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Protein

Probable ATP-dependent RNA helicase DDX58

Gene

Ddx58

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi811 – 8111ZincPROSITE-ProRule annotation
Metal bindingi814 – 8141ZincPROSITE-ProRule annotation
Metal bindingi865 – 8651ZincPROSITE-ProRule annotation
Metal bindingi870 – 8701ZincPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi265 – 2728ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • double-stranded DNA binding Source: MGI
  • double-stranded RNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB-KW
  • identical protein binding Source: MGI
  • single-stranded RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX58 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 58
RIG-I-like receptor 1
Short name:
RLR-1
Retinoic acid-inducible gene 1 protein
Short name:
RIG-1
Retinoic acid-inducible gene I protein
Short name:
RIG-I
Gene namesi
Name:Ddx58
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2442858. Ddx58.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Tight junction

Pathology & Biotechi

Disruption phenotypei

Death between E12.5 and E14 due to liver apoptosis. Those who are born alive show growth retardation and die within 3 weeks.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 926926Probable ATP-dependent RNA helicase DDX58PRO_0000144094Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki154 – 154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki164 – 164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei771 – 7711Phosphothreonine; by CK2By similarity
Modified residuei859 – 8591N6-acetyllysineBy similarity

Post-translational modificationi

ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response (By similarity).By similarity
Sumoylated, probably by MUL1; inhibiting its polyubiquitination.By similarity
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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6Q899.
MaxQBiQ6Q899.
PaxDbiQ6Q899.
PeptideAtlasiQ6Q899.
PRIDEiQ6Q899.

PTM databases

iPTMnetiQ6Q899.
PhosphoSiteiQ6Q899.

Expressioni

Inductioni

By interferon (IFN).

Gene expression databases

BgeeiQ6Q899.
CleanExiMM_DDX58.
ExpressionAtlasiQ6Q899. baseline and differential.
GenevisibleiQ6Q899. MM.

Interactioni

Subunit structurei

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 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.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CblP226823EBI-6841237,EBI-640919
SiglecgQ80ZE37EBI-6841237,EBI-6841023

GO - Molecular functioni

Protein-protein interaction databases

BioGridi230926. 5 interactions.
DIPiDIP-61741N.
IntActiQ6Q899. 3 interactions.
STRINGi10090.ENSMUSP00000042433.

Structurei

Secondary structure

1
926
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi246 – 25611Combined sources
Beta strandi261 – 2644Combined sources
Helixi271 – 28414Combined sources
Beta strandi294 – 2974Combined sources
Helixi301 – 31616Combined sources
Turni317 – 3193Combined sources
Beta strandi322 – 3254Combined sources
Turni327 – 3293Combined sources
Helixi330 – 3323Combined sources
Helixi335 – 3417Combined sources
Beta strandi343 – 3475Combined sources
Helixi349 – 3579Combined sources
Beta strandi359 – 3613Combined sources
Helixi364 – 3663Combined sources
Beta strandi368 – 3725Combined sources
Helixi375 – 3773Combined sources
Helixi383 – 39513Combined sources
Beta strandi405 – 4117Combined sources
Helixi421 – 43414Combined sources
Beta strandi438 – 4414Combined sources
Helixi447 – 4515Combined sources
Beta strandi459 – 4635Combined sources
Helixi471 – 48818Combined sources
Helixi492 – 4954Combined sources
Helixi496 – 4994Combined sources
Beta strandi505 – 5073Combined sources
Helixi508 – 52215Combined sources
Helixi529 – 55830Combined sources
Helixi561 – 57515Combined sources
Helixi583 – 59210Combined sources
Helixi595 – 6039Combined sources
Helixi605 – 6073Combined sources
Helixi610 – 62516Combined sources
Beta strandi631 – 6344Combined sources
Helixi638 – 65013Combined sources
Helixi652 – 6543Combined sources
Beta strandi659 – 6613Combined sources
Beta strandi693 – 6975Combined sources
Beta strandi711 – 7177Combined sources
Turni733 – 7353Combined sources
Beta strandi738 – 7447Combined sources
Helixi746 – 77126Combined sources
Helixi774 – 79320Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TBKX-ray2.14A240-794[»]
ProteinModelPortaliQ6Q899.
SMRiQ6Q899. Positions 1-188, 240-925.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6Q899.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8787CARD 1Add
BLAST
Domaini92 – 17281CARD 2Add
BLAST
Domaini252 – 431180Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini611 – 777167Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini791 – 926136RLR CTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 926708Interaction with ZC3HAV1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi373 – 3764DECH box

Domaini

The helicase domain is responsible for dsRNA recognition. Interacts with IFIT3 (via N-terminus).By similarity
The 2 CARD domains are responsible for interaction with and signaling through MAVS/IPS1 and for association with the actin cytoskeleton.By similarity
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.
The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination.By similarity

