Q16666 (IF16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-interferon-inducible protein 16
Short name=Ifi-16

Alternative name(s):
Interferon-inducible myeloid differentiation transcriptional activator

Gene names

Name:	IFI16
Synonyms:	IFNGIP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	785 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Ref.4 Ref.13 Ref.14 Ref.15 Ref.21 Ref.24 Ref.25 Ref.26 Ref.28
Subunit structure	Forms homooligomers; isoform 2 can self-associate or associate with isoform 1 or isoform 3. Interacts with TMEM173, AIM2, PYCARD and CASP1. Interacts with BRCA1, TP53, E2F1, RB1 and SP1. Ref.9 Ref.14 Ref.15 Ref.21 Ref.24 Ref.26
Subcellular location	Nucleus. Cytoplasm. Note: Cellular distribution is dependent on the acetylation status of the multipartite nuclear localization signal (NLS); NLS acetylation promotes cytoplasmic localization. Ref.10 Ref.26 Ref.29
Tissue specificity	Expressed in peripheral blood leukocytes, fibroblasts and lymphoid cells. Present in myeloid precursors (CD34+) and throughout monocyte development, but its expression is down-regulated in erythroid and polymorphonuclear precursor cells. Present in prostate, ovary and breast (at protein level). Ref.4
Induction	Strongly induced by IFNG/IFN-gamma and, to a lesser extent, by alpha interferon. In HL-60 cells, maximum induction by IFNG/IFN-gamma occurs within 12 hours whereas, for IFN-alpha, only 10-fold induction was observed after 36 hours. Induced in vitro by dimethylsulfoxide, retinoic acid and 1,25 dihydroxyvitamin D3. Induced in monocytes by IFN-alpha and viral dsDNA. Induced by glucose restriction. Ref.4 Ref.10 Ref.11 Ref.12 Ref.21 Ref.25
Domain	The HIN-20 domains mediates dsDNA binding via electrostatic interactions (Ref.31).
Post-translational modification	Lysine acetylation in the multipartite nuclear localization signal (NLS) regulates the subcellular location. In vitro can be acetylated by p300/EP300 coupled to cytoplasmic localization. Phosphorylated on Ser and Thr. Ref.9 Ref.29 Isoform 3 seems to show a minor degree of complex carbohydrate addition.
Sequence similarities	Belongs to the HIN-200 family. Contains 1 DAPIN domain. Contains 2 HIN-200 domains.
Sequence caution	The sequence AAF20997.1 differs from that shown. Reason: Frameshift at position 776. The sequence AAF20997.1 differs from that shown. Reason: Intron retention. The sequence BAC04462.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAD92226.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAG58950.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Apoptosis Autophagy Immunity Inflammatory response Innate immunity Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of cysteine-type endopeptidase activity Inferred from mutant phenotype Ref.24. Source: UniProtKB activation of innate immune response Inferred from direct assay Ref.24. Source: UniProtKB autophagy Inferred from electronic annotation. Source: UniProtKB-KW cell proliferation Non-traceable author statement Ref.12. Source: UniProtKB cellular response to glucose starvation Inferred from direct assay Ref.25. Source: UniProtKB cellular response to ionizing radiation Inferred from direct assay Ref.15. Source: UniProtKB defense response to virus Inferred from mutant phenotype Ref.24. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Inferred from electronic annotation. Source: UniProtKB-KW intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Inferred from direct assay Ref.15. Source: MGI monocyte differentiation Inferred from direct assay Ref.12. Source: UniProtKB negative regulation of DNA binding Inferred from direct assay Ref.28. Source: UniProtKB negative regulation of cysteine-type endopeptidase activity Inferred from direct assay Ref.26. Source: UniProtKB negative regulation of innate immune response Inferred from direct assay Ref.26. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.4. Source: UniProtKB negative regulation of viral genome replication Inferred from direct assay Ref.28. Source: UniProtKB positive regulation of interleukin-1 beta production Inferred from direct assay Ref.24. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.14. Source: UniProtKB regulation of autophagy Inferred from expression pattern Ref.25. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nuclear speck Inferred from direct assay PubMed 19158679. Source: MGI nucleolus Inferred from direct assay. Source: HPA
Molecular_function	double-stranded DNA binding Inferred from direct assay Ref.10. Source: UniProtKB transcription factor binding Inferred from direct assay Ref.4Ref.28. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	9	EBI-2867186,EBI-349905
TMEM173	Q86WV6	2	EBI-2867186,EBI-2800345
TP53	P04637	3	EBI-6273540,EBI-366083

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16666-1)

Also known as: IFI 16A;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q16666-2)

Also known as: IFI 16B;

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

Note: Major isoform.

