Q14653 (IRF3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interferon regulatory factor 3
Short name=IRF-3

Gene names

Name:

IRF3

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	427 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates interferon-stimulated response element (ISRE) promoter activation. Functions as a molecular switch for antiviral activity. DsRNA generated during the course of an viral infection leads to IRF3 phosphorylation on the C-terminal serine/threonine cluster. This induces a conformational change, leading to its dimerization, nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of genes under the control of ISRE. The complex binds to the IE and PRDIII regions on the IFN-alpha and IFN-beta promoters respectively. IRF-3 does not have any transcription activation domains.
Subunit structure	Homodimer; phosphorylation-induced. Interacts with CREBBP. May interact with MAVS. Interacts with IKBKE and TBK1. Interacts with TICAM1 and TICAM2. Interacts with rotavirus A NSP1 (via C-terminus); this interaction leads to the proteasome-dependent degradation of IRF3. Interacts with RBCK1. Interacts with TRIM21. Interacts with HERC5. Ref.12 Ref.13 Ref.14 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22
Subcellular location	Cytoplasm. Nucleus. Note: Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm. Ref.8
Tissue specificity	Expressed constitutively in a variety of tissues.
Post-translational modification	Constitutively phosphorylated on many serines residues. C-terminal serine/threonine cluster is phosphorylated in response of induction by IKBKE and TBK1. Ser-385 and Ser-386 may be specifically phosphorylated in response to induction. An alternate model propose that the five serine/threonine residues between 396 and 405 are phosphorylated in response to a viral infection. Phosphorylation, and subsequent activation of IRF3 is inhibited by vaccinia virus protein E3. Ref.9 Ref.10 Ref.16 Ubiquitinated; ubiquitination involves RBCK1 leading to proteasomal degradation. Polyubiquitinated; ubiquitination involves TRIM21 leading to proteasomal degradation. Ref.20 Ref.21 ISGylated by HERC5 resulting in sustained IRF3 activation and in the inhibition of IRF3 ubiquitination by disrupting PIN1 binding. The phosphorylation state of IRF3 does not alter ISGylation. Ref.22
Sequence similarities	Belongs to the IRF family. Contains 1 IRF tryptophan pentad repeat DNA-binding domain.

Ontologies

Keywords
Biological process	Antiviral defense Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Disulfide bond Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	MyD88-independent toll-like receptor signaling pathway Traceable author statement. Source: Reactome Toll signaling pathway Traceable author statement. Source: Reactome interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of type I interferon production Traceable author statement. Source: Reactome response to virus Inferred from electronic annotation. Source: UniProtKB-KW toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome endosome membrane Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular function	protein homodimerization activity Inferred from physical interaction. Source: BHF-UCL sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro transcription cofactor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		8	EBI-2650369,EBI-2650369
CREBBP	Q92793	2	EBI-2650369,EBI-81215
MAFB	Q9Y5Q3	4	EBI-2650369,EBI-3649340
SGTA	O43765	3	EBI-2650369,EBI-347996
TBK1	Q9UHD2	2	EBI-2650369,EBI-356402

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 427

427

Interferon regulatory factor 3

PRO_0000154553

Regions

DNA binding

5 – 111

107

IRF tryptophan pentad repeat

Region

200 – 360

161

Involved in HERC5 binding

Motif

139 – 149

11

Nuclear export signal

Compositional bias

151 – 191

41

Pro-rich

Amino acid modifications

Modified residue

123

1

Phosphoserine By similarity

Disulfide bond

267 ↔ 289

Ref.23 Ref.24

Cross-link

193

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) Ref.22

Cross-link

360

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) Ref.22

Cross-link

366

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) Ref.22

Natural variations

Natural variant

96

1

R → Q.
Corresponds to variant rs968457 [ dbSNP | Ensembl ].

VAR_011901

Natural variant

107

1

Y → F.
Corresponds to variant rs34745118 [ dbSNP | Ensembl ].

