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O95786

- DDX58_HUMAN

UniProt

O95786 - DDX58_HUMAN

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Protein

Probable ATP-dependent RNA helicase DDX58

Gene

DDX58

Organism
Homo sapiens (Human)
Status
Reviewed - 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: Human respiratory syncytial virus and measles virus (MeV), 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 reovirus. 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.13 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Zinc.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi810 – 8101Zinc
Metal bindingi813 – 8131Zinc
Metal bindingi864 – 8641Zinc
Metal bindingi869 – 8691Zinc

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi264 – 2718ATPCurated

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. double-stranded DNA binding Source: Ensembl
  3. double-stranded RNA binding Source: UniProtKB
  4. helicase activity Source: UniProtKB-KW
  5. identical protein binding Source: IntAct
  6. single-stranded RNA binding Source: UniProtKB
  7. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. cytoplasmic pattern recognition receptor signaling pathway in response to virus Source: UniProtKB
  2. detection of virus Source: BHF-UCL
  3. innate immune response Source: UniProtKB
  4. negative regulation of type I interferon production Source: Reactome
  5. positive regulation of defense response to virus by host Source: UniProtKB
  6. positive regulation of interferon-alpha production Source: UniProtKB
  7. positive regulation of interferon-beta production Source: UniProtKB
  8. positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  9. positive regulation of transcription factor import into nucleus Source: BHF-UCL
  10. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  11. regulation of cell migration Source: UniProtKB
  12. regulation of type III interferon production Source: UniProtKB
  13. response to exogenous dsRNA Source: Ensembl
  14. response to virus Source: UniProtKB
  15. RIG-I signaling pathway Source: UniProtKB
  16. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Antiviral defense, Host-virus interaction, Immunity, Innate immunity

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:19102. DDX58.

Subcellular locationi

Cytoplasm. Cell projectionruffle membrane. Cytoplasmcytoskeleton. Cell junctiontight junction
Note: Colocalized with TRIM25 at cytoplasmic perinuclear bodies. Associated with the actin cytoskeleton at membrane ruffles.

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. ruffle membrane Source: UniProtKB
  5. tight junction Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi55 – 551T → I: No IRF3 signaling activity; no effect on dsRNA binding. 1 Publication
Mutagenesisi99 – 991K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication
Mutagenesisi154 – 1541K → R: Reduction of ubiquitination. Reduction of INFB induction. 1 Publication
Mutagenesisi164 – 1641K → R: Reduction of ubiquitination. Reduction of INFB induction. 1 Publication
Mutagenesisi169 – 1691K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication
Mutagenesisi172 – 1721K → R: Complete loss of ubiquitination; No interaction with MAVS/IPS1; No induction of IFN-beta. 2 Publications
Mutagenesisi181 – 1811K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication
Mutagenesisi190 – 1901K → R: Little or no effect on ubiquitination of the 2 CARD domains.
Mutagenesisi193 – 1931K → R: Little or no effect on ubiquitination of the 2 CARD domains. 1 Publication
Mutagenesisi270 – 2701K → A: No IRF3 signaling activity. 2 Publications

Organism-specific databases

PharmGKBiPA134994272.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 925925Probable ATP-dependent RNA helicase DDX58PRO_0000144093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki154 – 154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki164 – 164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki172 – 172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei770 – 7701Phosphothreonine; by CK21 Publication
Modified residuei854 – 8541Phosphoserine; by CK21 Publication
Modified residuei855 – 8551Phosphoserine; by CK21 Publication
Modified residuei858 – 8581N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated in resting cells and dephosphorylated in RNA virus-infected cells. Phosphorylation at Thr-770, Ser-854 and Ser-855 results in inhibition of its activity while dephosphorylation at these sites results in its activation.1 Publication
ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation negatively regulates its function in antiviral signaling response.3 Publications
Sumoylated, probably by MUL1; inhibiting its polyubiquitination.2 Publications
Ubiquitinated. Undergoes 'Lys-48'- and 'Lys-63'-linked ubiquitination. Lys-172 is the critical site for TRIM25-mediated ubiquitination, for MAVS/IPS1 binding and to induce anti-viral signal transduction. Lys-154, Lys-164 and Lys-172 are critical sites for RNF135-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.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95786.
PaxDbiO95786.
PRIDEiO95786.

