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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
  • identical protein binding Source: IntAct
  • 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

ReactomeiR-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3270619. 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
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)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.

Polymorphism and mutation databases

BioMutaiIFI16.
DMDMi118572657.

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 – 1061PhosphoserineCombined sources1 Publication
Cross-linki116 – 116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei128 – 1281N6-acetyllysine1 Publication
Modified residuei153 – 1531PhosphoserineCombined sources1 Publication
Modified residuei168 – 1681Phosphoserine1 Publication
Modified residuei174 – 1741Phosphoserine1 Publication
Modified residuei214 – 2141N6-acetyllysineCombined sources1 Publication
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 SUMO1); alternateCombined sources
Cross-linki561 – 561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei575 – 5751PhosphoserineCombined sources
Modified residuei598 – 5981N6-acetyllysine1 Publication
Modified residuei614 – 6141N6-acetyllysine1 Publication
Cross-linki683 – 683Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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.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.
PhosphoSiteiQ16666.
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

  • identical protein binding Source: IntAct
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109654. 388 interactions.
DIPiDIP-42868N.
IntActiQ16666. 172 interactions.
MINTiMINT-1781545.
STRINGi9606.ENSP00000357113.

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[»]
4QGUX-ray2.54A/B192-393[»]
ProteinModelPortaliQ16666.
SMRiQ16666. Positions 1-93, 198-389, 575-766.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16666.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 8888PyrinPROSITE-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 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

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]
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)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.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
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. Positions 1-93, 198-389, 575-766.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109654. 388 interactions.
DIPiDIP-42868N.
IntActiQ16666. 172 interactions.
MINTiMINT-1781545.
STRINGi9606.ENSP00000357113.

PTM databases

iPTMnetiQ16666.
PhosphoSiteiQ16666.
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.
GeneCardsiIFI16.
H-InvDBHIX0001194.
HGNCiHGNC:5395. IFI16.
HPAiCAB016293.
HPA002134.
MIMi147586. gene.
neXtProtiNX_Q16666.
PharmGKBiPA29642.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-HSA-1834941. STING mediated induction of host immune responses.
R-HSA-3270619. IRF3-mediated induction of type I IFN.

Miscellaneous databases

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

Gene expression databases

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

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]
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: September 7, 2016
This is version 176 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.