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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

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

General annotation (Comments)

Function	May function as a transcriptional repressor. Could have a role in the regulation of hematopoeitic 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 the senescence of prostate epithelial cells. Ref.4 Ref.13
Subunit structure	Isoform 1, isoform 2 and isoform 3 can homo- and hetero-dimerize. Binds double-stranded DNA and cell cycle regulatory factors including p53 and the retinoblastoma protein.
Subcellular location	Nucleus Ref.10.
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. Ref.4 Ref.10 Ref.11 Ref.12
Post-translational modification	Phosphorylated on Ser and Thr. Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 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 BAC04462.1 differs from that shown. Reason: Probable cloning artifact. The sequence BAD92226.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding
Molecular function	Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis Inferred from direct assay. Source: MGI cell proliferation Non-traceable author statement Ref.12. Source: UniProtKB monocyte differentiation Inferred from direct assay Ref.12. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.13. Source: UniProtKB response to virus Non-traceable author statement. 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. Source: MGI nucleolus Inferred from direct assay. Source: MGI
Molecular function	double-stranded DNA binding Inferred from direct assay Ref.10. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TMEM173	Q86WV6	2	EBI-2867186,EBI-2800345

Alternative products

This entry describes 3 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.

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

Motif

124 – 131

8

Nuclear localization signal Potential

Compositional bias

1 – 150

150

Lys-rich

Compositional bias

258 – 261

4

Poly-Ile

Amino acid modifications

Modified residue

106

1

Phosphoserine Ref.15 Ref.17 Ref.18

Modified residue

153

1

Phosphoserine Ref.14 Ref.16 Ref.17 Ref.18

Modified residue

214

1

N6-acetyllysine Ref.19

Cross-link

561

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

Natural variations

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.7 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.7
Corresponds to variant rs1057027 [ dbSNP | Ensembl ].

VAR_029489

Natural variant

413

1

Y → N. Ref.4 Ref.5 Ref.7
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

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

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

Helix

622 – 624

3

Beta strand

629 – 634

6

Beta strand

636 – 638

3

Beta strand

641 – 644

4

Beta strand

648 – 652

5

Helix

655 – 657

3

Helix

663 – 667

5

Helix

675 – 678

4

Beta strand

685 – 699

15

Beta strand

702 – 708

7

Beta strand

713 – 720

8

Helix

721 – 724

4

Beta strand

732 – 742

11

Beta strand

748 – 751

4

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

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: 1526658] [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: 7959953] [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: 12894224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, INDUCTION, VARIANTS THR-179; SER-409 AND ASN-413.
[5]	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.
[6]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS THR-179; SER-409 AND ASN-413. Tissue: Uterus.
[8]	"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: 14702039] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-179. Tissue: Hippocampus.
[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: 9718316] [Abstract] Cited for: ALTERNATIVE SPLICING, 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: 7536752] [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: 7806273] [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: 9766636] [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: 9642285] [Abstract] Cited for: FUNCTION.
[14]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, 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: 18669648] [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: 19690332] [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [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: 20388717] [Abstract] Cited for: SUMOYLATION AT LYS-561. Tissue: Cervix carcinoma.
[21]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"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.
[23]	"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.
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.
AK094968 mRNA. Translation: BAC04462.1. Sequence problems.

IPI

IPI00003443.
IPI00217474.
IPI00217475.
IPI00384836.

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	[»]

ProteinModelPortal

Q16666.

SMR

Q16666. Positions 1-93, 198-389, 576-761.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42868N.

IntAct

Q16666. 6 interactions.

MINT

MINT-1781545.

STRING

Q16666.

PTM databases

PhosphoSite

Q16666.

Polymorphism databases

DMDM

118572657.

Proteomic databases

PRIDE

Q16666.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295809; ENSP00000295809; ENSG00000163565.

GeneID

3428.

KEGG

hsa:3428.

NMPDR

fig|9606.3.peg.2390.

UCSC

uc001ftg.1. human.

Organism-specific databases

CTD

3428.

GeneCards

GC01P158969.

HGNC

HGNC:5395. IFI16.

HPA

CAB016293.
HPA002134.

MIM

147586. gene.

neXtProt

NX_Q16666.

PharmGKB

PA29642.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13079.

GeneTree

ENSGT00390000013296.

HOVERGEN

HBG006122.

InParanoid

Q16666.

OMA

MTSIGPA.

PhylomeDB

Q16666.

Gene expression databases

ArrayExpress

Q16666.

Bgee

Q16666.

Genevestigator

Q16666.

GermOnline

ENSG00000163565. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.40.50.140. OB_NA_bd_sub. 4 hits.

Pfam

PF02760. HIN. 2 hits.
PF02758. PAAD_DAPIN. 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

NextBio

13516.

SOURCE

Search...

Entry information

Entry name

IF16_HUMAN

Accession

Primary (citable) accession number: Q16666
Secondary accession number(s): 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:	January 25, 2012
This is version 126 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.