PTM databases

PhosphoSiteiO95786.

Expressioni

Tissue specificityi

Present in vascular smooth cells (at protein level).1 Publication

Inductioni

By bacterial lipopolysaccharides (LPS) in endothelial cells. By interferon (IFN).5 Publications

Gene expression databases

BgeeiO95786.
CleanExiHS_DDX58.
ExpressionAtlasiO95786. baseline and differential.
GenevestigatoriO95786.

Organism-specific databases

HPAiCAB012643.
HPA047193.

Interactioni

Subunit structurei

Monomer; maintained as a monomer in an autoinhibited state. Upon viral dsRNA binding and conformation shift, homomultimerizes and interacts with MAVS/IPS1. 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 protein Z of Guanarito virus, Machupo virus, Junin arenavirus and Sabia virus. This interaction disrupts its interaction with MAVS/IPS1, impeding downstream IRF3 and NF-kappa-B activation and resulting in decreased IFN-beta induction. Interacts (via CARD domain) with Human respiratory syncytial virus A non-structural protein 2 (NS2) and this interaction disrupts its interaction with MAVS/IPS1, impeding downstream IRF3 activation. Interacts with Rotavirus A non-structural protein 1 (NSP1) and this interaction induces down-regulation of DDX58/RIG-I. Interacts with DDX60. Interacts with isoform 2 of ZC3HAV1 (via zinc-fingers) in an RNA-dependent manner.19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-995350,EBI-995350
1BP045432EBI-995350,EBI-3648048From a different organism.
Casp12Q920D54EBI-995350,EBI-1374296From a different organism.
CYLDQ9NQC72EBI-995350,EBI-2117940
DDX3XO005712EBI-995350,EBI-353779
MAVSQ7Z43412EBI-995350,EBI-995373
NSSP216993EBI-995350,EBI-6693910From a different organism.
STAT1P422244EBI-995350,EBI-1057697
US11P044874EBI-995350,EBI-6150681From a different organism.
WRNIP1Q96S552EBI-995350,EBI-2513471
ZQ6IUF93EBI-995350,EBI-3647473From a different organism.
ZQ6IVU53EBI-995350,EBI-3647294From a different organism.
ZQ6UY622EBI-995350,EBI-3647496From a different organism.
ZQ6UY713EBI-995350,EBI-3647448From a different organism.
ZC3HAV1Q7Z2W43EBI-995350,EBI-922540
ZC3HAV1Q7Z2W4-24EBI-995350,EBI-922559

Protein-protein interaction databases

BioGridi117121. 36 interactions.
DIPiDIP-35444N.
IntActiO95786. 19 interactions.
MINTiMINT-2799116.
STRINGi9606.ENSP00000369213.

Structurei

Secondary structure

1
925
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi97 – 10913
Helixi111 – 1177
Turni120 – 1234
Helixi124 – 1274
Turni128 – 1303
Helixi133 – 14513
Helixi148 – 16114
Helixi166 – 17813
Helixi182 – 1854
Helixi245 – 25511
Beta strandi260 – 2634
Helixi270 – 28415
Beta strandi293 – 2964
Helixi300 – 31314
Turni314 – 3185
Beta strandi321 – 3244
Beta strandi326 – 3283
Beta strandi330 – 3323
Helixi334 – 3396
Beta strandi342 – 3465
Helixi348 – 3569
Helixi363 – 3653
Beta strandi367 – 3726
Helixi374 – 3763
Beta strandi377 – 3815
Helixi382 – 39514
Beta strandi404 – 4107
Helixi420 – 43314
Beta strandi438 – 4403
Helixi446 – 4527
Beta strandi457 – 4626
Helixi470 – 48920
Helixi493 – 4953
Beta strandi496 – 4983
Beta strandi504 – 5063
Helixi507 – 51812
Helixi519 – 5213
Helixi531 – 55727
Helixi560 – 57516
Helixi581 – 59111
Helixi594 – 6029
Helixi604 – 6063
Helixi609 – 62214
Beta strandi630 – 6334
Helixi637 – 64913
Helixi651 – 6533
Beta strandi658 – 6603
Beta strandi668 – 6703
Helixi675 – 6839
Beta strandi694 – 7007
Helixi706 – 7083
Beta strandi710 – 7167
Helixi721 – 7277
Beta strandi737 – 7437
Helixi745 – 76824
Helixi773 – 79321
Beta strandi801 – 8044
Beta strandi806 – 8105
Turni811 – 8133
Beta strandi816 – 8194
Helixi820 – 8223
Beta strandi823 – 8264
Turni827 – 8293
Beta strandi830 – 8334
Helixi836 – 8394
Beta strandi842 – 8465
Beta strandi856 – 8649
Turni867 – 8693
Beta strandi872 – 8798
Beta strandi882 – 8876
Helixi889 – 8913
Beta strandi892 – 8965
Turni897 – 8993
Beta strandi902 – 9043
Turni908 – 9103
Helixi920 – 9223

