GRAIL is a type I transmembrane protein that localizes to the endocytic pathway and contains a PA (protease associated) domain and a RING-type zinc finger domain. It is a ubiquitin-protein isopeptide ligase (E3) necessary for the induction of CD4(+) T cell anergy in vivo and induced expression of this protein was observed in anergic CD4 (+) T cells, which suggested a role in the induction of anergic phenotype. It is differentially expressed in naturally occurring and peripherally induced CD25 (+) T regulatory cells and the expression is linked to the conversion of these cells to a regulatory phenotype. Expression of GRAIL in retrovirally transduced T cell hybridomas limits activation-induced IL-2 and IL-4 cytokine production. It also functions in the patterning of the dorsal ectoderm and sensitizes ectoderm to respond to neural-inducing signals.
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Protein Aliases: E3 ubiquitin-protein ligase RNF128; Gene related to anergy in lymphocytes protein; Goliath-related E3 ubiquitin-protein ligase 1; GRAIL; RING finger protein 128; RING-type E3 ubiquitin transferase RNF128; RP11-150F24.1
Gene Aliases: 1300002C13Rik; AI987883; GRAIL; Greul1; MNCb-3816; RGD1566282; RNF128