Ifi202
entrez
26388
canonical
uniprot
Q9R002
canonical
ensembl
ENSMUSG00000026535
resolver
ensp
ENSMUSP00000000266
resolver
enst
ENSMUST00000000266
resolver
genesymbol
Ifi202
resolver
genesymbol_syn
Ifi202a
resolver
genesymbol_syn
Ifi202b
resolver
uniprot
E9QLD9
resolver
uniprot
P15091
resolver
uniprot
Q38JF1
resolver
uniprot
Q7TMN6
resolver
uniprot
Q8VEL7
resolver
uniprot_entry
IFI2_MOUSE
resolver
uniprot_sec
E9QLD9
resolver
uniprot_sec
P15091
resolver
uniprot_sec
Q38JF1
resolver
uniprot_sec
Q7TMN6
resolver
uniprot_sec
Q8VEL7
resolver
amino_acid_sequence
MSNRNLRSSTNSEFSEGQHQTPSSDSSGHGEDQPQASPGPNKKSHTPKKNISKGAVLHEKPMTVMVLTATEPFNYKEGKENMFHATVATESQYYRVKVFNMDLKEKFTENKFITISKYFNSSGILEINETATVSEAAPNQIIEVPKNIIRSAKETLKISKIKELDSGTLIYGVFAVEKKKVNDKSITFKIKDNEDNIKVVWDKKQHNINYEKGDKLQLFSFHLRKGNGKPILHSGNHSFIKGEKLLKESFEGDGYHKGPKQVVALKATKLFTYDSIKSKKMFHATVATDTEFFRVMVFEENLEKKFIPGNTIALSDYFGMYGSLAIHEYSSVSEVKSQNKEDSSSSDERLIEHLKICDLHLQTKERLVDGEFKVYRKSTGNNCICYGIWDDTGAMKVVVSGQLTSVNCEIGNTIRLVCFELTSNADEWFLRSTRYSYMEVIMPEK
uniprot
proteins
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). {ECO:0000269|PubMed:16670293, ECO:0000269|PubMed:19131592, ECO:0000269|PubMed:23567559, ECO:0000269|PubMed:23850291, ECO:0000269|PubMed:24419611, ECO:0000269|PubMed:8524315}.
uniprot
proteins
mass_dalton
50466
uniprot
proteins
mutagenesis
MUTAGEN 48; /note="K->A: Reduced DNA-binding. Strongly reduces affinity for DNA; when associated with A-53 and W-54."; /evidence="ECO:0000269|PubMed:23567559, ECO:0000269|PubMed:23850291"; MUTAGEN 53; /note="K->A: Reduced DNA-binding. Strongly reduces affinity for DNA; when associated with A-48 and W-54."; /evidence="ECO:0000269|PubMed:23567559, ECO:0000269|PubMed:23850291"; MUTAGEN 54; /note="G->W: Strongly reduces affinity for DNA; when associated with A-48 and A-53."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 76; /note="K->A: Strongly reduces affinity for DNA; when associated with A-79 and A-236."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 79; /note="K->A: Strongly reduces affinity for DNA; when associated with A-76 and A-236."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 84; /note="H->F: Loss of interaction with TP53BP1; when associated with F-283."; /evidence="ECO:0000269|PubMed:8910340"; MUTAGEN 84; /note="H->G: Abolished homomultimerization."; /evidence="ECO:0000269|PubMed:9821952"; MUTAGEN 150; /note="R->E: Does not affect DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 166; /note="S->A: Strongly reduces affinity for DNA; when associated with."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 166; /note="S->E: Reduced DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 180; /note="K->E: Abolished DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 182..185; /note="NDKS->ADAA: Strongly reduces affinity for DNA."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 182; /note="N->E: Abolished DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 184; /note="K->E: Does not affect DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 185; /note="S->E: Abolished DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 187; /note="T->A: Strongly reduces affinity for DNA; when associated with A-189 and A-198."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 187; /note="T->E: Abolished DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 189; /note="K->A: Strongly reduces affinity for DNA; when associated with A-187 and A-198."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 198; /note="K->A: Strongly reduces affinity for DNA; when associated with A-187 and A-189."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 198; /note="K->E: Abolished DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 222..224; /note="HLR->ALA: Strongly reduces affinity for DNA."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 222; /note="H->E: Abolished DNA-binding."; /evidence="ECO:0000269|PubMed:24419611"; MUTAGEN 224; /note="R->E: Abolished DNA-binding."; /evidence="ECO:0000269|PubMed:23850291, ECO:0000269|PubMed:24419611"; MUTAGEN 226; /note="G->W: Strongly reduces affinity for DNA; when associated with A-166; A-227 and A-229."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 227; /note="N->A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-229."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 229; /note="K->A: Strongly reduces affinity for DNA; when associated with A-166; W-226 and A-227."; /evidence="ECO:0000269|PubMed:23567559"; MUTAGEN 236; /note="N->A: Does not affect DNA-binding. Strongly reduces affinity for DNA; when associated with A-76 and A-79."; /evidence="ECO:0000269|PubMed:23567559, ECO:0000269|PubMed:23850291"; MUTAGEN 283; /note="H->F: Loss of interaction with TP53BP1; when associated with F-84."; /evidence="ECO:0000269|PubMed:8910340"; MUTAGEN 283; /note="H->G: Abolished homomultimerization."; /evidence="ECO:0000269|PubMed:9821952"; MUTAGEN 321; /note="Y->R: Impaired homotetramerization."; /evidence="ECO:0000269|PubMed:23850291"; MUTAGEN 376; /note="R->E: Promotes formation of a homodimer."; /evidence="ECO:0000269|PubMed:23850291"; MUTAGEN 381..382; /note="NN->AA: Impaired homotetramerization."; /evidence="ECO:0000269|PubMed:23850291"; MUTAGEN 396; /note="K->A: Impaired homotetramerization."; /evidence="ECO:0000269|PubMed:23850291"; MUTAGEN 420; /note="E->A: Impaired homotetramerization."; /evidence="ECO:0000269|PubMed:23850291"; MUTAGEN 424; /note="N->A: Impaired homotetramerization."; /evidence="ECO:0000269|PubMed:23850291"; MUTAGEN 431; /note="R->A: Impaired homotetramerization."; /evidence="ECO:0000269|PubMed:23850291"; MUTAGEN 434..435; /note="RY->AA: Impaired homotetramerization."; /evidence="ECO:0000269|PubMed:23850291
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. {ECO:0000269|PubMed:8454910}.
uniprot
proteins
protein_family
HIN-200 family
uniprot
proteins
pubmed
10493828
uniprot
proteins
pubmed
11567633
uniprot
proteins
pubmed
14764608
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16670293
uniprot
proteins
pubmed
19131592
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
23567559
uniprot
proteins
pubmed
23850291
uniprot
proteins
pubmed
24419611
uniprot
proteins
pubmed
2477366
uniprot
proteins
pubmed
8454910
uniprot
proteins
pubmed
8524315
uniprot
proteins
pubmed
8910340
uniprot
proteins
pubmed
9821952
uniprot
proteins
sequence_length
445
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19131592, ECO:0000269|PubMed:8454910}. Nucleus {ECO:0000269|PubMed:8454910}. Note=Accumulates first in the cytoplasm, and is translocated to the nucleus after a delay, where it is primarily chromatin-associated. {ECO:0000269|PubMed:8454910}.
uniprot
proteins