Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Probable ATP-dependent RNA helicase DDX58 (EC 3.6.4.13) (DEAD box protein 58) (RIG-I-like receptor 1) (RLR-1) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I)

 DDX58_MOUSE             Reviewed;         926 AA.
Q6Q899; A2AP28; Q8C320; Q8C5I3; Q8C7T2;
08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 136.
RecName: Full=Probable ATP-dependent RNA helicase DDX58;
EC=3.6.4.13;
AltName: Full=DEAD box protein 58;
AltName: Full=RIG-I-like receptor 1;
Short=RLR-1;
AltName: Full=Retinoic acid-inducible gene 1 protein;
Short=RIG-1;
AltName: Full=Retinoic acid-inducible gene I protein;
Short=RIG-I;
Name=Ddx58;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wei J., Gu J.;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
FUNCTION.
PubMed=16039576; DOI=10.1016/j.immuni.2005.04.010;
Kato H., Sato S., Yoneyama M., Yamamoto M., Uematsu S., Matsui K.,
Tsujimura T., Takeda K., Fujita T., Takeuchi O., Akira S.;
"Cell type-specific involvement of RIG-I in antiviral response.";
Immunity 23:19-28(2005).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16625202; DOI=10.1038/nature04734;
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.;
"Differential roles of MDA5 and RIG-I helicases in the recognition of
RNA viruses.";
Nature 441:101-105(2006).
[7]
FUNCTION.
PubMed=17942531; DOI=10.1128/JVI.01080-07;
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.;
"Distinct RIG-I and MDA5 signaling by RNA viruses in innate
immunity.";
J. Virol. 82:335-345(2008).
[8]
FUNCTION.
PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
Chiu Y.-H., Macmillan J.B., Chen Z.J.;
"RNA polymerase III detects cytosolic DNA and induces type I
interferons through the RIG-I pathway.";
Cell 138:576-591(2009).
[9]
FUNCTION.
PubMed=19576794; DOI=10.1016/j.immuni.2009.05.008;
Schlee M., Roth A., Hornung V., Hagmann C.A., Wimmenauer V.,
Barchet W., Coch C., Janke M., Mihailovic A., Wardle G., Juranek S.,
Kato H., Kawai T., Poeck H., Fitzgerald K.A., Takeuchi O., Akira S.,
Tuschl T., Latz E., Ludwig J., Hartmann G.;
"Recognition of 5' triphosphate by RIG-I helicase requires short blunt
double-stranded RNA as contained in panhandle of negative-strand
virus.";
Immunity 31:25-34(2009).
[10]
FUNCTION.
PubMed=19609254; DOI=10.1038/ni.1779;
Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A.,
Hornung V.;
"RIG-I-dependent sensing of poly(dA:dT) through the induction of an
RNA polymerase III-transcribed RNA intermediate.";
Nat. Immunol. 10:1065-1072(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[12]
REVIEW ON FUNCTION.
PubMed=21175414; DOI=10.1615/CritRevImmunol.v30.i6.10;
Matsumiya T., Stafforini D.M.;
"Function and regulation of retinoic acid-inducible gene-I.";
Crit. Rev. Immunol. 30:489-513(2010).
[13]
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).
[14]
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).
[15]
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).
[16]
REVIEW ON FUNCTION.
PubMed=21496944; DOI=10.1016/j.ejcb.2011.01.015;
Schmidt A., Rothenfusser S., Hopfner K.P.;
"Sensing of viral nucleic acids by RIG-I: from translocation to
translation.";
Eur. J. Cell Biol. 91:78-85(2012).
[17]
INTERACTION WITH SIGLEC10; CBL AND PTPN11, UBIQUITINATION AT LYS-813,
AND MUTAGENESIS OF LYS-813.
PubMed=23374343; DOI=10.1016/j.cell.2013.01.011;
Chen W., Han C., Xie B., Hu X., Yu Q., Shi L., Wang Q., Li D.,
Wang J., Zheng P., Liu Y., Cao X.;
"Induction of Siglec-G by RNA viruses inhibits the innate immune
response by promoting RIG-I degradation.";
Cell 152:467-478(2013).
