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Interferon-induced helicase C domain-containing protein 1 (EC 3.6.4.13) (Clinically amyopathic dermatomyositis autoantigen 140 kDa) (CADM-140 autoantigen) (Helicase with 2 CARD domains) (Helicard) (Interferon-induced with helicase C domain protein 1) (Melanoma differentiation-associated protein 5) (MDA-5) (Murabutide down-regulated protein) (RIG-I-like receptor 2) (RLR-2) (RNA helicase-DEAD box protein 116)

 IFIH1_HUMAN             Reviewed;        1025 AA.
Q9BYX4; Q2NKL6; Q6DC96; Q86X56; Q96MX8; Q9H3G6;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 3.
30-AUG-2017, entry version 157.
RecName: Full=Interferon-induced helicase C domain-containing protein 1;
EC=3.6.4.13;
AltName: Full=Clinically amyopathic dermatomyositis autoantigen 140 kDa;
Short=CADM-140 autoantigen;
AltName: Full=Helicase with 2 CARD domains;
Short=Helicard;
AltName: Full=Interferon-induced with helicase C domain protein 1;
AltName: Full=Melanoma differentiation-associated protein 5;
Short=MDA-5;
AltName: Full=Murabutide down-regulated protein;
AltName: Full=RIG-I-like receptor 2;
Short=RLR-2;
AltName: Full=RNA helicase-DEAD box protein 116;
Name=IFIH1; Synonyms=MDA5, RH116;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Melanoma;
PubMed=11805321; DOI=10.1073/pnas.022637199;
Kang D.-C., Gopalkrishnan R.V., Wu Q., Jankowsky E., Pyle A.M.,
Fisher P.B.;
"mda-5: an interferon-inducible putative RNA helicase with double-
stranded RNA-dependent ATPase activity and melanoma growth-suppressive
properties.";
Proc. Natl. Acad. Sci. U.S.A. 99:637-642(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND VARIANT ARG-843.
TISSUE=Spleen;
PubMed=14645903; DOI=10.1099/vir.0.19300-0;
Cocude C., Truong M.-J., Billaut-Mulot O., Delsart V., Darcissac E.,
Capron A., Mouton Y., Bahr G.M.;
"A novel cellular RNA helicase, RH116, differentially regulates cell
growth, programmed cell death and human immunodeficiency virus type 1
replication.";
J. Gen. Virol. 84:3215-3225(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS ARG-843 AND THR-946.
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 475-1025 (ISOFORM 1), AND VARIANTS
ARG-843 AND THR-946.
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
MUTAGENESIS OF ASP-251 AND GLU-444, AND TISSUE SPECIFICITY.
PubMed=12015121; DOI=10.1016/S0960-9822(02)00842-4;
Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K.,
Tschopp J.;
"Overexpression of Helicard, a CARD-containing helicase cleaved during
apoptosis, accelerates DNA degradation.";
Curr. Biol. 12:838-843(2002).
[6]
ERRATUM.
Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K.,
Tschopp J.;
Curr. Biol. 12:1633-1633(2002).
[7]
INTERACTION WITH PARAMYXOVIRUSES V PROTEIN.
PubMed=15563593; DOI=10.1073/pnas.0407639101;
Andrejeva J., Childs K.S., Young D.F., Carlos T.S., Stock N.,
Goodbourn S., Randall R.E.;
"The V proteins of paramyxoviruses bind the IFN-inducible RNA
helicase, mda-5, and inhibit its activation of the IFN-beta
promoter.";
Proc. Natl. Acad. Sci. U.S.A. 101:17264-17269(2004).
[8]
INTERACTION WITH MAVS/IPS1.
PubMed=16127453; DOI=10.1038/ni1243;
Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H.,
Ishii K.J., Takeuchi O., Akira S.;
"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I
interferon induction.";
Nat. Immunol. 6:981-988(2005).
[9]
INTERACTION WITH MAVS/IPS1.
PubMed=16177806; DOI=10.1038/nature04193;
Meylan E., Curran J., Hofmann K., Moradpour D., Binder M.,
Bartenschlager R., Tschopp J.;
"Cardif is an adaptor protein in the RIG-I antiviral pathway and is
targeted by hepatitis C virus.";
Nature 437:1167-1172(2005).
[10]
UBIQUITINATION.
PubMed=17460044; DOI=10.1073/pnas.0611551104;
Arimoto K., Takahashi H., Hishiki T., Konishi H., Fujita T.,
Shimotohno K.;
"Negative regulation of the RIG-I signaling by the ubiquitin ligase
RNF125.";
Proc. Natl. Acad. Sci. U.S.A. 104:7500-7505(2007).
[11]
INTERACTION WITH IKBKE; MAVS AND TKFC.
PubMed=17600090; DOI=10.1073/pnas.0700544104;
Diao F., Li S., Tian Y., Zhang M., Xu L.G., Zhang Y., Wang R.P.,
Chen D., Zhai Z., Zhong B., Tien P., Shu H.B.;
"Negative regulation of MDA5- but not RIG-I-mediated innate antiviral
signaling by the dihydroxyacetone kinase.";
Proc. Natl. Acad. Sci. U.S.A. 104:11706-11711(2007).
