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Q16666 (IF16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-interferon-inducible protein 16

Short name=Ifi-16
Alternative name(s):
Interferon-inducible myeloid differentiation transcriptional activator
Gene names
Name:IFI16
Synonyms:IFNGIP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length785 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.4 Ref.13 Ref.14 Ref.15 Ref.21 Ref.24 Ref.25 Ref.26 Ref.28

Subunit structure

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. Ref.9 Ref.14 Ref.15 Ref.21 Ref.24 Ref.26 Ref.28

Subcellular location

Nucleus. Cytoplasm. Note: Cellular distribution is dependent on the acetylation status of the multipartite nuclear localization signal (NLS); NLS acetylation promotes cytoplasmic localization. Ref.10 Ref.26 Ref.29

Tissue specificity

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). Ref.4

Induction

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. Ref.4 Ref.10 Ref.11 Ref.12 Ref.21 Ref.25

Domain

The HIN-20 domains mediates dsDNA binding via electrostatic interactions (Ref.31).

Post-translational modification

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. Ref.29

Phosphorylated on Ser and Thr. Ref.9 Ref.29

Isoform 3 seems to show a minor degree of complex carbohydrate addition.

Sequence similarities

Belongs to the HIN-200 family.

Contains 1 DAPIN domain.

Contains 2 HIN-200 domains.

Sequence caution

The sequence AAF20997.1 differs from that shown. Reason: Frameshift at position 776.

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 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.

Ontologies

Keywords
   Biological processApoptosis
Autophagy
Immunity
Inflammatory response
Innate immunity
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity

Inferred from mutant phenotype Ref.24. Source: UniProtKB

activation of innate immune response

Inferred from direct assay Ref.24. Source: UniProtKB

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Non-traceable author statement Ref.12. Source: UniProtKB

cellular response to glucose starvation

Inferred from direct assay Ref.25. Source: UniProtKB

cellular response to ionizing radiation

Inferred from direct assay Ref.15. Source: UniProtKB

defense response to virus

Inferred from mutant phenotype Ref.24. Source: UniProtKB

hemopoiesis

Non-traceable author statement Ref.12. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from mutant phenotype Ref.25. Source: UniProtKB

intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from direct assay Ref.15. Source: MGI

monocyte differentiation

Inferred from direct assay Ref.12. Source: UniProtKB

myeloid cell differentiation

Non-traceable author statement Ref.10. Source: UniProtKB

negative regulation of DNA binding

Inferred from direct assay Ref.28. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity

Inferred from direct assay Ref.26. Source: UniProtKB

negative regulation of innate immune response

Inferred from direct assay Ref.26. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.4. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of viral genome replication

Inferred from direct assay Ref.28. Source: UniProtKB

positive regulation of cytokine production

Traceable author statement Ref.26. Source: UniProtKB

positive regulation of interleukin-1 beta production

Inferred from direct assay Ref.24. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

regulation of autophagy

Inferred from expression pattern Ref.25. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nuclear speck

Inferred from direct assay PubMed 19158679. Source: MGI

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Inferred from direct assay Ref.15. Source: MGI

nucleus

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functiondouble-stranded DNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

transcription factor binding

Inferred from direct assay Ref.4Ref.28. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16666-1)

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.
Isoform 2 (identifier: Q16666-2)

Also known as: IFI 16B;

The sequence of this isoform differs from the canonical sequence as follows:
     444-499: Missing.
Note: Major isoform.
Isoform 3 (identifier: Q16666-3)

Also known as: IFI 16C;

The sequence of this isoform differs from the canonical sequence as follows:
     444-555: Missing.
Isoform 4 (identifier: Q16666-6)

The sequence of this isoform differs from the canonical sequence as follows:
     128-183: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 785785Gamma-interferon-inducible protein 16
PRO_0000153723

Regions

Domain1 – 8888DAPIN
Domain189 – 389201HIN-200 1
Domain562 – 761200HIN-200 2
Region192 – 393202Interaction with TP53 C-terminus
Region571 – 766196Interaction with TP53 core domain
Motif96 – 1005Nuclear localization signal
Motif128 – 1314Nuclear localization signal
Motif134 – 1363Nuclear localization signal
Motif140 – 1434Nuclear localization signal
Compositional bias1 – 150150Lys-rich
Compositional bias258 – 2614Poly-Ile

