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FLASH GENE
Symbol RNF135 contributors: mct - updated : 14-02-2023
HGNC name ring finger protein 135
HGNC id 21158
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • N-terminal RING finger domain,
  • a RING finger domain, involved in protein-protein and protein-DNA interactions
  • a B30.2/SPRY domain at the C terminus, and PRY motifs
  • a central coiled-coil domain,
  • a C-terminal P/SPRY domain
    • HOMOLOGY
    interspecies homolog to rattus Rnf135 (63.7 pc)
    homolog to murine Rnf135 (61.2 pc)
    Homologene
    FAMILY
  • zinc finger family
    • CATEGORY enzyme , tumor suppressor
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,cytosolic,granule
    basic FUNCTION
  • acting as an ubiquitin ligase
  • RNF135 is a novel factor of the DDX58 pathway involved in the evoking of human innate immunity against RNA virus infection, and activates DDX58 through ubiquitination of its C-terminal region
  • is an E3 ubiquitin ligase of DDX58 and specifically stimulates DDX58-mediated innate antiviral activity.
  • is essential for regulating DDX58-mediated innate immune response against RNA virus infection
  • involvement of RNF135 and ADAP2 in the increased risk of malignancy observed in NF1-microdeleted patients
  • biological effects of RNF135 in glioblastoma cell proliferation, migration and cell cycle, and its role in the progression of glioblastoma may be associated with the ERK signal transduction pathway
  • essential E3 ligase in antiviral immunity, that promotes the antiviral signaling activity of the viral RNA receptor DDX58 through both Ub-dependent and -independent manners
  • RNF135 functions as a tumor suppressor and is involved in tumor immune microenvironment in hepatocellular carcinoma
  • mediates retinoic acid-inducible gene-I polyubiquitination and is essential for viral-induced expression of type I IFNs in dendritic cells and macrophages
  • function of RNF135 in T cells, which is to suppress the antitumor immune response through modulating Th1 and CTLs
    • CELLULAR PROCESS protein, degradation
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    a component
    INTERACTION
    DNA
    RNA
    small molecule metal binding,
  • Zn2+
    • protein
  • interacting with DDX58
  • RNF135 was dispensable for DDX58 RNA binding activity but required for TRIM25 to activate DDX58
    • N-terminal RING finger domain, a central coiled-coil domain, and a C-terminal P/SPRY domain
  • play a central role in the activation of the retinoic acid-inducible gene I (DDX58), and is a novel ZAP cofactor
  • interacts with ZAP via its P/SPRY domain and the ubiquitin ligase activity of RNF135 is not required to stimulate ZAP-mediated virus inhibition
    • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) NF1DEL
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional     --low  
    in tumor Schwann cells from malignant peripheral nerve sheath tumors (MPNSTs) biopsies and in MPNST cell line
    tumoral       gain of function
    in glioblastoma tissues compared with normal brain (NB) tissues
    Susceptibility
    Variant & Polymorphism
    Candidate gene overgrowth
    Marker
    Therapy target
    ANIMAL & CELL MODELS