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Protein

Gamma-interferon-inducible protein 16

Gene

IFI16

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • core promoter binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • activation of cysteine-type endopeptidase activity Source: UniProtKB
  • activation of innate immune response Source: UniProtKB
  • autophagy Source: UniProtKB-KW
  • cell proliferation Source: UniProtKB
  • cellular response to glucose starvation Source: UniProtKB
  • cellular response to ionizing radiation Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • hemopoiesis Source: UniProtKB
  • inflammatory response Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  • monocyte differentiation Source: UniProtKB
  • myeloid cell differentiation Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity Source: UniProtKB
  • negative regulation of DNA binding Source: UniProtKB
  • negative regulation of innate immune response Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
  • positive regulation of cytokine production Source: UniProtKB
  • positive regulation of interleukin-1 beta production Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of type I interferon production Source: Reactome
  • regulation of autophagy Source: UniProtKB
  • regulation of gene expression, epigenetic Source: UniProtKB
  • 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

BioCyciZFISH:ENSG00000163565-MONOMER.
ReactomeiR-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
SIGNORiQ16666.

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
Proteomesi
  • UP000005640 Componenti: 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

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • nuclear speck Source: MGI
  • nucleolus Source: HPA
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi96 – 100Missing : Predominant cytoplasmic localization. 1 Publication5
Mutagenesisi99K → Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state). 1 Publication1
Mutagenesisi99K → R: Minor effect on nuclear localization (mimics acetylated state). 1 Publication1
Mutagenesisi128 – 131Missing : Predominant nuclear, some cytoplasmic localization. 1 Publication4
Mutagenesisi128K → Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state). 1 Publication1
Mutagenesisi128K → R: Minor effect on nuclear localization (mimics acetylated state). 1 Publication1
Mutagenesisi134 – 136Missing : Mostly nuclear, minor cytoplasmic localization. 1 Publication3
Mutagenesisi140 – 143Missing : Mostly nuclear, minor cytoplasmic localization. 1 Publication4
Mutagenesisi218Y → A: Abolishes TP53-mediated transcriptional activation; when associated with A-267. 1 Publication1
Mutagenesisi222E → A: Abolishes TP53-mediated transcriptional activation; when associated with A-272. 1 Publication1
Mutagenesisi267Y → A: Abolishes TP53-mediated transcriptional activation; when associated with A-218. 1 Publication1
Mutagenesisi272E → A: Abolishes TP53-mediated transcriptional activation; when associated with A-222. 1 Publication1
Mutagenesisi627K → A: Impairs DNA binding; when associated with A-663; A-667; A-670; A-674; A-732; A-734 and A-759. 1 Publication1
Mutagenesisi663K → A: Impairs DNA binding; when associated with A-627; A-667; A-670; A-674; A-732; A-734 and A-759. 1 Publication1
Mutagenesisi667R → A: Impairs DNA binding; when associated with A-627; A-663; A-670; A-674; A-732; A-734 and A-759. 1 Publication1
Mutagenesisi670S → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-674; A-732; A-734 and A-759. 1 Publication1
Mutagenesisi674K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A-732; A-734 and A-759. 1 Publication1
Mutagenesisi732K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-734 and A-759. 1 Publication1
Mutagenesisi734K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-759. 1 Publication1
Mutagenesisi759K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-734. 1 Publication1

Organism-specific databases

DisGeNETi3428.
OpenTargetsiENSG00000163565.
PharmGKBiPA29642.

Polymorphism and mutation databases

BioMutaiIFI16.
DMDMi118572657.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001537231 – 785Gamma-interferon-inducible protein 16Add BLAST785

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei45N6-acetyllysine1 Publication1
Modified residuei95Phosphoserine1 Publication1
Modified residuei99N6-acetyllysine1 Publication1
Modified residuei106PhosphoserineCombined sources1 Publication1
Cross-linki116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei128N6-acetyllysine1 Publication1
Modified residuei153PhosphoserineCombined sources1 Publication1
Modified residuei168Phosphoserine1 Publication1
Modified residuei174Phosphoserine1 Publication1
Modified residuei214N6-acetyllysineCombined sources1 Publication1
Modified residuei444N6-acetyllysine1 Publication1
Modified residuei451N6-acetyllysine1 Publication1
Modified residuei561N6-acetyllysine; alternate1 Publication1
Cross-linki561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei575PhosphoserineCombined sources1
Modified residuei598N6-acetyllysine1 Publication1
Modified residuei614N6-acetyllysine1 Publication1
Cross-linki683Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei780Phosphoserine1 Publication1

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.1 Publication
Phosphorylated on Ser and Thr.2 Publications
Isoform 3 seems to show a minor degree of complex carbohydrate addition.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ16666.
MaxQBiQ16666.
PaxDbiQ16666.
PeptideAtlasiQ16666.
PRIDEiQ16666.

