Q9R002 · IFI2_MOUSE
- ProteinInterferon-activable protein 202
- GeneIfi202
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids445 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
DNA-binding protein involved in innate immune response and has anti-inflammatory activity (PubMed:19131592, PubMed:23567559, PubMed:23850291).
Inhibits caspase activation in response to cytosolic DNA by preventing activation of the AIM2 inflammasome, probably by sequestering cytoplasmic DNA and preventing its being bound by AIM2 (PubMed:19131592, PubMed:23567559, PubMed:23850291).
Also inhibits activation of the AIM2 inflammasome via a direct interaction with AIM2, which prevents the interaction between AIM2 and PYCARD and formation of the AIM2 inflammasome (PubMed:23850291).
Binds double-stranded DNA (dsDNA) in the cytosol (PubMed:19131592, PubMed:23567559, PubMed:23850291, PubMed:24419611).
Has anti-apoptotic effects due to inhibition of the transcriptional activity of TP53/p53 (PubMed:16670293).
Inhibits the transcriptional activity of several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin (PubMed:8524315).
Inhibits caspase activation in response to cytosolic DNA by preventing activation of the AIM2 inflammasome, probably by sequestering cytoplasmic DNA and preventing its being bound by AIM2 (PubMed:19131592, PubMed:23567559, PubMed:23850291).
Also inhibits activation of the AIM2 inflammasome via a direct interaction with AIM2, which prevents the interaction between AIM2 and PYCARD and formation of the AIM2 inflammasome (PubMed:23850291).
Binds double-stranded DNA (dsDNA) in the cytosol (PubMed:19131592, PubMed:23567559, PubMed:23850291, PubMed:24419611).
Has anti-apoptotic effects due to inhibition of the transcriptional activity of TP53/p53 (PubMed:16670293).
Inhibits the transcriptional activity of several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin (PubMed:8524315).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 84 | Mediates interaction with TP53BP1 | ||||
Sequence: H | ||||||
Site | 283 | Mediates interaction with TP53BP1 | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | molecular adaptor activity | |
Biological Process | activation of innate immune response | |
Biological Process | cellular response to interferon-beta | |
Biological Process | inflammatory response | |
Biological Process | innate immune response | |
Biological Process | negative regulation of AIM2 inflammasome complex assembly | |
Biological Process | negative regulation of cysteine-type endopeptidase activity involved in apoptotic process | |
Biological Process | negative regulation of innate immune response | |
Biological Process | protein homooligomerization | |
Biological Process | protein homotetramerization |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameInterferon-activable protein 202
- Short namesIfi-202
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9R002
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 48 | Reduced DNA-binding. Strongly reduces affinity for DNA; when associated with A-53 and W-54. | ||||
Sequence: K → A | ||||||
Mutagenesis | 53 | Reduced DNA-binding. Strongly reduces affinity for DNA; when associated with A-48 and W-54. | ||||
Sequence: K → A | ||||||
Mutagenesis | 54 | Strongly reduces affinity for DNA; when associated with A-48 and A-53. | ||||
Sequence: G → W | ||||||
Mutagenesis | 76 | Strongly reduces affinity for DNA; when associated with A-79 and A-236. | ||||
Sequence: K → A | ||||||
Mutagenesis | 79 | Strongly reduces affinity for DNA; when associated with A-76 and A-236. | ||||
Sequence: K → A | ||||||
Mutagenesis | 84 | Loss of interaction with TP53BP1; when associated with F-283. | ||||
Sequence: H → F | ||||||
Mutagenesis | 84 | Abolished homomultimerization. | ||||
Sequence: H → G | ||||||
Mutagenesis | 150 | Does not affect DNA-binding. | ||||
Sequence: R → E | ||||||
Mutagenesis | 166 | Strongly reduces affinity for DNA; when associated with. | ||||
Sequence: S → A | ||||||
Mutagenesis | 166 | Reduced DNA-binding. | ||||
Sequence: S → E | ||||||