-!- 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: 5'-
triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in
length). In addition to the 5'-triphosphate moiety, blunt-end base
pairing at the 5'-end of the RNA is very essential. Overhangs at
the non-triphosphorylated end of the dsRNA RNA have no major
impact on its activity. A 3'overhang at the 5'triphosphate end
decreases and any 5'overhang at the 5' triphosphate end abolishes
its activity. 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. Detects both positive
and negative strand RNA viruses including members of the families
Paramyxoviridae: newcastle disease virus (NDV) and Sendai virus
(SeV), Rhabdoviridae: vesicular stomatitis virus (VSV),
Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese
encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus
(DENV) and west Nile virus (WNV). It also detects rotavirus and
orthoreovirus. Also involved in antiviral signaling in response to
viruses containing a dsDNA genome such as Epstein-Barr virus
(EBV). Detects dsRNA produced from non-self dsDNA by RNA
polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs).
May play important roles in granulocyte production and
differentiation, bacterial phagocytosis and in the regulation of
cell migration. {ECO:0000269|PubMed:16039576,
ECO:0000269|PubMed:16625202, ECO:0000269|PubMed:17942531,
ECO:0000269|PubMed:19576794, ECO:0000269|PubMed:19609254,
ECO:0000269|PubMed:19631370}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Monomer; maintained as a monomer in an autoinhibited
state. Upon viral dsRNA binding and conformation shift,
homomultimerizes and interacts (via tandem CARD domain) with
MAVS/IPS1 promoting its filamentation. Interacts with DHX58/LGP2,
IKBKE, TBK1 and TMEM173/STING. Interacts (via CARD domain) with
TRIM25 (via SPRY domain). Interacts with RNF135. Interacts with
CYLD. Interacts with NLRC5; blocks the interaction of MAVS/IPS1 to
DDX58. Interacts with SRC. Interacts with DDX60. Interacts with
isoform 2 of ZC3HAV1 (via zinc-fingers) in an RNA-dependent
manner. Interacts (via tandem CARD domain) with SEC14L1; the
interaction is direct and impairs the interaction of DDX58 with
MAVS/IPS1. Interacts with VCP/p97; interaction is direct and leads
to recruit RNF125 and subsequent ubiquitination and degradation
(By similarity). Interacts with NOP53; may regulate DDX58 through
USP15-mediated 'Lys-63'-linked deubiquitination (By similarity).
Interacts with SIGLEC10, CBL and PTPN11; these interactions are
involved in 'Lys-48'-linked deubiquitination and degradation
following infection with RNA viruses (PubMed:23374343). Interacts
with LRRC25. {ECO:0000250|UniProtKB:O95786,
ECO:0000269|PubMed:23374343}.
-!- INTERACTION:
P22682:Cbl; NbExp=3; IntAct=EBI-6841237, EBI-640919;
Q80ZE3:Siglec10; NbExp=7; IntAct=EBI-6841237, EBI-6841023;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell projection,
ruffle membrane {ECO:0000250}. Cytoplasm, cytoskeleton
{ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
Note=Colocalized with TRIM25 at cytoplasmic perinuclear bodies.
Associated with the actin cytoskeleton at membrane ruffles.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q6Q899-1; Sequence=Displayed;
Name=2;
IsoId=Q6Q899-2; Sequence=VSP_016055, VSP_016060;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q6Q899-3; Sequence=VSP_016058, VSP_016059;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q6Q899-4; Sequence=VSP_016056, VSP_016057;
Note=No experimental confirmation available.;
-!- INDUCTION: By interferon (IFN).
-!- DOMAIN: The helicase domain is responsible for dsRNA recognition.
Interacts with IFIT3 (via N-terminus). {ECO:0000250}.
-!- DOMAIN: The 2 CARD domains are responsible for interaction with
and signaling through MAVS/IPS1 and for association with the actin
cytoskeleton. {ECO:0000250}.
-!- DOMAIN: The RLR CTR domain controls homomultimerization and
interaction with MAVS/IPS1. In the absence of viral infection, the
protein is maintained as a monomer in an autoinhibited state with
the CARD domains masked through intramolecular interactions
mediated by the RLR CTR domain. Upon binding to viral RNA in the
presence of ATP, the RLR CTR domain induces a conformational
change exposing the CARD domain and promotes dimerization and CARD
interactions with the adapter protein MAVS/IPS1 leading to the
induction of downstream signaling.
-!- DOMAIN: The second CARD domain is the primary site for 'Lys-63'-
linked ubiquitination. {ECO:0000250}.
-!- PTM: Phosphorylated in resting cells and dephosphorylated in RNA
virus-infected cells. Phosphorylation at Thr-771 results in
inhibition of its activity while dephosphorylation at these sites
results in its activation. {ECO:0000250|UniProtKB:O95786}.
