| Modification Notes |
GRAIL, also known as ring finger protein 128, is a 428 amino acid type I transmembrane protein localized to the intracytoplasmic membrane. GRAIL contains a protease-associated (PA) domain and a RING finger domain, which binds to E2 ubiquitin-conjugating enzymes. When under anergic conditions, GRAIL functions as an E3 ubiquitin-protein ligase that inhibits IL-2, IL-4 and various other cytokines. GRAIL is also thought to be involved in the patterning of the dorsal ectoderm during development. Expressed in an asymmetric perinuclear punctate manner, GRAIL colocalizes with Rab 7, GRP 78 and Syntaxin 5. GRAIL is expressed as 2 isoforms produced by alternative splicing. |