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Protein

Interferon-induced helicase C domain-containing protein 1

Gene

IFIH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 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) and mengo encephalomyocarditis virus (ENMG). 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.5 Publications

Miscellaneous

In HIV-1 infected HeLa-CD4 cells, overexpression of IFIH1 results in a great increase in the level of secreted viral p24 protein.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi907ZincPROSITE-ProRule annotation1
Metal bindingi910ZincPROSITE-ProRule annotation1
Metal bindingi962ZincPROSITE-ProRule annotation1
Metal bindingi964ZincPROSITE-ProRule annotation1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: InterPro
  • double-stranded RNA binding Source: UniProtKB
  • helicase activity Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • ribonucleoprotein complex binding Source: UniProtKB
  • single-stranded RNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular response to exogenous dsRNA Source: UniProtKB
  • cytoplasmic pattern recognition receptor signaling pathway in response to virus Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • detection of virus Source: BHF-UCL
  • innate immune response Source: UniProtKB
  • MDA-5 signaling pathway Source: UniProtKB
  • negative regulation of type I interferon production Source: Reactome
  • positive regulation of interferon-alpha production Source: UniProtKB
  • positive regulation of interferon-alpha secretion Source: UniProtKB
  • positive regulation of interferon-beta production Source: UniProtKB
  • positive regulation of interferon-beta secretion Source: UniProtKB
  • positive regulation of interleukin-6 secretion Source: UniProtKB
  • positive regulation of response to cytokine stimulus Source: UniProtKB
  • positive regulation of tumor necrosis factor secretion Source: UniProtKB
  • protein deubiquitination Source: Reactome
  • protein sumoylation Source: UniProtKB
  • regulation of type III interferon production Source: UniProtKB
  • response to virus Source: UniProtKB
  • viral process Source: UniProtKB-KW

Keywordsi

Molecular functionHelicase, Hydrolase, RNA-binding
Biological processAntiviral defense, Host-virus interaction, Immunity, Innate immunity
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-168928. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-5689896. Ovarian tumor domain proteases.
R-HSA-918233. TRAF3-dependent IRF activation pathway.
R-HSA-933541. TRAF6 mediated IRF7 activation.
R-HSA-933542. TRAF6 mediated NF-kB activation.
R-HSA-933543. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon-induced helicase C domain-containing protein 1 (EC:3.6.4.13)
Alternative name(s):
Clinically amyopathic dermatomyositis autoantigen 140 kDa
Short name:
CADM-140 autoantigen
Helicase with 2 CARD domains
Short name:
Helicard
Interferon-induced with helicase C domain protein 1
Melanoma differentiation-associated protein 5
Short name:
MDA-5
Murabutide down-regulated protein
RIG-I-like receptor 2
Short name:
RLR-2
RNA helicase-DEAD box protein 116
Gene namesi
Name:IFIH1
Synonyms:MDA5, RH116
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18873. IFIH1.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Diabetes mellitus, insulin-dependent, 19 (IDDM19)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
See also OMIM:610155
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021595946A → T Associated with susceptibility to IDDM19. 3 PublicationsCorresponds to variant dbSNP:rs1990760Ensembl.1
IFIH1 is the CADM-140 autoantigen, involved in clinically amyopathic dermatomyositis (CADM). This is a chronic inflammatory disorder that shows typical skin manifestations of dermatomyositis but has no or little evidence of clinical myositis. Anti-CADM-140 antibodies appear to be specific to dermatomyositis, especially CADM. Patients with anti-CADM-140 antibodies frequently develop life-threatening acute progressive interstitial lung disease (ILD).2 Publications
Aicardi-Goutieres syndrome 7 (AGS7)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood.
See also OMIM:615846
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071375337R → G in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777447Ensembl.1
Natural variantiVAR_071376372L → F in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness. 1 PublicationCorresponds to variant dbSNP:rs587777576Ensembl.1
Natural variantiVAR_071377393D → V in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777449Ensembl.1
Natural variantiVAR_071378452A → T in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness. 1 PublicationCorresponds to variant dbSNP:rs587777575Ensembl.1
Natural variantiVAR_071379495G → R in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs672601336Ensembl.1
Natural variantiVAR_071380720R → Q in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777445Ensembl.1
Natural variantiVAR_071381779R → C in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777448Ensembl.1
Natural variantiVAR_071382779R → H in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; enhances IFNB1 promoter activation; no loss of ATP hydrolysis. 2 PublicationsCorresponds to variant dbSNP:rs587777446Ensembl.1
Singleton-Merten syndrome 1 (SGMRT1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder with variable expression. Core features are marked aortic calcification, dental anomalies, osteopenia, acro-osteolysis, and to a lesser extend glaucoma, psoriasis, muscle weakness, and joint laxity. Dental anomalies include delayed eruption and immature root formation of anterior permanent teeth, early loss of permanent teeth due to short roots, acute root resorption, high caries, and aggressive alveolar bone loss. Additional clinical manifestations include particular facial characteristics and abnormal joint and muscle ligaments.
See also OMIM:182250
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073666822R → Q in SGMRT1; gain-of-function mutation resulting in enhanced INFB1 induction. 1 PublicationCorresponds to variant dbSNP:rs376048533Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi251D → A: No cleavage and no acceleration of DNA degradation. 1 Publication1
Mutagenesisi444E → A: No acceleration of DNA degradation, no binding to ATP, and no helicase activity. 1 Publication1
Mutagenesisi828S → A: Promotes multimerization after polyI:C stimulation; greatly enhances signaling. 1 Publication1
Mutagenesisi828S → D: Inhibits multimerization after polyI:C stimulation. 1 Publication1
Mutagenesisi829T → A: Moderately increases signaling. 1 Publication1