[12]
INVOLVEMENT IN CLINICALLY AMYOPATHIC DERMATOMYOSITIS, AND
IDENTIFICATION AS CADM-140 AUTOANTIGEN.
PubMed=19565506; DOI=10.1002/art.24621;
Sato S., Hoshino K., Satoh T., Fujita T., Kawakami Y., Fujita T.,
Kuwana M.;
"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.";
Arthritis Rheum. 60:2193-2200(2009).
[13]
FUNCTION.
PubMed=19211564; DOI=10.1074/jbc.M807365200;
Bamming D., Horvath C.M.;
"Regulation of signal transduction by enzymatically inactive antiviral
RNA helicase proteins MDA5, RIG-I, and LGP2.";
J. Biol. Chem. 284:9700-9712(2009).
[14]
FUNCTION.
PubMed=19656871; DOI=10.1128/JVI.00770-09;
Pichlmair A., Schulz O., Tan C.P., Rehwinkel J., Kato H., Takeuchi O.,
Akira S., Way M., Schiavo G., Reis e Sousa C.;
"Activation of MDA5 requires higher-order RNA structures generated
during virus infection.";
J. Virol. 83:10761-10769(2009).
[15]
INTERACTION WITH PCBP2.
PubMed=19881509; DOI=10.1038/ni.1815;
You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z.;
"PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin
ligase AIP4.";
Nat. Immunol. 10:1300-1308(2009).
[16]
INTERACTION WITH NLRC5.
PubMed=20434986; DOI=10.1016/j.cell.2010.03.040;
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.;
"NLRC5 negatively regulates the NF-kappaB and type I interferon
signaling pathways.";
Cell 141:483-496(2010).
[17]
UBIQUITINATION, AND DEUBIQUITINATION BY USP17L2.
PubMed=20368735; DOI=10.1038/cr.2010.41;
Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.;
"The ubiquitin-specific protease 17 is involved in virus-triggered
type I IFN signaling.";
Cell Res. 20:802-811(2010).
[18]
INVOLVEMENT IN CLINICALLY AMYOPATHIC DERMATOMYOSITIS, IDENTIFICATION
AS CADM-140 AUTOANTIGEN, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20015976; DOI=10.1093/rheumatology/kep375;
Nakashima R., Imura Y., Kobayashi S., Yukawa N., Yoshifuji H.,
Nojima T., Kawabata D., Ohmura K., Usui T., Fujii T., Okawa K.,
Mimori T.;
"The RIG-I-like receptor IFIH1/MDA5 is a dermatomyositis-specific
autoantigen identified by the anti-CADM-140 antibody.";
Rheumatology 49:433-440(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
REVIEW ON FUNCTION.
PubMed=21616437; DOI=10.1016/j.immuni.2011.05.003;
Loo Y.M., Gale M. Jr.;
"Immune signaling by RIG-I-like receptors.";
Immunity 34:680-692(2011).
[22]
REVIEW ON FUNCTION.
PubMed=21884169; DOI=10.1111/j.1600-065X.2011.01052.x;
Kato H., Takahasi K., Fujita T.;
"RIG-I-like receptors: cytoplasmic sensors for non-self RNA.";
Immunol. Rev. 243:91-98(2011).
[23]
FUNCTION.
PubMed=21742966; DOI=10.4049/jimmunol.1100361;
Jiang M., Osterlund P., Sarin L.P., Poranen M.M., Bamford D.H.,
Guo D., Julkunen I.;
"Innate immune responses in human monocyte-derived dendritic cells are
highly dependent on the size and the 5' phosphorylation of RNA
molecules.";
J. Immunol. 187:1713-1721(2011).
[24]
REVIEW ON FUNCTION.
PubMed=20950133; DOI=10.1089/jir.2010.0057;
Onoguchi K., Yoneyama M., Fujita T.;
"Retinoic acid-inducible gene-I-like receptors.";
J. Interferon Cytokine Res. 31:27-31(2011).
[25]
INTERACTION WITH DDX60.
PubMed=21791617; DOI=10.1128/MCB.01368-10;
Miyashita M., Oshiumi H., Matsumoto M., Seya T.;
"DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting
RIG-I-like receptor-mediated signaling.";
Mol. Cell. Biol. 31:3802-3819(2011).
[26]
SUMOYLATION, AND INTERACTION WITH PIAS2-BETA.
PubMed=21156324; DOI=10.1016/j.molimm.2010.09.003;
Fu J., Xiong Y., Xu Y., Cheng G., Tang H.;
"MDA5 is SUMOylated by PIAS2? in the upregulation of type I interferon
signaling.";
Mol. Immunol. 48:415-422(2011).
[27]
REVIEW ON FUNCTION.