Isoform 3 (identifier: Q16666-3)

Also known as: IFI 16C;

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

Isoform 4 (identifier: Q16666-6)

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

Note: No experimental confirmation available.

Isoform 5 (identifier: Q16666-7)

The sequence of this isoform differs from the canonical sequence as follows:
     249-619: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 785

785

Gamma-interferon-inducible protein 16

PRO_0000153723

Regions

Domain

1 – 88

88

DAPIN

Domain

189 – 389

201

HIN-200 1

Domain

562 – 761

200

HIN-200 2

Region

192 – 393

202

Interaction with TP53 C-terminus

Region

571 – 766

196

Interaction with TP53 core domain

Motif

96 – 100

5

Nuclear localization signal

Motif

128 – 131

4

Nuclear localization signal

Motif

134 – 136

3

Nuclear localization signal

Motif

140 – 143

4

Nuclear localization signal

Compositional bias

1 – 150

150

Lys-rich

Compositional bias

258 – 261

4

Poly-Ile

Amino acid modifications

Modified residue

95

1

Phosphoserine

Modified residue

99

1

N6-acetyllysine Ref.29

Modified residue

106

1

Phosphoserine Ref.16 Ref.17 Ref.18 Ref.22 Ref.29

Modified residue

153

1

Phosphoserine Ref.17 Ref.18 Ref.22 Ref.29

Modified residue

174

1

Phosphoserine Ref.29

Modified residue

214

1

N6-acetyllysine Ref.19 Ref.29

Modified residue

444

1

N6-acetyllysine Ref.29

Modified residue

451

1

N6-acetyllysine Ref.29

Modified residue

561

1

N6-acetyllysine; alternate Ref.29

Modified residue

575

1

Phosphoserine Ref.22

Modified residue

598

1

N6-acetyllysine Ref.29

Modified residue

614

1

N6-acetyllysine Ref.29

Modified residue

780

1

Phosphoserine Ref.29

Cross-link

561

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1); alternate Ref.20

Natural variations

Alternative sequence

128 – 183

56

Missing in isoform 4.

VSP_044691

Alternative sequence

249 – 619

371

Missing in isoform 5.

VSP_044692

Alternative sequence

444 – 555

112

Missing in isoform 3.

VSP_002675

Alternative sequence

444 – 499

56

Missing in isoform 2.

VSP_002676

Natural variant

103

1

D → H. Ref.1 Ref.2 Ref.3
Corresponds to variant rs1057018 [ dbSNP | Ensembl ].

VAR_029486

Natural variant

179

1

S → T. Ref.4 Ref.5 Ref.8
Corresponds to variant rs866484 [ dbSNP | Ensembl ].

VAR_029487

Natural variant

202

1

K → E.
Corresponds to variant rs11585341 [ dbSNP | Ensembl ].

VAR_029488

Natural variant

409

1

R → S. Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs1057027 [ dbSNP | Ensembl ].

VAR_029489

Natural variant

413

1

Y → N. Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs1057028 [ dbSNP | Ensembl ].

VAR_029490

Natural variant

723

1

T → S.
Corresponds to variant rs6940 [ dbSNP | Ensembl ].

VAR_029491

Natural variant

779

1

T → S.
Corresponds to variant rs6940 [ dbSNP | Ensembl ].

