Protein detail

RIGI

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

Entry name
RIGI
UniProt ID
O95786
EVMP confidence score
0.40
Supporting publications (n)
3
Transmembrane count
Protein classification
Disease related genesEnzymesHuman disease related genesPotential drug targetsPredicted intracellular proteins
Basic Information
Protein Names
Antiviral innate immune response receptor RIG-I (ATP-dependent RNA helicase DDX58) (EC 3.6.4.13) (DEAD box protein 58) (RIG-I-like receptor 1) (RLR-1) (RNA sensor RIG-I) (Retinoic acid-inducible gene 1 protein) (RIG-1) (Retinoic acid-inducible gene I protein) (RIG-I)
Protein Class (5)
Disease related genesEnzymesHuman disease related genesPotential drug targetsPredicted intracellular proteins
Protein Function (6)
  • Predicted intracellular proteins
  • Human disease related genes:Congenital malformations:Congenital malformations of the musculoskeletal system
  • Potential drug targets
  • Enzymes
  • ENZYME proteins:Hydrolases
  • Disease related genes
Ensembl
ENSG00000107201
Entrez Gene Symbol
RIGI
Gene Synonym (6)
DDX58DKFZp434J1111FLJ13599RIG-1RIG-IRIG1
Gene Description
RNA sensor RIG-I
Chromosome
9
Position
32455302-32526208
Supporting publications (n)
3
EVMP confidence score
0.40
Function & Pathway
Protein Function (6)
  • Predicted intracellular proteins
  • Human disease related genes:Congenital malformations:Congenital malformations of the musculoskeletal system
  • Potential drug targets
  • Enzymes
  • ENZYME proteins:Hydrolases
  • Disease related genes
Cellular Component (6)
Molecular Function (12)
Page 1 of 2
Biological Process (3)
KEGG (10)
Reactome (29)
Page 1 of 3
Canonical Pathways
M198 Pid syndecan 1 pathway
Mediation Categories (4)
Clinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediation
Relations & Evidence49

Enzyme-Mediated Modification (20)

20 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
RIGIDAPK1P53355T671phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIDAPK1P53355S764phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIDAPK1P53355T770phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIDAPK1P53355S8phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIDAPK1P53355T674phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIDAPK1P53355T667phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIIKBKEQ14164S855phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIPRKCAP17252T170phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIPRKCAP17252S8phosphorylationPhosphoSitePhosphoSite_ProtMapperProtMapper
RIGIVCLP18206S8phosphorylationREACH_ProtMapperProtMapperProtMapper:25011106
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Ligand-Receptor Signaling (9)

9 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorOmniPathYes
intracellularintracellularLOCATE
intracellularintracellularComPPI
intracellularintracellularGO_Intercell
intracellularintracellularUniProt_location
intracellularintracellularOmniPath
tight_junctiontight_junctionGO_IntercellYesYes
tight_junctiontight_junctionOmniPathYesYes
receptorreceptorscConnectYes

Regulatory Interaction Network (14)