PubMed=21245900; DOI=10.1038/ni0211-114;
Garcia-Sastre A.;
"2 methylate or not 2 methylate: viral evasion of the type I
interferon response.";
Nat. Immunol. 12:114-115(2011).
[28]
FUNCTION.
PubMed=21217758; DOI=10.1038/ni.1979;
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.;
"Ribose 2'-O-methylation provides a molecular signature for the
distinction of self and non-self mRNA dependent on the RNA sensor
Mda5.";
Nat. Immunol. 12:137-143(2011).
[29]
SUBUNIT.
PubMed=22160685; DOI=10.1073/pnas.1113651108;
Peisley A., Lin C., Wu B., Orme-Johnson M., Liu M., Walz T., Hur S.;
"Cooperative assembly and dynamic disassembly of MDA5 filaments for
viral dsRNA recognition.";
Proc. Natl. Acad. Sci. U.S.A. 108:21010-21015(2011).
[30]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN US11.
PubMed=22301138; DOI=10.1128/JVI.06713-11;
Xing J., Wang S., Lin R., Mossman K.L., Zheng C.;
"Herpes simplex virus 1 tegument protein US11 downmodulates the RLR
signaling pathway via direct interaction with RIG-I and MDA-5.";
J. Virol. 86:3528-3540(2012).
[31]
INTERACTION WITH ANKRD17.
PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037;
Menning M., Kufer T.A.;
"A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and
Nod2-mediated inflammatory responses.";
FEBS Lett. 587:2137-2142(2013).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
PHOSPHORYLATION AT SER-828, AND MUTAGENESIS OF SER-828 AND THR-829.
PubMed=25865883; DOI=10.1016/j.celrep.2015.03.027;
Takashima K., Oshiumi H., Takaki H., Matsumoto M., Seya T.;
"RIOK3-mediated phosphorylation of MDA5 interferes with its assembly
and attenuates the innate immune response.";
Cell Rep. 11:192-200(2015).
[34]
VARIANT THR-946, AND POSSIBLE ASSOCIATION WITH IDDM19.
PubMed=16699517; DOI=10.1038/ng1800;
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.;
"A genome-wide association study of nonsynonymous SNPs identifies a
type 1 diabetes locus in the interferon-induced helicase (IFIH1)
region.";
Nat. Genet. 38:617-619(2006).
[35]
INVOLVEMENT IN AGS7, VARIANTS AGS7 PHE-372; THR-452 AND HIS-779, AND
CHARACTERIZATION OF VARIANTS AGS7 PHE-372; THR-452 AND HIS-779.
PubMed=24995871; DOI=10.1016/j.ajhg.2014.06.007;
Oda H., Nakagawa K., Abe J., Awaya T., Funabiki M., Hijikata A.,
Nishikomori R., Funatsuka M., Ohshima Y., Sugawara Y., Yasumi T.,
Kato H., Shirai T., Ohara O., Fujita T., Heike T.;
"Aicardi-Goutieres syndrome is caused by IFIH1 mutations.";
Am. J. Hum. Genet. 95:121-125(2014).
[36]
INVOLVEMENT IN AGS7, VARIANTS AGS7 GLY-337; VAL-393; ARG-495; GLN-720;
HIS-779 AND CYS-779, AND CHARACTERIZATION OF VARIANTS AGS7 GLY-337;
VAL-393; ARG-495; GLN-720; HIS-779 AND CYS-779.
PubMed=24686847; DOI=10.1038/ng.2933;
Rice G.I., del Toro Duany Y., Jenkinson E.M., Forte G.M.,
Anderson B.H., Ariaudo G., Bader-Meunier B., Baildam E.M., Battini R.,
Beresford M.W., Casarano M., Chouchane M., Cimaz R., Collins A.E.,
Cordeiro N.J., Dale R.C., Davidson J.E., De Waele L., Desguerre I.,
Faivre L., Fazzi E., Isidor B., Lagae L., Latchman A.R., Lebon P.,
Li C., Livingston J.H., Lourenco C.M., Mancardi M.M.,
Masurel-Paulet A., McInnes I.B., Menezes M.P., Mignot C.,
O'Sullivan J., Orcesi S., Picco P.P., Riva E., Robinson R.A.,
Rodriguez D., Salvatici E., Scott C., Szybowska M., Tolmie J.L.,
Vanderver A., Vanhulle C., Vieira J.P., Webb K., Whitney R.N.,
Williams S.G., Wolfe L.A., Zuberi S.M., Hur S., Crow Y.J.;
"Gain-of-function mutations in IFIH1 cause a spectrum of human disease
phenotypes associated with upregulated type I interferon signaling.";
Nat. Genet. 46:503-509(2014).
[37]
INVOLVEMENT IN SGMRT1, VARIANT SGMRT1 GLN-822, AND CHARACTERIZATION OF
VARIANT SGMRT1 GLN-822.
