Protein:IFI16 |
Protein Summary |
 Gene summary |
| Gene name: IFI16 | ASpdb.0 ID: 3428 | Gene | Gene symbol | IFI16 | Gene ID | 3428 |
| Gene name | interferon gamma inducible protein 16 |
| Synonyms | IFNGIP1|PYHIN2 |
| Cytomap | 1q23.1 |
| Type of gene | protein-coding |
| Description | gamma-interferon-inducible protein 16interferon-gamma induced protein IFI 16interferon-inducible myeloid differentiation transcriptional activator |
| Modification date | 20240416 |
| UniProtAcc | Q16666 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | IFI16 | GO:0000122 | negative regulation of transcription by RNA polymerase II | 12894224 |
| Gene | IFI16 | GO:0002218 | activation of innate immune response | 21575908 |
| Gene | IFI16 | GO:0003690 | double-stranded DNA binding | 7536752 |
| Gene | IFI16 | GO:0005634 | nucleus | 7536752|19158679|24413532|24531343 |
| Gene | IFI16 | GO:0005654 | nucleoplasm | 14654789 |
| Gene | IFI16 | GO:0005730 | nucleolus | 14654789 |
| Gene | IFI16 | GO:0005829 | cytosol | - |
| Gene | IFI16 | GO:0008134 | transcription factor binding | 12894224|22291595 |
| Gene | IFI16 | GO:0016607 | nuclear speck | 19158679 |
| Gene | IFI16 | GO:0030224 | monocyte differentiation | 9766636 |
| Gene | IFI16 | GO:0032731 | positive regulation of interleukin-1 beta production | 21575908 |
| Gene | IFI16 | GO:0042149 | cellular response to glucose starvation | 21573174 |
| Gene | IFI16 | GO:0042771 | intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator | 14654789 |
| Gene | IFI16 | GO:0043392 | negative regulation of DNA binding | 22291595 |
| Gene | IFI16 | GO:0045071 | negative regulation of viral genome replication | 22291595 |
| Gene | IFI16 | GO:0045824 | negative regulation of innate immune response | 22046441 |
| Gene | IFI16 | GO:0045892 | negative regulation of DNA-templated transcription | 9642285 |
| Gene | IFI16 | GO:0045944 | positive regulation of transcription by RNA polymerase II | 11146555 |
| Gene | IFI16 | GO:0051607 | defense response to virus | 21478870 |
| Gene | IFI16 | GO:0071479 | cellular response to ionizing radiation | 14654789 |
| Gene | IFI16 | GO:2000117 | negative regulation of cysteine-type endopeptidase activity | 22046441 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| Q16666-1 | Q16666-1_3rnu_B.pdb | 3RNU | X-ray | 2.5 | B | 571 | 766 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| Q16666 | IFI16 | Q16666-1 | Q16666-2 | 785 | 729 | 444 | 499 | Deletion | none | none | 443 | 443 |
| Q16666 | IFI16 | Q16666-1 | Q16666-3 | 785 | 673 | 444 | 555 | Deletion | none | none | 443 | 443 |
| Q16666 | IFI16 | Q16666-1 | Q16666-6 | 785 | 729 | 128 | 183 | Deletion | none | none | 127 | 127 |
| Multiple sequence alignment of our canonical and alternatively spliced IFI16 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of IFI16 |
| UniProt-id | ENSG | ENST | ENSP |
| Q16666-1 | ENSG00000163565.20 | ENST00000295809.12 | ENSP00000295809.7 |
| Q16666-2 | ENSG00000163565.20 | ENST00000368131.8 | ENSP00000357113.4 |
| Q16666-2 | ENSG00000163565.20 | ENST00000368132.7 | ENSP00000357114.3 |
| Q16666-3 | ENSG00000163565.20 | ENST00000448393.6 | ENSP00000404325.2 |
| Q16666-6 | ENSG00000163565.20 | ENST00000359709.7 | ENSP00000352740.3 |
| UniProt-id | NM ID | NP ID |
| Q16666-2 | NM_005531.2 | NP_005522.2 |
| Q16666-6 | NM_001206567.1 | NP_001193496.1 |
| Amino acid sequences of our canonical and alternatively spliced IFI16 |
| accession_id | Protein sequence |
| Q16666-1 | MGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVK GPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQKRKKSTKEKAGPKGSKVSEEQTQPPSPAGAGMSTAMGRSPSPKTSLSAPPNSS STENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSL LEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGD KLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTIS KMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHT PQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKII AIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHG |
| Q16666-2 | MGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVK GPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQKRKKSTKEKAGPKGSKVSEEQTQPPSPAGAGMSTAMGRSPSPKTSLSAPPNSS STENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSL LEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGD KLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTIS KMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQ KKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSF VNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSS |
| Q16666-3 | MGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVK GPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQKRKKSTKEKAGPKGSKVSEEQTQPPSPAGAGMSTAMGRSPSPKTSLSAPPNSS STENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSL LEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGD KLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKLKPRLKT EPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVAD VNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAP |
| Q16666-6 | MGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVK GPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQNPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQ TQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKT VNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGDKLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSE ASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTKSEDTIS KMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQ KKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSF VNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSS |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| IFI16 (go to UniProt):Q16666 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Q16666 | Region | 91 | 191 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=128;End=183 |
| Q16666 | Motif | 128 | 131 | Note=Nuclear localization signal | Type=Deletion;Start=128;End=183 |
| Q16666 | Motif | 134 | 136 | Note=Nuclear localization signal | Type=Deletion;Start=128;End=183 |
| Q16666 | Motif | 140 | 143 | Note=Nuclear localization signal | Type=Deletion;Start=128;End=183 |
| Q16666 | Compositional bias | 123 | 142 | Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=128;End=183 |
| Q16666 | Compositional bias | 164 | 191 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=128;End=183 |
Gene Isoform Structures and Expression Levels for IFI16 |
| Gene structures of our canonical and alternative spliced genes of IFI16 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of Q16666-1 |
| 3D view using mol* of Q16666-2 |
| 3D view using mol* of Q16666-3 |
| 3D view using mol* of Q16666-6 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of Q16666-1 |
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| pLDDT distribution across the protein length of Q16666-2 |
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| pLDDT distribution across the protein length of Q16666-3 |
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| pLDDT distribution across the protein length of Q16666-6 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of Q16666-1 |
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| Ramachandran plot of Q16666-2 |
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| Ramachandran plot of Q16666-3 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| Q16666-1 | 1.017 | 161 | 0.955 | 432.523 | 0.525 | 0.723 | 0.997 | 0.136 | 1.285 | 0.105 | 1.07 | 210,211,212,213,214,230,231,232,238,239,240,241,26 7,268,269,270,297,298,299,300,301,302,303,314,315, 316,317,318,319,363,364,365,387,389 |
| Q16666-2 | 1.044 | 136 | 0.97 | 433.895 | 0.513 | 0.763 | 1.068 | 0.188 | 1.311 | 0.143 | 1.087 | 210,211,212,213,232,238,239,241,268,269,270,297,29 8,299,300,301,302,310,314,315,316,317,318,319,363, 365,387,389 |
| Q16666-3 | 1.005 | 204 | 1.024 | 633.178 | 0.512 | 0.705 | 0.877 | 0.328 | 1.04 | 0.315 | 1.247 | 372,373,452,453,454,455,456,457,458,459,497,498,49 9,500,525,526,527,528,552,553,556,557,558,559,561, 565,566,569,572,573,574,575,576,628 |
| Q16666-6 | 1.033 | 305 | 1.057 | 1353.821 | 0.576 | 0.734 | 0.932 | 0.692 | 0.993 | 0.697 | 0.717 | 268,270,272,273,274,275,277,279,290,314,315,316,31 7,319,321,323,508,509,510,511,512,513,514,515,516, 518,520,522,528,530,545,546,547,553,554,555,556,55 7,581,583,584,585,586,612,613,614,615,616,617,621, 622,625,627,628,629,630,631,632,633,634,678,680 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of Q16666-1_Q16666-1_3rnu_B.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q16666-1_3rnu_B_Q16666-2.pdb |
| 3D view using mol* of Q16666-1_3rnu_B_Q16666-3.pdb |
| 3D view using mol* of Q16666-1_3rnu_B_Q16666-6.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of Q16666-1_Q16666-2.pdb |
| 3D view using mol* of Q16666-1_Q16666-3.pdb |
| 3D view using mol* of Q16666-1_Q16666-6.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/Q16666-1_vs_Q16666-2.png |
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| ./stats/secondary_structure/figure/Q16666-1_vs_Q16666-3.png |
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| ./stats/secondary_structure/figure/Q16666-1_vs_Q16666-6.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/Q16666-1_vs_Q16666-2.png |
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| ./stats/relative_asa/Q16666-1_vs_Q16666-3.png |
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| ./stats/relative_asa/Q16666-1_vs_Q16666-6.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to IFI16 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to IFI16 |
| Previous studies relating to the alternative splicing of IFI16 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
Clinically important variants in IFI16 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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