarditis virus (ENMG). 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.2 Ref.11 Ref.12 Ref.21 Ref.26

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Zinc.

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 Simian virus 5, Human parainfluenza virus 2, Mumps virus, Sendai virus and Hendra virus. Binding to paramyxoviruses V proteins prevents IFN-beta induction, and the further establishment of an antiviral state. Interacts with PCBP2. Interacts with NLRC5. Interacts with PIAS2-beta. Interacts with DDX60. Ref.7 Ref.8 Ref.9 Ref.13 Ref.14 Ref.23 Ref.24 Ref.27

Subcellular location

Cytoplasm. Nucleus Potential. Note: May be found in the nucleus, during apoptosis. Ref.1 Ref.2

Tissue specificity

Widely expressed, at a low level. Expression is detected at slightly highest levels in placenta, pancreas and spleen and at barely levels in detectable brain, testis and lung. Ref.1 Ref.2 Ref.5

Induction

By interferon (IFN) and TNF. Ref.1

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 By similarity.

Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta. Ref.24

Ubiquitinated. USP17/UPS17L2-dependent deubiquitination positively regulates the receptor. Ref.15

Involvement in disease

Diabetes mellitus, insulin-dependent, 19 (IDDM19) [MIM:610155]: A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry. Ref.28

IFIH1 is the CADM-140 autoantigen, involved in clinically amyopathic dermatomyositis (CADM). This is a chronic inflammatory disorder that shows typical skin manifestations of dermatomyositis but has no or little evidence of clinical myositis. Anti-CADM-140 antibodies appear to be specific to dermatomyositis, especially CADM. Patients with anti-CADM-140 antibodies frequently develop life-threatening acute progressive interstitial lung disease (ILD). Ref.10 Ref.16

Miscellaneous

In HIV-1 infected HeLa-CD4 cells, overexpression of IFIH1 results in a great increase in the level of secreted viral p24 protein.

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 AAH78180.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAB71141.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAntiviral defense
Host-virus interaction
Immunity
Innate immunity
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDiabetes mellitus
   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_processcytoplasmic pattern recognition receptor signaling pathway in response to virus

Traceable author statement Ref.19. Source: UniProtKB

detection of virus

Traceable author statement PubMed 17079289. Source: BHF-UCL

innate immune response

Traceable author statement Ref.19. Source: UniProtKB

negative regulation of type I interferon production

Traceable author statement. Source: Reactome

positive regulation of interferon-alpha production

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of interferon-beta production

Inferred from mutant phenotype Ref.11Ref.12. Source: UniProtKB

protein sumoylation

Inferred from direct assay Ref.24. Source: UniProtKB

regulation of apoptotic process

Inferred from electronic annotation. Source: InterPro

regulation of type III interferon production

Traceable author statement Ref.19. Source: UniProtKB

response to virus

Traceable author statement Ref.19. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

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 direct assay Ref.12. Source: UniProtKB

helicase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.14Ref.24Ref.23. Source: UniProtKB

ribonucleoprotein complex binding

Inferred from physical interaction Ref.13. Source: UniProtKB

single-stranded RNA binding

Inferred from direct assay Ref.12. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.30Ref.29. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MAVSQ7Z4345EBI-6115771,EBI-995373
P/VP112072EBI-6115771,EBI-6148694From a different organism.
P/VP309272EBI-6115771,EBI-6599165From a different organism.
P/VQ9EMA92EBI-6115771,EBI-6598728From a different organism.
US11P044874EBI-6115771,EBI-6150681From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BYX4-1)

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: Q9BYX4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     208-221: EIENLSQVDGPQVE → GICNFTEEDSSNSA
     222-1025: 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_0000102012

Regions

Domain7 – 9791CARD 1
Domain110 – 19081CARD 2
Domain316 – 509194Helicase ATP-binding
Domain700 – 882183Helicase C-terminal