-!- PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon
IFN-beta stimulation. ISGylation negatively regulates its function
in antiviral signaling response. {ECO:0000250|UniProtKB:O95786}.
-!- PTM: Sumoylated, probably by MUL1; inhibiting its
polyubiquitination. {ECO:0000250|UniProtKB:O95786}.
-!- PTM: Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked
ubiquitination. Lys-154 and Lys-164 are critical sites for RNF135-
mediated and TRIM4-mediated ubiquitination. Deubiquitinated by
CYLD, a protease that selectively cleaves 'Lys-63'-linked
ubiquitin chains. Also probably deubiquitinated by USP17L2/USP17
that cleaves 'Lys-48'-and 'Lys-63'-linked ubiquitin chains and
positively regulates the receptor. Ubiquitinated at Lys-181 by
RNF125, leading to its degradation: ubiquitination takes place
upon viral infection and is enhanced 'Lys-63'-linked
ubiquitination of the CARD domains, which promote interaction with
VCP/p97 and subsequent recruitment of RNF125 (By similarity).
Ubiquitinated at Lys-813 by CBL, leading to its degradation:
ubiquitination takes place upon viral infection and involves 'Lys-
48'-linked ubiquitination (PubMed:23374343).
{ECO:0000250|UniProtKB:O95786, ECO:0000269|PubMed:23374343}.
-!- DISRUPTION PHENOTYPE: Death between E12.5 and E14 due to liver
apoptosis. Those who are born alive show growth retardation and
die within 3 weeks. {ECO:0000269|PubMed:16625202}.
-!- SIMILARITY: Belongs to the helicase family. RLR subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AY553221; AAS59532.1; -; mRNA.
EMBL; AL831793; CAM27574.1; -; Genomic_DNA.
EMBL; CH466538; EDL05445.1; -; Genomic_DNA.
EMBL; AK049305; BAC33670.1; -; mRNA.
EMBL; AK078287; BAC37205.1; -; mRNA.
EMBL; AK087261; BAC39830.1; -; mRNA.
CCDS; CCDS18043.1; -. [Q6Q899-1]
RefSeq; NP_766277.3; NM_172689.3. [Q6Q899-1]
UniGene; Mm.86382; -.
PDB; 3TBK; X-ray; 2.14 A; A=240-794.
PDB; 6BZH; X-ray; 2.50 A; A/B/C/D/E=2-189.
PDBsum; 3TBK; -.
PDBsum; 6BZH; -.
ProteinModelPortal; Q6Q899; -.
SMR; Q6Q899; -.
BioGrid; 230926; 5.
DIP; DIP-61741N; -.
IntAct; Q6Q899; 4.
STRING; 10090.ENSMUSP00000042433; -.
iPTMnet; Q6Q899; -.
PhosphoSitePlus; Q6Q899; -.
SwissPalm; Q6Q899; -.
EPD; Q6Q899; -.
PaxDb; Q6Q899; -.
PeptideAtlas; Q6Q899; -.
PRIDE; Q6Q899; -.
DNASU; 230073; -.
Ensembl; ENSMUST00000037907; ENSMUSP00000042433; ENSMUSG00000040296. [Q6Q899-1]
GeneID; 230073; -.
KEGG; mmu:230073; -.
UCSC; uc008she.1; mouse. [Q6Q899-2]
UCSC; uc008shf.1; mouse. [Q6Q899-1]
UCSC; uc008shg.1; mouse. [Q6Q899-3]
UCSC; uc008shh.1; mouse. [Q6Q899-4]
CTD; 23586; -.
MGI; MGI:2442858; Ddx58.
eggNOG; KOG0354; Eukaryota.
eggNOG; COG1111; LUCA.
GeneTree; ENSGT00510000046789; -.
HOGENOM; HOG000230911; -.
HOVERGEN; HBG052325; -.
InParanoid; Q6Q899; -.
KO; K12646; -.
OMA; ESWDFQK; -.
OrthoDB; EOG091G01PQ; -.
TreeFam; TF330258; -.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
EvolutionaryTrace; Q6Q899; -.
PRO; PR:Q6Q899; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000040296; -.
CleanEx; MM_DDX58; -.
ExpressionAtlas; Q6Q899; baseline and differential.