VAR_049643

Natural variant

377

1

E → K.
Corresponds to variant rs1049486 [ dbSNP | Ensembl ].

VAR_011902

Natural variant

427

1

S → T. Ref.2 Ref.3
Corresponds to variant rs7251 [ dbSNP | Ensembl ].

VAR_011903

Experimental info

Mutagenesis

77 – 78

2

KR → NG: Abolishes nuclear localization. Ref.8

Mutagenesis

86 – 87

2

RK → LQ: No effect on subcellular localization. Ref.8

Mutagenesis

139 – 140

2

IL → MM: Abolishes nuclear export. Ref.8

Mutagenesis

193

1

K → R: Highly diminished ISGylation; when associated with R-360 and R-366. Ref.8 Ref.22

Mutagenesis

360

1

K → R: Highly diminished ISGylation; when associated with R-193 and R-366. Ref.8 Ref.22

Mutagenesis

366

1

K → R: Highly diminished ISGylation; when associated with R-193 and R-360. Ref.8 Ref.22

Mutagenesis

385 – 386

2

SS → AA: Complete loss of viral infection induced phosphorylation. Ref.7 Ref.8

Mutagenesis

385

1

S → A, D or E: Complete loss of viral infection induced phosphorylation. Ref.7 Ref.8

Mutagenesis

386

1

S → A, D or E: Complete loss of viral infection induced phosphorylation. Ref.7 Ref.8

Mutagenesis

396 – 405

10

SNSHPLSLTS → ANAHPLALAA: Complete loss of viral infection induced phosphorylation. Ref.6 Ref.8

Mutagenesis

396 – 405

10

SNSHPLSLTS → DNDHPLDLDD: Acts as a constitutively activated IRF3. Ref.6 Ref.8

Mutagenesis

396 – 398

3

SNS → ANA: Complete loss of viral infection induced phosphorylation. Ref.8

Mutagenesis

402 – 405

4

SLTS → ALAA: Complete loss of viral infection induced phosphorylation. Ref.8

Secondary structure

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427

Helix Strand Turn

Details...

Helix

8 – 18

11

Beta strand

25 – 28

4

Turn

29 – 31

3

Beta strand

32 – 37

6

Helix

48 – 51

4

Helix

52 – 60

9

Helix

73 – 85

13

Beta strand

88 – 95

8

Beta strand

104 – 109

6

Helix

191 – 195

5

Beta strand

202 – 210

9

Beta strand

213 – 221

9

Beta strand

226 – 229

4

Beta strand

240 – 244

5

Helix

248 – 250

3

Helix

255 – 267

13

Beta strand

272 – 277

6

Beta strand

280 – 285

6

Beta strand

287 – 289

3

Beta strand

291 – 296

6

Beta strand

308 – 310

3

Beta strand

313 – 315

3

Beta strand

317 – 321

5

Helix

322 – 333

12

Beta strand

343 – 348

6

Helix

357 – 360

4

Beta strand

363 – 369

7

Helix

370 – 380

11

Beta strand

386 – 391

6

Beta strand

401 – 404

4

Helix

405 – 416

12

Sequences

	Sequence		Length	Mass (Da)
	Q14653 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: F536676FA78B0110	FASTA	427	47,219
	10 20 30 40 50 60 MGTPKPRILP WLVSQLDLGQ LEGVAWVNKS RTRFRIPWKH GLRQDAQQED FGIFQAWAEA 70 80 90 100 110 120 TGAYVPGRDK PDLPTWKRNF RSALNRKEGL RLAEDRSKDP HDPHKIYEFV NSGVGDFSQP 130 140 150 160 170 180 DTSPDTNGGG STSDTQEDIL DELLGNMVLA PLPDPGPPSL AVAPEPCPQP LRSPSLDNPT 190 200 210 220 230 240 PFPNLGPSEN PLKRLLVPGE EWEFEVTAFY RGRQVFQQTI SCPEGLRLVG SEVGDRTLPG 250 260 270 280 290 300 WPVTLPDPGM SLTDRGVMSY VRHVLSCLGG GLALWRAGQW LWAQRLGHCH TYWAVSEELL 310 320 330 340 350 360 PNSGHGPDGE VPKDKEGGVF DLGPFIVDLI TFTEGSGRSP RYALWFCVGE SWPQDQPWTK 370 380 390 400 410 420 RLVMVKVVPT CLRALVEMAR VGGASSLENT VDLHISNSHP LSLTSDQYKA YLQDLVEGMD FQGPGES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a member of the interferon regulatory factor family that binds to the interferon-stimulated response element and activates expression of interferon-induced genes." Au W.W.-C., Moore P.P.A., Lowther W.W., Juang Y.-T., Pitha P.M. Proc. Natl. Acad. Sci. U.S.A. 92:11657-11661(1995) [PubMed: 8524823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Retina.
[2]	"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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-427. Tissue: Spleen.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-427.
[4]	"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]. Tissue: Eye.
[5]	"Mapping of human interferon regulatory factor 3 (IRF3) to chromosome 19q13.3-13.4 by an intragenic polymorphic marker." Bellingham J., Gregory-Evans K., Gregory-Evans C.Y. Ann. Hum. Genet. 62:231-234(1998) [PubMed: 9803267] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-413.
[6]	"Virus-dependent phosphorylation of the IRF-3 transcription factor regulates nuclear translocation, transactivation potential, and proteasome-mediated degradation." Lin R., Heylbroeck C., Pitha P.M., Hiscott J. Mol. Cell. Biol. 18:2986-2996(1998) [PubMed: 9566918] [Abstract] Cited for: MUTAGENESIS OF 385-SER-SER-386 AND 396-SER--SER-405.
[7]	"Analyses of virus-induced homomeric and heteromeric protein associations between IRF-3 and coactivator CBP/p300." Suhara W., Yoneyama M., Iwamura T., Yoshimura S., Tamura K., Namiki H., Aimoto S., Fujita T. J. Biochem. 128:301-307(2000) [PubMed: 10920266] [Abstract] Cited for: MUTAGENESIS OF SER-385 AND SER-386.
[8]	"Regulated nuclear-cytoplasmic localization of interferon regulatory factor 3, a subunit of double-stranded RNA-activated factor 1." Kumar K.P., McBride K.M., Weaver B.K., Dingwall C., Reich N.C. Mol. Cell. Biol. 20:4159-4168(2000) [PubMed: 10805757] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 77-LYS-ARG-78; 86-ARG-LYS-87 AND 139-ILE-LEU-140.
[9]	"Identification of distinct signaling pathways leading to the phosphorylation of interferon regulatory factor 3." Servant M.J., ten Oever B., LePage C., Conti L., Gessani S., Julkunen I., Lin R., Hiscott J. J. Biol. Chem. 276:355-363(2001) [PubMed: 11035028] [Abstract] Cited for: PHOSPHORYLATION.
[10]	"IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L protein." Smith E.J., Marie I.J., Prakash A., Garcia-Sastre A., Levy D.E. J. Biol. Chem. 276:8951-8957(2001) [PubMed: 11124948] [Abstract] Cited for: INHIBITION OF PHOSPHORYLATION BY VACCINIA VIRUS PROTEIN E3.
[11]	"Control of IRF-3 activation by phosphorylation." Yoneyama M., Suhara W., Fujita T. J. Interferon Cytokine Res. 22:73-76(2002) [PubMed: 11846977] [Abstract] Cited for: REVIEW.
[12]	"A novel Toll/IL-1 receptor domain-containing adapter that preferentially activates the IFN-beta promoter in the Toll-like receptor signaling." Yamamoto M., Sato S., Mori K., Hoshino K., Takeuchi O., Takeda K., Akira S. J. Immunol. 169:6668-6672(2002) [PubMed: 12471095] [Abstract] Cited for: INTERACTION WITH TICAM1.
[13]	"Interferon regulatory factor 3 is a cellular partner of rotavirus NSP1." Graff J.W., Mitzel D.N., Weisend C.M., Flenniken M.L., Hardy M.E. J. Virol. 76:9545-9550(2002) [PubMed: 12186937] [Abstract] Cited for: INTERACTION WITH ROTAVIRUS A NSP1.
[14]	"LPS-TLR4 signaling to IRF-3/7 and NF-kappaB involves the toll adapters TRAM and TRIF." Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A., Latz E., Monks B., Pitha P.M., Golenbock D.T. J. Exp. Med. 198:1043-1055(2003) [PubMed: 14517278] [Abstract] Cited for: INTERACTION WITH TICAM2.
[15]	Erratum Fitzgerald K.A., Rowe D.C., Barnes B.J., Caffrey D.R., Visintin A., Latz E., Monks B., Pitha P.M., Golenbock D.T. J. Exp. Med. 198:1451-1451(2003)
[16]	"Triggering the interferon antiviral response through an IKK-related pathway." Sharma S., tenOever B.R., Grandvaux N., Zhou G.-P., Lin R., Hiscott J. Science 300:1148-1151(2003) [PubMed: 12702806] [Abstract] Cited for: PHOSPHORYLATION.
[17]	"Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways." Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B. J. Biol. Chem. 279:15652-15661(2004) [PubMed: 14739303] [Abstract] Cited for: INTERACTION WITH TICAM1.
[18]	"SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways." Huang J., Liu T., Xu L.-G., Chen D., Zhai Z., Shu H.-B. EMBO J. 24:4018-4028(2005) [PubMed: 16281057] [Abstract] Cited for: INTERACTION WITH IKBKE AND TBK1.
[19]	"VISA is an adapter protein required for virus-triggered IFN-beta Signaling." Xu L.-G., Wang Y.-Y., Han K.-J., Li L.-Y., Zhai Z., Shu H.-B. Mol. Cell 19:727-740(2005) [PubMed: 16153868] [Abstract] Cited for: INTERACTION WITH MAVS.
[20]	"Negative feedback regulation of cellular antiviral signaling by RBCK1-mediated degradation of IRF3." Zhang M., Tian Y., Wang R.P., Gao D., Zhang Y., Diao F.C., Chen D.Y., Zhai Z.H., Shu H.B. Cell Res. 18:1096-1104(2008) [PubMed: 18711448] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH RBCK1.
[21]	"The E3 ubiquitin ligase Ro52 negatively regulates IFN-beta production post-pathogen recognition by polyubiquitin-mediated degradation of IRF3." Higgs R., Ni Gabhann J., Ben Larbi N., Breen E.P., Fitzgerald K.A., Jefferies C.A. J. Immunol. 181:1780-1786(2008) [PubMed: 18641315] [Abstract] Cited for: INTERACTION WITH TRIM21, POLYUBIQUITINATION.
[22]	"Positive regulation of interferon regulatory factor 3 activation by Herc5 via ISG15 modification." Shi H.X., Yang K., Liu X., Liu X.Y., Wei B., Shan Y.F., Zhu L.H., Wang C. Mol. Cell. Biol. 30:2424-2436(2010) [PubMed: 20308324] [Abstract] Cited for: ISGYLATION AT LYS-193; LYS-360 AND LYS-366, MUTAGENESIS OF LYS-193; LYS-360 AND LYS-366, INTERACTION WITH HERC5.
[23]	"X-ray crystal structure of IRF-3 and its functional implications." Takahasi K., Suzuki N.N., Horiuchi M., Mori M., Suhara W., Okabe Y., Fukuhara Y., Terasawa H., Akira S., Fujita T., Inagaki F. Nat. Struct. Biol. 10:922-927(2003) [PubMed: 14555995] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 175-427, DISULFIDE BOND.
[24]	"Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus-induced phosphoactivation." Qin B.Y., Liu C., Lam S.S., Srinath H., Delston R., Correia J.J., Derynck R., Lin K. Nat. Struct. Biol. 10:913-921(2003) [PubMed: 14555996] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 173-427, DISULFIDE BOND.
[25]	"Crystal structure of ATF-2/c-Jun and IRF-3 bound to the interferon-beta enhancer." Panne D., Maniatis T., Harrison S.C. EMBO J. 23:4384-4393(2004) [PubMed: 15510218] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-112.
[26]	"Crystal structure of IRF-3 in complex with CBP." Qin B.Y., Liu C., Srinath H., Lam S.S., Correia J.J., Derynck R., Lin K. Structure 13:1269-1277(2005) [PubMed: 16154084] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 173-394.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z56281 mRNA. Translation: CAA91227.1.
AK292027 mRNA. Translation: BAF84716.1.
CH471177 Genomic DNA. Translation: EAW52510.1.
BC071721 mRNA. Translation: AAH71721.1.
U86636 Genomic DNA. Translation: AAC68818.1.

IPI

IPI00291901.

RefSeq

NP_001562.1. NM_001571.5.

UniGene

Hs.289052.
Hs.75254.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J2F	X-ray	2.30	A/B	175-427	[»]
1QWT	X-ray	2.10	A/B	173-427	[»]
1T2K	X-ray	3.00	A/B	1-112	[»]
1ZOQ	X-ray	2.37	A/B	196-386	[»]
2O61	X-ray	2.80	A	9-111	[»]
2O6G	X-ray	3.10	E/F/G/H	1-123	[»]
2PI0	X-ray	2.31	A/B/C/D	1-113	[»]
3A77	X-ray	1.80	A/B/C/D	189-427	[»]
3QU6	X-ray	2.30	A/B/C	1-113	[»]

ProteinModelPortal

Q14653.

SMR

Q14653. Positions 1-112, 189-427.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41448N.

IntAct

Q14653. 8 interactions.

MINT

MINT-253351.

STRING

Q14653.

PTM databases

PhosphoSite

Q14653.

Polymorphism databases

DMDM

2497442.

Proteomic databases

PeptideAtlas

Q14653.

PRIDE

Q14653.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309877; ENSP00000310127; ENSG00000126456.
ENST00000377139; ENSP00000366344; ENSG00000126456.

GeneID

3661.

KEGG

hsa:3661.

UCSC

uc002pou.2. human.

Organism-specific databases

CTD

3661.

GeneCards

GC19M050162.

H-InvDB

HIX0015338.

HGNC

HGNC:6118. IRF3.

HPA

CAB013018.
HPA004895.

MIM

603734. gene.

neXtProt

NX_Q14653.

PharmGKB

PA29917.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG05018.

HOVERGEN

HBG105601.

PhylomeDB

Q14653.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q14653.

Bgee

Q14653.

CleanEx

HS_IRF3.

Genevestigator

Q14653.

GermOnline

ENSG00000126456. Homo sapiens.

Family and domain databases

InterPro

IPR019817. Interferon_reg_fac_CS.
IPR001346. Interferon_reg_fact_DNA-bd_dom.
IPR019471. Interferon_reg_factor-3.
IPR017855. SMAD_dom-like.
IPR008984. SMAD_FHA_domain.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:2.60.200.10. MH2_Dwarfin-type. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K05411.

Pfam

PF00605. IRF. 1 hit.
PF10401. IRF-3. 1 hit.
[Graphical view]

PRINTS

PR00267. INTFRNREGFCT.

SMART

SM00348. IRF. 1 hit.
[Graphical view]

SUPFAM

SSF49879. SMAD_FHA. 1 hit.

PROSITE

PS00601. IRF_1. 1 hit.
PS51507. IRF_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

14319.

SOURCE

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Entry information

Entry name

IRF3_HUMAN

Accession

Primary (citable) accession number: Q14653
Secondary accession number(s): A8K7L2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 113 of the entry and version 1 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.