Sites

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

Amino acid modifications

Modified residue6451Phosphoserine By similarity

Natural variations

Alternative sequence208 – 22114EIENL…GPQVE → GICNFTEEDSSNSA in isoform 2.
VSP_013337
Alternative sequence222 – 1025804Missing in isoform 2.
VSP_013338
Natural variant4601H → R.
Corresponds to variant rs10930046 [ dbSNP | Ensembl ].
VAR_031226
Natural variant8431H → R. Ref.2 Ref.3 Ref.4
Corresponds to variant rs3747517 [ dbSNP | Ensembl ].
VAR_021594
Natural variant9461A → T Associated with susceptibility to IDDM19. Ref.3 Ref.4 Ref.28
Corresponds to variant rs1990760 [ dbSNP | Ensembl ].
VAR_021595

Experimental info

Mutagenesis2511D → A: No cleavage and no acceleration of DNA degradation. Ref.5
Mutagenesis4441E → A: No acceleration of DNA degradation, no binding to ATP, and no helicase activity. Ref.5
Sequence conflict4391L → F in AAG54076. Ref.2
Sequence conflict4751N → H in BAB71141. Ref.4
Sequence conflict5921E → K in AAG34368. Ref.1
Sequence conflict5981R → S in AAG54076. Ref.2
Sequence conflict6091E → K in AAG54076. Ref.2
Sequence conflict7821K → R in BAB71141. Ref.4

Secondary structure

............................................................. 1025
Helix Strand Turn

Details...

Sequences

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

Last modified March 20, 2007. Version 3.
Checksum: 789CFB4824B92DC9

FASTA1,025116,689
        10         20         30         40         50         60 
MSNGYSTDEN FRYLISCFRA RVKMYIQVEP VLDYLTFLPA EVKEQIQRTV ATSGNMQAVE 

        70         80         90        100        110        120 
LLLSTLEKGV WHLGWTREFV EALRRTGSPL AARYMNPELT DLPSPSFENA HDEYLQLLNL 

       130        140        150        160        170        180 
LQPTLVDKLL VRDVLDKCME EELLTIEDRN RIAAAENNGN ESGVRELLKR IVQKENWFSA 

       190        200        210        220        230        240 
FLNVLRQTGN NELVQELTGS DCSESNAEIE NLSQVDGPQV EEQLLSTTVQ PNLEKEVWGM 

       250        260        270        280        290        300 
ENNSSESSFA DSSVVSESDT SLAEGSVSCL DESLGHNSNM GSDSGTMGSD SDEENVAARA 

       310        320        330        340        350        360 
SPEPELQLRP YQMEVAQPAL EGKNIIICLP TGSGKTRVAV YIAKDHLDKK KKASEPGKVI 

       370        380        390        400        410        420 
VLVNKVLLVE QLFRKEFQPF LKKWYRVIGL SGDTQLKISF PEVVKSCDII ISTAQILENS 

       430        440        450        460        470        480 
LLNLENGEDA GVQLSDFSLI IIDECHHTNK EAVYNNIMRH YLMQKLKNNR LKKENKPVIP 

       490        500        510        520        530        540 
LPQILGLTAS PGVGGATKQA KAEEHILKLC ANLDAFTIKT VKENLDQLKN QIQEPCKKFA 

       550        560        570        580        590        600 
IADATREDPF KEKLLEIMTR IQTYCQMSPM SDFGTQPYEQ WAIQMEKKAA KEGNRKERVC 

       610        620        630        640        650        660 
AEHLRKYNEA LQINDTIRMI DAYTHLETFY NEEKDKKFAV IEDDSDEGGD DEYCDGDEDE 

       670        680        690        700        710        720 
DDLKKPLKLD ETDRFLMTLF FENNKMLKRL AENPEYENEK LTKLRNTIME QYTRTEESAR 

       730        740        750        760        770        780 
GIIFTKTRQS AYALSQWITE NEKFAEVGVK AHHLIGAGHS SEFKPMTQNE QKEVISKFRT 

       790        800        810        820        830        840 
GKINLLIATT VAEEGLDIKE CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVAHSGSGV 

       850        860        870        880        890        900 
IEHETVNDFR EKMMYKAIHC VQNMKPEEYA HKILELQMQS IMEKKMKTKR NIAKHYKNNP 

       910        920        930        940        950        960 
SLITFLCKNC SVLACSGEDI HVIEKMHHVN MTPEFKELYI VRENKALQKK CADYQINGEI 

       970        980        990       1000       1010       1020 
ICKCGQAWGT MMVHKGLDLP CLKIRNFVVV FKNNSTKKQY KKWVELPITF PNLDYSECCL 


FSDED 

« Hide

Isoform 2 [UniParc].