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LWDNMR-A95-190[»]
2LWENMR-A95-190[»]
2QFBX-ray3.00A/B/C/D/E/F/G/H/I/J802-925[»]
2QFDX-ray2.70A/B/C/D/E/F/G/H/I/J802-925[»]
2RMJNMR-A792-925[»]
2YKGX-ray2.50A230-925[»]
3LRNX-ray2.60A/B803-923[»]
3LRRX-ray2.15A/B803-923[»]
3NCUX-ray2.55A/B792-925[»]
3OG8X-ray2.40A/B802-925[»]
3TMIX-ray2.90A232-925[»]
3ZD6X-ray2.80A230-925[»]
3ZD7X-ray2.50A230-925[»]
4AY2X-ray2.80A239-925[»]
4BPBX-ray2.58A230-925[»]
4NQKX-ray3.70A/B/C/D1-200[»]
4ON9X-ray2.71A/B230-793[»]
4P4HX-ray3.40A/B/C/D/E/F/G/H1-201[»]
ProteinModelPortaliO95786.
SMRiO95786. Positions 1-188, 240-925.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8787CARD 1Add
BLAST
Domaini92 – 17281CARD 2Add
BLAST
Domaini251 – 430180Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini610 – 776167Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni218 – 925708Interaction with ZC3HAV1Add
BLAST
Regioni735 – 925191Repressor domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi372 – 3754DECH box

Domaini

The repressor 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 repressor domain. Upon binding to viral RNA in the presence of ATP, the repressor 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 helicase domain is responsible for dsRNA recognition.
The 2 CARD domains are responsible for interaction with and signaling through MAVS/IPS1 and for association with the actin cytoskeleton.
The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination.