PubMed=25620204; DOI=10.1016/j.ajhg.2014.12.014;
Rutsch F., MacDougall M., Lu C., Buers I., Mamaeva O., Nitschke Y.,
Rice G.I., Erlandsen H., Kehl H.G., Thiele H., Nurnberg P., Hohne W.,
Crow Y.J., Feigenbaum A., Hennekam R.C.;
"A specific IFIH1 gain-of-function mutation causes Singleton-Merten
syndrome.";
Am. J. Hum. Genet. 96:275-282(2015).
[38]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 893-1017 IN COMPLEX WITH
ZINC IONS.
PubMed=19531363; DOI=10.1016/j.abb.2009.06.008;
Li X., Lu C., Stewart M., Xu H., Strong R.K., Igumenova T., Li P.;
"Structural basis of double-stranded RNA recognition by the RIG-I like
receptor MDA5.";
Arch. Biochem. Biophys. 488:23-33(2009).
[39]
STRUCTURE BY NMR OF 896-1025 IN COMPLEX WITH ZINC IONS.
PubMed=19380577; DOI=10.1074/jbc.M109.007179;
Takahasi K., Kumeta H., Tsuduki N., Narita R., Shigemoto T., Hirai R.,
Yoneyama M., Horiuchi M., Ogura K., Fujita T., Inagaki F.;
"Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal
domains: identification of the RNA recognition loop in RIG-I-like
receptors.";
J. Biol. Chem. 284:17465-17474(2009).
[40]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 277-490.
Structural genomics consortium (SGC);
"Human dech-box RNA helicase mda5 (melanoma differentiation-associated
protein 5), dech-domain.";
Submitted (FEB-2009) to the PDB data bank.
-!- 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.
{ECO:0000269|PubMed:14645903, ECO:0000269|PubMed:19211564,
ECO:0000269|PubMed:19656871, ECO:0000269|PubMed:21217758,
ECO:0000269|PubMed:21742966}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: 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 (via the CARD domains) with TKFC, the interaction is
inhibited by viral infection (PubMed:17600090). Interacts with
PCBP2. Interacts with NLRC5. Interacts with PIAS2-beta. Interacts
with DDX60. Interacts with ANKRD17. Interacts with IKBKE
(PubMed:17600090). 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 herpes simplex virus 1 protein US11; this
interaction prevents the interaction of MAVS/IPS1 to IFIH1.
{ECO:0000269|PubMed:15563593, ECO:0000269|PubMed:16127453,
ECO:0000269|PubMed:16177806, ECO:0000269|PubMed:17600090,
ECO:0000269|PubMed:19380577, ECO:0000269|PubMed:19531363,
ECO:0000269|PubMed:19881509, ECO:0000269|PubMed:20434986,
ECO:0000269|PubMed:21156324, ECO:0000269|PubMed:21791617,
ECO:0000269|PubMed:22160685, ECO:0000269|PubMed:22301138,
ECO:0000269|PubMed:23711367}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-6115771, EBI-6115771;
Q7Z434:MAVS; NbExp=5; IntAct=EBI-6115771, EBI-995373;
P11207:P/V (xeno); NbExp=2; IntAct=EBI-6115771, EBI-6148694;
P30927:P/V (xeno); NbExp=2; IntAct=EBI-6115771, EBI-6599165;
Q9EMA9:P/V (xeno); NbExp=2; IntAct=EBI-6115771, EBI-6598728;
O14730:RIOK3; NbExp=6; IntAct=EBI-6115771, EBI-1047061;
P04487:US11 (xeno); NbExp=4; IntAct=EBI-6115771, EBI-6150681;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11805321,
ECO:0000269|PubMed:14645903}. Nucleus {ECO:0000305}. Note=May be
found in the nucleus, during apoptosis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BYX4-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYX4-2; Sequence=VSP_013337, VSP_013338;
Note=No experimental confirmation available.;
-!- 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.
{ECO:0000269|PubMed:11805321, ECO:0000269|PubMed:12015121,
ECO:0000269|PubMed:14645903}.
-!- INDUCTION: By interferon (IFN) and TNF.
{ECO:0000269|PubMed:11805321}.
-!- PTM: Sumoylated. Sumoylation positively regulates its role in type
I interferon induction and is enhanced by PIAS2-beta.
{ECO:0000269|PubMed:21156324}.
-!- PTM: Ubiquitinated by RNF125, leading to its degradation by the
proteasome (PubMed:17460044). USP17/UPS17L2-dependent
deubiquitination positively regulates the receptor
(PubMed:20368735). {ECO:0000269|PubMed:17460044,
ECO:0000269|PubMed:20368735}.
-!- PTM: 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. {ECO:0000250|UniProtKB:Q8R5F7}.
-!- 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. {ECO:0000269|PubMed:16699517}. Note=Disease
susceptibility may be associated with variations affecting the
gene represented in this entry.
-!- DISEASE: Note=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). {ECO:0000269|PubMed:19565506,
ECO:0000269|PubMed:20015976}.
