E3 ubiquitin-protein ligase RNF128; RING finger protein 128; gene related to anergy in lymphocytes protein (RNF128, GRAIL)

Function: 1) E3 ubiquitin-protein ligase, catalyzes formation of polyubiquitin chains 2) inhibitor of cytokine gene transcription - inhibits IL2 & IL4 transcription via E3 ligase activity 3) induction of the anergic phenotyp 4) patterning of dorsal ectoderm - sensitizes ectoderm to neural-inducing signals 5) ubiquitin conjugation, 3rd step 6) induced under anergic conditions 7) up-regulated during T cell anergy induction following signaling through the T cell antigen receptor 8) binds to E2 ubiquitin-conjugating enzyme - requires intact RING finger 9) auto-ubiquitinated 10) controls the development of T cell clonal anergy by ubiquitination Structure: - contains 1 PA domain (protease associated) domain) contains 1 RING-type zinc finger Compartment: - intracytoplasmic membrane, perinuclear region - localized in an asymmetric perinuclear punctate manner - localizes to the internal pool of the transferrin recycling endosomal pathway - partially colocalized with endoplasmic reticulum resident HSPA5, with Golgi resident STX5, & with the late endosomal GTPase RAB7 Alternative splicing: named isoforms=2

General

glycoprotein ring finger protein E3 ubiquitin ligase; ubiquitin-ligating enzyme E3; N end-recognizing protein

Properties

SIZE: MW = 47 kD entity length = 428 aa COMPARTMENT: cytoplasm cell nucleus golgi endoplasmic reticulum endosome MOTIF: signal sequence {1-38} N-glycosylation site {N48} N-glycosylation site {N59} PA {75-183} MOTIF: N-glycosylation site {N101} transmembrane domain {208-228} RING-finger {277-318} EFFECTOR-BOUND: Zn+2 FOR-BINDING-OF: DNA motif

Database Correlations

OMIM 300439 UniProt Q8TEB7 PFAM correlations

References

UniProt :accession Q8TEB7