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1111.
GeneTreeiENSGT00510000046789.
HOGENOMiHOG000230911.
HOVERGENiHBG052325.
InParanoidiO95786.
KOiK12646.
OMAiKCKAFAC.
PhylomeDBiO95786.
TreeFamiTF330258.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR011029. DEATH-like_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR021673. RIG-I_C-RD.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
SM00487. 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.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95786-1) [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
MTTEQRRSLQ AFQDYIRKTL DPTYILSYMA PWFREEEVQY IQAEKNNKGP
60 70 80 90 100
MEAATLFLKF LLELQEEGWF RGFLDALDHA GYSGLYEAIE SWDFKKIEKL
110 120 130 140 150
EEYRLLLKRL QPEFKTRIIP TDIISDLSEC LINQECEEIL QICSTKGMMA
160 170 180 190 200
GAEKLVECLL RSDKENWPKT LKLALEKERN KFSELWIVEK GIKDVETEDL
210 220 230 240 250
EDKMETSDIQ IFYQEDPECQ NLSENSCPPS EVSDTNLYSP FKPRNYQLEL
260 270 280 290 300
ALPAMKGKNT IICAPTGCGK TFVSLLICEH HLKKFPQGQK GKVVFFANQI
310 320 330 340 350
PVYEQQKSVF SKYFERHGYR VTGISGATAE NVPVEQIVEN NDIIILTPQI
360 370 380 390 400
LVNNLKKGTI PSLSIFTLMI FDECHNTSKQ HPYNMIMFNY LDQKLGGSSG
410 420 430 440 450
PLPQVIGLTA SVGVGDAKNT DEALDYICKL CASLDASVIA TVKHNLEELE
460 470 480 490 500
QVVYKPQKFF RKVESRISDK FKYIIAQLMR DTESLAKRIC KDLENLSQIQ
510 520 530 540 550
NREFGTQKYE QWIVTVQKAC MVFQMPDKDE ESRICKALFL YTSHLRKYND
560 570 580 590 600
ALIISEHARM KDALDYLKDF FSNVRAAGFD EIEQDLTQRF EEKLQELESV
610 620 630 640 650
SRDPSNENPK LEDLCFILQE EYHLNPETIT ILFVKTRALV DALKNWIEGN
660 670 680 690 700
PKLSFLKPGI LTGRGKTNQN TGMTLPAQKC ILDAFKASGD HNILIATSVA
710 720 730 740 750
DEGIDIAQCN LVILYEYVGN VIKMIQTRGR GRARGSKCFL LTSNAGVIEK
760 770 780 790 800
EQINMYKEKM MNDSILRLQT WDEAVFREKI LHIQTHEKFI RDSQEKPKPV
810 820 830 840 850
PDKENKKLLC RKCKALACYT ADVRVIEECH YTVLGDAFKE CFVSRPHPKP
860 870 880 890 900
KQFSSFEKRA KIFCARQNCS HDWGIHVKYK TFEIPVIKIE SFVVEDIATG
910 920
VQTLYSKWKD FHFEKIPFDP AEMSK
Length:925
Mass (Da):106,600
Last modified:November 8, 2005 - v2
Checksum:iBF0D501C395BAE25
GO
Isoform 2 (identifier: O95786-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     36-80: Missing.

Note: No experimental confirmation available.

Show »
Length:880
Mass (Da):101,377
Checksum:i4B1603B6F2F37A66
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71R → C.1 Publication
Corresponds to variant rs10813831 [ dbSNP | Ensembl ].
VAR_023747
Natural varianti580 – 5801D → E.2 Publications
Corresponds to variant rs17217280 [ dbSNP | Ensembl ].
VAR_023748

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei36 – 8045Missing in isoform 2. 1 PublicationVSP_016054Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF038963 mRNA. Translation: AAD19826.1.
AL353671, AL161783 Genomic DNA. Translation: CAH71251.1.
AL161783, AL353671 Genomic DNA. Translation: CAH72600.1.
CH471071 Genomic DNA. Translation: EAW58548.1.
BC132786 mRNA. Translation: AAI32787.1.
BC136610 mRNA. Translation: AAI36611.1.
BX647917 mRNA. Translation: CAI46068.1.
AL137608 mRNA. Translation: CAB70840.1.
CCDSiCCDS6526.1. [O95786-1]
PIRiT46312.
RefSeqiNP_055129.2. NM_014314.3. [O95786-1]
UniGeneiHs.190622.