-!- DISEASE: Aicardi-Goutieres syndrome 7 (AGS7) [MIM:615846]: A form
of Aicardi-Goutieres syndrome, a genetically heterogeneous disease
characterized by cerebral atrophy, leukoencephalopathy,
intracranial calcifications, chronic cerebrospinal fluid (CSF)
lymphocytosis, increased CSF alpha-interferon, and negative
serologic investigations for common prenatal infection. Clinical
features as thrombocytopenia, hepatosplenomegaly and elevated
hepatic transaminases along with intermittent fever may
erroneously suggest an infective process. Severe neurological
dysfunctions manifest in infancy as progressive microcephaly,
spasticity, dystonic posturing and profound psychomotor
retardation. Death often occurs in early childhood.
{ECO:0000269|PubMed:24686847, ECO:0000269|PubMed:24995871}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Singleton-Merten syndrome 1 (SGMRT1) [MIM:182250]: An
autosomal dominant disorder with variable expression. Core
features are marked aortic calcification, dental anomalies,
osteopenia, acro-osteolysis, and to a lesser extend glaucoma,
psoriasis, muscle weakness, and joint laxity. Dental anomalies
include delayed eruption and immature root formation of anterior
permanent teeth, early loss of permanent teeth due to short roots,
acute root resorption, high caries, and aggressive alveolar bone
loss. Additional clinical manifestations include particular facial
characteristics and abnormal joint and muscle ligaments.
{ECO:0000269|PubMed:25620204}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: In HIV-1 infected HeLa-CD4 cells, overexpression of
IFIH1 results in a great increase in the level of secreted viral
p24 protein.
-!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH78180.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAB71141.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF095844; AAG34368.1; -; mRNA.
EMBL; AY017378; AAG54076.1; -; mRNA.
EMBL; BC046208; AAH46208.1; -; mRNA.
EMBL; BC078180; AAH78180.1; ALT_SEQ; mRNA.
EMBL; BC111750; AAI11751.1; -; mRNA.
EMBL; AK056293; BAB71141.1; ALT_INIT; mRNA.
CCDS; CCDS2217.1; -. [Q9BYX4-1]
RefSeq; NP_071451.2; NM_022168.3. [Q9BYX4-1]
UniGene; Hs.163173; -.
PDB; 2RQB; NMR; -; A=896-1025.
PDB; 3B6E; X-ray; 1.60 A; A=277-490.
PDB; 3GA3; X-ray; 1.45 A; A=893-1017.
PDB; 4GL2; X-ray; 3.56 A; A/B=306-1017.
PDBsum; 2RQB; -.
PDBsum; 3B6E; -.
PDBsum; 3GA3; -.
PDBsum; 4GL2; -.
ProteinModelPortal; Q9BYX4; -.
SMR; Q9BYX4; -.
BioGrid; 122082; 15.
DIP; DIP-42607N; -.
IntAct; Q9BYX4; 21.
MINT; MINT-3381993; -.
STRING; 9606.ENSP00000263642; -.
iPTMnet; Q9BYX4; -.
PhosphoSitePlus; Q9BYX4; -.
BioMuta; IFIH1; -.
DMDM; 134047802; -.
EPD; Q9BYX4; -.
MaxQB; Q9BYX4; -.
PaxDb; Q9BYX4; -.
PeptideAtlas; Q9BYX4; -.
PRIDE; Q9BYX4; -.
Ensembl; ENST00000263642; ENSP00000263642; ENSG00000115267. [Q9BYX4-1]
Ensembl; ENST00000421365; ENSP00000408450; ENSG00000115267. [Q9BYX4-2]
GeneID; 64135; -.
KEGG; hsa:64135; -.
UCSC; uc002uce.5; human. [Q9BYX4-1]
CTD; 64135; -.
DisGeNET; 64135; -.
GeneCards; IFIH1; -.
HGNC; HGNC:18873; IFIH1.
HPA; HPA002656; -.
MalaCards; IFIH1; -.
MIM; 182250; phenotype.
MIM; 606951; gene.
MIM; 610155; phenotype.
MIM; 615846; phenotype.
neXtProt; NX_Q9BYX4; -.
OpenTargets; ENSG00000115267; -.
Orphanet; 51; Aicardi-Goutieres syndrome.
PharmGKB; PA134889215; -.
eggNOG; KOG0354; Eukaryota.
eggNOG; COG1111; LUCA.
GeneTree; ENSGT00510000046789; -.
HOGENOM; HOG000230992; -.
HOVERGEN; HBG106019; -.
InParanoid; Q9BYX4; -.
KO; K12647; -.
OMA; YNNIMRR; -.
OrthoDB; EOG091G01PQ; -.
PhylomeDB; Q9BYX4; -.
TreeFam; TF330258; -.
Reactome; R-HSA-168928; RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-918233; TRAF3-dependent IRF activation pathway.
Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-HSA-933543; NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
Reactome; R-HSA-936440; Negative regulators of RIG-I/MDA5 signaling.
ChiTaRS; IFIH1; human.