Genevisible; Q6Q899; MM.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
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; ISO:MGI.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0071360; P:cellular response to exogenous dsRNA; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0009597; P:detection of virus; ISO:MGI.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; ISS:UniProtKB.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; ISO:MGI.
GO; GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; ISS:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
GO; GO:0035549; P:positive regulation of interferon-beta secretion; ISS:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI.
GO; GO:0009615; P:response to virus; IMP:UniProtKB.
GO; GO:0039529; P:RIG-I signaling pathway; ISO:MGI.
CDD; cd00079; HELICc; 1.
Gene3D; 2.170.150.30; -; 1.
InterPro; IPR031964; CARD_dom.
InterPro; IPR006935; Helicase/UvrB_N.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038557; RLR_C_sf.
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; 3.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51789; RLR_CTR; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Antiviral defense;
ATP-binding; Cell junction; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Helicase; Hydrolase;
Immunity; Innate immunity; Isopeptide bond; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
RNA-binding; Tight junction; Ubl conjugation; Zinc.
CHAIN 1 926 Probable ATP-dependent RNA helicase
DDX58.
/FTId=PRO_0000144094.
DOMAIN 1 87 CARD 1.
DOMAIN 92 172 CARD 2.
DOMAIN 252 431 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 611 777 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 791 926 RLR CTR. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
NP_BIND 265 272 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 219 926 Interaction with ZC3HAV1. {ECO:0000250}.
MOTIF 373 376 DECH box.
METAL 811 811 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 814 814 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 865 865 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
METAL 870 870 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU01125}.
MOD_RES 771 771 Phosphothreonine; by CK2.
{ECO:0000250|UniProtKB:O95786}.
MOD_RES 859 859 N6-acetyllysine.
{ECO:0000250|UniProtKB:O95786}.
CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O95786}.
CROSSLNK 164 164 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O95786}.
CROSSLNK 181 181 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O95786}.
CROSSLNK 813 813 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:23374343}.
VAR_SEQ 1 454 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016055.
VAR_SEQ 192 227 FKRAESKADEDDGAEASSIQIFIQEEPECQNLSQNP -> G
VLQERTLDPAALLPVLPTLLSIRGAVHFRYQRLYP (in
isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016056.
VAR_SEQ 228 926 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016057.
VAR_SEQ 407 410 VGLT -> FPIF (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016058.
VAR_SEQ 411 926 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016059.
VAR_SEQ 455 460 YKPQKI -> MPLTPV (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_016060.
MUTAGEN 813 813 K->R: Greatly decreases 'K-48'-linked
ubiquitination.
{ECO:0000269|PubMed:23374343}.
CONFLICT 4 4 E -> A (in Ref. 1; AAS59532).
{ECO:0000305}.
CONFLICT 282 282 H -> R (in Ref. 1; AAS59532).
{ECO:0000305}.
CONFLICT 604 604 D -> G (in Ref. 1; AAS59532).
{ECO:0000305}.
HELIX 2 11 {ECO:0000244|PDB:6BZH}.
HELIX 13 19 {ECO:0000244|PDB:6BZH}.
HELIX 22 24 {ECO:0000244|PDB:6BZH}.
HELIX 26 29 {ECO:0000244|PDB:6BZH}.
TURN 30 32 {ECO:0000244|PDB:6BZH}.
HELIX 35 47 {ECO:0000244|PDB:6BZH}.
HELIX 50 61 {ECO:0000244|PDB:6BZH}.
HELIX 69 80 {ECO:0000244|PDB:6BZH}.
HELIX 83 91 {ECO:0000244|PDB:6BZH}.
HELIX 95 98 {ECO:0000244|PDB:6BZH}.
HELIX 101 109 {ECO:0000244|PDB:6BZH}.
HELIX 111 117 {ECO:0000244|PDB:6BZH}.
HELIX 120 127 {ECO:0000244|PDB:6BZH}.
HELIX 128 130 {ECO:0000244|PDB:6BZH}.
HELIX 133 146 {ECO:0000244|PDB:6BZH}.
HELIX 148 160 {ECO:0000244|PDB:6BZH}.
HELIX 167 177 {ECO:0000244|PDB:6BZH}.
HELIX 181 185 {ECO:0000244|PDB:6BZH}.
HELIX 246 256 {ECO:0000244|PDB:3TBK}.
STRAND 261 264 {ECO:0000244|PDB:3TBK}.
HELIX 271 284 {ECO:0000244|PDB:3TBK}.
STRAND 294 297 {ECO:0000244|PDB:3TBK}.