Genome annotation databases

EnsembliENST00000379883; ENSP00000369213; ENSG00000107201. [O95786-1]
GeneIDi23586.
KEGGihsa:23586.
UCSCiuc003zra.3. human. [O95786-1]
uc010mjk.1. human. [O95786-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF038963 mRNA. Translation: AAD19826.1 .
AL353671 , AL161783 Genomic DNA. Translation: CAH71251.1 .
AL161783 , AL353671 Genomic DNA. Translation: CAH72600.1 .
CH471071 Genomic DNA. Translation: EAW58548.1 .
BC132786 mRNA. Translation: AAI32787.1 .
BC136610 mRNA. Translation: AAI36611.1 .
BX647917 mRNA. Translation: CAI46068.1 .
AL137608 mRNA. Translation: CAB70840.1 .
CCDSi CCDS6526.1. [O95786-1 ]
PIRi T46312.
RefSeqi NP_055129.2. NM_014314.3. [O95786-1 ]
UniGenei Hs.190622.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LWD NMR - A 95-190 [» ]
2LWE NMR - A 95-190 [» ]
2QFB X-ray 3.00 A/B/C/D/E/F/G/H/I/J 802-925 [» ]
2QFD X-ray 2.70 A/B/C/D/E/F/G/H/I/J 802-925 [» ]
2RMJ NMR - A 792-925 [» ]
2YKG X-ray 2.50 A 230-925 [» ]
3LRN X-ray 2.60 A/B 803-923 [» ]
3LRR X-ray 2.15 A/B 803-923 [» ]
3NCU X-ray 2.55 A/B 792-925 [» ]
3OG8 X-ray 2.40 A/B 802-925 [» ]
3TMI X-ray 2.90 A 232-925 [» ]
3ZD6 X-ray 2.80 A 230-925 [» ]
3ZD7 X-ray 2.50 A 230-925 [» ]
4AY2 X-ray 2.80 A 239-925 [» ]
4BPB X-ray 2.58 A 230-925 [» ]
4NQK X-ray 3.70 A/B/C/D 1-200 [» ]
4ON9 X-ray 2.71 A/B 230-793 [» ]
4P4H X-ray 3.40 A/B/C/D/E/F/G/H 1-201 [» ]
ProteinModelPortali O95786.
SMRi O95786. Positions 1-188, 240-925.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117121. 36 interactions.
DIPi DIP-35444N.
IntActi O95786. 19 interactions.
MINTi MINT-2799116.
STRINGi 9606.ENSP00000369213.

PTM databases

PhosphoSitei O95786.

Proteomic databases

MaxQBi O95786.
PaxDbi O95786.
PRIDEi O95786.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379883 ; ENSP00000369213 ; ENSG00000107201 . [O95786-1 ]
GeneIDi 23586.
KEGGi hsa:23586.
UCSCi uc003zra.3. human. [O95786-1 ]
uc010mjk.1. human. [O95786-2 ]

Organism-specific databases

CTDi 23586.
GeneCardsi GC09M032447.
HGNCi HGNC:19102. DDX58.
HPAi CAB012643.
HPA047193.
MIMi 609631. gene.
neXtProti NX_O95786.
PharmGKBi PA134994272.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1111.
GeneTreei ENSGT00510000046789.
HOGENOMi HOG000230911.
HOVERGENi HBG052325.
InParanoidi O95786.
KOi K12646.
OMAi KCKAFAC.
PhylomeDBi O95786.
TreeFami TF330258.

Enzyme and pathway databases

Reactomei REACT_115831. ISG15 antiviral mechanism.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_24938. TRAF6 mediated IRF7 activation.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_25039. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

Miscellaneous databases

ChiTaRSi DDX58. human.
EvolutionaryTracei O95786.
GeneWikii RIG-I.
GenomeRNAii 23586.
NextBioi 46208.
PROi O95786.
SOURCEi Search...

