Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q16666

- IF16_HUMAN

UniProt

Q16666 - IF16_HUMAN

Protein

Gamma-interferon-inducible protein 16

Gene

IFI16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 3 (28 Nov 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.12 Publications

    GO - Molecular functioni

    1. double-stranded DNA binding Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. activation of cysteine-type endopeptidase activity Source: UniProtKB
    2. activation of innate immune response Source: UniProtKB
    3. autophagy Source: UniProtKB-KW
    4. cell proliferation Source: UniProtKB
    5. cellular response to glucose starvation Source: UniProtKB
    6. cellular response to ionizing radiation Source: UniProtKB
    7. defense response to virus Source: UniProtKB
    8. hemopoiesis Source: UniProtKB
    9. inflammatory response Source: UniProtKB-KW
    10. innate immune response Source: Reactome
    11. intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
    12. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
    13. monocyte differentiation Source: UniProtKB
    14. myeloid cell differentiation Source: UniProtKB
    15. negative regulation of cysteine-type endopeptidase activity Source: UniProtKB
    16. negative regulation of DNA binding Source: UniProtKB
    17. negative regulation of innate immune response Source: UniProtKB
    18. negative regulation of transcription, DNA-templated Source: UniProtKB
    19. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    20. negative regulation of viral genome replication Source: UniProtKB
    21. positive regulation of cytokine production Source: UniProtKB
    22. positive regulation of interleukin-1 beta production Source: UniProtKB
    23. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    24. positive regulation of type I interferon production Source: Reactome
    25. regulation of autophagy Source: UniProtKB
    26. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Apoptosis, Autophagy, Immunity, Inflammatory response, Innate immunity, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_147841. STING mediated induction of host immune responses.
    REACT_163993. IRF3-mediated induction of type I IFN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-interferon-inducible protein 16
    Short name:
    Ifi-16
    Alternative name(s):
    Interferon-inducible myeloid differentiation transcriptional activator
    Gene namesi
    Name:IFI16
    Synonyms:IFNGIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:5395. IFI16.

    Subcellular locationi

    Nucleus. Cytoplasm
    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.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nuclear speck Source: MGI
    5. nucleolus Source: HPA
    6. nucleoplasm Source: MGI
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi96 – 1005Missing: Predominant cytoplasmic localization.
    Mutagenesisi99 – 991K → Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state). 1 Publication
    Mutagenesisi99 – 991K → R: Minor effect on nuclear localization (mimics acetylated state). 1 Publication
    Mutagenesisi128 – 1314Missing: Predominant nuclear, some cytoplasmic localization. 1 Publication
    Mutagenesisi128 – 1281K → Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state). 1 Publication
    Mutagenesisi128 – 1281K → R: Minor effect on nuclear localization (mimics acetylated state). 1 Publication
    Mutagenesisi134 – 1363Missing: Mostly nuclear, minor cytoplasmic localization.
    Mutagenesisi140 – 1434Missing: Mostly nuclear, minor cytoplasmic localization.
    Mutagenesisi218 – 2181Y → A: Abolishes TP53-mediated transcriptional activation; when associated with A-267. 1 Publication
    Mutagenesisi222 – 2221E → A: Abolishes TP53-mediated transcriptional activation; when associated with A-272. 1 Publication
    Mutagenesisi267 – 2671Y → A: Abolishes TP53-mediated transcriptional activation; when associated with A-218. 1 Publication
    Mutagenesisi272 – 2721E → A: Abolishes TP53-mediated transcriptional activation; when associated with A-222. 1 Publication
    Mutagenesisi627 – 6271K → A: Impairs DNA binding; when associated with A-663; A-667; A-670; A-674; A-732; A-734 and A-759. 1 Publication
    Mutagenesisi663 – 6631K → A: Impairs DNA binding; when associated with A-627; A-667; A-670; A-674; A-732; A-734 and A-759. 1 Publication
    Mutagenesisi667 – 6671R → A: Impairs DNA binding; when associated with A-627; A-663; A-670; A-674; A-732; A-734 and A-759. 1 Publication
    Mutagenesisi670 – 6701S → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-674; A-732; A-734 and A-759. 1 Publication
    Mutagenesisi674 – 6741K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A-732; A-734 and A-759. 1 Publication
    Mutagenesisi732 – 7321K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-734 and A-759. 1 Publication
    Mutagenesisi734 – 7341K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-759. 1 Publication
    Mutagenesisi759 – 7591K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-734. 1 Publication

