dbPTM

IRF3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IRF3_MOUSE
UniProt AC	P70671
Protein Name	Interferon regulatory factor 3
Gene Name	Irf3
Organism	Mus musculus (Mouse).
Sequence Length	419
Subcellular Localization	Cytoplasm . Nucleus . Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect. When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm.
Protein Description	Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages..
Protein Sequence	METPKPRILPWLVSQLDLGQLEGVAWLDESRTRFRIPWKHGLRQDAQMADFGIFQAWAEASGAYTPGKDKPDVSTWKRNFRSALNRKEVLRLAADNSKDPYDPHKVYEFVTPGARDFVHLGASPDTNGKSSLPHSQENLPKLFDGLILGPLKDEGSSDLAIVSDPSQQLPSPNVNNFLNPAPQENPLKQLLAEEQWEFEVTAFYRGRQVFQQTLFCPGGLRLVGSTADMTLPWQPVTLPDPEGFLTDKLVKEYVGQVLKGLGNGLALWQAGQCLWAQRLGHSHAFWALGEELLPDSGRGPDGEVHKDKDGAVFDLRPFVADLIAFMEGSGHSPRYTLWFCMGEMWPQDQPWVKRLVMVKVVPTCLKELLEMAREGGASSLKTVDLHISNSQPISLTSDQYKAYLQDLVEDMDFQATGNI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----METPKPRILP -----CCCCCCCCHH	35.00	-
14	Phosphorylation	RILPWLVSQLDLGQL CCHHHHHHHCCCCCC	23.90	-
74	Phosphorylation	GKDKPDVSTWKRNFR CCCCCCHHHHHHHHH	35.61	25338131
75	Phosphorylation	KDKPDVSTWKRNFRS CCCCCHHHHHHHHHH	34.55	-
77	Malonylation	KPDVSTWKRNFRSAL CCCHHHHHHHHHHHH	37.24	26320211
87	Ubiquitination	FRSALNRKEVLRLAA HHHHHCHHHHHHHHH	51.61	-
97	Phosphorylation	LRLAADNSKDPYDPH HHHHHCCCCCCCCHH	38.70	-
105	Acetylation	KDPYDPHKVYEFVTP CCCCCHHHHEEEECC	52.48	23954790
105	Malonylation	KDPYDPHKVYEFVTP CCCCCHHHHEEEECC	52.48	26320211
107	Phosphorylation	PYDPHKVYEFVTPGA CCCHHHHEEEECCCC	14.41	25367039
111	Phosphorylation	HKVYEFVTPGARDFV HHHEEEECCCCCCCE	22.71	23984901
123	Phosphorylation	DFVHLGASPDTNGKS CCEECCCCCCCCCCC	22.85	25521595
126	Phosphorylation	HLGASPDTNGKSSLP ECCCCCCCCCCCCCC	49.62	21082442
130	Phosphorylation	SPDTNGKSSLPHSQE CCCCCCCCCCCCCCC	38.21	27087446
131	Phosphorylation	PDTNGKSSLPHSQEN CCCCCCCCCCCCCCC	49.78	27087446
135	Phosphorylation	GKSSLPHSQENLPKL CCCCCCCCCCCHHHH	36.93	27087446
152	Sumoylation	GLILGPLKDEGSSDL CEEEECCCCCCCCCE	57.79	-
152	Sumoylation	GLILGPLKDEGSSDL CEEEECCCCCCCCCE	57.79	-
171	Phosphorylation	DPSQQLPSPNVNNFL CHHHCCCCCCCCCCC	37.38	30352176
230	Phosphorylation	VGSTADMTLPWQPVT ECEECCEECCCCCCC	30.16	-
237	Phosphorylation	TLPWQPVTLPDPEGF ECCCCCCCCCCCCCC	38.98	-
246	Phosphorylation	PDPEGFLTDKLVKEY CCCCCCCCHHHHHHH	28.91	-
332	Phosphorylation	FMEGSGHSPRYTLWF HHHCCCCCCCCEEEE	18.01	-
366	Ubiquitination	KVVPTCLKELLEMAR HHHHHHHHHHHHHHH	48.76	22790023
378	Phosphorylation	MAREGGASSLKTVDL HHHHCCCCCCEEEEE	39.21	30352176
379	Phosphorylation	AREGGASSLKTVDLH HHHCCCCCCEEEEEE	33.09	27149854
382	Phosphorylation	GGASSLKTVDLHISN CCCCCCEEEEEEECC	25.25	24719451
388	Phosphorylation	KTVDLHISNSQPISL EEEEEEECCCCCCCC	21.49	28725479
390	Phosphorylation	VDLHISNSQPISLTS EEEEECCCCCCCCCH	30.46	-
396	Phosphorylation	NSQPISLTSDQYKAY CCCCCCCCHHHHHHH	24.38	21106850

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
171	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS
379	S	Phosphorylation	Kinase	TBK1	Q9WUN2	Uniprot
388	S	Phosphorylation	Kinase	IKKE	Q9R0T8	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IRF3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of IRF3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
TRI26_MOUSE	Trim26	physical	25763818

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IRF3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-135, ANDMASS SPECTROMETRY.	19367708 [Abstract]