Amino acid modifications

Modified residue451N6-acetyllysine Ref.29
Modified residue951Phosphoserine
Modified residue991N6-acetyllysine Ref.29
Modified residue1061Phosphoserine Ref.16 Ref.17 Ref.18 Ref.22 Ref.29
Modified residue1281N6-acetyllysine Ref.29
Modified residue1531Phosphoserine Ref.17 Ref.18 Ref.22 Ref.29
Modified residue1681Phosphoserine Ref.29
Modified residue1741Phosphoserine Ref.29
Modified residue2141N6-acetyllysine Ref.19 Ref.29
Modified residue4441N6-acetyllysine Ref.29
Modified residue4511N6-acetyllysine Ref.29
Modified residue5611N6-acetyllysine; alternate Ref.29
Modified residue5751Phosphoserine Ref.22
Modified residue5981N6-acetyllysine Ref.29
Modified residue6141N6-acetyllysine Ref.29
Modified residue7801Phosphoserine Ref.29
Cross-link561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate Ref.20

Natural variations

Alternative sequence128 – 18356Missing in isoform 4.
VSP_044691
Alternative sequence444 – 555112Missing in isoform 3.
VSP_002675
Alternative sequence444 – 49956Missing in isoform 2.
VSP_002676
Natural variant1031D → H. Ref.1 Ref.2 Ref.3
Corresponds to variant rs1057018 [ dbSNP | Ensembl ].
VAR_029486
Natural variant1791S → T. Ref.4 Ref.5 Ref.8
Corresponds to variant rs866484 [ dbSNP | Ensembl ].
VAR_029487
Natural variant2021K → E.
Corresponds to variant rs11585341 [ dbSNP | Ensembl ].
VAR_029488
Natural variant4091R → S. Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs1057027 [ dbSNP | Ensembl ].
VAR_029489
Natural variant4131Y → N. Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs1057028 [ dbSNP | Ensembl ].
VAR_029490
Natural variant7231T → S.
Corresponds to variant rs6940 [ dbSNP | Ensembl ].
VAR_029491
Natural variant7791T → S.
Corresponds to variant rs6940 [ dbSNP | Ensembl ].
VAR_057582

Experimental info

Mutagenesis96 – 1005Missing: Predominant cytoplasmic localization. Ref.29
Mutagenesis991K → Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state). Ref.29
Mutagenesis991K → R: Minor effect on nuclear localization (mimics acetylated state). Ref.29
Mutagenesis128 – 1314Missing: Predominant nuclear, some cytoplasmic localization. Ref.29
Mutagenesis1281K → Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state). Ref.29
Mutagenesis1281K → R: Minor effect on nuclear localization (mimics acetylated state). Ref.29
Mutagenesis134 – 1363Missing: Mostly nuclear, minor cytoplasmic localization. Ref.29
Mutagenesis140 – 1434Missing: Mostly nuclear, minor cytoplasmic localization. Ref.29
Mutagenesis2181Y → A: Abolishes TP53-mediated transcriptional activation; when associated with A-267. Ref.30
Mutagenesis2221E → A: Abolishes TP53-mediated transcriptional activation; when associated with A-272. Ref.30
Mutagenesis2671Y → A: Abolishes TP53-mediated transcriptional activation; when associated with A-218. Ref.30
Mutagenesis2721E → A: Abolishes TP53-mediated transcriptional activation; when associated with A-222. Ref.30
Mutagenesis6271K → A: Impairs DNA binding; when associated with A-663; A-667; A-670; A-674; A-732; A-734 and A-759. Ref.31
Mutagenesis6631K → A: Impairs DNA binding; when associated with A-627; A-667; A-670; A-674; A-732; A-734 and A-759. Ref.31
Mutagenesis6671R → A: Impairs DNA binding; when associated with A-627; A-663; A-670; A-674; A-732; A-734 and A-759. Ref.31
Mutagenesis6701S → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-674; A-732; A-734 and A-759. Ref.31
Mutagenesis6741K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A-732; A-734 and A-759. Ref.31
Mutagenesis7321K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-734 and A-759. Ref.31
Mutagenesis7341K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-759. Ref.31
Mutagenesis7591K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-734. Ref.31
Sequence conflict4011S → G in BAG58950. Ref.5
Sequence conflict5441P → S in BAG58950. Ref.5
Sequence conflict6831K → R in AAM96005. Ref.4
Sequence conflict7231T → N in AAA58683. Ref.1
Sequence conflict7231T → N in AAB32519. Ref.2
Sequence conflict7371C → S in AAA58683. Ref.1
Sequence conflict7371C → S in AAB32519. Ref.2

Secondary structure

.............................................................................. 785
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (IFI 16A) [UniParc].