Keywords - Diseasei

Aicardi-Goutieres syndrome, Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNETi64135.
MalaCardsiIFIH1.
MIMi182250. phenotype.
610155. phenotype.
615846. phenotype.
OpenTargetsiENSG00000115267.
Orphaneti51. Aicardi-Goutieres syndrome.
PharmGKBiPA134889215.

Polymorphism and mutation databases

BioMutaiIFIH1.
DMDMi134047802.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001020121 – 1025Interferon-induced helicase C domain-containing protein 1Add BLAST1025

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei289PhosphoserineBy similarity1
Modified residuei291PhosphoserineBy similarity1
Modified residuei301PhosphoserineBy similarity1
Modified residuei645PhosphoserineBy similarity1
Modified residuei828Phosphoserine; by RIOK31 Publication1

Post-translational modificationi

Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta.1 Publication
Ubiquitinated by RNF125, leading to its degradation by the proteasome (PubMed:17460044). USP17/UPS17L2-dependent deubiquitination positively regulates the receptor (PubMed:20368735).2 Publications
During apoptosis, processed into 3 cleavage products. The helicase-containing fragment, once liberated from the CARD domains, translocate from the cytoplasm to the nucleus. The processed protein significantly sensitizes cells to DNA degradation.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei208 – 209CleavageBy similarity2
Sitei216 – 217CleavageBy similarity2
Sitei251 – 252CleavageBy similarity2

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9BYX4.
MaxQBiQ9BYX4.
PaxDbiQ9BYX4.
PeptideAtlasiQ9BYX4.
PRIDEiQ9BYX4.

PTM databases

iPTMnetiQ9BYX4.
PhosphoSitePlusiQ9BYX4.

Expressioni

Tissue specificityi

Widely expressed, at a low level. Expression is detected at slightly highest levels in placenta, pancreas and spleen and at barely levels in detectable brain, testis and lung.3 Publications

Inductioni

By interferon (IFN) and TNF.1 Publication

Gene expression databases

BgeeiENSG00000115267.
CleanExiHS_IFIH1.
GenevisibleiQ9BYX4. HS.

Organism-specific databases

HPAiHPA002656.

Interactioni

Subunit structurei

Monomer in the absence of ligands and homodimerizes in the presence of dsRNA ligands. Can assemble into helical or linear polymeric filaments on long dsRNA. Interacts with MAVS/IPS1. Interacts (via the CARD domains) with TKFC, the interaction is inhibited by viral infection (PubMed:17600090). Interacts with PCBP2. Interacts with NLRC5. Interacts with PIAS2-beta. Interacts with DDX60. Interacts with ANKRD17. Interacts with IKBKE (PubMed:17600090). Interacts with V protein of Simian virus 5, Human parainfluenza virus 2, Mumps virus, Sendai virus and Hendra virus. Binding to paramyxoviruses V proteins prevents IFN-beta induction, and the further establishment of an antiviral state. Interacts with herpes simplex virus 1 protein US11; this interaction prevents the interaction of MAVS/IPS1 to IFIH1.13 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi122082. 15 interactors.
DIPiDIP-42607N.
IntActiQ9BYX4. 21 interactors.
MINTiMINT-3381993.
STRINGi9606.ENSP00000263642.

