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Q8R5F7

- IFIH1_MOUSE

UniProt

Q8R5F7 - IFIH1_MOUSE

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Protein

Interferon-induced helicase C domain-containing protein 1

Gene

Ifih1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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), 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.5 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Zinc.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei208 – 2092Cleavage
Sitei216 – 2172Cleavage
Sitei251 – 2522Cleavage
Metal bindingi907 – 9071ZincBy similarity
Metal bindingi910 – 9101ZincBy similarity
Metal bindingi962 – 9621ZincBy similarity
Metal bindingi964 – 9641ZincBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: InterPro
  3. double-stranded RNA binding Source: UniProtKB
  4. helicase activity Source: UniProtKB-KW
  5. ribonucleoprotein complex binding Source: Ensembl
  6. single-stranded RNA binding Source: UniProtKB
  7. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. defense response to virus Source: UniProtKB-KW
  2. innate immune response Source: UniProtKB
  3. positive regulation of interferon-alpha production Source: UniProtKB
  4. positive regulation of interferon-beta production Source: UniProtKB
  5. protein sumoylation Source: UniProtKB
  6. regulation of apoptotic process Source: InterPro
  7. response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198521. TRAF6 mediated IRF7 activation.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_202898. TRAF6 mediated NF-kB activation.
REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_219118. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon-induced helicase C domain-containing protein 1 (EC:3.6.4.13)
Alternative name(s):
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
RIG-I-like receptor 2
Short name:
RLR-2
Gene namesi
Name:Ifih1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1918836. Ifih1.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus Curated
Note: May be found in the nucleus, during apoptosis.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10251025Interferon-induced helicase C domain-containing protein 1PRO_0000102013Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei645 – 6451Phosphoserine1 Publication
Modified residuei648 – 6481Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication
Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta (By similarity).By similarity
Ubiquitinated. USP17L2/USP17-dependent deubiquitination positively regulates the receptor (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8R5F7.
PaxDbiQ8R5F7.
PRIDEiQ8R5F7.

PTM databases

PhosphoSiteiQ8R5F7.

Expressioni

Tissue specificityi

Expression is prominent in lung, liver, kidney, heart and spleen (at protein level). Widely expressed at low level.1 Publication

Inductioni

By interferon (IFN).

Gene expression databases

BgeeiQ8R5F7.
CleanExiMM_IFIH1.
ExpressionAtlasiQ8R5F7. baseline and differential.
GenevestigatoriQ8R5F7.

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 with V protein of Sendai virus. Binding to paramyxoviruses V proteins prevents IFN-beta induction, and the further establishment of an antiviral state (By similarity). Interacts with PCBP2 (By similarity). Interacts with NLRC5 (By similarity). Interacts with PIAS2-beta (By similarity). Interacts with DDX60 (By similarity).By similarity

Protein-protein interaction databases

BioGridi214799. 2 interactions.
DIPiDIP-60085N.
IntActiQ8R5F7. 1 interaction.
MINTiMINT-4118007.

Structurei

Secondary structure

1
1025
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi550 – 56516
Helixi577 – 59317
Helixi596 – 61722
Helixi620 – 64021
Helixi671 – 69121
Helixi694 – 6963

