Phospho-IRF3 (S386) Recombinant Rabbit Monoclonal Antibody - BSA and Azide free [SU03-28] (HA750138)

UNIPROT #

Q14653

PROTEIN NAME

Phospho-IRF3 (S386)

SYNONYMS

IIAE7 antibody;Interferon regulatory factor 3 antibody;IRF 3 antibody;IRF-3 antibody;IRF3 antibody;IRF3_HUMAN antibody;MGC94729 antibody

SEQUENCE SIMILARITIES

Belongs to the IRF family.

TISSUE SPECIFICITY

Expressed constitutively in a variety of tissues.

POST-TRANSLATIONAL MODIFICATION

Constitutively phosphorylated on many Ser/Thr residues. Activated following phosphorylation by TBK1 and IKBKE. Innate adapter protein MAVS, STING1 or TICAM1 are first activated by viral RNA, cytosolic DNA, and bacterial lipopolysaccharide (LPS), respectively, leading to activation of the kinases TBK1 and IKBKE. These kinases then phosphorylate the adapter proteins on the pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1. Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce IFNs.; (Microbial infection) Phosphorylation and subsequent activation of IRF3 is inhibited by vaccinia virus protein E3.; Ubiquitinated; ubiquitination involves RBCK1 leading to proteasomal degradation. Polyubiquitinated; ubiquitination involves TRIM21 leading to proteasomal degradation.; 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.

SUBCELLULAR LOCATION

Cytoplasm, Nucleus, Mitochondrion.

FUNCTION

Interferon regulatory factor 3, also known as IRF3, is an interferon regulatory factor. IRF3 is a member of the interferon regulatory transcription factor (IRF) family. IRF3 was originally discovered as a homolog of IRF1 and IRF2. IRF3 has been further characterized and shown to contain several functional domains including a nuclear export signal, a DNA-binding domain, a C-terminal IRF association domain and several regulatory phosphorylation sites. IRF3 is found in an inactive cytoplasmic form that upon serine/threonine phosphorylation forms a complex with CREBBP. The complex translocates into the nucleus for the transcriptional activation of interferons alpha and beta, and further interferon-induced genes.