Structurei

Secondary structure

11025
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi293 – 299Combined sources7
Helixi310 – 320Combined sources11
Beta strandi325 – 328Combined sources4
Helixi332 – 352Combined sources21
Beta strandi359 – 365Combined sources7
Helixi366 – 375Combined sources10
Helixi377 – 381Combined sources5
Turni382 – 384Combined sources3
Beta strandi387 – 389Combined sources3
Helixi400 – 406Combined sources7
Beta strandi408 – 413Combined sources6
Helixi414 – 422Combined sources9
Helixi434 – 436Combined sources3
Beta strandi438 – 442Combined sources5
Helixi454 – 473Combined sources20
Beta strandi483 – 488Combined sources6
Helixi900 – 902Combined sources3
Beta strandi903 – 907Combined sources5
Turni908 – 910Combined sources3
Beta strandi913 – 916Combined sources4
Helixi917 – 919Combined sources3
Beta strandi921 – 923Combined sources3
Turni924 – 926Combined sources3
Beta strandi927 – 929Combined sources3
Helixi934 – 937Combined sources4
Beta strandi938 – 942Combined sources5
Turni945 – 947Combined sources3
Beta strandi955 – 962Combined sources8
Beta strandi967 – 974Combined sources8
Beta strandi977 – 982Combined sources6
Helixi984 – 986Combined sources3
Beta strandi987 – 991Combined sources5
Turni992 – 995Combined sources4
Beta strandi996 – 998Combined sources3
Helixi1003 – 1005Combined sources3
Helixi1015 – 1017Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2RQBNMR-A896-1025[»]
3B6EX-ray1.60A277-490[»]
3GA3X-ray1.45A893-1017[»]
4GL2X-ray3.56A/B306-1017[»]
ProteinModelPortaliQ9BYX4.
SMRiQ9BYX4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BYX4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 97CARD 1Add BLAST91
Domaini110 – 190CARD 2Add BLAST81
Domaini316 – 509Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST194
Domaini700 – 882Helicase C-terminalPROSITE-ProRule annotationAdd BLAST183
Domaini893 – 1020RLR CTRPROSITE-ProRule annotationAdd BLAST128

Sequence similaritiesi

Belongs to the helicase family. RLR subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0354. Eukaryota.
COG1111. LUCA.
GeneTreeiENSGT00510000046789.
HOGENOMiHOG000230992.
HOVERGENiHBG106019.
InParanoidiQ9BYX4.
KOiK12647.
OMAiYNNIMRR.
OrthoDBiEOG091G01PQ.
PhylomeDBiQ9BYX4.
TreeFamiTF330258.

Family and domain databases

InterProiView protein in InterPro
IPR031964. CARD_dom.
IPR006935. Helicase/UvrB_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR021673. RLR_CTR.
PfamiView protein in Pfam
PF16739. CARD_2. 2 hits.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
SMARTiView protein in SMART
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
SUPFAMiSSF52540. SSF52540. 6 hits.
PROSITEiView protein in PROSITE
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51789. RLR_CTR. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BYX4-1) [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
MSNGYSTDEN FRYLISCFRA RVKMYIQVEP VLDYLTFLPA EVKEQIQRTV
60 70 80 90 100
ATSGNMQAVE LLLSTLEKGV WHLGWTREFV EALRRTGSPL AARYMNPELT
110 120 130 140 150
DLPSPSFENA HDEYLQLLNL LQPTLVDKLL VRDVLDKCME EELLTIEDRN
160 170 180 190 200
RIAAAENNGN ESGVRELLKR IVQKENWFSA FLNVLRQTGN NELVQELTGS
210 220 230 240 250
DCSESNAEIE NLSQVDGPQV EEQLLSTTVQ PNLEKEVWGM ENNSSESSFA
260 270 280 290 300
DSSVVSESDT SLAEGSVSCL DESLGHNSNM GSDSGTMGSD SDEENVAARA
310 320 330 340 350
SPEPELQLRP YQMEVAQPAL EGKNIIICLP TGSGKTRVAV YIAKDHLDKK
360 370 380 390 400
KKASEPGKVI VLVNKVLLVE QLFRKEFQPF LKKWYRVIGL SGDTQLKISF
410 420 430 440 450
PEVVKSCDII ISTAQILENS LLNLENGEDA GVQLSDFSLI IIDECHHTNK
460 470 480 490 500
EAVYNNIMRH YLMQKLKNNR LKKENKPVIP LPQILGLTAS PGVGGATKQA
510 520 530 540 550
KAEEHILKLC ANLDAFTIKT VKENLDQLKN QIQEPCKKFA IADATREDPF
560 570 580 590 600
KEKLLEIMTR IQTYCQMSPM SDFGTQPYEQ WAIQMEKKAA KEGNRKERVC
610 620 630 640 650
AEHLRKYNEA LQINDTIRMI DAYTHLETFY NEEKDKKFAV IEDDSDEGGD
660 670 680 690 700
DEYCDGDEDE DDLKKPLKLD ETDRFLMTLF FENNKMLKRL AENPEYENEK
710 720 730 740 750
LTKLRNTIME QYTRTEESAR GIIFTKTRQS AYALSQWITE NEKFAEVGVK
760 770 780 790 800
AHHLIGAGHS SEFKPMTQNE QKEVISKFRT GKINLLIATT VAEEGLDIKE
810 820 830 840 850
CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVAHSGSGV IEHETVNDFR
860 870 880 890 900
EKMMYKAIHC VQNMKPEEYA HKILELQMQS IMEKKMKTKR NIAKHYKNNP
910 920 930 940 950
SLITFLCKNC SVLACSGEDI HVIEKMHHVN MTPEFKELYI VRENKALQKK
960 970 980 990 1000
CADYQINGEI ICKCGQAWGT MMVHKGLDLP CLKIRNFVVV FKNNSTKKQY
1010 1020
KKWVELPITF PNLDYSECCL FSDED
Length:1,025
Mass (Da):116,689
Last modified:March 20, 2007 - v3
Checksum:i789CFB4824B92DC9
GO
Isoform 2 (identifier: Q9BYX4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     208-221: EIENLSQVDGPQVE → GICNFTEEDSSNSA
     222-1025: Missing.