    Organism-specific databases

    PharmGKBiPA29642.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 785785Gamma-interferon-inducible protein 16PRO_0000153723Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei45 – 451N6-acetyllysine1 Publication
    Modified residuei95 – 951Phosphoserine1 Publication
    Modified residuei99 – 991N6-acetyllysine1 Publication
    Modified residuei106 – 1061Phosphoserine6 Publications
    Modified residuei128 – 1281N6-acetyllysine1 Publication
    Modified residuei153 – 1531Phosphoserine5 Publications
    Modified residuei168 – 1681Phosphoserine2 Publications
    Modified residuei174 – 1741Phosphoserine2 Publications
    Modified residuei214 – 2141N6-acetyllysine2 Publications
    Modified residuei444 – 4441N6-acetyllysine1 Publication
    Modified residuei451 – 4511N6-acetyllysine1 Publication
    Modified residuei561 – 5611N6-acetyllysine; alternate1 Publication
    Cross-linki561 – 561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate
    Modified residuei575 – 5751Phosphoserine2 Publications
    Modified residuei598 – 5981N6-acetyllysine1 Publication
    Modified residuei614 – 6141N6-acetyllysine1 Publication
    Modified residuei780 – 7801Phosphoserine2 Publications

    Post-translational modificationi

    Ubiquitinated by human herpes simplex virus 1 (HHV-1) ICP0 protein; leading to degradation by the proteasome.
    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.2 Publications
    Phosphorylated on Ser and Thr.6 Publications
    Isoform 3 seems to show a minor degree of complex carbohydrate addition.

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ16666.
    PaxDbiQ16666.
    PRIDEiQ16666.

    PTM databases

    PhosphoSiteiQ16666.

    Expressioni

    Tissue specificityi

    Expressed in peripheral blood leukocytes, fibroblasts and lymphoid cells. Present in myeloid precursors (CD34+) and throughout monocyte development, but its expression is down-regulated in erythroid and polymorphonuclear precursor cells. Present in prostate, ovary and breast (at protein level).1 Publication

    Inductioni

    Strongly induced by IFNG/IFN-gamma and, to a lesser extent, by alpha interferon. In HL-60 cells, maximum induction by IFNG/IFN-gamma occurs within 12 hours whereas, for IFN-alpha, only 10-fold induction was observed after 36 hours. Induced in vitro by dimethylsulfoxide, retinoic acid and 1,25 dihydroxyvitamin D3. Induced in monocytes by IFN-alpha and viral dsDNA. Induced by glucose restriction.4 Publications

    Gene expression databases

    ArrayExpressiQ16666.
    BgeeiQ16666.
    GenevestigatoriQ16666.

    Organism-specific databases

    HPAiCAB016293.
    HPA002134.

    Interactioni

    Subunit structurei

    Forms homooligomers; isoform 2 can self-associate or associate with isoform 1 or isoform 3. Interacts with TMEM173, AIM2, PYCARD and CASP1. Interacts with BRCA1, TP53, E2F1, RB1 and SP1. Interacts with MTA1.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARP102753EBI-2867186,EBI-608057
    BRCA1P383989EBI-2867186,EBI-349905
    TMEM173Q86WV62EBI-2867186,EBI-2800345
    TP53P046373EBI-6273540,EBI-366083

    Protein-protein interaction databases

    BioGridi109654. 10 interactions.
    DIPiDIP-42868N.
    IntActiQ16666. 13 interactions.
    MINTiMINT-1781545.