EvolutionaryTrace; Q9BYX4; -.
GeneWiki; MDA5; -.
GenomeRNAi; 64135; -.
PRO; PR:Q9BYX4; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115267; -.
CleanEx; HS_IFIH1; -.
Genevisible; Q9BYX4; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043021; F:ribonucleoprotein complex binding; IPI:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
GO; GO:0039528; P:cytoplasmic pattern recognition receptor signaling pathway in response to virus; TAS:UniProtKB.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0009597; P:detection of virus; TAS:BHF-UCL.
GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
GO; GO:0039530; P:MDA-5 signaling pathway; IDA:UniProtKB.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IMP:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IMP:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; IMP:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:UniProtKB.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO; GO:0034344; P:regulation of type III interferon production; TAS:UniProtKB.
GO; GO:0009615; P:response to virus; TAS:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR031964; CARD_dom.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR021673; RLR_CTR.
Pfam; PF16739; CARD_2; 2.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF04851; ResIII; 1.
Pfam; PF11648; RIG-I_C-RD; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 6.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51789; RLR_CTR; 1.
1: Evidence at protein level;
3D-structure; Aicardi-Goutieres syndrome; Alternative splicing;
Antiviral defense; ATP-binding; Complete proteome; Cytoplasm;
Diabetes mellitus; Disease mutation; Helicase; Host-virus interaction;
Hydrolase; Immunity; Innate immunity; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc.
CHAIN 1 1025 Interferon-induced helicase C domain-
containing protein 1.
/FTId=PRO_0000102012.
DOMAIN 7 97 CARD 1.
DOMAIN 110 190 CARD 2.
DOMAIN 316 509 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 700 882 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 893 1020 RLR CTR. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 907 907 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 910 910 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 962 962 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 964 964 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
SITE 208 209 Cleavage. {ECO:0000250}.
SITE 216 217 Cleavage. {ECO:0000250}.
SITE 251 252 Cleavage. {ECO:0000250}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R5F7}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R5F7}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R5F7}.
MOD_RES 645 645 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R5F7}.
MOD_RES 828 828 Phosphoserine; by RIOK3.
{ECO:0000269|PubMed:25865883}.
VAR_SEQ 208 221 EIENLSQVDGPQVE -> GICNFTEEDSSNSA (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013337.
VAR_SEQ 222 1025 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_013338.
VARIANT 337 337 R -> G (in AGS7; enhances the interferon
signaling pathway activation; enhances
the stability of filament formation;
enhances dsRNA binding activity; no loss
of ATP hydrolysis; dbSNP:rs587777447).
{ECO:0000269|PubMed:24686847}.
/FTId=VAR_071375.
VARIANT 372 372 L -> F (in AGS7; enhances IFNB1 promoter
activation; loss of ligand-induced
responsiveness; dbSNP:rs587777576).
{ECO:0000269|PubMed:24995871}.
/FTId=VAR_071376.
VARIANT 393 393 D -> V (in AGS7; enhances the interferon
signaling pathway activation; enhances
the stability of filament formation;
enhances dsRNA binding activity; no loss
of ATP hydrolysis; dbSNP:rs587777449).
{ECO:0000269|PubMed:24686847}.
/FTId=VAR_071377.
VARIANT 452 452 A -> T (in AGS7; enhances IFNB1 promoter
activation; loss of ligand-induced
responsiveness; dbSNP:rs587777575).
{ECO:0000269|PubMed:24995871}.
/FTId=VAR_071378.
VARIANT 460 460 H -> R (in dbSNP:rs10930046).
/FTId=VAR_031226.
VARIANT 495 495 G -> R (in AGS7; enhances the interferon
signaling pathway activation; enhances
the stability of filament formation;
enhances dsRNA binding activity; no loss
of ATP hydrolysis; dbSNP:rs672601336).
{ECO:0000269|PubMed:24686847}.
/FTId=VAR_071379.
VARIANT 720 720 R -> Q (in AGS7; enhances the interferon
signaling pathway activation; enhances
the stability of filament formation;
enhances dsRNA binding activity; no loss
of ATP hydrolysis; dbSNP:rs587777445).
{ECO:0000269|PubMed:24686847}.
/FTId=VAR_071380.
VARIANT 779 779 R -> C (in AGS7; enhances the interferon
signaling pathway activation; enhances
the stability of filament formation;
enhances dsRNA binding activity; no loss
of ATP hydrolysis; dbSNP:rs587777448).
{ECO:0000269|PubMed:24686847}.
/FTId=VAR_071381.
VARIANT 779 779 R -> H (in AGS7; enhances the interferon
signaling pathway activation; enhances
the stability of filament formation;
enhances dsRNA binding activity; enhances
IFNB1 promoter activation; no loss of ATP
hydrolysis; dbSNP:rs587777446).
{ECO:0000269|PubMed:24686847,
ECO:0000269|PubMed:24995871}.
/FTId=VAR_071382.
