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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 – 9071Zinc By similarity
Metal bindingi910 – 9101Zinc By similarity
Metal bindingi962 – 9621Zinc By similarity
Metal bindingi964 – 9641Zinc By 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. protein binding Source: MGI
  6. ribonucleoprotein complex binding Source: Ensembl
  7. single-stranded RNA binding Source: UniProtKB
  8. zinc ion binding Source: UniProtKB
Complete GO annotation...

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. Nucleus Reviewed prediction
Note: May be found in the nucleus, during apoptosis.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
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 1
PRO_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.
Sumoylated. Sumoylation positively regulates its role in type I interferon induction and is enhanced by PIAS2-beta By similarity.
Ubiquitinated. USP17L2/USP17-dependent deubiquitination positively regulates the receptor 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

ArrayExpressiQ8R5F7.
BgeeiQ8R5F7.
CleanExiMM_IFIH1.
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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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 8-199, 300-1025.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 2 CARD domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1111.
GeneTreeiENSGT00510000046789.
HOVERGENiHBG106019.
InParanoidiA2AUY7.
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

MSIVCSAEDS FRNLILFFRP RLKMYIQVEP VLDHLIFLSA ETKEQILKKI     50
NTCGNTSAAE LLLSTLEQGQ WPLGWTQMFV EALEHSGNPL AARYVKPTLT 100
DLPSPSSETA HDECLHLLTL LQPTLVDKLL INDVLDTCFE KGLLTVEDRN 150
RISAAGNSGN ESGVRELLRR IVQKENWFST FLDVLRQTGN DALFQELTGG 200
GCPEDNTDLA NSSHRDGPAA NECLLPAVDE SSLETEAWNV DDILPEASCT 250
DSSVTTESDT SLAEGSVSCF DESLGHNSNM GRDSGTMGSD SDESVIQTKR 300
VSPEPELQLR PYQMEVAQPA LDGKNIIICL PTGSGKTRVA VYITKDHLDK 350
KKQASESGKV IVLVNKVMLA EQLFRKEFNP YLKKWYRIIG LSGDTQLKIS 400
FPEVVKSYDV IISTAQILEN SLLNLESGDD DGVQLSDFSL IIIDECHHTN 450
KEAVYNNIMR RYLKQKLRNN DLKKQNKPAI PLPQILGLTA SPGVGAAKKQ 500
SEAEKHILNI CANLDAFTIK TVKENLGQLK HQIKEPCKKF VIADDTRENP 550
FKEKLLEIMA SIQTYCQKSP MSDFGTQHYE QWAIQMEKKA AKDGNRKDRV 600
CAEHLRKYNE ALQINDTIRM IDAYSHLETF YTDEKEKKFA VLNDSDKSDD 650
EASSCNDQLK GDVKKSLKLD ETDEFLMNLF FDNKKMLKKL AENPKYENEK 700
LIKLRNTILE QFTRSEESSR GIIFTKTRQS TYALSQWIME NAKFAEVGVK 750
AHHLIGAGHS SEVKPMTQTE QKEVISKFRT GEINLLIATT VAEEGLDIKE 800
CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVTSSGSGV TEREIVNDFR 850
EKMMYKAINR VQNMKPEEYA HKILELQVQS ILEKKMKVKR SIAKQYNDNP 900
SLITLLCKNC SMLVCSGENI HVIEKMHHVN MTPEFKGLYI VRENKALQKK 950
FADYQTNGEI ICKCGQAWGT MMVHKGLDLP CLKIRNFVVN FKNNSPKKQY 1000
KKWVELPIRF PDLDYSEYCL YSDED 1025
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei207 – 25549Missing in isoform 2.
VSP_013339Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti100 – 1001T → I in AAH80200. 1 Publication
Sequence conflicti339 – 3391V → E in BAE31652. 1 Publication
Sequence conflicti412 – 4143IST → TRP in AAH25508. 1 Publication
Sequence conflicti624 – 6241Y → H in AAH25508. 1 Publication
Sequence conflicti629 – 6291T → A in AAM21359. 1 Publication
Sequence conflicti647 – 6471K → E in AAH25508. 1 Publication
Sequence conflicti647 – 6471K → E in AAH04031. 1 Publication
Sequence conflicti647 – 6471K → E in AAH80200. 1 Publication
Sequence conflicti889 – 8891K → E in BAB31303. 1 Publication

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 8-199, 300-1025.
ModBasei Search...

Protein-protein interaction databases

BioGridi 214799. 1 interaction.
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 A2AUY7.
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

ArrayExpressi Q8R5F7.
Bgeei Q8R5F7.
CleanExi MM_IFIH1.
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: September 3, 2014
This is version 109 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

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