Sequence similaritiesi

Belongs to the helicase family. RLR subfamily.Curated
Contains 2 CARD domains.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 RLR CTR (RLR C-terminal regulatory) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0354. Eukaryota.
COG1111. LUCA.
GeneTreeiENSGT00510000046789.
HOGENOMiHOG000230911.
HOVERGENiHBG052325.
InParanoidiQ6Q899.
KOiK12646.
OMAiRTTDRFK.
OrthoDBiEOG7RV9FC.
TreeFamiTF330258.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR031964. CARD_dom.
IPR011029. DEATH-like_dom.
IPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR021673. RIG-I_C-RD.
[Graphical view]
PfamiPF16739. CARD_2. 2 hits.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51789. RLR_CTR. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6Q899-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTAEQRQNLQ AFRDYIKKIL DPTYILSYMS SWLEDEEVQY IQAEKNNKGP
60 70 80 90 100
MEAASLFLQY LLKLQSEGWF QAFLDALYHA GYCGLCEAIE SWDFQKIEKL
110 120 130 140 150
EEHRLLLRRL EPEFKATVDP NDILSELSEC LINQECEEIR QIRDTKGRMA
160 170 180 190 200
GAEKMAECLI RSDKENWPKV LQLALEKDNS KFSELWIVDK GFKRAESKAD
210 220 230 240 250
EDDGAEASSI QIFIQEEPEC QNLSQNPGPP SEASSNNLHS PLKPRNYQLE
260 270 280 290 300
LALPAKKGKN TIICAPTGCG KTFVSLLICE HHLKKFPCGQ KGKVVFFANQ
310 320 330 340 350
IPVYEQQATV FSRYFERLGY NIASISGATS DSVSVQHIIE DNDIIILTPQ
360 370 380 390 400
ILVNNLNNGA IPSLSVFTLM IFDECHNTSK NHPYNQIMFR YLDHKLGESR
410 420 430 440 450
DPLPQVVGLT ASVGVGDAKT AEEAMQHICK LCAALDASVI ATVRDNVAEL
460 470 480 490 500
EQVVYKPQKI SRKVASRTSN TFKCIISQLM KETEKLAKDV SEELGKLFQI
510 520 530 540 550
QNREFGTQKY EQWIVGVHKA CSVFQMADKE EESRVCKALF LYTSHLRKYN
560 570 580 590 600
DALIISEDAQ MTDALNYLKA FFHDVREAAF DETERELTRR FEEKLEELEK
610 620 630 640 650
VSRDPSNENP KLRDLYLVLQ EEYHLKPETK TILFVKTRAL VDALKKWIEE
660 670 680 690 700
NPALSFLKPG ILTGRGRTNR ATGMTLPAQK CVLEAFRASG DNNILIATSV
710 720 730 740 750
ADEGIDIAEC NLVILYEYVG NVIKMIQTRG RGRARDSKCF LLTSSADVIE
760 770 780 790 800
KEKANMIKEK IMNESILRLQ TWDEMKFGKT VHRIQVNEKL LRDSQHKPQP
810 820 830 840 850
VPDKENKKLL CGKCKNFACY TADIRVVETS HYTVLGDAFK ERFVCKPHPK
860 870 880 890 900
PKIYDNFEKK AKIFCAKQNC SHDWGIFVRY KTFEIPVIKI ESFVVEDIVS
910 920
GVQNRHSKWK DFHFERIQFD PAEMSV
Length:926
Mass (Da):105,975
Last modified:July 27, 2011 - v2
Checksum:i119FC0F88BC56957
GO
Isoform 2 (identifier: Q6Q899-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-454: Missing.
     455-460: YKPQKI → MPLTPV

Note: No experimental confirmation available.
Show »
Length:472
Mass (Da):54,658
Checksum:iD4614CA1A8BAC4EF
GO
Isoform 3 (identifier: Q6Q899-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-410: VGLT → FPIF
     411-926: Missing.

Note: No experimental confirmation available.
Show »
Length:410
Mass (Da):46,841
Checksum:iECC9E3D2D2BC5FE0
GO
Isoform 4 (identifier: Q6Q899-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     192-227: FKRAESKADEDDGAEASSIQIFIQEEPECQNLSQNP → GVLQERTLDPAALLPVLPTLLSIRGAVHFRYQRLYP
     228-926: Missing.

Note: No experimental confirmation available.
Show »
Length:227
Mass (Da):26,479
Checksum:i4FCBEE047EFB9AD0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41E → A in AAS59532 (Ref. 1) Curated
Sequence conflicti282 – 2821H → R in AAS59532 (Ref. 1) Curated
Sequence conflicti604 – 6041D → G in AAS59532 (Ref. 1) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 454454Missing in isoform 2. 1 PublicationVSP_016055Add
BLAST
Alternative sequencei192 – 22736FKRAE…LSQNP → GVLQERTLDPAALLPVLPTL LSIRGAVHFRYQRLYP in isoform 4. 1 PublicationVSP_016056Add
BLAST
Alternative sequencei228 – 926699Missing in isoform 4. 1 PublicationVSP_016057Add
BLAST
Alternative sequencei407 – 4104VGLT → FPIF in isoform 3. 1 PublicationVSP_016058
Alternative sequencei411 – 926516Missing in isoform 3. 1 PublicationVSP_016059Add
BLAST
Alternative sequencei455 – 4606YKPQKI → MPLTPV in isoform 2. 1 PublicationVSP_016060

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY553221 mRNA. Translation: AAS59532.1.
AL831793 Genomic DNA. Translation: CAM27574.1.
CH466538 Genomic DNA. Translation: EDL05445.1.
AK049305 mRNA. Translation: BAC33670.1.
AK078287 mRNA. Translation: BAC37205.1.
AK087261 mRNA. Translation: BAC39830.1.
CCDSiCCDS18043.1. [Q6Q899-1]
RefSeqiNP_766277.3. NM_172689.3. [Q6Q899-1]
UniGeneiMm.86382.