Gene expression databases

Bgeei O95786.
CleanExi HS_DDX58.
ExpressionAtlasi O95786. baseline and differential.
Genevestigatori O95786.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR011545. DEAD/DEAH_box_helicase_dom.
IPR011029. DEATH-like_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR021673. RIG-I_C-RD.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 3 hits.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "RIG-I, a human homolog gene of RNA helicase, is induced by retinoic acid during the differentiation of acute promyelocytic leukemia cell."
    Sun Y.-W.
    Thesis (1997), Shanghai Institute of Hematology, China
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-580.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-580, INDUCTION.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-748 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-925 (ISOFORMS 1/2), VARIANT CYS-7.
    Tissue: Skin and Testis.
  7. "Retinoic acid-inducible gene-I is induced by interferon-gamma and regulates the expression of interferon-gamma stimulated gene 15 in MCF-7 cells."
    Cui X.-F., Imaizumi T., Yoshida H., Borden E.C., Satoh K.
    Biochem. Cell Biol. 82:401-405(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, SUBCELLULAR LOCATION.
  8. "Expression of retinoic acid-inducible gene-I in vascular smooth muscle cells stimulated with interferon-gamma."
    Imaizumi T., Yagihashi N., Hatakeyama M., Yamashita K., Ishikawa A., Taima K., Yoshida H., Inoue I., Fujita T., Yagihashi S., Satoh K.
    Life Sci. 75:1171-1180(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. "The RNA helicase RIG-I has an essential function in double-stranded RNA-induced innate antiviral responses."
    Yoneyama M., Kikuchi M., Natsukawa T., Shinobu N., Imaizumi T., Miyagishi M., Taira K., Akira S., Fujita T.
    Nat. Immunol. 5:730-737(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, MUTAGENESIS OF LYS-270, SUBCELLULAR LOCATION, BINDING TO DOUBLE-STRANDED RNA, FUNCTION.
  10. "Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-kappaB and IRF 3."
    Seth R.B., Sun L., Ea C.-K., Chen Z.J.
    Cell 122:669-682(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAVS/IPS1.
  11. "SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways."
    Huang J., Liu T., Xu L.-G., Chen D., Zhai Z., Shu H.-B.
    EMBO J. 24:4018-4028(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IKBKE AND TBK1.
  12. "Regulating intracellular antiviral defense and permissiveness to hepatitis C virus RNA replication through a cellular RNA helicase, RIG-I."
    Sumpter R. Jr., Loo Y.-M., Foy E., Li K., Yoneyama M., Fujita T., Lemon S.M., Gale M. Jr.
    J. Virol. 79:2689-2699(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, MUTAGENESIS OF THR-55 AND LYS-270, BINDING TO DOUBLE-STRANDED RNA, FUNCTION.
  13. "VISA is an adapter protein required for virus-triggered IFN-beta Signaling."
    Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B.
    Mol. Cell 19:727-740(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAVS/IPS1.
  14. "IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction."
    Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J., Takeuchi O., Akira S.
    Nat. Immunol. 6:981-988(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAVS/IPS1.
  15. "Human ISG15 conjugation targets both IFN-induced and constitutively expressed proteins functioning in diverse cellular pathways."
    Zhao C., Denison C., Huibregtse J.M., Gygi S.P., Krug R.M.
    Proc. Natl. Acad. Sci. U.S.A. 102:10200-10205(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ISGYLATION.
  16. "TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity."
    Gack M.U., Shin Y.C., Joo C.H., Urano T., Liang C., Sun L., Takeuchi O., Akira S., Chen Z., Inoue S., Jung J.U.
    Nature 446:916-920(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM25, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF LYS-99; LYS-169; LYS-172; LYS-181 AND LYS-193.
  17. "Regulation of innate antiviral defenses through a shared repressor domain in RIG-I and LGP2."
    Saito T., Hirai R., Loo Y.-M., Owen D., Johnson C.L., Sinha S.C., Akira S., Fujita T., Gale M. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 104:582-587(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, REPRESSOR DOMAIN, INTERACTION WITH DHX58.
  18. Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH CYLD.
  19. "Negative feedback regulation of RIG-I-mediated antiviral signaling by interferon-induced ISG15 conjugation."
    Kim M.J., Hwang S.Y., Imaizumi T., Yoo J.Y.
    J. Virol. 82:1474-1483(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION.
  20. "STING is an endoplasmic reticulum adaptor that facilitates innate immune signalling."
    Ishikawa H., Barber G.N.
    Nature 455:674-678(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMEM173.
  21. "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.
  22. "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.
