TRAIP
Description
The TRAIP (TRAF interacting protein) is a protein-coding gene located on chromosome 3.
TRAIP (TRAF-interacting protein) is a protein encoded by the TRAIP gene in humans. It contains a RING finger motif and a coiled-coil domain. This protein interacts with TRAF1, TRAF2, and CYLD, and its interaction with TRAF2 inhibits NF-kappa-B activation. TRAIP is involved in mitotic DNA synthesis (MiDAS), a DNA repair mechanism that salvages incompletely replicated DNA during S phase, particularly in response to replication stress. TRAIP disassembles the replication complex at stalled forks, facilitating DNA repair. TRAIP interacts with FLII, TRAF1, and TRAF2.
TRAIP is an E3 ubiquitin ligase that plays a critical role in protecting genome stability during DNA replication. It functions in the repair of interstrand cross-links (ICLs) and DNA-protein cross-links (DPCs), ensuring proper replication and transcription. TRAIP also participates in translesion synthesis, a process that bypasses DNA lesions and maintains genomic integrity. It regulates the spindle assembly checkpoint and acts as a negative regulator of innate immune signaling by inhibiting NF-kappa-B activation and suppressing antiviral responses.
TRAIP is also known as RNF206, SCKL9, TRIP.