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)

Protein symbol
RIGI
UniProt ID
EVMP score
0.50
Frequency
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
Disease related genesEnzymesHuman disease related genesPotential drug targetsPredicted intracellular proteins
Protein Function
  • 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
Entrez Gene Symbol
Gene Synonym
DDX58DKFZp434J1111FLJ13599RIG-1RIG-IRIG1
Gene Description
RNA sensor RIG-I
Chromosome
9
Position
32455302-32526208
Frequency
3
EVMP Score
0.50
Fluorescence & Localization
Function & Pathway
Protein Function
  • 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
Canonical Pathways
M198 Pid syndecan 1 pathway
Mediation Categories
Clinical-translation mediationFusion and delivery mediationImmune mediationMetabolism mediation
Relations & Evidence

Enzyme-Mediated Modification

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 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorOmniPathNoYesNoNoNo
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo
tight_junctiontight_junctionGO_IntercellYesYesNoNoNo
tight_junctiontight_junctionOmniPathYesYesNoNoNo
receptorreceptorscConnectNoYesNoNoNo

Regulatory Interaction Network

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
RN135Q8IUD6RIGIO95786YesYesNoSIGNORHINTBioGRIDInnateDBSPIKE_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
TRI25Q14258RIGIO95786YesYesNoWangMacrophageKEGG-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
RN125Q96EQ8RIGIO95786YesNoYesMacrophageKEGG-MEDICUSSIGNORHINTInnateDBWangHINT:17460044SIGNOR:17460044HINT:26471729InnateDB:17460044Macrophage:17460044
CSK21P68400RIGIO95786YesNoYesPhosphoSite_MIMPMIMPPhosphoSite_norefSIGNORiPTMnetProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperPhosphoSite:26354181SIGNOR:21068236ProtMapper:21068236
TERAP55072RIGIO95786YesNoYesSIGNORSIGNOR:26471729
DAPK1P53355RIGIO95786YesNoYesSparser_ProtMapperPhosphoSite_norefSIGNORProtMapperREACH_ProtMapperPhosphoSitePhosphoSite_ProtMapperSIGNOR:30985869PhosphoSite:28132841PhosphoSite:20406818ProtMapper:30985869SIGNOR:28132841ProtMapper:33462384PhosphoSite:21068236
TRI58Q8NG06RIGIO95786YesYesNoSIGNORSIGNOR:23499489
COMPLEX:Q96EP0_Q9BYM8RIGIO95786YesNoYesSIGNORSIGNOR:21292167
CSK22P19784RIGIO95786YesNoYesSIGNORSIGNOR:21068236
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Protein Complex Composition

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 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
  • Helicase family
  • RLR subfamily
Sequence Similarities
Belongs to the helicase family. RLR subfamily.
Clinical Relevance
Disease Involvement
Disease variant
Drug Targets
Clinical trial target
Interaction Protein
ENSG00000088888ENSG00000101695ENSG00000121060ENSG00000124535
Interaction Count
4
Interaction Dataset
intact_biogrid