CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017889
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Interferon-induced helicase C domain-containing protein 1 
Protein Synonyms/Alias
 Helicase with 2 CARD domains; Helicard; Interferon induced with helicase C domain protein 1; Melanoma differentiation-associated protein 5; MDA-5; RIG-I-like receptor 2; RLR-2 
Gene Name
 Ifih1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
477NDLKKQNKPAIPLPQubiquitination[1]
523AFTIKTVKENLGQLKubiquitination[1]
950ENKALQKKFADYQTNubiquitination[1]
983GLDLPCLKIRNFVVNubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 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 mRNA lacking 2'-O- methylation at their 5' cap and long-dsRNA (>1 kb in length). 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. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and theiler's murine encephalomyelitis virus (TMEV). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines. 
Sequence Annotation
 DOMAIN 7 97 CARD 1.
 DOMAIN 110 190 CARD 2.
 DOMAIN 317 510 Helicase ATP-binding.
 DOMAIN 700 872 Helicase C-terminal.
 METAL 907 907 Zinc (By similarity).
 METAL 910 910 Zinc (By similarity).
 METAL 962 962 Zinc (By similarity).
 METAL 964 964 Zinc (By similarity).
 MOD_RES 289 289 Phosphoserine.
 MOD_RES 302 302 Phosphoserine.
 MOD_RES 645 645 Phosphoserine.
 MOD_RES 648 648 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Antiviral defense; ATP-binding; Complete proteome; Cytoplasm; Helicase; Hydrolase; Immunity; Innate immunity; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1025 AA 
Protein Sequence
MSIVCSAEDS FRNLILFFRP RLKMYIQVEP VLDHLIFLSA ETKEQILKKI NTCGNTSAAE 60
LLLSTLEQGQ WPLGWTQMFV EALEHSGNPL AARYVKPTLT DLPSPSSETA HDECLHLLTL 120
LQPTLVDKLL INDVLDTCFE KGLLTVEDRN RISAAGNSGN ESGVRELLRR IVQKENWFST 180
FLDVLRQTGN DALFQELTGG GCPEDNTDLA NSSHRDGPAA NECLLPAVDE SSLETEAWNV 240
DDILPEASCT DSSVTTESDT SLAEGSVSCF DESLGHNSNM GRDSGTMGSD SDESVIQTKR 300
VSPEPELQLR PYQMEVAQPA LDGKNIIICL PTGSGKTRVA VYITKDHLDK KKQASESGKV 360
IVLVNKVMLA EQLFRKEFNP YLKKWYRIIG LSGDTQLKIS FPEVVKSYDV IISTAQILEN 420
SLLNLESGDD DGVQLSDFSL IIIDECHHTN KEAVYNNIMR RYLKQKLRNN DLKKQNKPAI 480
PLPQILGLTA SPGVGAAKKQ SEAEKHILNI CANLDAFTIK TVKENLGQLK HQIKEPCKKF 540
VIADDTRENP FKEKLLEIMA SIQTYCQKSP MSDFGTQHYE QWAIQMEKKA AKDGNRKDRV 600
CAEHLRKYNE ALQINDTIRM IDAYSHLETF YTDEKEKKFA VLNDSDKSDD EASSCNDQLK 660
GDVKKSLKLD ETDEFLMNLF FDNKKMLKKL AENPKYENEK LIKLRNTILE QFTRSEESSR 720
GIIFTKTRQS TYALSQWIME NAKFAEVGVK AHHLIGAGHS SEVKPMTQTE QKEVISKFRT 780
GEINLLIATT VAEEGLDIKE CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVTSSGSGV 840
TEREIVNDFR EKMMYKAINR VQNMKPEEYA HKILELQVQS ILEKKMKVKR SIAKQYNDNP 900
SLITLLCKNC SMLVCSGENI HVIEKMHHVN MTPEFKGLYI VRENKALQKK FADYQTNGEI 960
ICKCGQAWGT MMVHKGLDLP CLKIRNFVVN FKNNSPKKQY KKWVELPIRF PDLDYSEYCL 1020
YSDED 1025 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0043021; F:ribonucleoprotein complex binding; IEA:Compara.
 GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0045087; P:innate immune response; IMP:UniProtKB.
 GO:0032727; P:positive regulation of interferon-alpha production; ISS:UniProtKB.
 GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
 GO:0016925; P:protein sumoylation; ISS:UniProtKB.
 GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
 GO:0009615; P:response to virus; IMP:UniProtKB. 
Interpro
 IPR001315; CARD.
 IPR011029; DEATH-like_dom.
 IPR006935; Helicase/UvrB_dom.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR021673; RIG-I_C-RD. 
Pfam
 PF00619; CARD
 PF00271; Helicase_C
 PF04851; ResIII
 PF11648; RIG-I_C-RD 
SMART
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS50209; CARD
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS