IFI16
entrez
3428
canonical
uniprot
Q16666
canonical
ensembl
ENSG00000163565
resolver
ensp
ENSP00000295809
resolver
ensp
ENSP00000352740
resolver
ensp
ENSP00000357113
resolver
ensp
ENSP00000404325
resolver
ensp
ENSP00000572887
resolver
genesymbol
IFI16
resolver
genesymbol_syn
IFNGIP1
resolver
hgnc
HGNC:5395
resolver
uniprot
A0A346JEQ3
resolver
uniprot
B4DJT8
resolver
uniprot
H3BLV7
resolver
uniprot
Q59GX0
resolver
uniprot
Q5T3W7
resolver
uniprot
Q5T3W8
resolver
uniprot
Q5T3X0
resolver
uniprot
Q5T3X1
resolver
uniprot
Q5T3X2
resolver
uniprot
Q8N9E5
resolver
uniprot
Q8NEQ7
resolver
uniprot
Q96AJ5
resolver
uniprot
Q9UH78
resolver
uniprot_entry
IF16_HUMAN
resolver
uniprot_sec
A0A346JEQ3
resolver
uniprot_sec
B4DJT8
resolver
uniprot_sec
H3BLV7
resolver
uniprot_sec
Q59GX0
resolver
uniprot_sec
Q5T3W7
resolver
uniprot_sec
Q5T3W8
resolver
uniprot_sec
Q5T3X0
resolver
uniprot_sec
Q5T3X1
resolver
uniprot_sec
Q5T3X2
resolver
uniprot_sec
Q8N9E5
resolver
uniprot_sec
Q8NEQ7
resolver
uniprot_sec
Q96AJ5
resolver
uniprot_sec
Q9UH78
resolver
amino_acid_sequence
MGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVKGPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQKRKKSTKEKAGPKGSKVSEEQTQPPSPAGAGMSTAMGRSPSPKTSLSAPPNSSSTENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGDKLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSSMETSPDFFF
uniprot
proteins
function
FUNCTION: Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Necessary to activate the IRF3 signaling cascade during human herpes simplex virus 1 (HHV-1) infection and promotes the assembly of heterochromatin on herpesviral DNA and inhibition of viral immediate-early gene expression and replication. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. {ECO:0000269|PubMed:11146555, ECO:0000269|PubMed:12894224, ECO:0000269|PubMed:14654789, ECO:0000269|PubMed:20890285, ECO:0000269|PubMed:21573174, ECO:0000269|PubMed:21575908, ECO:0000269|PubMed:22046441, ECO:0000269|PubMed:22291595, ECO:0000269|PubMed:23027953, ECO:0000269|PubMed:24198334, ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:9642285}.; FUNCTION: [Isoform IFI16-beta]: Isoform that specifically inhibits the AIM2 inflammasome (PubMed:30104205). Binds double-stranded DNA (dsDNA) in the cytoplasm, impeding its detection by AIM2 (PubMed:30104205). Also prevents the interaction between AIM2 and PYCARD/ASC via its interaction with AIM2, thereby inhibiting assembly of the AIM2 inflammasome (PubMed:30104205). This isoform also weakly induce production of type I interferon-beta (IFNB1) via its interaction with STING1 (PubMed:30104205). {ECO:0000269|PubMed:30104205}.
uniprot
proteins
mass_dalton
88256
uniprot
proteins
mutagenesis
MUTAGEN 96..100; /note="Missing: Predominant cytoplasmic localization."; /evidence="ECO:0000269|PubMed:22691496"; MUTAGEN 99; /note="K->Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state)."; /evidence="ECO:0000269|PubMed:22691496"; MUTAGEN 99; /note="K->R: Minor effect on nuclear localization (mimics acetylated state)."; /evidence="ECO:0000269|PubMed:22691496"; MUTAGEN 128..131; /note="Missing: Predominant nuclear, some cytoplasmic localization."; /evidence="ECO:0000269|PubMed:22691496"; MUTAGEN 128; /note="K->Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state)."; /evidence="ECO:0000269|PubMed:22691496"; MUTAGEN 128; /note="K->R: Minor effect on nuclear localization (mimics acetylated state)."; /evidence="ECO:0000269|PubMed:22691496"; MUTAGEN 134..136; /note="Missing: Mostly nuclear, minor cytoplasmic localization."; /evidence="ECO:0000269|PubMed:22691496"; MUTAGEN 140..143; /note="Missing: Mostly nuclear, minor cytoplasmic localization."; /evidence="ECO:0000269|PubMed:22691496"; MUTAGEN 218; /note="Y->A: Abolishes TP53-mediated transcriptional activation; when associated with A-267."; /evidence="ECO:0000269|PubMed:21397192"; MUTAGEN 222; /note="E->A: Abolishes TP53-mediated transcriptional activation; when associated with A-272."; /evidence="ECO:0000269|PubMed:21397192"; MUTAGEN 267; /note="Y->A: Abolishes TP53-mediated transcriptional activation; when associated with A-218."; /evidence="ECO:0000269|PubMed:21397192"; MUTAGEN 272; /note="E->A: Abolishes TP53-mediated transcriptional activation; when associated with A-222."; /evidence="ECO:0000269|PubMed:21397192"; MUTAGEN 627; /note="K->A: Impairs DNA binding; when associated with A-663; A-667; A-670; A-674; A-732; A-734 and A-759."; /evidence="ECO:0000269|PubMed:22483801"; MUTAGEN 663; /note="K->A: Impairs DNA binding; when associated with A-627; A-667; A-670; A-674; A-732; A-734 and A-759."; /evidence="ECO:0000269|PubMed:22483801"; MUTAGEN 667; /note="R->A: Impairs DNA binding; when associated with A-627; A-663; A-670; A-674; A-732; A-734 and A-759."; /evidence="ECO:0000269|PubMed:22483801"; MUTAGEN 670; /note="S->A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-674; A-732; A-734 and A-759."; /evidence="ECO:0000269|PubMed:22483801"; MUTAGEN 674; /note="K->A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A-732; A-734 and A-759."; /evidence="ECO:0000269|PubMed:22483801"; MUTAGEN 732; /note="K->A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-734 and A-759."; /evidence="ECO:0000269|PubMed:22483801"; MUTAGEN 734; /note="K->A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-759."; /evidence="ECO:0000269|PubMed:22483801"; MUTAGEN 759; /note="K->A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-734."; /evidence="ECO:0000269|PubMed:22483801
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by human herpes simplex virus 1 (HHV-1) ICP0 protein; leading to degradation by the proteasome.; PTM: Lysine acetylation in the multipartite nuclear localization signal (NLS) regulates the subcellular location. In vitro can be acetylated by p300/EP300 coupled to cytoplasmic localization. {ECO:0000269|PubMed:22691496}.; PTM: Phosphorylated on Ser and Thr. {ECO:0000269|PubMed:22691496, ECO:0000269|PubMed:9718316}.; PTM: Isoform 3 seems to show a minor degree of complex carbohydrate addition.
uniprot
proteins
protein_family
HIN-200 family
uniprot
proteins
pubmed
11146555
uniprot
proteins
pubmed
12894224
uniprot
proteins
pubmed
14654789
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
1526658
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20388717
uniprot
proteins
pubmed
20890285
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21397192
uniprot
proteins
pubmed
21573174
uniprot
proteins
pubmed
21575908
uniprot
proteins
pubmed
22046441
uniprot
proteins
pubmed
22291595
uniprot
proteins
pubmed
22483801
uniprot
proteins
pubmed
22618232
uniprot
proteins
pubmed
22691496
uniprot
proteins
pubmed
23027953
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24198334
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24413532
uniprot
proteins
pubmed
24531343
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30104205
uniprot
proteins
pubmed
7536752
uniprot
proteins
pubmed
7806273
uniprot
proteins
pubmed
7959953
uniprot
proteins
pubmed
9642285
uniprot
proteins
pubmed
9718316
uniprot
proteins
pubmed
9766636
uniprot
proteins
sequence_length
785
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24413532, ECO:0000269|PubMed:24531343, ECO:0000269|PubMed:7536752}. Cytoplasm {ECO:0000269|PubMed:22691496}. Note=Cellular distribution is dependent on the acetylation status of the multipartite nuclear localization signal (NLS); NLS acetylation promotes cytoplasmic localization. Localizes in the nucleus during human herpes simplex virus 1 (HHV-1) infection. {ECO:0000269|PubMed:22691496}.; SUBCELLULAR LOCATION: [Isoform IFI16-beta]: Cytoplasm {ECO:0000269|PubMed:30104205}.
uniprot
proteins