Genome annotation databases

EnsembliENSMUST00000037907; ENSMUSP00000042433; ENSMUSG00000040296. [Q6Q899-1]
GeneIDi230073.
KEGGimmu:230073.
UCSCiuc008she.1. mouse. [Q6Q899-2]
uc008shf.1. mouse. [Q6Q899-1]
uc008shg.1. mouse. [Q6Q899-3]
uc008shh.1. mouse. [Q6Q899-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY553221 mRNA. Translation: AAS59532.1.
AL831793 Genomic DNA. Translation: CAM27574.1.
CH466538 Genomic DNA. Translation: EDL05445.1.
AK049305 mRNA. Translation: BAC33670.1.
AK078287 mRNA. Translation: BAC37205.1.
AK087261 mRNA. Translation: BAC39830.1.
CCDSiCCDS18043.1. [Q6Q899-1]
RefSeqiNP_766277.3. NM_172689.3. [Q6Q899-1]
UniGeneiMm.86382.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TBKX-ray2.14A240-794[»]
ProteinModelPortaliQ6Q899.
SMRiQ6Q899. Positions 1-188, 240-925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230926. 5 interactions.
DIPiDIP-61741N.
IntActiQ6Q899. 3 interactions.
STRINGi10090.ENSMUSP00000042433.

PTM databases

iPTMnetiQ6Q899.
PhosphoSiteiQ6Q899.

Proteomic databases

EPDiQ6Q899.
MaxQBiQ6Q899.
PaxDbiQ6Q899.
PeptideAtlasiQ6Q899.
PRIDEiQ6Q899.

Protocols and materials databases

DNASUi230073.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037907; ENSMUSP00000042433; ENSMUSG00000040296. [Q6Q899-1]
GeneIDi230073.
KEGGimmu:230073.
UCSCiuc008she.1. mouse. [Q6Q899-2]
uc008shf.1. mouse. [Q6Q899-1]
uc008shg.1. mouse. [Q6Q899-3]
uc008shh.1. mouse. [Q6Q899-4]

Organism-specific databases

CTDi23586.
MGIiMGI:2442858. Ddx58.

Phylogenomic databases

eggNOGiKOG0354. Eukaryota.
COG1111. LUCA.
GeneTreeiENSGT00510000046789.
HOGENOMiHOG000230911.
HOVERGENiHBG052325.
InParanoidiQ6Q899.
KOiK12646.
OMAiRTTDRFK.
OrthoDBiEOG7RV9FC.
TreeFamiTF330258.

Enzyme and pathway databases

ReactomeiR-MMU-936440. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

ChiTaRSiDdx58. mouse.
EvolutionaryTraceiQ6Q899.
PROiQ6Q899.
SOURCEiSearch...

Gene expression databases

BgeeiQ6Q899.
CleanExiMM_DDX58.
ExpressionAtlasiQ6Q899. baseline and differential.
GenevisibleiQ6Q899. MM.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR031964. CARD_dom.
IPR011029. DEATH-like_dom.
IPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR021673. RIG-I_C-RD.
[Graphical view]
PfamiPF16739. CARD_2. 2 hits.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51789. RLR_CTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Wei J., Gu J.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Olfactory bulb.
  5. Cited for: FUNCTION.
  6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: FUNCTION.
  8. "RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway."
    Chiu Y.-H., Macmillan J.B., Chen Z.J.
    Cell 138:576-591(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Recognition of 5' triphosphate by RIG-I helicase requires short blunt double-stranded RNA as contained in panhandle of negative-strand virus."
    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.
    Immunity 31:25-34(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate."
    Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A., Hornung V.
    Nat. Immunol. 10:1065-1072(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Spleen.
  12. "Function and regulation of retinoic acid-inducible gene-I."
    Matsumiya T., Stafforini D.M.
    Crit. Rev. Immunol. 30:489-513(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  13. "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.
  14. "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.
  15. Cited for: REVIEW ON FUNCTION.
  16. "Sensing of viral nucleic acids by RIG-I: from translocation to translation."
    Schmidt A., Rothenfusser S., Hopfner K.P.
    Eur. J. Cell Biol. 91:78-85(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.

Entry informationi

Entry nameiDDX58_MOUSE
AccessioniPrimary (citable) accession number: Q6Q899
Secondary accession number(s): A2AP28
, Q8C320, Q8C5I3, Q8C7T2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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