14 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
RIGIO95786MAVSQ7Z434YesYesYesWangMacrophageKEGG-MEDICUSSIGNORHPRDHINTBioGRIDIntActInnateDBDIPSPIKE_LCSPIKEInnateDB:18207245InnateDB:19881509HINT:25018021Macrophage:16301520HINT:34544279HINT:22844514InnateDB:21200404HINT:33976430BioGRID:20554965BioGRID:16177806InnateDB:21102435HINT:17709747BioGRID:29263274IntAct:19193793IntAct:20007272DIP:21844353InnateDB:23843640HINT:21844353InnateDB:22844514HPRD:16177806IntAct:17190814IntAct:26494172DIP:26494172HINT:20080758InnateDB:16127453InnateDB:18977754IntAct:17709747IntAct:22301138InnateDB:21844353BioGRID:37870297DIP:16585524HINT:19036819DIP:17190814BioGRID:33976430SPIKE:16177806HINT:24478431HINT:33372174Macrophage:16125763DIP:18200010HINT:18948594IntAct:33976430Macrophage:16127453HINT:21903422HINT:22301138HINT:19193793DIP:17709747Macrophage:16713980InnateDB:21903422SPIKE_LC:17145710HINT:16177806HINT:19164550BioGRID:34544279HINT:18977754HINT:20007272InnateDB:16153868Macrophage:16153868IntAct:34544279HINT:16153868HINT:21102435SPIKE_LC:16177806HINT:17190814DIP:19164550HINT:35075101HINT:17020950DIP:20080758HINT:21419663InnateDB:19036819Macrophage:17020950InnateDB:20406818IntAct:35075101InnateDB:21419663InnateDB:17190814IntAct:21102435InnateDB:18948594IntAct:24478431IntAct:18200010HINT:16585524IntAct:19164550HINT:18200010InnateDB:23499489InnateDB:16585524InnateDB:17020950HINT:16127453IntAct:16177806InnateDB:16177806IntAct:16585524Macrophage:16177806IntAct:33372174HINT:18207245HINT:26494172HINT:20406818Macrophage:16785313SIGNOR:19052324HINT:19881509
RN135Q8IUD6RIGIO95786YesYesSIGNORHINTBioGRIDInnateDBSPIKE_LCLit-BM-17SPIKEHINT:33536170HINT:19484123InnateDB:23950712HINT:37951994Lit-BM-17:19017631Lit-BM-17:19484123HINT:33373584BioGRID:35089988SIGNOR:19017631SPIKE_LC:19017631SPIKE:19017631HINT:31006531Lit-BM-17:23950712InnateDB:19484123HINT:19017631InnateDB:19017631
TRI25Q14258RIGIO95786YesYesWangMacrophageKEGG-MEDICUSSIGNORHINTBioGRIDIntActInnateDBSPIKE_LCSPIKEHINT:19675569SIGNOR:17392790HINT:25172487IntAct:34471099InnateDB:20406818HINT:34471099HINT:20818395IntAct:35075101BioGRID:37628607InnateDB:23950712HINT:34452305InnateDB:18948594BioGRID:36975005HINT:31600868InnateDB:20818395SIGNOR:24493797IntAct:24478431InnateDB:17392790BioGRID:32513696Macrophage:17392790SPIKE_LC:18353649BioGRID:32295922HINT:23264040SPIKE:18353649HINT:24478431BioGRID:36146771BioGRID:33770145BioGRID:34452305HINT:17392790HINT:35075101HINT:18948594BioGRID:30902577BioGRID:27122586BioGRID:34529741HINT:20406818
RN125Q96EQ8RIGIO95786YesYesMacrophageKEGG-MEDICUSSIGNORHINTInnateDBWangHINT:17460044SIGNOR:17460044HINT:26471729InnateDB:17460044Macrophage:17460044
CSK21P68400RIGIO95786YesYesPhosphoSite_MIMPMIMPPhosphoSite_norefSIGNORiPTMnetProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperPhosphoSite:26354181SIGNOR:21068236ProtMapper:21068236
TERAP55072RIGIO95786YesYesSIGNORSIGNOR:26471729
DAPK1P53355RIGIO95786YesYesSparser_ProtMapperPhosphoSite_norefSIGNORProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapperSIGNOR:30985869PhosphoSite:28132841PhosphoSite:20406818ProtMapper:30985869SIGNOR:28132841ProtMapper:33462384PhosphoSite:21068236
TRI58Q8NG06RIGIO95786YesYesSIGNORSIGNOR:23499489
COMPLEX:Q96EP0_Q9BYM8RIGIO95786YesYesSIGNORSIGNOR:21292167
CSK22P19784RIGIO95786YesYesSIGNORSIGNOR:21068236
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Protein Complex Composition (5)

5 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
Ubiquitin E3 ligase (TRIM25DDX58)RIGITRIM25O95786Q142581:1CompleatCORUMCompleat:HC525CORUM:271717392790
NSMCE1NSMCE2NSMCE3NSMCE4APDE6DRIGISMC5SMC6O43924O95786Q8IY18Q8WV22Q96MF7Q96MG7Q96SB8Q9NXX61:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC7679
RIGIO9578610PDBPDB:3lrnPDB:7baiPDB:5f9hPDB:3ncuPDB:5f98PDB:7bahPDB:4on9PDB:3lrrPDB:3og8PDB:6kyvPDB:5f9fPDB:2qfdPDB:7mk1PDB:2qfb
RIGIUBCO95786P0CG484:6PDBPDB:4nqk
MAVSRIGIUBA52O95786P62987Q7Z4348:5:8PDBPDB:4p4h

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationWestern BlottingMass SpectrometryFlow Cytometry138207106
Sequence, Structure & Domains