HELIX 301 316 {ECO:0000244|PDB:3TBK}.
TURN 317 319 {ECO:0000244|PDB:3TBK}.
STRAND 322 325 {ECO:0000244|PDB:3TBK}.
TURN 327 329 {ECO:0000244|PDB:3TBK}.
HELIX 330 332 {ECO:0000244|PDB:3TBK}.
HELIX 335 341 {ECO:0000244|PDB:3TBK}.
STRAND 343 347 {ECO:0000244|PDB:3TBK}.
HELIX 349 357 {ECO:0000244|PDB:3TBK}.
STRAND 359 361 {ECO:0000244|PDB:3TBK}.
HELIX 364 366 {ECO:0000244|PDB:3TBK}.
STRAND 368 372 {ECO:0000244|PDB:3TBK}.
HELIX 375 377 {ECO:0000244|PDB:3TBK}.
HELIX 383 395 {ECO:0000244|PDB:3TBK}.
STRAND 405 411 {ECO:0000244|PDB:3TBK}.
HELIX 421 434 {ECO:0000244|PDB:3TBK}.
STRAND 438 441 {ECO:0000244|PDB:3TBK}.
HELIX 447 451 {ECO:0000244|PDB:3TBK}.
STRAND 459 463 {ECO:0000244|PDB:3TBK}.
HELIX 471 488 {ECO:0000244|PDB:3TBK}.
HELIX 492 495 {ECO:0000244|PDB:3TBK}.
HELIX 496 499 {ECO:0000244|PDB:3TBK}.
STRAND 505 507 {ECO:0000244|PDB:3TBK}.
HELIX 508 522 {ECO:0000244|PDB:3TBK}.
HELIX 529 558 {ECO:0000244|PDB:3TBK}.
HELIX 561 575 {ECO:0000244|PDB:3TBK}.
HELIX 583 592 {ECO:0000244|PDB:3TBK}.
HELIX 595 603 {ECO:0000244|PDB:3TBK}.
HELIX 605 607 {ECO:0000244|PDB:3TBK}.
HELIX 610 625 {ECO:0000244|PDB:3TBK}.
STRAND 631 634 {ECO:0000244|PDB:3TBK}.
HELIX 638 650 {ECO:0000244|PDB:3TBK}.
HELIX 652 654 {ECO:0000244|PDB:3TBK}.
STRAND 659 661 {ECO:0000244|PDB:3TBK}.
STRAND 693 697 {ECO:0000244|PDB:3TBK}.
STRAND 711 717 {ECO:0000244|PDB:3TBK}.
TURN 733 735 {ECO:0000244|PDB:3TBK}.
STRAND 738 744 {ECO:0000244|PDB:3TBK}.
HELIX 746 771 {ECO:0000244|PDB:3TBK}.
HELIX 774 793 {ECO:0000244|PDB:3TBK}.
SEQUENCE 926 AA; 105975 MW; 119FC0F88BC56957 CRC64;
MTAEQRQNLQ AFRDYIKKIL DPTYILSYMS SWLEDEEVQY IQAEKNNKGP MEAASLFLQY
LLKLQSEGWF QAFLDALYHA GYCGLCEAIE SWDFQKIEKL EEHRLLLRRL EPEFKATVDP
NDILSELSEC LINQECEEIR QIRDTKGRMA GAEKMAECLI RSDKENWPKV LQLALEKDNS
KFSELWIVDK GFKRAESKAD EDDGAEASSI QIFIQEEPEC QNLSQNPGPP SEASSNNLHS
PLKPRNYQLE LALPAKKGKN TIICAPTGCG KTFVSLLICE HHLKKFPCGQ KGKVVFFANQ
IPVYEQQATV FSRYFERLGY NIASISGATS DSVSVQHIIE DNDIIILTPQ ILVNNLNNGA
IPSLSVFTLM IFDECHNTSK NHPYNQIMFR YLDHKLGESR DPLPQVVGLT ASVGVGDAKT
AEEAMQHICK LCAALDASVI ATVRDNVAEL EQVVYKPQKI SRKVASRTSN TFKCIISQLM
KETEKLAKDV SEELGKLFQI QNREFGTQKY EQWIVGVHKA CSVFQMADKE EESRVCKALF
LYTSHLRKYN DALIISEDAQ MTDALNYLKA FFHDVREAAF DETERELTRR FEEKLEELEK
VSRDPSNENP KLRDLYLVLQ EEYHLKPETK TILFVKTRAL VDALKKWIEE NPALSFLKPG
ILTGRGRTNR ATGMTLPAQK CVLEAFRASG DNNILIATSV ADEGIDIAEC NLVILYEYVG
NVIKMIQTRG RGRARDSKCF LLTSSADVIE KEKANMIKEK IMNESILRLQ TWDEMKFGKT
VHRIQVNEKL LRDSQHKPQP VPDKENKKLL CGKCKNFACY TADIRVVETS HYTVLGDAFK
ERFVCKPHPK PKIYDNFEKK AKIFCAKQNC SHDWGIFVRY KTFEIPVIKI ESFVVEDIVS
GVQNRHSKWK DFHFERIQFD PAEMSV


Related products :

Catalog number Product name Quantity
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