VARIANT 822 822 R -> Q (in SGMRT1; gain-of-function
mutation resulting in enhanced INFB1
induction; dbSNP:rs376048533).
{ECO:0000269|PubMed:25620204}.
/FTId=VAR_073666.
VARIANT 843 843 H -> R (in dbSNP:rs3747517).
{ECO:0000269|PubMed:14645903,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_021594.
VARIANT 946 946 A -> T (associated with susceptibility to
IDDM19; dbSNP:rs1990760).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16699517}.
/FTId=VAR_021595.
MUTAGEN 251 251 D->A: No cleavage and no acceleration of
DNA degradation.
{ECO:0000269|PubMed:12015121}.
MUTAGEN 444 444 E->A: No acceleration of DNA degradation,
no binding to ATP, and no helicase
activity. {ECO:0000269|PubMed:12015121}.
MUTAGEN 828 828 S->A: Promotes multimerization after
polyI:C stimulation; greatly enhances
signaling. {ECO:0000269|PubMed:25865883}.
MUTAGEN 828 828 S->D: Inhibits multimerization after
polyI:C stimulation.
{ECO:0000269|PubMed:25865883}.
MUTAGEN 829 829 T->A: Moderately increases signaling.
{ECO:0000269|PubMed:25865883}.
CONFLICT 439 439 L -> F (in Ref. 2; AAG54076).
{ECO:0000305}.
CONFLICT 475 475 N -> H (in Ref. 4; BAB71141).
{ECO:0000305}.
CONFLICT 592 592 E -> K (in Ref. 1; AAG34368).
{ECO:0000305}.
CONFLICT 598 598 R -> S (in Ref. 2; AAG54076).
{ECO:0000305}.
CONFLICT 609 609 E -> K (in Ref. 2; AAG54076).
{ECO:0000305}.
CONFLICT 782 782 K -> R (in Ref. 4; BAB71141).
{ECO:0000305}.
HELIX 293 299 {ECO:0000244|PDB:3B6E}.
HELIX 310 320 {ECO:0000244|PDB:3B6E}.
STRAND 325 328 {ECO:0000244|PDB:3B6E}.
HELIX 332 352 {ECO:0000244|PDB:3B6E}.
STRAND 359 365 {ECO:0000244|PDB:3B6E}.
HELIX 366 375 {ECO:0000244|PDB:3B6E}.
HELIX 377 381 {ECO:0000244|PDB:3B6E}.
TURN 382 384 {ECO:0000244|PDB:3B6E}.
STRAND 387 389 {ECO:0000244|PDB:3B6E}.
HELIX 400 406 {ECO:0000244|PDB:3B6E}.
STRAND 408 413 {ECO:0000244|PDB:3B6E}.
HELIX 414 422 {ECO:0000244|PDB:3B6E}.
HELIX 434 436 {ECO:0000244|PDB:3B6E}.
STRAND 438 442 {ECO:0000244|PDB:3B6E}.
HELIX 454 473 {ECO:0000244|PDB:3B6E}.
STRAND 483 488 {ECO:0000244|PDB:3B6E}.
HELIX 900 902 {ECO:0000244|PDB:3GA3}.
STRAND 903 907 {ECO:0000244|PDB:3GA3}.
TURN 908 910 {ECO:0000244|PDB:3GA3}.
STRAND 913 916 {ECO:0000244|PDB:3GA3}.
HELIX 917 919 {ECO:0000244|PDB:3GA3}.
STRAND 921 923 {ECO:0000244|PDB:3GA3}.
TURN 924 926 {ECO:0000244|PDB:3GA3}.
STRAND 927 929 {ECO:0000244|PDB:3GA3}.
HELIX 934 937 {ECO:0000244|PDB:3GA3}.
STRAND 938 942 {ECO:0000244|PDB:3GA3}.
TURN 945 947 {ECO:0000244|PDB:3GA3}.
STRAND 955 962 {ECO:0000244|PDB:3GA3}.
STRAND 967 974 {ECO:0000244|PDB:3GA3}.
STRAND 977 982 {ECO:0000244|PDB:3GA3}.
HELIX 984 986 {ECO:0000244|PDB:3GA3}.
STRAND 987 991 {ECO:0000244|PDB:3GA3}.
TURN 992 995 {ECO:0000244|PDB:3GA3}.
STRAND 996 998 {ECO:0000244|PDB:3GA3}.
HELIX 1003 1005 {ECO:0000244|PDB:3GA3}.
HELIX 1015 1017 {ECO:0000244|PDB:3GA3}.