    Structurei

    Secondary structure

    1
    785
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi205 – 2128
    Beta strandi216 – 2194
    Beta strandi225 – 23410
    Beta strandi239 – 2446
    Helixi247 – 2537
    Beta strandi254 – 2574
    Beta strandi259 – 2679
    Beta strandi270 – 2734
    Beta strandi278 – 2814
    Helixi284 – 2863
    Helixi292 – 2987
    Helixi304 – 3074
    Beta strandi315 – 32713
    Beta strandi329 – 33810
    Beta strandi341 – 3488
    Helixi349 – 3513
    Beta strandi361 – 37212
    Beta strandi375 – 3795
    Beta strandi385 – 3884
    Beta strandi578 – 5858
    Beta strandi589 – 5924
    Turni593 – 5964
    Beta strandi597 – 6059
    Beta strandi610 – 6156
    Helixi618 – 6203
    Turni621 – 6244
    Beta strandi629 – 6346
    Beta strandi636 – 6383
    Beta strandi641 – 6444
    Beta strandi648 – 6525
    Beta strandi655 – 6573
    Helixi663 – 6708
    Helixi675 – 6795
    Beta strandi685 – 69915
    Beta strandi702 – 7098
    Beta strandi712 – 7187
    Helixi720 – 7245
    Beta strandi732 – 74110
    Turni744 – 7474
    Beta strandi749 – 76113
    Turni764 – 7663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2OQ0X-ray2.00A/B/C/D192-393[»]
    3B6YX-ray2.35A/B571-766[»]
    3RLNX-ray2.25A571-766[»]
    3RLOX-ray1.80A571-766[»]
    3RNUX-ray2.50A/B/C/D571-766[»]
    ProteinModelPortaliQ16666.
    SMRiQ16666. Positions 1-93, 198-389, 575-766.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16666.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8888DAPINPROSITE-ProRule annotationAdd
    BLAST
    Domaini189 – 389201HIN-200 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini562 – 761200HIN-200 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni192 – 393202Interaction with TP53 C-terminusAdd
    BLAST
    Regioni571 – 766196Interaction with TP53 core domainAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi96 – 1005Nuclear localization signal
    Motifi128 – 1314Nuclear localization signal
    Motifi134 – 1363Nuclear localization signal
    Motifi140 – 1434Nuclear localization signal

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 150150Lys-richAdd
    BLAST
    Compositional biasi258 – 2614Poly-Ile

    Domaini

    The HIN-20 domains mediates dsDNA binding via electrostatic interactions.1 Publication

    Sequence similaritiesi

    Belongs to the HIN-200 family.Curated
    Contains 1 DAPIN domain.PROSITE-ProRule annotation
    Contains 2 HIN-200 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG81691.
    HOVERGENiHBG006122.
    InParanoidiQ16666.
    OMAiGPFMTSI.
    OrthoDBiEOG7ZD1V8.
    PhylomeDBiQ16666.
    TreeFamiTF337385.

    Family and domain databases

    Gene3Di2.40.50.140. 4 hits.
    InterProiIPR004020. DAPIN.
    IPR004021. HIN200/IF120x.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PfamiPF02760. HIN. 2 hits.
    PF02758. PYRIN. 1 hit.
    [Graphical view]
    PROSITEiPS50824. DAPIN. 1 hit.
    PS50834. HIN_200. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16666-1) [UniParc]FASTAAdd to Basket