Sequences

Length
925
Mass
106,600
Sequence
MTTEQRRSLQAFQDYIRKTLDPTYILSYMAPWFREEEVQYIQAEKNNKGPMEAATLFLKFLLELQEEGWFRGFLDALDHAGYSGLYEAIESWDFKKIEKLEEYRLLLKRLQPEFKTRIIPTDIISDLSECLINQECEEILQICSTKGMMAGAEKLVECLLRSDKENWPKTLKLALEKERNKFSELWIVEKGIKDVETEDLEDKMETSDIQIFYQEDPECQNLSENSCPPSEVSDTNLYSPFKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKGKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENNDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYLDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIATVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICKDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLYTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFEEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVDALKNWIEGNPKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGDHNILIATSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKECFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEMSK
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=O95786-1; Sequence=Displayed; Name=2; IsoId=O95786-2; Sequence=VSP_016054
Alternative Sequence
36..80; Missing (in isoform 2)

3D Structural Models

Turn
26..32; 83..85; 183..185; 314..318; 811..813; 827..829; 867..869; 897..899
Helix
2..11; 13..19; 22..25; 35..48; 50..63; 69..80; 86..91; 95..99; 101..117; 120..127; 128..130; 133..146; 148..160; 167..177; 245..255; 270..284; 300..313; 334..339; 348..356; 363..365; 374..376; 382..395; 420..433; 446..452; 470..489; 493..495; 507..518; 531..557; 560..575; 581..591; 594..602; 604..606; 609..622; 637..649; 651..653; 675..683; 706..708; 721..726; 727..731; 745..768; 773..793; 820..822; 838..840; 889..891; 908..910; 920..922
Beta Strand
260..263; 265..267; 293..296; 321..324; 326..328; 330..332; 342..346; 358..360; 367..372; 378..381; 396..398; 404..410; 438..440; 443..445; 457..462; 496..498; 504..506; 526..528; 630..633; 658..660; 667..670; 686..690; 694..700; 701..703; 710..716; 733..735; 737..743; 801..804; 806..810; 816..819; 823..826; 830..833; 835..837; 842..846; 853..855; 856..865; 872..879; 882..887; 892..896; 902..904
3D Structure
Electron microscopy (16); NMR spectroscopy (3); X-ray crystallography (23)

Domain & Motif Annotations

Motif
372..375; DECH box
Domain (CC)
The RLR CTR domain controls homooligomerization 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 with the RLR CTR domain. Upon binding to viral RNA and ubiquitination by RNF135, a conformational change releases the autoinhibition promoting further homooligomerization, interaction of the CARD domains with the adapter protein MAVS/IPS1 and activation of the downstream RIG-I signaling pathway.; DOMAIN: The helicase domain is responsible for dsRNA recognition.; DOMAIN: The 2 CARD domains are responsible for interaction with and signaling through MAVS/IPS1 and for association with the actin cytoskeleton.; DOMAIN: The second CARD domain is the primary site for 'Lys-63'-linked ubiquitination.
Domain (FT)
1..87; CARD 1; 92..172; CARD 2; 251..430; Helicase ATP-binding; 610..776; Helicase C-terminal; 794..925; RLR CTR
Region
218..925; Interaction with ZC3HAV1; 735..925; Mediates interaction with RNF135
Protein Families (2)
  • Helicase family
  • RLR subfamily
Sequence Similarities
Belongs to the helicase family. RLR subfamily.
Clinical Relevance
Disease Involvement
Disease variant
Drug Targets
Clinical trial target
Drugs (2)
INARIGIVIR SOPROXILNULL
Antibody (3)
CAB012643HPA047193HPA073217
Interaction Protein (4)
ENSG00000088888ENSG00000101695ENSG00000121060ENSG00000124535
Interaction Count
4
Interaction Dataset
intact_biogrid
Supporting Publications3
PMIDTitleRelated sentences
27086912Comparative proteomics of exosomes secreted by tumoral Jurkat T cells and normal human T cell blasts unravels a potential tumorigenic role for valosin-containing protein.No related sentences available
33893753Label-free quantitative proteomic analysis of extracellular vesicles released from fibroblasts derived from patients with spinal muscular atrophy.No related sentences available
38716512Assessment of urine sample collection and processing variables for extracellular vesicle-based proteomics.No related sentences available