Mutagenesis | 180 | Abolished DNA-binding. | ||||
Sequence: K → E | ||||||
Mutagenesis | 182 | Abolished DNA-binding. | ||||
Sequence: N → E | ||||||
Mutagenesis | 182-185 | Strongly reduces affinity for DNA. | ||||
Sequence: NDKS → ADAA | ||||||
Mutagenesis | 184 | Does not affect DNA-binding. | ||||
Sequence: K → E | ||||||
Mutagenesis | 185 | Abolished DNA-binding. | ||||
Sequence: S → E | ||||||
Mutagenesis | 187 | Strongly reduces affinity for DNA; when associated with A-189 and A-198. | ||||
Sequence: T → A | ||||||
Mutagenesis | 187 | Abolished DNA-binding. | ||||
Sequence: T → E | ||||||
Mutagenesis | 189 | Strongly reduces affinity for DNA; when associated with A-187 and A-198. | ||||
Sequence: K → A | ||||||
Mutagenesis | 198 | Strongly reduces affinity for DNA; when associated with A-187 and A-189. | ||||
Sequence: K → A | ||||||
Mutagenesis | 198 | Abolished DNA-binding. | ||||
Sequence: K → E | ||||||
Mutagenesis | 222 | Abolished DNA-binding. | ||||
Sequence: H → E | ||||||
Mutagenesis | 222-224 | Strongly reduces affinity for DNA. | ||||
Sequence: HLR → ALA | ||||||
Mutagenesis | 224 | Abolished DNA-binding. | ||||
Sequence: R → E | ||||||
Mutagenesis | 226 | Strongly reduces affinity for DNA; when associated with A-166; A-227 and A-229. | ||||
Sequence: G → W | ||||||
Mutagenesis | 227 | Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-229. | ||||
Sequence: N → A | ||||||
Mutagenesis | 229 | Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-227. | ||||
Sequence: K → A | ||||||
Mutagenesis | 236 | Does not affect DNA-binding. Strongly reduces affinity for DNA; when associated with A-76 and A-79. | ||||
Sequence: N → A | ||||||
Mutagenesis | 283 | Loss of interaction with TP53BP1; when associated with F-84. | ||||
Sequence: H → F | ||||||
Mutagenesis | 283 | Abolished homomultimerization. | ||||
Sequence: H → G | ||||||
Mutagenesis | 321 | Impaired homotetramerization. | ||||
Sequence: Y → R | ||||||
Mutagenesis | 376 | Promotes formation of a homodimer. | ||||
Sequence: R → E | ||||||
Mutagenesis | 381-382 | Impaired homotetramerization. | ||||
Sequence: NN → AA | ||||||
Mutagenesis | 396 | Impaired homotetramerization. | ||||
Sequence: K → A | ||||||
Mutagenesis | 420 | Impaired homotetramerization. | ||||
Sequence: E → A | ||||||
Mutagenesis | 424 | Impaired homotetramerization. | ||||
Sequence: N → A | ||||||
Mutagenesis | 431 | Impaired homotetramerization. | ||||
Sequence: R → A | ||||||
Mutagenesis | 434-435 | Impaired homotetramerization. | ||||
Sequence: RY → AA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 37 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000153719 | 1-445 | Interferon-activable protein 202 | |||
Sequence: MSNRNLRSSTNSEFSEGQHQTPSSDSSGHGEDQPQASPGPNKKSHTPKKNISKGAVLHEKPMTVMVLTATEPFNYKEGKENMFHATVATESQYYRVKVFNMDLKEKFTENKFITISKYFNSSGILEINETATVSEAAPNQIIEVPKNIIRSAKETLKISKIKELDSGTLIYGVFAVEKKKVNDKSITFKIKDNEDNIKVVWDKKQHNINYEKGDKLQLFSFHLRKGNGKPILHSGNHSFIKGEKLLKESFEGDGYHKGPKQVVALKATKLFTYDSIKSKKMFHATVATDTEFFRVMVFEENLEKKFIPGNTIALSDYFGMYGSLAIHEYSSVSEVKSQNKEDSSSSDERLIEHLKICDLHLQTKERLVDGEFKVYRKSTGNNCICYGIWDDTGAMKVVVSGQLTSVNCEIGNTIRLVCFELTSNADEWFLRSTRYSYMEVIMPEK |
Post-translational modification
Phosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homomultimer; homotetramerizes (via HIN-200 domain 2), enhancing affinity for double-stranded DNA (dsDNA) (PubMed:23850291, PubMed:9821952).
Interacts (via HIN-200 domain 2) with AIM2 (via HIN-200 domain); preventing activation of the AIM2 inflammasome (PubMed:23850291).
Binds to several transcription factors, including NF-kappa-B p50 (NFKB1) and p65 (RELA), FOS, JUN, E2F1, E2F4, MYOD1 and myogenin (PubMed:8524315).
Also binds TP53/p53, the hypophosphorylated, growth-inhibitory form of the retinoblastoma protein and the p53-binding protein 1 (TP53BP1) (PubMed:16670293, PubMed:8910340).
Interacts (via HIN-200 domain 2) with AIM2 (via HIN-200 domain); preventing activation of the AIM2 inflammasome (PubMed:23850291).
Binds to several transcription factors, including NF-kappa-B p50 (NFKB1) and p65 (RELA), FOS, JUN, E2F1, E2F4, MYOD1 and myogenin (PubMed:8524315).