VAR_057582

Experimental info

Mutagenesis

96 – 100

5

Missing: Predominant cytoplasmic localization. Ref.29

Mutagenesis

99

1

K → Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state). Ref.29

Mutagenesis

99

1

K → R: Minor effect on nuclear localization (mimics acetylated state). Ref.29

Mutagenesis

128 – 131

4

Missing: Predominant nuclear, some cytoplasmic localization. Ref.29

Mutagenesis

128

1

K → Q: Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state). Ref.29

Mutagenesis

128

1

K → R: Minor effect on nuclear localization (mimics acetylated state). Ref.29

Mutagenesis

134 – 136

3

Missing: Mostly nuclear, minor cytoplasmic localization. Ref.29

Mutagenesis

140 – 143

4

Missing: Mostly nuclear, minor cytoplasmic localization. Ref.29

Mutagenesis

218

1

Y → A: Abolishes TP53-mediated transcriptional activation; when associated with A-267. Ref.30

Mutagenesis

222

1

E → A: Abolishes TP53-mediated transcriptional activation; when associated with A-272. Ref.30

Mutagenesis

267

1

Y → A: Abolishes TP53-mediated transcriptional activation; when associated with A-218. Ref.30

Mutagenesis

272

1

E → A: Abolishes TP53-mediated transcriptional activation; when associated with A-222. Ref.30

Mutagenesis

627

1

K → A: Impairs DNA binding; when associated with A-663; A-667; A-670; A-674; A-732; A-734 and A-759. Ref.31

Mutagenesis

663

1

K → A: Impairs DNA binding; when associated with A-627; A-667; A-670; A-674; A-732; A-734 and A-759. Ref.31

Mutagenesis

667

1

R → A: Impairs DNA binding; when associated with A-627; A-663; A-670; A-674; A-732; A-734 and A-759. Ref.31

Mutagenesis

670

1

S → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-674; A-732; A-734 and A-759. Ref.31

Mutagenesis

674

1

K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A-732; A-734 and A-759. Ref.31

Mutagenesis

732

1

K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-734 and A-759. Ref.31

Mutagenesis

734

1

K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-759. Ref.31

Mutagenesis

759

1

K → A: Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-734. Ref.31

Sequence conflict

401

1

S → G in BAG58950. Ref.5

Sequence conflict

544

1

P → S in BAG58950. Ref.5

Sequence conflict

683

1

K → R in AAM96005. Ref.4

Sequence conflict

723

1

T → N in AAA58683. Ref.1

Sequence conflict

723

1

T → N in AAB32519. Ref.2

Sequence conflict

737

1

C → S in AAA58683. Ref.1

Sequence conflict

737

1

C → S in AAB32519. Ref.2

Secondary structure

1

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785

Helix Strand Turn

Details...