    Also known as: IFI 16A

    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

    MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD    50
    LMEEKFRGDA GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK 100
    EVDATSPAPS TSSTVKTEGA EATPGAQKRK KSTKEKAGPK GSKVSEEQTQ 150
    PPSPAGAGMS TAMGRSPSPK TSLSAPPNSS STENPKTVAK CQVTPRRNVL 200
    QKRPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF HVKVLNTSLK 250
    EKFNGKKIII ISDYLEYDSL LEVNEESTVS EAGPNQTFEV PNKIINRAKE 300
    TLKIDILHKQ ASGNIVYGVF MLHKKTVNQK TTIYEIQDDR GKMDVVGTGQ 350
    CHNIPCEEGD KLQLFCFRLR KKNQMSKLIS EMHSFIQIKK KTNPRNNDPK 400
    SMKLPQEQRQ LPYPSEASTT FPESHLRTPQ MPPTTPSSSF FTKKSEDTIS 450
    KMNDFMRMQI LKEGSHFPGP FMTSIGPAES HPHTPQMPPS TPSSSFLTTK 500
    SEDTISKMND FMRMQILKEG SHFPGPFMTS IGPAESHPHT PQMPPSTPSS 550
    SFLTTLKPRL KTEPEEVSIE DSAQSDLKEV MVLNATESFV YEPKEQKKMF 600
    HATVATENEV FRVKVFNIDL KEKFTPKKII AIANYVCRNG FLEVYPFTLV 650
    ADVNADRNME IPKGLIRSAS VTPKINQLCS QTKGSFVNGV FEVHKKNVRG 700
    EFTYYEIQDN TGKMEVVVHG RLTTINCEEG DKLKLTCFEL APKSGNTGEL 750
    RSVIHSHIKV IKTRKNKKDI LNPDSSMETS PDFFF 785
    Length:785
    Mass (Da):88,256
    Last modified:November 28, 2006 - v3
    Checksum:i216CD103D8F5206A
    GO
    Isoform 2 (identifier: Q16666-2) [UniParc]FASTAAdd to Basket

    Also known as: IFI 16B

    The sequence of this isoform differs from the canonical sequence as follows:
         444-499: Missing.

    Note: Major isoform.

    Show »
    Length:729
    Mass (Da):82,096
    Checksum:i27C820A058DE6A92
    GO
    Isoform 3 (identifier: Q16666-3) [UniParc]FASTAAdd to Basket

    Also known as: IFI 16C

    The sequence of this isoform differs from the canonical sequence as follows:
         444-555: Missing.

    Show »
    Length:673
    Mass (Da):75,936
    Checksum:i4D80A41BD9AA13A5
    GO
    Isoform 4 (identifier: Q16666-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-183: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:729
    Mass (Da):82,588
    Checksum:iFEB03DF1E8B09D0A
    GO

    Sequence cautioni

    The sequence AAF20997.1 differs from that shown. Reason: Intron retention.
    The sequence BAC04462.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAF20997.1 differs from that shown. Reason: Frameshift at position 776.
    The sequence BAD92226.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAG58950.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti401 – 4011S → G in BAG58950. (PubMed:14702039)Curated
    Sequence conflicti544 – 5441P → S in BAG58950. (PubMed:14702039)Curated
    Sequence conflicti683 – 6831K → R in AAM96005. (PubMed:12894224)Curated
    Sequence conflicti723 – 7231T → N in AAA58683. (PubMed:1526658)Curated
    Sequence conflicti723 – 7231T → N in AAB32519. (PubMed:7959953)Curated
    Sequence conflicti737 – 7371C → S in AAA58683. (PubMed:1526658)Curated
    Sequence conflicti737 – 7371C → S in AAB32519. (PubMed:7959953)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031D → H.3 Publications
    Corresponds to variant rs1057018 [ dbSNP | Ensembl ].
    VAR_029486
    Natural varianti179 – 1791S → T.3 Publications
    Corresponds to variant rs866484 [ dbSNP | Ensembl ].
    VAR_029487
    Natural varianti202 – 2021K → E.
    Corresponds to variant rs11585341 [ dbSNP | Ensembl ].
    VAR_029488
    Natural varianti409 – 4091R → S.4 Publications
    Corresponds to variant rs1057027 [ dbSNP | Ensembl ].
    VAR_029489
    Natural varianti413 – 4131Y → N.4 Publications
    Corresponds to variant rs1057028 [ dbSNP | Ensembl ].
    VAR_029490
    Natural varianti723 – 7231T → S.
    Corresponds to variant rs6940 [ dbSNP | Ensembl ].
    VAR_029491
    Natural varianti779 – 7791T → S.
    Corresponds to variant rs6940 [ dbSNP | Ensembl ].
    VAR_057582