PTM databases

iPTMnetiQ16666.
PhosphoSitePlusiQ16666.
SwissPalmiQ16666.

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

BgeeiENSG00000163565.
ExpressionAtlasiQ16666. baseline and differential.
GenevisibleiQ16666. HS.

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

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109654. 390 interactors.
DIPiDIP-42868N.
IntActiQ16666. 172 interactors.
MINTiMINT-1781545.
STRINGi9606.ENSP00000357113.

Structurei

Secondary structure

1785
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi205 – 212Combined sources8
Beta strandi216 – 219Combined sources4
Beta strandi225 – 234Combined sources10
Beta strandi239 – 244Combined sources6
Helixi247 – 253Combined sources7
Beta strandi254 – 257Combined sources4
Beta strandi259 – 267Combined sources9
Beta strandi270 – 273Combined sources4
Beta strandi278 – 281Combined sources4
Helixi284 – 286Combined sources3
Helixi292 – 298Combined sources7
Helixi304 – 307Combined sources4
Beta strandi315 – 327Combined sources13
Beta strandi329 – 338Combined sources10
Beta strandi341 – 348Combined sources8
Helixi349 – 351Combined sources3
Beta strandi361 – 372Combined sources12
Beta strandi375 – 379Combined sources5
Beta strandi385 – 388Combined sources4
Beta strandi578 – 585Combined sources8
Beta strandi589 – 592Combined sources4
Turni593 – 596Combined sources4
Beta strandi597 – 605Combined sources9
Beta strandi610 – 615Combined sources6
Helixi618 – 620Combined sources3
Turni621 – 624Combined sources4
Beta strandi629 – 634Combined sources6
Beta strandi636 – 638Combined sources3
Beta strandi641 – 644Combined sources4
Beta strandi648 – 652Combined sources5
Beta strandi655 – 657Combined sources3
Helixi663 – 670Combined sources8
Helixi675 – 679Combined sources5
Beta strandi685 – 699Combined sources15
Beta strandi702 – 709Combined sources8
Beta strandi712 – 718Combined sources7
Helixi720 – 724Combined sources5
Beta strandi732 – 741Combined sources10
Turni744 – 747Combined sources4
Beta strandi749 – 761Combined sources13
Turni764 – 766Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QGUX-ray2.54A/B192-393[»]
ProteinModelPortaliQ16666.
SMRiQ16666.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16666.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 88PyrinPROSITE-ProRule annotationAdd BLAST88
Domaini189 – 389HIN-200 1PROSITE-ProRule annotationAdd BLAST201
Domaini562 – 761HIN-200 2PROSITE-ProRule annotationAdd BLAST200

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni192 – 393Interaction with TP53 C-terminusAdd BLAST202
Regioni571 – 766Interaction with TP53 core domainAdd BLAST196

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi96 – 100Nuclear localization signal5
Motifi128 – 131Nuclear localization signal4
Motifi134 – 136Nuclear localization signal3
Motifi140 – 143Nuclear localization signal4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 150Lys-richAdd BLAST150
Compositional biasi258 – 261Poly-Ile4

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410J5NP. Eukaryota.
ENOG410Y78B. LUCA.
GeneTreeiENSGT00390000013296.
HOGENOMiHOG000033871.
HOVERGENiHBG006122.
InParanoidiQ16666.
OMAiGPFMTSI.
OrthoDBiEOG091G02W0.
PhylomeDBiQ16666.
TreeFamiTF337385.

Family and domain databases

InterProiIPR004020. DAPIN.
IPR004021. HIN200/IF120x.
[Graphical view]
PfamiPF02760. HIN. 2 hits.
PF02758. PYRIN. 1 hit.
[Graphical view]
SMARTiSM01289. 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. AlignAdd to basket

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti401S → G in BAG58950 (PubMed:14702039).Curated1
Sequence conflicti544P → S in BAG58950 (PubMed:14702039).Curated1
Sequence conflicti683K → R in AAM96005 (PubMed:12894224).Curated1
Sequence conflicti723T → N in AAA58683 (PubMed:1526658).Curated1
Sequence conflicti723T → N in AAB32519 (PubMed:7959953).Curated1
Sequence conflicti737C → S in AAA58683 (PubMed:1526658).Curated1
Sequence conflicti737C → S in AAB32519 (PubMed:7959953).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029486103D → H.3 PublicationsCorresponds to variant rs1057018dbSNPEnsembl.1
Natural variantiVAR_029487179S → T.3 PublicationsCorresponds to variant rs866484dbSNPEnsembl.1
Natural variantiVAR_029488202K → E.Corresponds to variant rs11585341dbSNPEnsembl.1
Natural variantiVAR_029489409R → S.4 PublicationsCorresponds to variant rs1057027dbSNPEnsembl.1
Natural variantiVAR_029490413Y → N.4 PublicationsCorresponds to variant rs1057028dbSNPEnsembl.1
Natural variantiVAR_029491723T → S.Corresponds to variant rs6940dbSNPEnsembl.1
Natural variantiVAR_057582779T → S.Corresponds to variant rs6940dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044691128 – 183Missing in isoform 4. 1 PublicationAdd BLAST56
Alternative sequenceiVSP_002675444 – 555Missing in isoform 3. CuratedAdd BLAST112
Alternative sequenceiVSP_002676444 – 499Missing in isoform 2. 5 PublicationsAdd BLAST56

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.4. human. [Q16666-1]

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QGUX-ray2.54A/B192-393[»]
ProteinModelPortaliQ16666.
SMRiQ16666.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109654. 390 interactors.
DIPiDIP-42868N.
IntActiQ16666. 172 interactors.
MINTiMINT-1781545.
STRINGi9606.ENSP00000357113.

PTM databases

iPTMnetiQ16666.
PhosphoSitePlusiQ16666.
SwissPalmiQ16666.

Polymorphism and mutation databases

BioMutaiIFI16.
DMDMi118572657.

Proteomic databases

EPDiQ16666.
MaxQBiQ16666.
PaxDbiQ16666.
PeptideAtlasiQ16666.
PRIDEiQ16666.

Protocols and materials databases

DNASUi3428.
Structural Biology KnowledgebaseSearch...

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.4. human. [Q16666-1]

Organism-specific databases

CTDi3428.
DisGeNETi3428.
GeneCardsiIFI16.
H-InvDBHIX0001194.
HGNCiHGNC:5395. IFI16.
HPAiCAB016293.
HPA002134.
MIMi147586. gene.
neXtProtiNX_Q16666.
OpenTargetsiENSG00000163565.
PharmGKBiPA29642.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J5NP. Eukaryota.
ENOG410Y78B. LUCA.
GeneTreeiENSGT00390000013296.
HOGENOMiHOG000033871.
HOVERGENiHBG006122.
InParanoidiQ16666.
OMAiGPFMTSI.
OrthoDBiEOG091G02W0.
PhylomeDBiQ16666.
TreeFamiTF337385.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000163565-MONOMER.
ReactomeiR-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3270619. IRF3-mediated induction of type I IFN.
SIGNORiQ16666.

Miscellaneous databases

ChiTaRSiIFI16. human.
EvolutionaryTraceiQ16666.
GeneWikiiIFI16.
GenomeRNAii3428.
PROiQ16666.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163565.
ExpressionAtlasiQ16666. baseline and differential.
GenevisibleiQ16666. HS.

Family and domain databases

InterProiIPR004020. DAPIN.
IPR004021. HIN200/IF120x.
[Graphical view]
PfamiPF02760. HIN. 2 hits.
PF02758. PYRIN. 1 hit.
[Graphical view]
SMARTiSM01289. PYRIN. 1 hit.
[Graphical view]
PROSITEiPS50824. DAPIN. 1 hit.
PS50834. HIN_200. 2 hits.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 178 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.