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TS9X-ray2.00A545-697[»]
ProteinModelPortaliQ8R5F7.
SMRiQ8R5F7. Positions 300-1025.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 9791CARD 1Add
BLAST
Domaini110 – 19081CARD 2Add
BLAST
Domaini317 – 510194Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini700 – 872173Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the helicase family. RLR subfamily.Curated
Contains 2 CARD domains.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1111.
GeneTreeiENSGT00510000046789.
HOVERGENiHBG106019.
InParanoidiQ8R5F7.
KOiK12647.
OMAiKCGQAWG.
OrthoDBiEOG7RV9FC.
PhylomeDBiQ8R5F7.
TreeFamiTF330258.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001315. 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.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8R5F7-1) [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
MSIVCSAEDS FRNLILFFRP RLKMYIQVEP VLDHLIFLSA ETKEQILKKI
60 70 80 90 100
NTCGNTSAAE LLLSTLEQGQ WPLGWTQMFV EALEHSGNPL AARYVKPTLT
110 120 130 140 150
DLPSPSSETA HDECLHLLTL LQPTLVDKLL INDVLDTCFE KGLLTVEDRN
160 170 180 190 200
RISAAGNSGN ESGVRELLRR IVQKENWFST FLDVLRQTGN DALFQELTGG
210 220 230 240 250
GCPEDNTDLA NSSHRDGPAA NECLLPAVDE SSLETEAWNV DDILPEASCT
260 270 280 290 300
DSSVTTESDT SLAEGSVSCF DESLGHNSNM GRDSGTMGSD SDESVIQTKR
310 320 330 340 350
VSPEPELQLR PYQMEVAQPA LDGKNIIICL PTGSGKTRVA VYITKDHLDK
360 370 380 390 400
KKQASESGKV IVLVNKVMLA EQLFRKEFNP YLKKWYRIIG LSGDTQLKIS
410 420 430 440 450
FPEVVKSYDV IISTAQILEN SLLNLESGDD DGVQLSDFSL IIIDECHHTN
460 470 480 490 500
KEAVYNNIMR RYLKQKLRNN DLKKQNKPAI PLPQILGLTA SPGVGAAKKQ
510 520 530 540 550
SEAEKHILNI CANLDAFTIK TVKENLGQLK HQIKEPCKKF VIADDTRENP
560 570 580 590 600
FKEKLLEIMA SIQTYCQKSP MSDFGTQHYE QWAIQMEKKA AKDGNRKDRV
610 620 630 640 650
CAEHLRKYNE ALQINDTIRM IDAYSHLETF YTDEKEKKFA VLNDSDKSDD
660 670 680 690 700
EASSCNDQLK GDVKKSLKLD ETDEFLMNLF FDNKKMLKKL AENPKYENEK
710 720 730 740 750
LIKLRNTILE QFTRSEESSR GIIFTKTRQS TYALSQWIME NAKFAEVGVK
760 770 780 790 800
AHHLIGAGHS SEVKPMTQTE QKEVISKFRT GEINLLIATT VAEEGLDIKE
810 820 830 840 850
CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVTSSGSGV TEREIVNDFR
860 870 880 890 900
EKMMYKAINR VQNMKPEEYA HKILELQVQS ILEKKMKVKR SIAKQYNDNP
910 920 930 940 950
SLITLLCKNC SMLVCSGENI HVIEKMHHVN MTPEFKGLYI VRENKALQKK
960 970 980 990 1000
FADYQTNGEI ICKCGQAWGT MMVHKGLDLP CLKIRNFVVN FKNNSPKKQY
1010 1020
KKWVELPIRF PDLDYSEYCL YSDED
Length:1,025
Mass (Da):115,971
Last modified:June 1, 2002 - v1
Checksum:i708FCAC690C9F6D8
GO
Isoform 2 (identifier: Q8R5F7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     207-255: Missing.

Note: No experimental confirmation available.

Show »
Length:976
Mass (Da):110,842
Checksum:iB9F6D84C207F1031
GO

Sequence cautioni

The sequence AAH25508.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001T → I in AAH80200. (PubMed:15489334)Curated
Sequence conflicti339 – 3391V → E in BAE31652. (PubMed:16141072)Curated
Sequence conflicti412 – 4143IST → TRP in AAH25508. (PubMed:15489334)Curated
Sequence conflicti624 – 6241Y → H in AAH25508. (PubMed:15489334)Curated
Sequence conflicti629 – 6291T → A in AAM21359. (PubMed:11805321)Curated
Sequence conflicti647 – 6471K → E in AAH25508. (PubMed:15489334)Curated
Sequence conflicti647 – 6471K → E in AAH04031. (PubMed:15489334)Curated
Sequence conflicti647 – 6471K → E in AAH80200. (PubMed:15489334)Curated
Sequence conflicti889 – 8891K → E in BAB31303. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei207 – 25549Missing in isoform 2. 1 PublicationVSP_013339Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY075132 mRNA. Translation: AAL77205.1.
AF374384 mRNA. Translation: AAM21359.1.
AK018602 mRNA. Translation: BAB31303.2.
AK037057 mRNA. Translation: BAC29687.2.
AK040519 mRNA. Translation: BAC30614.1.
AK153018 mRNA. Translation: BAE31652.1.
AL929246 Genomic DNA. Translation: CAM21790.1.
BC004031 mRNA. Translation: AAH04031.1.
BC019605 mRNA. Translation: AAH19605.1.
BC025508 mRNA. Translation: AAH25508.1. Different initiation.
BC080200 mRNA. Translation: AAH80200.1.
CCDSiCCDS16068.1. [Q8R5F7-1]
CCDS50594.1. [Q8R5F7-2]
RefSeqiNP_001157949.1. NM_001164477.1. [Q8R5F7-2]
NP_082111.2. NM_027835.3. [Q8R5F7-1]
UniGeneiMm.136224.