Note: No experimental confirmation available.
Show »
Length:221
Mass (Da):25,129
Checksum:i3C7139ECAC564BB5
GO

Sequence cautioni

The sequence AAH78180 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB71141 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti439L → F in AAG54076 (PubMed:14645903).Curated1
Sequence conflicti475N → H in BAB71141 (PubMed:14702039).Curated1
Sequence conflicti592E → K in AAG34368 (PubMed:11805321).Curated1
Sequence conflicti598R → S in AAG54076 (PubMed:14645903).Curated1
Sequence conflicti609E → K in AAG54076 (PubMed:14645903).Curated1
Sequence conflicti782K → R in BAB71141 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071375337R → G in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777447Ensembl.1
Natural variantiVAR_071376372L → F in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness. 1 PublicationCorresponds to variant dbSNP:rs587777576Ensembl.1
Natural variantiVAR_071377393D → V in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777449Ensembl.1
Natural variantiVAR_071378452A → T in AGS7; enhances IFNB1 promoter activation; loss of ligand-induced responsiveness. 1 PublicationCorresponds to variant dbSNP:rs587777575Ensembl.1
Natural variantiVAR_031226460H → R. Corresponds to variant dbSNP:rs10930046Ensembl.1
Natural variantiVAR_071379495G → R in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs672601336Ensembl.1
Natural variantiVAR_071380720R → Q in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777445Ensembl.1
Natural variantiVAR_071381779R → C in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; no loss of ATP hydrolysis. 1 PublicationCorresponds to variant dbSNP:rs587777448Ensembl.1
Natural variantiVAR_071382779R → H in AGS7; enhances the interferon signaling pathway activation; enhances the stability of filament formation; enhances dsRNA binding activity; enhances IFNB1 promoter activation; no loss of ATP hydrolysis. 2 PublicationsCorresponds to variant dbSNP:rs587777446Ensembl.1
Natural variantiVAR_073666822R → Q in SGMRT1; gain-of-function mutation resulting in enhanced INFB1 induction. 1 PublicationCorresponds to variant dbSNP:rs376048533Ensembl.1
Natural variantiVAR_021594843H → R3 PublicationsCorresponds to variant dbSNP:rs3747517Ensembl.1
Natural variantiVAR_021595946A → T Associated with susceptibility to IDDM19. 3 PublicationsCorresponds to variant dbSNP:rs1990760Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_013337208 – 221EIENL…GPQVE → GICNFTEEDSSNSA in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_013338222 – 1025Missing in isoform 2. 1 PublicationAdd BLAST804

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF095844 mRNA. Translation: AAG34368.1.
AY017378 mRNA. Translation: AAG54076.1.
BC046208 mRNA. Translation: AAH46208.1.
BC078180 mRNA. Translation: AAH78180.1. Sequence problems.
BC111750 mRNA. Translation: AAI11751.1.
AK056293 mRNA. Translation: BAB71141.1. Different initiation.
CCDSiCCDS2217.1. [Q9BYX4-1]
RefSeqiNP_071451.2. NM_022168.3. [Q9BYX4-1]
UniGeneiHs.163173.

Genome annotation databases

EnsembliENST00000263642; ENSP00000263642; ENSG00000115267. [Q9BYX4-1]
ENST00000421365; ENSP00000408450; ENSG00000115267. [Q9BYX4-2]
GeneIDi64135.
KEGGihsa:64135.
UCSCiuc002uce.5. human. [Q9BYX4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiIFIH1_HUMAN
AccessioniPrimary (citable) accession number: Q9BYX4
Secondary accession number(s): Q2NKL6
, Q6DC96, Q86X56, Q96MX8, Q9H3G6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: March 20, 2007
Last modified: August 30, 2017
This is version 157 of the entry and version 3 of the sequence. See 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 2
    Human chromosome 2: 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