TRIM16

The protein encoded by this gene is a tripartite motif (TRIM) family member that contains two B box domains and a coiled-coiled region that are characteristic of the B box zinc finger protein family. While it lacks a RING domain found in other TRIM proteins, the encoded protein can homodimerize or heterodimerize with other TRIM proteins and has E3 ubiquitin ligase activity. This gene is also a tumor suppressor and is involved in secretory autophagy. [provided by RefSeq, Jan 2017]

Full Name

TRIM16 Gene(Protein Coding) Tripartite Motif Containing 16

Function

E3 ubiquitin ligase that plays an essential role in the organization of autophagic response and ubiquitination upon lysosomal and phagosomal damages. Plays a role in the stress-induced biogenesis and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2 signaling and particularly by modulating the ubiquitination levels and thus stability of NRF2. Acts as a scaffold protein and facilitates autophagic degradation of protein aggregates by interacting with p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell against oxidative stress-induced cell death as a consequence of endomembrane damage.

Biological Process

Biological Process histone H3 acetylation Source:UniProtKB1 Publication
Biological Process histone H4 acetylation Source:UniProtKB1 Publication
Biological Process positive regulation of DNA-templated transcription Source:UniProtKB2 Publications
Biological Process positive regulation of interleukin-1 beta production Source:UniProtKB1 Publication
Biological Process positive regulation of keratinocyte differentiation Source:UniProtKB1 Publication
Biological Process positive regulation of retinoic acid receptor signaling pathway Source:UniProtKB1 Publication
Biological Process response to growth hormone Source:UniProtKB1 Publication
Biological Process response to organophosphorus Source:UniProtKB1 Publication
Biological Process response to retinoic acid Source:UniProtKB1 Publication

Cellular Location

Cytoplasm

PTM

Phosphorylated by ULK1.
Auto-ubiquitinates via its B-Boxes.