Genome annotation databases

EnsembliENSMUST00000028259; ENSMUSP00000028259; ENSMUSG00000026896. [Q8R5F7-1]
ENSMUST00000112459; ENSMUSP00000108078; ENSMUSG00000026896. [Q8R5F7-2]
GeneIDi71586.
KEGGimmu:71586.
UCSCiuc008jvm.2. mouse. [Q8R5F7-1]
uc012bvy.1. mouse. [Q8R5F7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY075132 mRNA. Translation: AAL77205.1 .
AF374384 mRNA. Translation: AAM21359.1 .
AK018602 mRNA. Translation: BAB31303.2 .
AK037057 mRNA. Translation: BAC29687.2 .
AK040519 mRNA. Translation: BAC30614.1 .
AK153018 mRNA. Translation: BAE31652.1 .
AL929246 Genomic DNA. Translation: CAM21790.1 .
BC004031 mRNA. Translation: AAH04031.1 .
BC019605 mRNA. Translation: AAH19605.1 .
BC025508 mRNA. Translation: AAH25508.1 . Different initiation.
BC080200 mRNA. Translation: AAH80200.1 .
CCDSi CCDS16068.1. [Q8R5F7-1 ]
CCDS50594.1. [Q8R5F7-2 ]
RefSeqi NP_001157949.1. NM_001164477.1. [Q8R5F7-2 ]
NP_082111.2. NM_027835.3. [Q8R5F7-1 ]
UniGenei Mm.136224.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3TS9 X-ray 2.00 A 545-697 [» ]
ProteinModelPortali Q8R5F7.
SMRi Q8R5F7. Positions 300-1025.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 214799. 2 interactions.
DIPi DIP-60085N.
IntActi Q8R5F7. 1 interaction.
MINTi MINT-4118007.

PTM databases

PhosphoSitei Q8R5F7.

Proteomic databases

MaxQBi Q8R5F7.
PaxDbi Q8R5F7.
PRIDEi Q8R5F7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028259 ; ENSMUSP00000028259 ; ENSMUSG00000026896 . [Q8R5F7-1 ]
ENSMUST00000112459 ; ENSMUSP00000108078 ; ENSMUSG00000026896 . [Q8R5F7-2 ]
GeneIDi 71586.
KEGGi mmu:71586.
UCSCi uc008jvm.2. mouse. [Q8R5F7-1 ]
uc012bvy.1. mouse. [Q8R5F7-2 ]

Organism-specific databases

CTDi 64135.
MGIi MGI:1918836. Ifih1.

Phylogenomic databases

eggNOGi COG1111.
GeneTreei ENSGT00510000046789.
HOVERGENi HBG106019.
InParanoidi Q8R5F7.
KOi K12647.
OMAi KCGQAWG.
OrthoDBi EOG7RV9FC.
PhylomeDBi Q8R5F7.
TreeFami TF330258.

Enzyme and pathway databases

Reactomei REACT_198521. TRAF6 mediated IRF7 activation.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_202898. TRAF6 mediated NF-kB activation.
REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_219118. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.

Miscellaneous databases

NextBioi 334053.
PROi Q8R5F7.
SOURCEi Search...

Gene expression databases

Bgeei Q8R5F7.
CleanExi MM_IFIH1.
ExpressionAtlasi Q8R5F7. baseline and differential.
Genevestigatori Q8R5F7.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
3.40.50.300. 2 hits.
InterProi 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.
[Graphical view ]
Pfami PF00619. CARD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation."
    Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J.
    Curr. Biol. 12:838-843(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CLEAVAGE SITES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. Erratum
    Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J.
    Curr. Biol. 12:1633-1633(2002)
  3. "mda-5: an interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties."
    Kang D.-C., Gopalkrishnan R.V., Wu Q., Jankowsky E., Pyle A.M., Fisher P.B.
    Proc. Natl. Acad. Sci. U.S.A. 99:637-642(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone marrow, Cecum, Thymus and Vagina.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Mammary gland.
  7. Cited for: FUNCTION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-648, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. Cited for: FUNCTION.
  10. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Activation of MDA5 requires higher-order RNA structures generated during virus infection."
    Pichlmair A., Schulz O., Tan C.P., Rehwinkel J., Kato H., Takeuchi O., Akira S., Way M., Schiavo G., Reis e Sousa C.
    J. Virol. 83:10761-10769(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Immune signaling by RIG-I-like receptors."
    Loo Y.M., Gale M. Jr.
    Immunity 34:680-692(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  13. "RIG-I-like receptors: cytoplasmic sensors for non-self RNA."
    Kato H., Takahasi K., Fujita T.
    Immunol. Rev. 243:91-98(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  14. Cited for: REVIEW ON FUNCTION.
  15. "2 methylate or not 2 methylate: viral evasion of the type I interferon response."
    Garcia-Sastre A.
    Nat. Immunol. 12:114-115(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  16. "Ribose 2'-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5."
    Zuest R., Cervantes-Barragan L., Habjan M., Maier R., Neuman B.W., Ziebuhr J., Szretter K.J., Baker S.C., Barchet W., Diamond M.S., Siddell S.G., Ludewig B., Thiel V.
    Nat. Immunol. 12:137-143(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA."
    Berke I.C., Modis Y.
    EMBO J. 31:1714-1726(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 545-697, SUBUNIT.

Entry informationi

Entry nameiIFIH1_MOUSE
AccessioniPrimary (citable) accession number: Q8R5F7
Secondary accession number(s): A2AUY7
, Q3U6S2, Q68EM4, Q8BYC9, Q8BZ01, Q8K5C7, Q8R144, Q8VE79, Q99KS4, Q9D2Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3