  23. "Riplet/RNF135, a RING finger protein, ubiquitinates RIG-I to promote interferon-beta induction during the early phase of viral infection."
    Oshiumi H., Matsumoto M., Hatakeyama S., Seya T.
    J. Biol. Chem. 284:807-817(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH RNF135.
  24. "Retinoic acid-induced gene-1 (RIG-I) associates with the actin cytoskeleton via caspase activation and recruitment domain-dependent interactions."
    Mukherjee A., Morosky S.A., Shen L., Weber C.R., Turner J.R., Kim K.S., Wang T., Coyne C.B.
    J. Biol. Chem. 284:6486-6494(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  25. "Regulation of signal transduction by enzymatically inactive antiviral RNA helicase proteins MDA5, RIG-I, and LGP2."
    Bamming D., Horvath C.M.
    J. Biol. Chem. 284:9700-9712(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling."
    Johnsen I.B., Nguyen T.T., Bergstroem B., Fitzgerald K.A., Anthonsen M.W.
    J. Biol. Chem. 284:19122-19131(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRC.
  27. "Human respiratory syncytial virus nonstructural protein NS2 antagonizes the activation of beta interferon transcription by interacting with RIG-I."
    Ling Z., Tran K.C., Teng M.N.
    J. Virol. 83:3734-3742(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRSV PROTEIN NS2.
  28. "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.
  29. "REUL is a novel E3 ubiquitin ligase and stimulator of retinoic-acid-inducible gene-I."
    Gao D., Yang Y.K., Wang R.P., Zhou X., Diao F.C., Li M.D., Zhai Z.H., Jiang Z.F., Chen D.Y.
    PLoS ONE 4:E5760-E5760(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-154; LYS-164 AND LYS-172, INTERACTION WITH RNF135, MUTAGENESIS OF LYS-154; LYS-164 AND LYS-172.
  30. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-858, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways."
    Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., Ji J., Shen P., Zheng S., Chen Z.J., Wang R.F.
    Cell 141:483-496(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NLRC5.
  32. "The ubiquitin-specific protease 17 is involved in virus-triggered type I IFN signaling."
    Chen R., Zhang L., Zhong B., Tan B., Liu Y., Shu H.B.
    Cell Res. 20:802-811(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP17L2.
  33. "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.
  34. "Z proteins of New World arenaviruses bind RIG-I and interfere with type I interferon induction."
    Fan L., Briese T., Lipkin W.I.
    J. Virol. 84:1785-1791(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEW WORLD ARENAVIRUSES PROTEIN Z.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "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.
  37. "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.
  38. "Innate immune responses in human monocyte-derived dendritic cells are highly dependent on the size and the 5' phosphorylation of RNA molecules."
    Jiang M., Osterlund P., Sarin L.P., Poranen M.M., Bamford D.H., Guo D., Julkunen I.
    J. Immunol. 187:1713-1721(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  39. "IFN-induced TPR protein IFIT3 potentiates antiviral signaling by bridging MAVS and TBK1."
    Liu X.Y., Chen W., Wei B., Shan Y.F., Wang C.
    J. Immunol. 187:2559-2568(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IFIT3.
  40. Cited for: REVIEW ON FUNCTION.
  41. "Phosphorylation of RIG-I by casein kinase II inhibits its antiviral response."
    Sun Z., Ren H., Liu Y., Teeling J.L., Gu J.
    J. Virol. 85:1036-1047(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-770; SER-854 AND SER-855.
  42. "DDX60, a DEXD/H box helicase, is a novel antiviral factor promoting RIG-I-like receptor-mediated signaling."
    Miyashita M., Oshiumi H., Matsumoto M., Seya T.
    Mol. Cell. Biol. 31:3802-3819(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX60.
  43. Cited for: INTERACTION WITH ZC3HAV1, SUBCELLULAR LOCATION.
  44. "Rotavirus nonstructural protein 1 antagonizes innate immune response by interacting with retinoic acid inducible gene I."
    Qin L., Ren L., Zhou Z., Lei X., Chen L., Xue Q., Liu X., Wang J., Hung T.
    Virol. J. 8:526-526(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ROTAVIRUS PROTEIN NSP1.
  45. "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.
  46. Cited for: SUMOYLATION BY MUL1.
  47. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 802-925 IN COMPLEX WITH ZINC IONS.
  48. "Nonself RNA-sensing mechanism of RIG-I helicase and activation of antiviral immune responses."
    Takahasi K., Yoneyama M., Nishihori T., Hirai R., Kumeta H., Narita R., Gale M. Jr., Inagaki F., Fujita T.
    Mol. Cell 29:428-440(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 792-925.

Entry informationi

Entry nameiDDX58_HUMAN
AccessioniPrimary (citable) accession number: O95786
Secondary accession number(s): A2RU81
, Q5HYE1, Q5VYT1, Q9NT04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: October 29, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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