Checksum: 3C7139ECAC564BB5
Show »

FASTA22125,129

References

« Hide 'large scale' references
[1]"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), INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Melanoma.
[2]"A novel cellular RNA helicase, RH116, differentially regulates cell growth, programmed cell death and human immunodeficiency virus type 1 replication."
Cocude C., Truong M.-J., Billaut-Mulot O., Delsart V., Darcissac E., Capron A., Mouton Y., Bahr G.M.
J. Gen. Virol. 84:3215-3225(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ARG-843.
Tissue: Spleen.
[3]"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] (ISOFORMS 1 AND 2), VARIANTS ARG-843 AND THR-946.
Tissue: Uterus.
[4]"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 [MRNA] OF 475-1025 (ISOFORM 1), VARIANTS ARG-843 AND THR-946.
[5]"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: MUTAGENESIS OF ASP-251 AND GLU-444, TISSUE SPECIFICITY.
[6]Erratum
Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J.
Curr. Biol. 12:1633-1633(2002)
[7]"The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter."
Andrejeva J., Childs K.S., Young D.F., Carlos T.S., Stock N., Goodbourn S., Randall R.E.
Proc. Natl. Acad. Sci. U.S.A. 101:17264-17269(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARAMYXOVIRUSES V PROTEIN.
[8]"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction."
Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J., Takeuchi O., Akira S.
Nat. Immunol. 6:981-988(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAVS/IPS1.
[9]"Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus."
Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J.
Nature 437:1167-1172(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAVS/IPS1.
[10]"RNA helicase encoded by melanoma differentiation-associated gene 5 is a major autoantigen in patients with clinically amyopathic dermatomyositis: Association with rapidly progressive interstitial lung disease."
Sato S., Hoshino K., Satoh T., Fujita T., Kawakami Y., Fujita T., Kuwana M.
Arthritis Rheum. 60:2193-2200(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CLINICALLY AMYOPATHIC DERMATOMYOSITIS, IDENTIFICATION AS CADM-140 AUTOANTIGEN.
[11]"Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2."
Bamming D., Horvath C.M.
J. Biol. Chem. 284:9700-9712(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"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.
[13]"PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4."
You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.
Nat. Immunol. 10:1300-1308(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCBP2.
[14]"NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways."
Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., Ji J., Shen P., Zheng S., Chen Z.J., Wang R.F.
Cell 141:483-496(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NLRC5.
[15]"The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling."
Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.
Cell Res. 20:802-811(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP17L2.
[16]"The RIG-I-like receptor IFIH1/MDA5 is a dermatomyositis-specific autoantigen identified by the anti-CADM-140 antibody."
Nakashima R., Imura Y., Kobayashi S., Yukawa N., Yoshifuji H., Nojima T., Kawabata D., Ohmura K., Usui T., Fujii T., Okawa K., Mimori T.
Rheumatology 49:433-440(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CLINICALLY AMYOPATHIC DERMATOMYOSITIS, IDENTIFICATION AS CADM-140 AUTOANTIGEN, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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.
[20]"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.
[21]"Innate immune responses in human monocyte-derived dendritic cells are highly dependent on the size and the 5' phosphorylation of RNA molecules."
Jiang M., Osterlund P., Sarin L.P., Poranen M.M., Bamford D.H., Guo D., Julkunen I.
J. Immunol. 187:1713-1721(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"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.
[23]"DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling."
Miyashita M., Oshiumi H., Matsumoto M., Seya T.
Mol. Cell. Biol. 31:3802-3819(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDX60.
[24]"MDA5 is SUMOylated by PIAS2? in the upregulation of type I interferon signaling."
Fu J., Xiong Y., Xu Y., Cheng G., Tang H.
Mol. Immunol. 48:415-422(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION, INTERACTION WITH PIAS2-BETA.
[25]"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.
[26]"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.
[27]"Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition."
Peisley A., Lin C., Wu B., Orme-Johnson M., Liu M., Walz T., Hur S.
Proc. Natl. Acad. Sci. U.S.A. 108:21010-21015(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[28]"A genome-wide association study of nonsynonymous SNPs identifies a type 1 diabetes locus in the interferon-induced helicase (IFIH1) region."
Smyth D.J., Cooper J.D., Bailey R., Field S., Burren O., Smink L.J., Guja C., Ionescu-Tirgoviste C., Widmer B., Dunger D.B., Savage D.A., Walker N.M., Clayton D.G., Todd J.A.
Nat. Genet. 38:617-619(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-946, ASSOCIATION WITH IDDM19.
[29]"Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5."
Li X., Lu C., Stewart M., Xu H., Strong R.K., Igumenova T., Li P.
Arch. Biochem. Biophys. 488:23-33(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 893-1017 IN COMPLEX WITH ZINC IONS.
[30]"Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors."
Takahasi K., Kumeta H., Tsuduki N., Narita R., Shigemoto T., Hirai R., Yoneyama M., Horiuchi M., Ogura K., Fujita T., Inagaki F.
J. Biol. Chem. 284:17465-17474(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 896-1025 IN COMPLEX WITH ZINC IONS.
[31]"Human dech-box RNA helicase mda5 (melanoma differentiation-associated protein 5), dech-domain."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 277-490.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF095844 mRNA. Translation: AAG34368.1.
AY017378 mRNA. Translation: AAG54076.1.
BC046208 mRNA. Translation: AAH46208.1.
BC078180 mRNA. Translation: AAH78180.1. Sequence problems.
BC111750 mRNA. Translation: AAI11751.1.
AK056293 mRNA. Translation: BAB71141.1. Different initiation.
CCDSCCDS2217.1. [Q9BYX4-1]
RefSeqNP_071451.2. NM_022168.3. [Q9BYX4-1]
UniGeneHs.163173.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQBNMR-A896-1025[»]
3B6EX-ray1.60A277-490[»]
3GA3X-ray1.45A893-1017[»]
4GL2X-ray3.56A/B306-1017[»]
ProteinModelPortalQ9BYX4.
SMRQ9BYX4. Positions 4-199, 292-1025.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122082. 11 interactions.
DIPDIP-42607N.
IntActQ9BYX4. 15 interactions.
MINTMINT-3381993.
STRING9606.ENSP00000263642.