Beta strand

205 – 212

8

Beta strand

216 – 219

4

Beta strand

225 – 234

10

Beta strand

239 – 244

6

Helix

247 – 253

7

Beta strand

254 – 257

4

Beta strand

259 – 267

9

Beta strand

270 – 273

4

Beta strand

278 – 281

4

Helix

284 – 286

3

Helix

292 – 298

7

Helix

304 – 307

4

Beta strand

315 – 327

13

Beta strand

329 – 338

10

Beta strand

341 – 348

8

Helix

349 – 351

3

Beta strand

361 – 372

12

Beta strand

375 – 379

5

Beta strand

385 – 388

4

Beta strand

578 – 585

8

Beta strand

589 – 592

4

Turn

593 – 596

4

Beta strand

597 – 605

9

Beta strand

610 – 615

6

Helix

618 – 620

3

Turn

621 – 624

4

Beta strand

629 – 634

6

Beta strand

636 – 638

3

Beta strand

641 – 644

4

Beta strand

648 – 652

5

Beta strand

655 – 657

3

Helix

663 – 670

8

Helix

675 – 679

5

Beta strand

685 – 699

15

Beta strand

702 – 709

8

Beta strand

712 – 718

7

Helix

720 – 724

5

Beta strand

732 – 741

10

Turn

744 – 747

4

Beta strand

749 – 761

13

Turn

764 – 766

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (IFI 16A) [UniParc]. Last modified November 28, 2006. Version 3. Checksum: 216CD103D8F5206A	FASTA	785	88,256
	10 20 30 40 50 60 MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD LMEEKFRGDA 70 80 90 100 110 120 GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK EVDATSPAPS TSSTVKTEGA 130 140 150 160 170 180 EATPGAQKRK KSTKEKAGPK GSKVSEEQTQ PPSPAGAGMS TAMGRSPSPK TSLSAPPNSS 190 200 210 220 230 240 STENPKTVAK CQVTPRRNVL QKRPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF 250 260 270 280 290 300 HVKVLNTSLK EKFNGKKIII ISDYLEYDSL LEVNEESTVS EAGPNQTFEV PNKIINRAKE 310 320 330 340 350 360 TLKIDILHKQ ASGNIVYGVF MLHKKTVNQK TTIYEIQDDR GKMDVVGTGQ CHNIPCEEGD 370 380 390 400 410 420 KLQLFCFRLR KKNQMSKLIS EMHSFIQIKK KTNPRNNDPK SMKLPQEQRQ LPYPSEASTT 430 440 450 460 470 480 FPESHLRTPQ MPPTTPSSSF FTKKSEDTIS KMNDFMRMQI LKEGSHFPGP FMTSIGPAES 490 500 510 520 530 540 HPHTPQMPPS TPSSSFLTTK SEDTISKMND FMRMQILKEG SHFPGPFMTS IGPAESHPHT 550 560 570 580 590 600 PQMPPSTPSS SFLTTLKPRL KTEPEEVSIE DSAQSDLKEV MVLNATESFV YEPKEQKKMF 610 620 630 640 650 660 HATVATENEV FRVKVFNIDL KEKFTPKKII AIANYVCRNG FLEVYPFTLV ADVNADRNME 670 680 690 700 710 720 IPKGLIRSAS VTPKINQLCS QTKGSFVNGV FEVHKKNVRG EFTYYEIQDN TGKMEVVVHG 730 740 750 760 770 780 RLTTINCEEG DKLKLTCFEL APKSGNTGEL RSVIHSHIKV IKTRKNKKDI LNPDSSMETS PDFFF
	Isoform 2 (IFI 16B) [UniParc]. Checksum: 27C820A058DE6A92	FASTA	729	82,096
	10 20 30 40 50 60 MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD LMEEKFRGDA 70 80 90 100 110 120 GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK EVDATSPAPS TSSTVKTEGA 130 140 150 160 170 180 EATPGAQKRK KSTKEKAGPK GSKVSEEQTQ PPSPAGAGMS TAMGRSPSPK TSLSAPPNSS 190 200 210 220 230 240 STENPKTVAK CQVTPRRNVL QKRPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF 250 260 270 280 290 300 HVKVLNTSLK EKFNGKKIII ISDYLEYDSL LEVNEESTVS EAGPNQTFEV PNKIINRAKE 310 320 330 340 350 360 TLKIDILHKQ ASGNIVYGVF MLHKKTVNQK TTIYEIQDDR GKMDVVGTGQ CHNIPCEEGD 370 380 390 400 410 420 KLQLFCFRLR KKNQMSKLIS EMHSFIQIKK KTNPRNNDPK SMKLPQEQRQ LPYPSEASTT 430 440 450 460 470 480 FPESHLRTPQ MPPTTPSSSF FTKKSEDTIS KMNDFMRMQI LKEGSHFPGP FMTSIGPAES 490 500 510 520 530 540 HPHTPQMPPS TPSSSFLTTL KPRLKTEPEE VSIEDSAQSD LKEVMVLNAT ESFVYEPKEQ 550 560 570 580 590 600 KKMFHATVAT ENEVFRVKVF NIDLKEKFTP KKIIAIANYV CRNGFLEVYP FTLVADVNAD 610 620 630 640 650 660 RNMEIPKGLI RSASVTPKIN QLCSQTKGSF VNGVFEVHKK NVRGEFTYYE IQDNTGKMEV 670 680 690 700 710 720 VVHGRLTTIN CEEGDKLKLT CFELAPKSGN TGELRSVIHS HIKVIKTRKN KKDILNPDSS METSPDFFF
	Isoform 3 (IFI 16C) [UniParc]. Checksum: 4D80A41BD9AA13A5	FASTA	673	75,936