Also binds TP53/p53, the hypophosphorylated, growth-inhibitory form of the retinoblastoma protein and the p53-binding protein 1 (TP53BP1) (PubMed:16670293, PubMed:8910340).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9R002 | Rb1 P13405 | 7 | EBI-3043899, EBI-971782 | |
XENO | Q9R002 | RB1 P06400 | 5 | EBI-3043899, EBI-491274 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-45 | Polar residues | ||||
Sequence: MSNRNLRSSTNSEFSEGQHQTPSSDSSGHGEDQPQASPGPNKKSH | ||||||
Region | 1-57 | Disordered | ||||
Sequence: MSNRNLRSSTNSEFSEGQHQTPSSDSSGHGEDQPQASPGPNKKSHTPKKNISKGAVL | ||||||
Domain | 46-243 | HIN-200 1 | ||||
Sequence: TPKKNISKGAVLHEKPMTVMVLTATEPFNYKEGKENMFHATVATESQYYRVKVFNMDLKEKFTENKFITISKYFNSSGILEINETATVSEAAPNQIIEVPKNIIRSAKETLKISKIKELDSGTLIYGVFAVEKKKVNDKSITFKIKDNEDNIKVVWDKKQHNINYEKGDKLQLFSFHLRKGNGKPILHSGNHSFIKGE | ||||||
Region | 82-89 | Required for homomultimerization | ||||
Sequence: MFHATVAT | ||||||
Domain | 244-441 | HIN-200 2 | ||||
Sequence: KLLKESFEGDGYHKGPKQVVALKATKLFTYDSIKSKKMFHATVATDTEFFRVMVFEENLEKKFIPGNTIALSDYFGMYGSLAIHEYSSVSEVKSQNKEDSSSSDERLIEHLKICDLHLQTKERLVDGEFKVYRKSTGNNCICYGIWDDTGAMKVVVSGQLTSVNCEIGNTIRLVCFELTSNADEWFLRSTRYSYMEVI | ||||||
Region | 281-288 | Required for homomultimerization | ||||
Sequence: MFHATVAT |
Domain
The HIN-200 domain 1 mediates non-specific double-stranded DNA (dsDNA)-binding via electrostatic interactions: it recognizes both strands of DNA (PubMed:23567559, PubMed:24419611).
The HIN-200 domain 2 mediates homotetramerization and interaction with AIM2 (PubMed:23850291).
The HIN-200 domain 2 mediates homotetramerization and interaction with AIM2 (PubMed:23850291).
Sequence similarities
Belongs to the HIN-200 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length445
- Mass (Da)50,466
- Last updated2011-07-27 v3
- Checksum5EA0E93E143C58EA
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-45 | Polar residues | ||||
Sequence: MSNRNLRSSTNSEFSEGQHQTPSSDSSGHGEDQPQASPGPNKKSH | ||||||
Sequence conflict | 13-15 | in Ref. 2; AAF04260 and 5; AAH55888 | ||||
Sequence: EFS → DLA | ||||||
Sequence conflict | 79 | in Ref. 3; ABB00055 | ||||
Sequence: K → N | ||||||
Sequence conflict | 92 | in Ref. 2; AAF04260 and 5; AAH18233 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 109 | in Ref. 3; ABB00055 | ||||
Sequence: E → G | ||||||
Sequence conflict | 111 | in Ref. 5; AAH18233 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 127 | in Ref. 3; ABB00055 | ||||
Sequence: I → F | ||||||
Sequence conflict | 141-142 | in Ref. 1; AAA39312, 2; AAF04260, 3; ABB00055 and 5; AAH18233/AAH55888 | ||||
Sequence: II → MF | ||||||
Sequence conflict | 187 | in Ref. 3; ABB00055 | ||||
Sequence: T → I | ||||||
Sequence conflict | 190 | in Ref. 3; ABB00055 | ||||
Sequence: I → V | ||||||
Sequence conflict | 204 | in Ref. 1; AAA39312, 2; AAF04260, 3; ABB00055 and 5; AAH18233/AAH55888 | ||||
Sequence: K → E | ||||||
Sequence conflict | 240 | in Ref. 2; AAF04260 | ||||
Sequence: I → V | ||||||
Sequence conflict | 350 | in Ref. 1; AAA39312, 2; AAF04260, 3; ABB00055 and 5; AAH18233/AAH55888 | ||||
Sequence: L → P | ||||||
Sequence conflict | 364 | in Ref. 1; AAA39312, 2; AAF04260, 3; ABB00055 and 5; AAH18233/AAH55888 | ||||
Sequence: K → E | ||||||
Sequence conflict | 368 | in Ref. 1; AAA39312 | ||||
Sequence: V → F | ||||||
Sequence conflict | 379 | in Ref. 1; AAA39312, 2; AAF04260, 3; ABB00055 and 5; AAH18233/AAH55888 | ||||
Sequence: T → S | ||||||
Sequence conflict | 432 | in Ref. 1; AAA39312, 2; AAF04260, 3; ABB00055 and 5; AAH18233/AAH55888 | ||||
Sequence: S → A |
Polymorphism
NZB mice express 10 to 100 fold more Ifi202 in spleen than B6 or NZW mice (PubMed:11567633).
This could account for the high susceptibility of NZB mice to systemic lupus (PubMed:11567633).
This could account for the high susceptibility of NZB mice to systemic lupus (PubMed:11567633).
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M31418 EMBL· GenBank· DDBJ | AAA39312.1 EMBL· GenBank· DDBJ | mRNA | ||
AF140672 EMBL· GenBank· DDBJ | AAF04260.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ222946 EMBL· GenBank· DDBJ | ABB00055.1 EMBL· GenBank· DDBJ | mRNA | ||
AC170584 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC018233 EMBL· GenBank· DDBJ | AAH18233.1 EMBL· GenBank· DDBJ | mRNA | ||
BC055888 EMBL· GenBank· DDBJ | AAH55888.1 EMBL· GenBank· DDBJ | mRNA |