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei128 – 18356Missing in isoform 4. 1 PublicationVSP_044691Add
    BLAST
    Alternative sequencei444 – 555112Missing in isoform 3. CuratedVSP_002675Add
    BLAST
    Alternative sequencei444 – 49956Missing in isoform 2. 5 PublicationsVSP_002676Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63838 mRNA. Translation: AAA58683.1.
    S75433
    , S75417, S75419, S75421, S75423, S75424, S75426, S75429, S75431 Genomic DNA. Translation: AAB32519.2.
    AF208043 mRNA. Translation: AAF20997.1. Sequence problems.
    AY138863 mRNA. Translation: AAM96005.1.
    AK094968 mRNA. Translation: BAC04462.1. Sequence problems.
    AK296228 mRNA. Translation: BAG58950.1. Different initiation.
    AB208989 mRNA. Translation: BAD92226.1. Different initiation.
    AL359753 Genomic DNA. Translation: CAI15081.1.
    AL359753 Genomic DNA. Translation: CAI15082.1.
    AL359753 Genomic DNA. Translation: CAI15083.1.
    AL359753 Genomic DNA. Translation: CAI15084.1.
    AL359753 Genomic DNA. Translation: CAI15085.1.
    AL359753 Genomic DNA. Translation: CAI15086.1.
    BC017059 mRNA. Translation: AAH17059.1.
    CCDSiCCDS1180.3. [Q16666-2]
    CCDS58039.1. [Q16666-6]
    PIRiI54501.
    RefSeqiNP_001193496.1. NM_001206567.1. [Q16666-6]
    NP_005522.2. NM_005531.2. [Q16666-2]
    UniGeneiHs.380250.

    Genome annotation databases

    EnsembliENST00000295809; ENSP00000295809; ENSG00000163565. [Q16666-1]
    ENST00000340979; ENSP00000342741; ENSG00000163565. [Q16666-3]
    ENST00000359709; ENSP00000352740; ENSG00000163565. [Q16666-6]
    ENST00000368131; ENSP00000357113; ENSG00000163565. [Q16666-2]
    ENST00000368132; ENSP00000357114; ENSG00000163565. [Q16666-2]
    ENST00000448393; ENSP00000404325; ENSG00000163565. [Q16666-3]
    GeneIDi3428.
    KEGGihsa:3428.
    UCSCiuc001ftg.3. human. [Q16666-2]