	10 20 30 40 50 60 MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD LMEEKFRGDA 70 80 90 100 110 120 GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK EVDATSPAPS TSSTVKTEGA 130 140 150 160 170 180 EATPGAQKRK KSTKEKAGPK GSKVSEEQTQ PPSPAGAGMS TAMGRSPSPK TSLSAPPNSS 190 200 210 220 230 240 STENPKTVAK CQVTPRRNVL QKRPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF 250 260 270 280 290 300 HVKVLNTSLK EKFNGKKIII ISDYLEYDSL LEVNEESTVS EAGPNQTFEV PNKIINRAKE 310 320 330 340 350 360 TLKIDILHKQ ASGNIVYGVF MLHKKTVNQK TTIYEIQDDR GKMDVVGTGQ CHNIPCEEGD 370 380 390 400 410 420 KLQLFCFRLR KKNQMSKLIS EMHSFIQIKK KTNPRNNDPK SMKLPQEQRQ LPYPSEASTT 430 440 450 460 470 480 FPESHLRTPQ MPPTTPSSSF FTKLKPRLKT EPEEVSIEDS AQSDLKEVMV LNATESFVYE 490 500 510 520 530 540 PKEQKKMFHA TVATENEVFR VKVFNIDLKE KFTPKKIIAI ANYVCRNGFL EVYPFTLVAD 550 560 570 580 590 600 VNADRNMEIP KGLIRSASVT PKINQLCSQT KGSFVNGVFE VHKKNVRGEF TYYEIQDNTG 610 620 630 640 650 660 KMEVVVHGRL TTINCEEGDK LKLTCFELAP KSGNTGELRS VIHSHIKVIK TRKNKKDILN 670 PDSSMETSPD FFF
	Isoform 4 [UniParc]. Checksum: FEB03DF1E8B09D0A	FASTA	729	82,588
	10 20 30 40 50 60 MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD LMEEKFRGDA 70 80 90 100 110 120 GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK EVDATSPAPS TSSTVKTEGA 130 140 150 160 170 180 EATPGAQNPK TVAKCQVTPR RNVLQKRPVI VKVLSTTKPF EYETPEMEKK IMFHATVATQ 190 200 210 220 230 240 TQFFHVKVLN TSLKEKFNGK KIIIISDYLE YDSLLEVNEE STVSEAGPNQ TFEVPNKIIN 250 260 270 280 290 300 RAKETLKIDI LHKQASGNIV YGVFMLHKKT VNQKTTIYEI QDDRGKMDVV GTGQCHNIPC 310 320 330 340 350 360 EEGDKLQLFC FRLRKKNQMS KLISEMHSFI QIKKKTNPRN NDPKSMKLPQ EQRQLPYPSE 370 380 390 400 410 420 ASTTFPESHL RTPQMPPTTP SSSFFTKKSE DTISKMNDFM RMQILKEGSH FPGPFMTSIG 430 440 450 460 470 480 PAESHPHTPQ MPPSTPSSSF LTTKSEDTIS KMNDFMRMQI LKEGSHFPGP FMTSIGPAES 490 500 510 520 530 540 HPHTPQMPPS TPSSSFLTTL KPRLKTEPEE VSIEDSAQSD LKEVMVLNAT ESFVYEPKEQ 550 560 570 580 590 600 KKMFHATVAT ENEVFRVKVF NIDLKEKFTP KKIIAIANYV CRNGFLEVYP FTLVADVNAD 610 620 630 640 650 660 RNMEIPKGLI RSASVTPKIN QLCSQTKGSF VNGVFEVHKK NVRGEFTYYE IQDNTGKMEV 670 680 690 700 710 720 VVHGRLTTIN CEEGDKLKLT CFELAPKSGN TGELRSVIHS HIKVIKTRKN KKDILNPDSS METSPDFFF
	Isoform 5 [UniParc]. Checksum: 0F50D070770DFDA0	FASTA	414	46,139
	10 20 30 40 50 60 MGKKYKNIVL LKGLEVINDY HFRMVKSLLS NDLKLNLKMR EEYDKIQIAD LMEEKFRGDA 70 80 90 100 110 120 GLGKLIKIFE DIPTLEDLAE TLKKEKLKVK GPALSRKRKK EVDATSPAPS TSSTVKTEGA 130 140 150 160 170 180 EATPGAQKRK KSTKEKAGPK GSKVSEEQTQ PPSPAGAGMS TAMGRSPSPK TSLSAPPNSS 190 200 210 220 230 240 STENPKTVAK CQVTPRRNVL QKRPVIVKVL STTKPFEYET PEMEKKIMFH ATVATQTQFF 250 260 270 280 290 300 HVKVLNTSLK EKFTPKKIIA IANYVCRNGF LEVYPFTLVA DVNADRNMEI PKGLIRSASV 310 320 330 340 350 360 TPKINQLCSQ TKGSFVNGVF EVHKKNVRGE FTYYEIQDNT GKMEVVVHGR LTTINCEEGD 370 380 390 400 410 KLKLTCFELA PKSGNTGELR SVIHSHIKVI KTRKNKKDIL NPDSSMETSP DFFF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel gene constitutively expressed in human lymphoid cells is inducible with interferon-gamma in myeloid cells." Trapani J.A., Browne K.A., Dawson M.J., Ramsay R.G., Eddy R.L., Show T.B., White P.C., Dupont B. Immunogenetics 36:369-376(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT HIS-103. Tissue: T-cell.
[2]	"Genomic organization of IFI16, an interferon-inducible gene whose expression is associated with human myeloid cell differentiation: correlation of predicted protein domains with exon organization." Trapani J.A., Dawson M.J., Apostolidis V.A., Browne K.A. Immunogenetics 40:415-424(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT HIS-103.
[3]	Jiang C., Zhang D., Peng Y., Zhang X., Han Z., Fu G., Chen Z. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT HIS-103. Tissue: Bone marrow.
[4]	"Role of IFI 16, a member of the interferon-inducible p200-protein family, in prostate epithelial cellular senescence." Xin H., Curry J., Johnstone R.W., Nickoloff B.J., Choubey D. Oncogene 22:4831-4840(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, INDUCTION, VARIANTS THR-179; SER-409 AND ASN-413.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , 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] (ISOFORMS 4 AND 5), 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[20]	"In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification." Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L. J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION AT LYS-561. Tissue: Cervix carcinoma.