EIAAB10826 DDX58,DEAD box protein 58,Homo sapiens,Human,Probable ATP-dependent RNA helicase DDX58,Retinoic acid-inducible gene 1 protein,Retinoic acid-inducible gene I protein,RIG-1,RIG-I
EIAAB10827 Ddx58,DEAD box protein 58,Mouse,Mus musculus,Probable ATP-dependent RNA helicase DDX58,Retinoic acid-inducible gene 1 protein,Retinoic acid-inducible gene I protein,RIG-1,RIG-I
MD-14-0511 Rabbit Anti-Retinoic acid Inducible Gene 1 protein (RIG-1) _ DEAD (Asp-Glu-Ala-Asp) box Protein 58 (DDX58) 100
129-10591 Rabbit Anti-Retinoic acid Inducible Gene 1 protein (RIG-1) _ DEAD (Asp-Glu-Ala-Asp) box Protein 58 (DDX58) 100
EIAAB42392 Homo sapiens,Human,RARRES3,RAR-responsive protein TIG3,Retinoic acid receptor responder protein 3,Retinoid-inducible gene 1 protein,RIG1,Tazarotene-induced gene 3 protein,TIG3
EIAAB33711 GPCR5A,GPRC5A,G-protein coupled receptor family C group 5 member A,Homo sapiens,Human,Orphan G-protein-coupling receptor PEIG-1,RAI3,RAIG1,RAIG-1,Retinoic acid-induced gene 1 protein,Retinoic acid-ind
18-461-10670 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10472 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10473 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10669 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-461-10751 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
18-003-44260 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein-coupling receptor PEIG-1 Polyclonal 0.05 mg Aff Pur
18-461-10340 Retinoic acid-induced protein 3 - G-protein coupled receptor family C group 5 member A; Retinoic acid-induced gene 1 protein; RAIG-1; Orphan G-protein coupling receptor PEIG-1 Polyclonal 0.05 ml
EIAAB33712 Gprc5a,G-protein coupled receptor family C group 5 member A,Mouse,Mus musculus,Rai3,Raig1,RAIG-1,Retinoic acid-induced gene 1 protein,Retinoic acid-induced protein 3
E91532Hu ELISA Kit for Retinoic Acid-Inducible Gene 1 Protein (RIG1) 96T/Kit
201-12-4788 Human Retinoic Acid Inducible Gene 1 Protein(RIG1)ELISA Kit 96T
QY-E01070 Human Retinoic Acid Inducible Gene 1 Protein(RIG1)ELISA Kit 96T
UB-E01070 Human Retinoic Acid Inducible Gene 1 Protein(RIG1)ELISA Kit 96T
RAE1E_MOUSE ELISA Kit FOR Retinoic acid early-inducible protein 1-epsilon; organism: Mouse; gene name: Raet1e 96T
E91532Hu ELISA Kit for Retinoic Acid Inducible Gene 1 Protein (RIG1) Organism: Homo sapiens (Human) 96T
RAE1B_MOUSE ELISA Kit FOR Retinoic acid early-inducible protein 1-beta; organism: Mouse; gene name: Raet1b 96T
RAE1C_MOUSE ELISA Kit FOR Retinoic acid early-inducible protein 1-gamma; organism: Mouse; gene name: Raet1c 96T
RAE1A_MOUSE ELISA Kit FOR Retinoic acid early-inducible protein 1-alpha; organism: Mouse; gene name: Raet1a 96T
RAE1D_MOUSE ELISA Kit FOR Retinoic acid early-inducible protein 1-delta; organism: Mouse; gene name: Raet1d 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur