TRAF2 Recombinant Rabbit Monoclonal Antibody - BSA and Azide free [SD205-06] (HA750297)

UNIPROT #

Q12933

PROTEIN NAME

TRAF2

SYNONYMS

E3 ubiquitin-protein ligase TRAF2 antibody;MGC:45012 antibody;OTTHUMP00000022625 antibody;OTTHUMP00000064745 antibody;TNF receptor associated factor 2 antibody;TNF receptor-associated factor 2 antibody;TNF receptor-associated protein antibody;TRAF 2 antibody;TRAF2 antibody;TRAF2_HUMAN antibody;TRAP 3 antibody;TRAP antibody;TRAP3 antibody;Tumor necrosis factor type 2 receptor associated protein 3 antibody;Tumor necrosis factor type 2 receptor-associated protein 3 antibody

SEQUENCE SIMILARITIES

Belongs to the TNF receptor-associated factor family. A subfamily.

POST-TRANSLATIONAL MODIFICATION

Phosphorylated at several serine residues within the first 128 amino acid residues. Phosphorylated at Thr-117 in response to signaling via TNF and TNFRSF1A. Phosphorylation at Thr-117 is required for 'Lys-63'-linked polyubiquitination, but not for 'Lys-48'-linked polyubiquitination. Phosphorylation at Thr-117 is important for interaction with IKKA and IKKB, activation of IKK and subsequent activation of NF-kappa-B.; Undergoes both 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination. Polyubiquitinated via 'Lys-63'-linked ubiquitin in response to TNF signaling; this requires prior phosphorylation at Thr-117. 'Lys-63'-linked polyubiquitination promotes TRAF2-mediated activation of NF-kappa-B. Can be polyubiquitinated at several Lys residues via 'Lys-48'-linked ubiquitin chains in response to TNF signaling, leading to proteasomal degradation. Autoubiquitinated, leading to its subsequent proteasomal degradation. Polyubiquitinated by BIRC2 and SIAH2, leading to its subsequent proteasomal degradation. Deubiquitinated by CYLD, a protease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Ubiquination is inhibited by LRRC19; inhibits proteasomal degradation.

SUBCELLULAR LOCATION

Cytoplasm.

FUNCTION

Tumor necrosis factor (TNF)-activated cell signaling is mediated primarily through the TNF receptor 1 (TNF-R1) and, to a lesser extent, TNF-R2. Both TNF receptors are members of the expanding TNF receptor superfamily, which includes the FAS antigen and CD40. Potential insight into an understanding of TNF receptor-mediated signaling was provided by the identification of two related proteins, TRAF1 and TRAF2 (for TNF receptor-associated factors 1 and 2, respectively). Both function to form heterodimeric complexes and associate with the cytoplasmic domain of TNF-R2. A third member of this protein family, alternatively designated CD40 bp, CRAF1, LAP1 or TRAF3, has been identified and shown to associate with the cytoplasmic domain of CD40. The similarity between a specific region of TRAF3 with regions of TRAF1 and TRAF2 define a “TRAF-C” domain that is necessary and sufficient for CD40 binding and homodimerization.