[21]	"IFI16 is an innate immune sensor for intracellular DNA." Unterholzner L., Keating S.E., Baran M., Horan K.A., Jensen S.B., Sharma S., Sirois C.M., Jin T., Latz E., Xiao T.S., Fitzgerald K.A., Paludan S.R., Bowie A.G. Nat. Immunol. 11:997-1004(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH TMEM173, INDUCTION.
[22]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-153 AND SER-575, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi Sarcoma-associated herpesvirus infection." Kerur N., Veettil M.V., Sharma-Walia N., Bottero V., Sadagopan S., Otageri P., Chandran B. Cell Host Microbe 9:363-375(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PYCARD AND CASP1.
[25]	"IFI16 induction by glucose restriction in human fibroblasts contributes to autophagy through activation of the ATM/AMPK/p53 pathway." Duan X., Ponomareva L., Veeranki S., Choubey D. PLoS ONE 6:E19532-E19532(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[26]	"IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes." Veeranki S., Duan X., Panchanathan R., Liu H., Choubey D. PLoS ONE 6:E27040-E27040(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AIM2.
[27]	"Preferential binding of IFI16 protein to cruciform structure and superhelical DNA." Brazda V., Coufal J., Liao J.C., Arrowsmith C.H. Biochem. Biophys. Res. Commun. 422:716-720(2012) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING.
[28]	"The intracellular DNA sensor IFI16 gene acts as restriction factor for human cytomegalovirus replication." Gariano G.R., Dell'Oste V., Bronzini M., Gatti D., Luganini A., De Andrea M., Gribaudo G., Gariglio M., Landolfo S. PLoS Pathog. 8:E1002498-E1002498(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERATION WITH SP1.
[29]	"Acetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16." Li T., Diner B.A., Chen J., Cristea I.M. Proc. Natl. Acad. Sci. U.S.A. 109:10558-10563(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MASS SPECTROMETRY, PHOSPHORYLATION AT SER-106; SER-153; SER-168; SER-174 AND SER-780, ACETYLATION AT LYS-45; LYS-99; LYS-128; LYS-214; LYS-444; LYS-451; LYS-561; LYS-598 AND LYS-614, MUTAGENESIS OF 96-ARG--LYS-100; LYS-99; LYS-128; 128-LYS--LYS-131; 134-LYS--LYS-136 AND 140-LYS--LYS-143.
[30]	"Interferon-inducible protein 16: insight into the interaction with tumor suppressor p53." Liao J.C., Lam R., Brazda V., Duan S., Ravichandran M., Ma J., Xiao T., Tempel W., Zuo X., Wang Y.X., Chirgadze N.Y., Arrowsmith C.H. Structure 19:418-429(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393, MUTAGENESIS OF TYR-218; GLU-222; TYR-267 AND GLU-272.
[31]	"Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor." Jin T., Perry A., Jiang J., Smith P., Curry J.A., Unterholzner L., Jiang Z., Horvath G., Rathinam V.A., Johnstone R.W., Hornung V., Latz E., Bowie A.G., Fitzgerald K.A., Xiao T.S. Immunity 36:561-571(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 571-766 IN COMPLEX WITH DOUBLE-STRANDED DNA, MUTAGENESIS OF LYS-627; LYS-663; ARG-667; SER-670; LYS-674; LYS-732; LYS-734 AND LYS-759.
[32]	"Crystal structure of the first HIN-200 domain of interferon-inducible protein 16." Northeast structural genomics consortium (NESG) Submitted (FEB-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393.
[33]	"Crystal structure analysis of the second HIN domain of IFI16." Northeast structural genomics consortium (NESG) Submitted (NOV-2007) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 571-766.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63838 mRNA. Translation: AAA58683.1.
S75433 , 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. Different initiation.
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.

