MGSSHHHHHH SSGLVPRGSH MSNVTASPTA PACPSDKPAP VQKPPSSGTS SEFEVVTPEE QNSPESSSHA NAMALGPLPR EDGNLMLHLQ RLETTLSVCA EEPDHGQLFT HLGRMALEFN RLASKVHKNE QRTSILQTLC EQLRKENEAL KAKLDKGLEQ RDQAAERLRE ENLELKKLLM SNGNKEGASG RPGSPKMEGT GKKAVAGQQQ ASVTAGKVPE VVALGAAEKK VKMLEQQRSE LLEVNKQWDQ HFRSMKQQYE QKITELRQKL ADLQKQVTDL EAEREQKQRD FDRKLLLAKS KIEMEETDKE QLTAEAKELR QKVKYLQDQL SPLTRQREYQ EKEIQRLNKA LEEALSIQTP PSSPPTAFGS PEGAGALLRK QELVTQNELL KQQVKIFEED FQRERSDRER MNEEKEELKK QVEKLQAQVT LSNAQLKAFK DEEKAREALR QQKRKAKA.
TNIP1 inhibits NF-κB activation and TNF-induced NF-κB-dependent gene expression by regulating the deubiquitination of IKBKG through its interaction with TAX1BP1 and A20/TNFAIP3 . This regulation is essential for controlling inflammation and preventing autoimmune diseases. TNIP1 also plays a role in the EGF-induced ERK1/ERK2 signaling pathway, which is involved in cell growth and differentiation .
TNIP1 is an intrinsically disordered protein, meaning it lacks a fixed or ordered three-dimensional structure under physiological conditions. This structural flexibility is contributed by its AHD1-UBAN domain, which allows TNIP1 to interact with various cellular, viral, and bacterial proteins . The AHD1-UBAN domain exists primarily as a pre-molten globule with limited secondary structure in solution, which may impact its function and interaction with multiple partners .
Research on TNIP1 has shown its involvement in various cellular processes and its potential as a therapeutic target. For instance, TNIP1’s interaction with the HIV-1 matrix protein suggests a role in viral replication and potential applications in antiviral therapies . Additionally, its regulation of leukocyte integrin activation during inflammation highlights its importance in immune response modulation .