PTM databases

PhosphoSiteQ9BYX4.

Polymorphism databases

DMDM134047802.

Proteomic databases

MaxQBQ9BYX4.
PaxDbQ9BYX4.
PRIDEQ9BYX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263642; ENSP00000263642; ENSG00000115267. [Q9BYX4-1]
ENST00000421365; ENSP00000408450; ENSG00000115267. [Q9BYX4-2]
GeneID64135.
KEGGhsa:64135.
UCSCuc002uce.4. human. [Q9BYX4-1]
uc002ucf.4. human. [Q9BYX4-2]

Organism-specific databases

CTD64135.
GeneCardsGC02M163123.
HGNCHGNC:18873. IFIH1.
HPAHPA002656.
MIM606951. gene.
610155. phenotype.
neXtProtNX_Q9BYX4.
PharmGKBPA134889215.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1111.
HOGENOMHOG000230992.
HOVERGENHBG106019.
InParanoidQ9BYX4.
KOK12647.
OMAKCGQAWG.
OrthoDBEOG7RV9FC.
PhylomeDBQ9BYX4.
TreeFamTF330258.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9BYX4.
BgeeQ9BYX4.
CleanExHS_IFIH1.
GenevestigatorQ9BYX4.

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]
SUPFAMSSF52540. SSF52540. 6 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIFIH1. human.
EvolutionaryTraceQ9BYX4.
GeneWikiMDA5.
GenomeRNAi64135.
NextBio66034.
PROQ9BYX4.
SOURCESearch...

Entry information

Entry nameIFIH1_HUMAN
AccessionPrimary (citable) accession number: Q9BYX4
Secondary accession number(s): Q2NKL6 expand/collapse secondary AC list , Q6DC96, Q86X56, Q96MX8, Q9H3G6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 20, 2007
Last modified: July 9, 2014
This is version 125 of the entry and version 3 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 2

Human chromosome 2: entries, gene names and cross-references to MIM