IPI

IPI00003443.
IPI00217474.
IPI00217475.
IPI00384836.
IPI00909417.

PIR

I54501.

RefSeq

NP_001193496.1. NM_001206567.1.
NP_005522.2. NM_005531.2.

UniGene

Hs.380250.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q16666.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42868N.

IntAct

Q16666. 11 interactions.

MINT

MINT-1781545.

PTM databases

PhosphoSite

Q16666.

Polymorphism databases

DMDM

118572657.

Proteomic databases

PaxDb

Q16666.

PRIDE

Q16666.

Protocols and materials databases

DNASU

3428.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295809; ENSP00000295809; ENSG00000163565.
ENST00000340979; ENSP00000342741; ENSG00000163565.
ENST00000359709; ENSP00000352740; ENSG00000163565.
ENST00000368131; ENSP00000357113; ENSG00000163565.
ENST00000368132; ENSP00000357114; ENSG00000163565.
ENST00000447473; ENSP00000407052; ENSG00000163565.
ENST00000448393; ENSP00000404325; ENSG00000163565.

GeneID

3428.

KEGG

hsa:3428.

UCSC

uc001ftf.1. human.
uc001ftg.3. human.

Organism-specific databases

CTD

3428.

GeneCards

GC01P158969.

H-InvDB

HIX0001194.

HGNC

HGNC:5395. IFI16.

HPA

CAB016293.
HPA002134.

MIM

147586. gene.

neXtProt

NX_Q16666.

PharmGKB

PA29642.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG81691.

HOVERGEN

HBG006122.

InParanoid

Q16666.

OMA

SIGPAES.

PhylomeDB

Q16666.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q16666.

Bgee

Q16666.

Genevestigator

Q16666.

GermOnline

ENSG00000163565. Homo sapiens.

Family and domain databases

Gene3D

2.40.50.140. 4 hits.

InterPro

IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
IPR004021. HIN200/IF120x.
IPR012340. NA-bd_OB-fold.
[Graphical view]

Pfam

PF02760. HIN. 2 hits.
PF02758. PYRIN. 1 hit.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.

PROSITE

PS50824. DAPIN. 1 hit.
PS50834. HIN_200. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

IFI16. human.

EvolutionaryTrace

Q16666.

GenomeRNAi

3428.

NextBio

13516.

SOURCE

Search...

Entry information

Entry name

IF16_HUMAN

Accession

Primary (citable) accession number: Q16666
Secondary accession number(s): B4DJT8 , H3BLV7, Q59GX0, Q5T3W7, Q5T3W8, Q5T3X0, Q5T3X1, Q5T3X2, Q8N9E5, Q8NEQ7, Q96AJ5, Q9UH78

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 28, 2006
Last modified:	May 1, 2013
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.