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Q16666

- IF16_HUMAN

UniProt

Q16666 - IF16_HUMAN

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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

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. core promoter binding Source: UniProtKB
  2. double-stranded DNA binding Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. poly(A) RNA binding Source: UniProtKB
  5. 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. regulation of gene expression, epigenetic Source: UniProtKB
  27. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi96 – 1005Missing: Predominant cytoplasmic localization. 1 Publication
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. 1 Publication
Mutagenesisi140 – 1434Missing: Mostly nuclear, minor cytoplasmic localization. 1 Publication
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 – 1061Phosphoserine5 Publications
Modified residuei128 – 1281N6-acetyllysine1 Publication
Modified residuei153 – 1531Phosphoserine4 Publications
Modified residuei168 – 1681Phosphoserine1 Publication
Modified residuei174 – 1741Phosphoserine1 Publication
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 – 5751Phosphoserine1 Publication
Modified residuei598 – 5981N6-acetyllysine1 Publication
Modified residuei614 – 6141N6-acetyllysine1 Publication
Modified residuei780 – 7801Phosphoserine1 Publication

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

BgeeiQ16666.
ExpressionAtlasiQ16666. baseline and differential.
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. 11 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 – 2128Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi225 – 23410Combined sources
Beta strandi239 – 2446Combined sources
Helixi247 – 2537Combined sources
Beta strandi254 – 2574Combined sources
Beta strandi259 – 2679Combined sources
Beta strandi270 – 2734Combined sources
Beta strandi278 – 2814Combined sources
Helixi284 – 2863Combined sources
Helixi292 – 2987Combined sources
Helixi304 – 3074Combined sources
Beta strandi315 – 32713Combined sources
Beta strandi329 – 33810Combined sources
Beta strandi341 – 3488Combined sources
Helixi349 – 3513Combined sources
Beta strandi361 – 37212Combined sources
Beta strandi375 – 3795Combined sources
Beta strandi385 – 3884Combined sources
Beta strandi578 – 5858Combined sources
Beta strandi589 – 5924Combined sources
Turni593 – 5964Combined sources
Beta strandi597 – 6059Combined sources
Beta strandi610 – 6156Combined sources
Helixi618 – 6203Combined sources
Turni621 – 6244Combined sources
Beta strandi629 – 6346Combined sources
Beta strandi636 – 6383Combined sources
Beta strandi641 – 6444Combined sources
Beta strandi648 – 6525Combined sources
Beta strandi655 – 6573Combined sources
Helixi663 – 6708Combined sources
Helixi675 – 6795Combined sources
Beta strandi685 – 69915Combined sources
Beta strandi702 – 7098Combined sources
Beta strandi712 – 7187Combined sources
Helixi720 – 7245Combined sources
Beta strandi732 – 74110Combined sources
Turni744 – 7474Combined sources
Beta strandi749 – 76113Combined sources
Turni764 – 7663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 576-761.
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.
GeneTreeiENSGT00390000013296.
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

        10         20         30         40         50
MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD
60 70 80 90 100
LMEEKFRGDA GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK
110 120 130 140 150
EVDATSPAPS TSSTVKTEGA EATPGAQKRK KSTKEKAGPK GSKVSEEQTQ
160 170 180 190 200
PPSPAGAGMS TAMGRSPSPK TSLSAPPNSS STENPKTVAK CQVTPRRNVL
210 220 230 240 250
QKRPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF HVKVLNTSLK
260 270 280 290 300
EKFNGKKIII ISDYLEYDSL LEVNEESTVS EAGPNQTFEV PNKIINRAKE
310 320 330 340 350
TLKIDILHKQ ASGNIVYGVF MLHKKTVNQK TTIYEIQDDR GKMDVVGTGQ
360 370 380 390 400
CHNIPCEEGD KLQLFCFRLR KKNQMSKLIS EMHSFIQIKK KTNPRNNDPK
410 420 430 440 450
SMKLPQEQRQ LPYPSEASTT FPESHLRTPQ MPPTTPSSSF FTKKSEDTIS
460 470 480 490 500
KMNDFMRMQI LKEGSHFPGP FMTSIGPAES HPHTPQMPPS TPSSSFLTTK
510 520 530 540 550
SEDTISKMND FMRMQILKEG SHFPGPFMTS IGPAESHPHT PQMPPSTPSS
560 570 580 590 600
SFLTTLKPRL KTEPEEVSIE DSAQSDLKEV MVLNATESFV YEPKEQKKMF
610 620 630 640 650
HATVATENEV FRVKVFNIDL KEKFTPKKII AIANYVCRNG FLEVYPFTLV
660 670 680 690 700
ADVNADRNME IPKGLIRSAS VTPKINQLCS QTKGSFVNGV FEVHKKNVRG
710 720 730 740 750
EFTYYEIQDN TGKMEVVVHG RLTTINCEEG DKLKLTCFEL APKSGNTGEL
760 770 780
RSVIHSHIKV IKTRKNKKDI LNPDSSMETS PDFFF
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.Curated
The sequence AAF20997.1 differs from that shown. Reason: Frameshift at position 776. Curated
The sequence BAC04462.1 differs from that shown. Reason: Probable cloning artifact.Curated
The sequence BAD92226.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAG58950.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 576-761.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109654. 11 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 ]
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.
GeneTreei ENSGT00390000013296.
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

Bgeei Q16666.
ExpressionAtlasi Q16666. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 156 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