Last modified November 28, 2006. Version 3.
Checksum: 216CD103D8F5206A

FASTA78588,256
        10         20         30         40         50         60 
MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD LMEEKFRGDA 

        70         80         90        100        110        120 
GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK EVDATSPAPS TSSTVKTEGA 

       130        140        150        160        170        180 
EATPGAQKRK KSTKEKAGPK GSKVSEEQTQ PPSPAGAGMS TAMGRSPSPK TSLSAPPNSS 

       190        200        210        220        230        240 
STENPKTVAK CQVTPRRNVL QKRPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF 

       250        260        270        280        290        300 
HVKVLNTSLK EKFNGKKIII ISDYLEYDSL LEVNEESTVS EAGPNQTFEV PNKIINRAKE 

       310        320        330        340        350        360 
TLKIDILHKQ ASGNIVYGVF MLHKKTVNQK TTIYEIQDDR GKMDVVGTGQ CHNIPCEEGD 

       370        380        390        400        410        420 
KLQLFCFRLR KKNQMSKLIS EMHSFIQIKK KTNPRNNDPK SMKLPQEQRQ LPYPSEASTT 

       430        440        450        460        470        480 
FPESHLRTPQ MPPTTPSSSF FTKKSEDTIS KMNDFMRMQI LKEGSHFPGP FMTSIGPAES 

       490        500        510        520        530        540 
HPHTPQMPPS TPSSSFLTTK SEDTISKMND FMRMQILKEG SHFPGPFMTS IGPAESHPHT 

       550        560        570        580        590        600 
PQMPPSTPSS SFLTTLKPRL KTEPEEVSIE DSAQSDLKEV MVLNATESFV YEPKEQKKMF 

       610        620        630        640        650        660 
HATVATENEV FRVKVFNIDL KEKFTPKKII AIANYVCRNG FLEVYPFTLV ADVNADRNME 

       670        680        690        700        710        720 
IPKGLIRSAS VTPKINQLCS QTKGSFVNGV FEVHKKNVRG EFTYYEIQDN TGKMEVVVHG 

       730        740        750        760        770        780 
RLTTINCEEG DKLKLTCFEL APKSGNTGEL RSVIHSHIKV IKTRKNKKDI LNPDSSMETS 


PDFFF 

« Hide

Isoform 2 (IFI 16B) [UniParc].

Checksum: 27C820A058DE6A92
Show »

FASTA72982,096
Isoform 3 (IFI 16C) [UniParc].

Checksum: 4D80A41BD9AA13A5
Show »

FASTA67375,936
Isoform 4 [UniParc].

Checksum: FEB03DF1E8B09D0A
Show »

FASTA72982,588

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"IFI16 is an innate immune sensor for intracellular DNA."
Unterholzner L., Keating S.E., Baran M., Horan K.A., Jensen S.B., Sharma S., Sirois C.M., Jin T., Latz E., Xiao T.S., Fitzgerald K.A., Paludan S.R., Bowie A.G.
Nat. Immunol. 11:997-1004(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M63838 mRNA. Translation: AAA58683.1.
S75433 expand/collapse EMBL AC list , 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.
PIRI54501.
RefSeqNP_001193496.1. NM_001206567.1.
NP_005522.2. NM_005531.2.
UniGeneHs.380250.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ16666.
SMRQ16666. Positions 1-93, 198-389, 575-766.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109654. 10 interactions.
DIPDIP-42868N.
IntActQ16666. 12 interactions.
MINTMINT-1781545.

PTM databases

PhosphoSiteQ16666.

Polymorphism databases

DMDM118572657.

Proteomic databases

PaxDbQ16666.
PRIDEQ16666.

Protocols and materials databases

DNASU3428.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295809; 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]
GeneID3428.
KEGGhsa:3428.
UCSCuc001ftg.3. human. [Q16666-2]

Organism-specific databases

CTD3428.
GeneCardsGC01P158969.
H-InvDBHIX0001194.
HGNCHGNC:5395. IFI16.
HPACAB016293.
HPA002134.
MIM147586. gene.
neXtProtNX_Q16666.
PharmGKBPA29642.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81691.
HOVERGENHBG006122.
InParanoidQ16666.
OMASIGPAES.
OrthoDBEOG7ZD1V8.
PhylomeDBQ16666.
TreeFamTF337385.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ16666.
BgeeQ16666.
GenevestigatorQ16666.

Family and domain databases

Gene3D2.40.50.140. 4 hits.
InterProIPR004020. DAPIN.
IPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamPF02760. HIN. 2 hits.
PF02758. PYRIN. 1 hit.
[Graphical view]
PROSITEPS50824. DAPIN. 1 hit.
PS50834. HIN_200. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIFI16. human.
EvolutionaryTraceQ16666.
GeneWikiIFI16.
GenomeRNAi3428.
NextBio13516.
PROQ16666.
SOURCESearch...

Entry information

Entry nameIF16_HUMAN
AccessionPrimary (citable) accession number: Q16666
Secondary accession number(s): B4DJT8 expand/collapse secondary AC list , H3BLV7, Q59GX0, Q5T3W7, Q5T3W8, Q5T3X0, Q5T3X1, Q5T3X2, Q8N9E5, Q8NEQ7, Q96AJ5, Q9UH78
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2006
Last modified: April 16, 2014
This is version 149 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM