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IRF3 (human)

Overview IRF3 interferon regulatory factor 3, a member of the interferon regulatory transcription factor (IRF) family. IRF3 is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP. This complex translocates to the nucleus and activates the transcription of interferons alpha and beta, as well as other interferon-induced genes. Note: This description may include information from UniProtKB. Protein type: DNA binding protein; Transcription factor Cellular Component: nucleoplasm; cytoplasm; endosome membrane; nucleus; cytosol Molecular Function: identical protein binding; protein binding; protein homodimerization activity; DNA binding; transcription cofactor activity; transcription factor activity Biological Process: transcription from RNA polymerase II promoter; negative regulation of interferon-beta biosynthetic process; positive regulation of I-kappaB kinase/NF-kappaB cascade; MyD88-independent toll-like receptor signaling pathway; cytokine and chemokine mediated signaling pathway; negative regulation of defense response to virus by host; toll-like receptor 3 signaling pathway; negative regulation of transcription from RNA polymerase II promoter; Toll signaling pathway; response to exogenous dsRNA; virus-host interaction; induction of apoptosis; lipopolysaccharide-mediated signaling pathway; positive regulation of interferon type I production; positive regulation of interferon-beta production; innate immune response; interferon type I biosynthetic process; defense response to virus; response to DNA damage stimulus; negative regulation of interferon type I production; toll-like receptor 4 signaling pathway; positive regulation of interferon-alpha production; positive regulation of cytokine secretion Reference #:  Q14653 (UniProtKB) Alt. Names/Synonyms: Interferon regulatory factor 3; IRF-3; IRF3 Gene Symbols: IRF3 Molecular weight: 47,219 Da Basal Isoelectric point: 5.17  Predict pI for various phosphorylation states CST Pathways:  Toll-like Receptors Pathway Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below IRF3 1J2F - A/B=175-427 (human) 1QWT - A/B=173-427 (human) 1T2K - A/B=1-112 (human) 1ZOQ - A/B=196-386 (human) 2O6G - E/F/G/H=1-123 (human) 2PI0 - A/B/C/D=1-113 (human) 3A77 - A/D/C/B=189-427 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1J2F 1QWT 1T2K 1ZOQ 2O6G 2PI0 3A77  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
transcription, altered: S173‑p, S339‑p, S385‑p, S386‑p, S396‑p, S398‑p, S402‑p, T404‑p, S405‑p activation: S385‑p, S386‑p, S396‑p, S398‑p, S402‑p, T404‑p, S405‑p intracellular localization: T135‑p, S385‑p, S386‑p, S396‑p, S398‑p, S402‑p, T404‑p, S405‑p molecular association, regulation: S339‑p, S385‑p, S386‑p, T390‑p, S396‑p, S398‑p, T404‑p, S405‑p phosphorylation: S173‑p, S386‑p, T390‑p, T404‑p, S405‑p protein conformation: S385‑p, S386‑p, T404‑p, S405‑p protein degradation: S339‑p, S396‑p protein stabilization: T135‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	2		S14-p	RILPWLVsQLDLGQL
0	1		K29-u	EGVAWVNkSRTRFRI
1	0		K70-s	AYVPGRDkPDLPTWK
1	1		K70-u	AYVPGRDkPDLPTWK
1	0		K87-s	FRSALNRkEGLRLAE
1	0		K87-u	FRSALNRkEGLRLAE
0	5		S123	DFSQPDTSPDTNGGG
0	1		T126	QPDTSPDTNGGGsTS
0	2		S131-p	PDTNGGGsTSDtQED
1	17		T135-p	GGGsTSDtQEDILDE
2	0		P153	NMVLAPLPDPGPPSL
2	2		S173-p	PCPQPLRsPsLDNPT
1	3		S175-p	PQPLRsPsLDNPTPF
0	1		K193-u	GPSENPLkRLLVPGE
2	0		S339-p	FTEGSGRsPRYALWF
0	6		T370-p	VMVKVVPtCLRALVE
0	1		R373	KVVPtCLRALVEMAR
7	1		S385-p	MARVGGAssLENtVD
8	2		S386-p	ARVGGAssLENtVDL
1	1		T390-p	GAssLENtVDLHIsN
21	2		S396-p	NtVDLHIsNsHPLsL
6	0		S398-p	VDLHIsNsHPLsLts
5	1		S402-p	IsNsHPLsLtsDQYK
5	0		T404-p	NsHPLsLtsDQYKAY
4	0		S405-p	sHPLsLtsDQYKAYL

	mouse
S14	RILPWLVSQLDLGQL
E29	EGVAWLDESRTRFRI
K70	AYTPGKDKPDVSTWK
K70	AYTPGKDKPDVSTWK
K87	FRSALNRKEVLRLAA
K87-u	FRSALNRkEVLRLAA
S123-p	DFVHLGAsPDtNGKS
T126-p	HLGAsPDtNGKSsLP
S131-p	PDtNGKSsLPHsQEN
S135-p	GKSsLPHsQENLPKL
K152-s	GLILGPLkDEGSSDL
S171	DPSQQLPSPNVNNFL
N173	SQQLPSPNVNNFLNP
K188	APQENPLKQLLAEEQ
S332	FMEGSGHSPRYTLWF
T363	VMVKVVPTCLkELLE
K366-u	KVVPTCLkELLEMAR
S378	MAREGGASSLKTVDL
S379	AREGGASSLKTVDLH
T382	GGASSLKTVDLHIsN
S388-p	KTVDLHIsNSQPISL
S390	VDLHIsNSQPISLtS
S394	IsNSQPISLtSDQYK
T396-p	NSQPISLtSDQYKAY
S397	SQPISLtSDQYKAYL

	rat
S14	LILPWLVSQLDLGQL
E29	KGVAWLDESRTKFRI
K70	AYTPGKDKPDLSTWK
K70	AYTPGKDKPDLSTWK
K87	FRSALNRKEVLRLAE
K87	FRSALNRKEVLRLAE
S124	DFVHLDtSPDTNGKS
T127	HLDtSPDTNGKSSLS
S132	PDTNGKSSLSDHQED
H136	GKSSLSDHQEDLLEL
P153	HMALGPLPDEGSSDL
S172	DPSQPPLSPIVNNFP
I174	SQPPLSPIVNNFPNP
R189	APQENPLRQLLAEEQ
S334	FMEGSRHSPRYTLWF
T365	VMVKVVPTCLKELLE
K368	KVVPTCLKELLEMAR
S380	MAREGGASSLKTVDL
S381	AREGGASSLKTVDLH
T384	GGASSLKTVDLHISN
S390	KTVDLHISNSQPISL
S392	VDLHISNSQPISLTS
S396	ISNSQPISLTSDQYK
T398	NSQPISLTSDQYKAC
S399	SQPISLTSDQYKACL

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