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Protein Page:
DDX58 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DDX58 an 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 which activates the IKK- related kinases TBK1 and IKBKE which phosphorylate interferon regulatory factors IRF3 and IRF7, in turn activating transcription of antiviral immunological genes, including IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory synctial 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. Maintained as a monomer in an autoinhibited state. Upon viral dsRNA binding and conformation shift, homomultimerizes and interacts with MAVS. Interacts with DHX58, IKBKE, TBK1 and STING. Interacts (via CARD domain) with TRIM25 (via SPRY domain). Interacts with RNF135. Interacts with CYLD. Interacts with NLRC5; blocks the interaction of MAVS 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, 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, impeding downstream IRF3 activation. Present in vascular smooth cells. Belongs to the helicase family. RLR subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.6.1.-; EC 3.6.4.13; Hydrolase
Cellular Component: tight junction; cytoplasm; cytosol; actin cytoskeleton
Molecular Function: identical protein binding; protein binding; single-stranded RNA binding; zinc ion binding; double-stranded DNA binding; double-stranded RNA binding; helicase activity; ATP binding
Biological Process: viral reproduction; metabolic process; response to virus; regulation of cell migration; response to exogenous dsRNA; detection of virus; positive regulation of interferon-beta production; positive regulation of transcription factor import into nucleus; innate immune response; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription factor activity; positive regulation of defense response to virus by host; negative regulation of interferon type I production; positive regulation of interferon-alpha production
Reference #:  O95786 (UniProtKB)
Alt. Names/Synonyms: DDX58; DEAD (Asp-Glu-Ala-Asp) box polypeptide 58; DEAD box protein 58; DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide; DKFZp434J1111; DKFZp686N19181; FLJ13599; Probable ATP-dependent RNA helicase DDX58; retinoic acid inducible gene I; Retinoic acid-inducible gene 1 protein; Retinoic acid-inducible gene I protein; RIG-1; RIG-I; RNA helicase RIG-I
Gene Symbols: DDX58
Molecular weight: 106,600 Da
Basal Isoelectric point: 6.03  Predict pI for various phosphorylation states
CST Pathways:  Toll-Like Receptor Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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DDX58

Protein Structure Not Found.


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Sites Implicated In
transcription, induced: T170‑p
enzymatic activity, inhibited: T770‑p, S854‑p, S855‑p
intracellular localization: S8‑p
molecular association, regulation: S8‑p, T170‑p, T770‑p, S854‑p, S855‑p
protein conformation: T170‑p
ubiquitination: S8‑p, T170‑p, K172‑ub

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
5 3 S8-p MTTEQRRsLQAFQDY
0 1 Y40-p FREEEVQyIQAEKNN
1 0 K99-ub WDFKKIEkLEEYRLL
1 0 K154-ub GMMAGAEkLVECLLR
1 0 K164-ub ECLLRSDkENWPktL
2 0 K169-ub SDkENWPktLkLALE
6 1 T170-p DkENWPktLkLALEK
5 0 K172-ub ENWPktLkLALEKER
1 0 K181-ub ALEKERNkFSELWIV
1 0 K190-ub SELWIVEkGIkDVEt
2 0 K193-ub WIVEkGIkDVEtEDL
0 1 T197-p kGIkDVEtEDLEDKM
0 1 K284 ICEHHLKKFPQGQKG
0 1 K292 FPQGQKGKVVFFANQ
0 1 N495 RICKDLENLSQIQNR
0 1 S599 EKLQELESVSRDPSN
0 4 K644-ub RALVDALkNWIEGNP
1 1 T770-p DSILRLQtWDEAVFR
0 1 V775 LQtWDEAVFREKILH
0 1 S793 HEKFIRDSQEkPKPV
0 1 K796-ub FIRDSQEkPKPVPDK
0 1 K851 SRPHPKPKQFssFEk
1 1 S854-p HPKPKQFssFEkRAK
1 1 S855-p PKPKQFssFEkRAKI
0 1 K858-ac KQFssFEkRAKIFCA
0 2 R859 QFssFEkRAKIFCAR
0 1 K861 ssFEkRAKIFCARQN
0 1 Y879-p DWGIHVKyKTFEIPV
0 1 K909-ac QTLYSKWkDFHFEKI
  mouse

 
N8 MTAEQRQNLQAFRDY
Y40 LEDEEVQYIQAEKNN
K99 WDFQKIEKLEEHRLL
K154 GRMAGAEKMAECLIR
K164 ECLIRSDKENWPKVL
K169 SDKENWPKVLQLALE
V170 DKENWPKVLQLALEK
Q172 ENWPKVLQLALEKDN
K181 ALEKDNSKFSELWIV
K190 SELWIVDKGFKRAES
K193 WIVDKGFKRAESKAD
S197 KGFKRAESKADEDDG
K285-ub ICEHHLKkFPCGQKG
K293-ub FPCGQKGkVVFFANQ
K496-ub DVSEELGkLFQIQNR
K600-ub EKLEELEkVSRDPSN
K645-ub RALVDALkKWIEENP
T771 ESILRLQTWDEMkFG
K776-ac LQTWDEMkFGKTVHR
S794-p NEKLLRDsQHKPQPV
K797 LLRDsQHKPQPVPDK
K852-ac CKPHPKPkIYDNFEK
D855 HPKPkIYDNFEKkAk
N856 PKPkIYDNFEKkAkI
K859 kIYDNFEKkAkIFCA
K860-ac IYDNFEKkAkIFCAK
K862-ac DNFEKkAkIFCAKQN
Y880 DWGIFVRYKTFEIPV
K910 QNRHSKWKDFHFERI
  duck

 
S8 MTADEKRSLQCYRRY
R40 LPDELRERIRKEEER
K98 WDFSKLEKLELHRQL
K152 SKAAGITKLIECLCR
K162 ECLCRSDKEHWPkSL
K167-ub SDKEHWPkSLQLALD
S168 DKEHWPkSLQLALDT
Q170 EHWPkSLQLALDTTG
R180 LDTTGYYRASELWDI
R188 ASELWDIREDNAkDV
K193-ub DIREDNAkDVDSEMT
S197 DNAkDVDSEMTDASE
N287 ICEHHFQNMPAGRKA
K295 MPAGRKAKVVFLATK
T496 RTIYSVDTLSQNSKK
A600 EKEPELIALSKDETN
K645 RALVSALKKCMEENP
K771 KAVEKIQKWDEETFA
T776 IQKWDEETFAKKIHN
S794 KERVLRDSRRKEIKP
K797 VLRDSRRKEIKPKVV
M853 TKPHKKPMQFDGFEK
D856 HKKPMQFDGFEKKSK
G857 KKPMQFDGFEKKSKM
K860 MQFDGFEKKSKMYCR
K861 QFDGFEKKSKMYCRN
K863 DGFEKKSKMYCRNNN
Y881 DWGITVKYLTFDNLP
K912 QMDFQKWKSINSSLK
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