    Polymorphism databases

    DMDMi118572657.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63838 mRNA. Translation: AAA58683.1 .
    S75433
    , S75417 , S75419 , S75421 , S75423 , S75424 , S75426 , S75429 , S75431 Genomic DNA. Translation: AAB32519.2 .
    AF208043 mRNA. Translation: AAF20997.1 . Sequence problems.
    AY138863 mRNA. Translation: AAM96005.1 .
    AK094968 mRNA. Translation: BAC04462.1 . Sequence problems.
    AK296228 mRNA. Translation: BAG58950.1 . Different initiation.
    AB208989 mRNA. Translation: BAD92226.1 . Different initiation.
    AL359753 Genomic DNA. Translation: CAI15081.1 .
    AL359753 Genomic DNA. Translation: CAI15082.1 .
    AL359753 Genomic DNA. Translation: CAI15083.1 .
    AL359753 Genomic DNA. Translation: CAI15084.1 .
    AL359753 Genomic DNA. Translation: CAI15085.1 .
    AL359753 Genomic DNA. Translation: CAI15086.1 .
    BC017059 mRNA. Translation: AAH17059.1 .
    CCDSi CCDS1180.3. [Q16666-2 ]
    CCDS58039.1. [Q16666-6 ]
    PIRi I54501.
    RefSeqi NP_001193496.1. NM_001206567.1. [Q16666-6 ]
    NP_005522.2. NM_005531.2. [Q16666-2 ]
    UniGenei Hs.380250.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OQ0 X-ray 2.00 A/B/C/D 192-393 [» ]
    3B6Y X-ray 2.35 A/B 571-766 [» ]
    3RLN X-ray 2.25 A 571-766 [» ]
    3RLO X-ray 1.80 A 571-766 [» ]
    3RNU X-ray 2.50 A/B/C/D 571-766 [» ]
    ProteinModelPortali Q16666.
    SMRi Q16666. Positions 1-93, 198-389, 575-766.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109654. 10 interactions.
    DIPi DIP-42868N.
    IntActi Q16666. 13 interactions.
    MINTi MINT-1781545.

    PTM databases

    PhosphoSitei Q16666.

    Polymorphism databases

    DMDMi 118572657.

    Proteomic databases

    MaxQBi Q16666.
    PaxDbi Q16666.
    PRIDEi Q16666.

    Protocols and materials databases

    DNASUi 3428.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295809 ; ENSP00000295809 ; ENSG00000163565 . [Q16666-1 ]
    ENST00000340979 ; ENSP00000342741 ; ENSG00000163565 . [Q16666-3 ]
    ENST00000359709 ; ENSP00000352740 ; ENSG00000163565 . [Q16666-6 ]
    ENST00000368131 ; ENSP00000357113 ; ENSG00000163565 . [Q16666-2 ]
    ENST00000368132 ; ENSP00000357114 ; ENSG00000163565 . [Q16666-2 ]
    ENST00000448393 ; ENSP00000404325 ; ENSG00000163565 . [Q16666-3 ]
    GeneIDi 3428.
    KEGGi hsa:3428.
    UCSCi uc001ftg.3. human. [Q16666-2 ]

    Organism-specific databases

    CTDi 3428.
    GeneCardsi GC01P158969.
    H-InvDB HIX0001194.
    HGNCi HGNC:5395. IFI16.
    HPAi CAB016293.
    HPA002134.
    MIMi 147586. gene.
    neXtProti NX_Q16666.
    PharmGKBi PA29642.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG81691.
    HOVERGENi HBG006122.
    InParanoidi Q16666.
    OMAi GPFMTSI.
    OrthoDBi EOG7ZD1V8.
    PhylomeDBi Q16666.
    TreeFami TF337385.

    Enzyme and pathway databases

    Reactomei REACT_147841. STING mediated induction of host immune responses.
    REACT_163993. IRF3-mediated induction of type I IFN.

    Miscellaneous databases

    ChiTaRSi IFI16. human.
    EvolutionaryTracei Q16666.
    GeneWikii IFI16.
    GenomeRNAii 3428.
    NextBioi 13516.
    PROi Q16666.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16666.
    Bgeei Q16666.
    Genevestigatori Q16666.

    Family and domain databases

    Gene3Di 2.40.50.140. 4 hits.
    InterProi IPR004020. DAPIN.
    IPR004021. HIN200/IF120x.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    Pfami PF02760. HIN. 2 hits.
    PF02758. PYRIN. 1 hit.
    [Graphical view ]
    PROSITEi PS50824. DAPIN. 1 hit.
    PS50834. HIN_200. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel gene constitutively expressed in human lymphoid cells is inducible with interferon-gamma in myeloid cells."
      Trapani J.A., Browne K.A., Dawson M.J., Ramsay R.G., Eddy R.L., Show T.B., White P.C., Dupont B.
      Immunogenetics 36:369-376(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT HIS-103.
      Tissue: T-cell.
    2. "Genomic organization of IFI16, an interferon-inducible gene whose expression is associated with human myeloid cell differentiation: correlation of predicted protein domains with exon organization."
      Trapani J.A., Dawson M.J., Apostolidis V.A., Browne K.A.
      Immunogenetics 40:415-424(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT HIS-103.
    3. Jiang C., Zhang D., Peng Y., Zhang X., Han Z., Fu G., Chen Z.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT HIS-103.
      Tissue: Bone marrow.
    4. "Role of IFI 16, a member of the interferon-inducible p200-protein family, in prostate epithelial cellular senescence."
      Xin H., Curry J., Johnstone R.W., Nickoloff B.J., Choubey D.
      Oncogene 22:4831-4840(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, INDUCTION, VARIANTS THR-179; SER-409 AND ASN-413.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANTS THR-179; SER-409 AND ASN-413.
      Tissue: Hippocampus and Thalamus.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS SER-409 AND ASN-413.
      Tissue: Brain.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANTS THR-179; SER-409 AND ASN-413.
      Tissue: Uterus.
    9. "Isotypic variants of the interferon-inducible transcriptional repressor IFI 16 arise through differential mRNA splicing."
      Johnstone R.W., Kershaw M.H., Trapani J.A.
      Biochemistry 37:11924-11931(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, SUBUNIT, PHOSPHORYLATION, GLYCOSYLATION.
    10. "IFI 16 gene encodes a nuclear protein whose expression is induced by interferons in human myeloid leukaemia cell lines."
      Dawson M.J., Trapani J.A.
      J. Cell. Biochem. 57:39-51(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, SUBCELLULAR LOCATION, DNA-BINDING.
    11. "The closely linked genes encoding the myeloid nuclear differentiation antigen (MNDA) and IFI16 exhibit contrasting haemopoietic expression."
      Dawson M.J., Trapani J.A., Briggs R.C., Nicholl J.K., Sutherland G.R., Baker E.
      Immunogenetics 41:40-43(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE-SPECIFIC INDUCTION.
    12. "The IFN-inducible nucleoprotein IFI 16 is expressed in cells of the monocyte lineage, but is rapidly and markedly down-regulated in other myeloid precursor populations."
      Dawson M.J., Elwood N.J., Johnstone R.W., Trapani J.A.
      J. Leukoc. Biol. 64:546-554(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFIC INDUCTION.
    13. "The human interferon-inducible protein, IFI 16, is a repressor of transcription."
      Johnstone R.W., Kerry J.A., Trapani J.A.
      J. Biol. Chem. 273:17172-17177(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Functional interaction between p53 and the interferon-inducible nucleoprotein IFI 16."
      Johnstone R.W., Wei W., Greenway A., Trapani J.A.
      Oncogene 19:6033-6042(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53.
    15. "A member of the Pyrin family, IFI16, is a novel BRCA1-associated protein involved in the p53-mediated apoptosis pathway."
      Aglipay J.A., Lee S.W., Okada S., Fujiuchi N., Ohtsuka T., Kwak J.C., Wang Y., Johnstone R.W., Deng C., Qin J., Ouchi T.
      Oncogene 22:8931-8938(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRCA1.
    16. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-214, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
      Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
      J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-561.
      Tissue: Cervix carcinoma.
    21. Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH TMEM173, INDUCTION.
    22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-153 AND SER-575, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi Sarcoma-associated herpesvirus infection."
      Kerur N., Veettil M.V., Sharma-Walia N., Bottero V., Sadagopan S., Otageri P., Chandran B.
      Cell Host Microbe 9:363-375(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PYCARD AND CASP1.
    25. "IFI16 induction by glucose restriction in human fibroblasts contributes to autophagy through activation of the ATM/AMPK/p53 pathway."
      Duan X., Ponomareva L., Veeranki S., Choubey D.
      PLoS ONE 6:E19532-E19532(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    26. "IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes."
      Veeranki S., Duan X., Panchanathan R., Liu H., Choubey D.
      PLoS ONE 6:E27040-E27040(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AIM2.
    27. "Preferential binding of IFI16 protein to cruciform structure and superhelical DNA."
      Brazda V., Coufal J., Liao J.C., Arrowsmith C.H.
      Biochem. Biophys. Res. Commun. 422:716-720(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING.
    28. "The intracellular DNA sensor IFI16 gene acts as restriction factor for human cytomegalovirus replication."
      Gariano G.R., Dell'Oste V., Bronzini M., Gatti D., Luganini A., De Andrea M., Gribaudo G., Gariglio M., Landolfo S.
      PLoS Pathog. 8:E1002498-E1002498(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SP1.
    29. "Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein."
      Orzalli M.H., DeLuca N.A., Knipe D.M.
      Proc. Natl. Acad. Sci. U.S.A. 109:E3008-E3017(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEASOMAL DEGRADATION.
    30. "Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16."
      Li T., Diner B.A., Chen J., Cristea I.M.
      Proc. Natl. Acad. Sci. U.S.A. 109:10558-10563(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-106; SER-153; SER-168; SER-174 AND SER-780, ACETYLATION AT LYS-45; LYS-99; LYS-128; LYS-214; LYS-444; LYS-451; LYS-561; LYS-598 AND LYS-614, MUTAGENESIS OF 96-ARG--LYS-100; LYS-99; LYS-128; 128-LYS--LYS-131; 134-LYS--LYS-136 AND 140-LYS--LYS-143.
    31. "Nuclear interferon-inducible protein 16 promotes silencing of herpesviral and transfected DNA."
      Orzalli M.H., Conwell S.E., Berrios C., DeCaprio J.A., Knipe D.M.
      Proc. Natl. Acad. Sci. U.S.A. 110:E4492-E4501(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    32. "Differential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1."
      Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y., Kim Y.N., Seong J.K., Lee M.O.
      Cancer Res. 74:1484-1494(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MTA1, SUBCELLULAR LOCATION.
    33. "Interferon-inducible protein 16: insight into the interaction with tumor suppressor p53."
      Liao J.C., Lam R., Brazda V., Duan S., Ravichandran M., Ma J., Xiao T., Tempel W., Zuo X., Wang Y.X., Chirgadze N.Y., Arrowsmith C.H.
      Structure 19:418-429(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393, MUTAGENESIS OF TYR-218; GLU-222; TYR-267 AND GLU-272.
    34. "Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor."
      Jin T., Perry A., Jiang J., Smith P., Curry J.A., Unterholzner L., Jiang Z., Horvath G., Rathinam V.A., Johnstone R.W., Hornung V., Latz E., Bowie A.G., Fitzgerald K.A., Xiao T.S.
      Immunity 36:561-571(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 571-766 IN COMPLEX WITH DOUBLE-STRANDED DNA, MUTAGENESIS OF LYS-627; LYS-663; ARG-667; SER-670; LYS-674; LYS-732; LYS-734 AND LYS-759.
    35. "Crystal structure of the first HIN-200 domain of interferon-inducible protein 16."
      Northeast structural genomics consortium (NESG)
      Submitted (FEB-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393.
    36. "Crystal structure analysis of the second HIN domain of IFI16."
      Northeast structural genomics consortium (NESG)
      Submitted (NOV-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 571-766.

    Entry informationi

    Entry nameiIF16_HUMAN
    AccessioniPrimary (citable) accession number: Q16666
    Secondary accession number(s): B4DJT8
    , H3BLV7, Q59GX0, Q5T3W7, Q5T3W8, Q5T3X0, Q5T3X1, Q5T3X2, Q8N9E5, Q8NEQ7, Q96AJ5, Q9UH78
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 154 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3