SEQUENCE 1025 AA; 116689 MW; 789CFB4824B92DC9 CRC64;
MSNGYSTDEN FRYLISCFRA RVKMYIQVEP VLDYLTFLPA EVKEQIQRTV ATSGNMQAVE
LLLSTLEKGV WHLGWTREFV EALRRTGSPL AARYMNPELT DLPSPSFENA HDEYLQLLNL
LQPTLVDKLL VRDVLDKCME EELLTIEDRN RIAAAENNGN ESGVRELLKR IVQKENWFSA
FLNVLRQTGN NELVQELTGS DCSESNAEIE NLSQVDGPQV EEQLLSTTVQ PNLEKEVWGM
ENNSSESSFA DSSVVSESDT SLAEGSVSCL DESLGHNSNM GSDSGTMGSD SDEENVAARA
SPEPELQLRP YQMEVAQPAL EGKNIIICLP TGSGKTRVAV YIAKDHLDKK KKASEPGKVI
VLVNKVLLVE QLFRKEFQPF LKKWYRVIGL SGDTQLKISF PEVVKSCDII ISTAQILENS
LLNLENGEDA GVQLSDFSLI IIDECHHTNK EAVYNNIMRH YLMQKLKNNR LKKENKPVIP
LPQILGLTAS PGVGGATKQA KAEEHILKLC ANLDAFTIKT VKENLDQLKN QIQEPCKKFA
IADATREDPF KEKLLEIMTR IQTYCQMSPM SDFGTQPYEQ WAIQMEKKAA KEGNRKERVC
AEHLRKYNEA LQINDTIRMI DAYTHLETFY NEEKDKKFAV IEDDSDEGGD DEYCDGDEDE
DDLKKPLKLD ETDRFLMTLF FENNKMLKRL AENPEYENEK LTKLRNTIME QYTRTEESAR
GIIFTKTRQS AYALSQWITE NEKFAEVGVK AHHLIGAGHS SEFKPMTQNE QKEVISKFRT
GKINLLIATT VAEEGLDIKE CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVAHSGSGV
IEHETVNDFR EKMMYKAIHC VQNMKPEEYA HKILELQMQS IMEKKMKTKR NIAKHYKNNP
SLITFLCKNC SVLACSGEDI HVIEKMHHVN MTPEFKELYI VRENKALQKK CADYQINGEI
ICKCGQAWGT MMVHKGLDLP CLKIRNFVVV FKNNSTKKQY KKWVELPITF PNLDYSECCL
FSDED


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EIAAB07140 ATP-dependent helicase CHD6,CHD5,CHD6,CHD-6,Chromodomain-helicase-DNA-binding protein 6,Homo sapiens,Human,KIAA1335,Radiation-induced gene B protein,RIGB
CSB-EQ028021HU Human Clinically amyopathic dermatomyositis autoantigen 140 kDa antibody(CADM-140 Ab) ELISA kit 96T
18-003-42774 Spliceosome RNA helicase BAT1 - EC 3.6.1.-; DEAD box protein UAP56; 56 kDa U2AF65-associated protein; ATP-dependent RNA helicase p47; HLA-B-associated transcript-1 Polyclonal 0.05 mg Aff Pur
EIAAB46583 ATP-dependent DNA helicase 2 subunit 2,ATP-dependent DNA helicase II 80 kDa subunit,CTC box-binding factor 85 kDa subunit,CTC85,CTCBF,DNA repair protein XRCC5,G22p2,Ku autoantigen protein p86 homolog,
EIAAB10766 DDX21,DEAD box protein 21,Gu-alpha,Homo sapiens,Human,Nucleolar RNA helicase 2,Nucleolar RNA helicase Gu,Nucleolar RNA helicase II,RH II_Gu
EIAAB10765 Ddx21,Ddx21a,DEAD box protein 21,Gu-alpha,Nucleolar RNA helicase 2,Nucleolar RNA helicase Gu,Nucleolar RNA helicase II,Rat,Rattus norvegicus,RH II_Gu
EIAAB10767 Ddx21,DEAD box protein 21,Gu-alpha,Mouse,Mus musculus,Nucleolar RNA helicase 2,Nucleolar RNA helicase Gu,Nucleolar RNA helicase II,RH II_Gu
EIAAB10772 ATP-dependent RNA helicase DDX25,Ddx25,DEAD box protein 25,Gonadotropin-regulated testicular RNA helicase,Grth,Rat,Rattus norvegicus
EIAAB10774 ATP-dependent RNA helicase DDX25,Ddx25,DEAD box protein 25,Gonadotropin-regulated testicular RNA helicase,Grth,Mouse,Mus musculus
20-372-60189 chromodomain helicase DNA binding protein 3 (CHD3). transcript variant 1. mRNA - Mouse monoclonal anti-human CHD3 antibody; EC 3.6.1.-; ATP-dependent helicase CHD3; CHD-3; Mi-2 autoantigen 240 kDa pro 0.1 mg
EIAAB10825 DDX58,DEAD box protein 58,Pig,Probable ATP-dependent RNA helicase DDX58,Retinoic acid-inducible gene 1 protein,Retinoic acid-inducible gene I protein,RHIV-1,RIG-1,RIG-I,RNA helicase induced by virus,S
EIAAB10771 ATP-dependent RNA helicase DDX25,DDX25,DEAD box protein 25,Gonadotropin-regulated testicular RNA helicase,GRTH,Homo sapiens,Human


 

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