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FLASH GENE
Symbol TRIM27 contributors: mct - updated : 30-04-2016
HGNC name tripartite motif-containing 27
HGNC id 9975
DNA
TYPE functioning gene
STRUCTURE 20.99 kb     8 Exon(s)
MAPPING cloned Y linked   status provisional
RNA
TRANSCRIPTS type messenger
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
8 - 2969 58.5 513 - 2013 23452853
  • RFP variant alpha,isoform alpha
  • distinct C terminus
  • - - 2700 40.8 358 - 2013 23452853
    EXPRESSION
    Type widely
       expressed in (based on citations)
    organ(s)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Endocrineparathyroid   highly
    Lymphoid/Immunelymph node   highly
    Urinarybladder   highly
    tissue
    SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
    Connectiveadipose  highly
    cell lineage
    cell lines
    fluid/secretion
    at STAGE
    PROTEIN
    PHYSICAL PROPERTIES
    STRUCTURE
    motifs/domains
  • a N terminal RING zinc
  • two B boxes domains linked to a leucine coiled-coil domain (RBCC) the so called tripartite domain (TRIM)
  • a C terminal B30-2-like (RFP) domain, also a SPRY domain
  • conjugated MetalloP
    HOMOLOGY
    Homologene
    FAMILY
  • B box family, RBCC (TRIM family)
  • C-IV TRIM family
  • CATEGORY transcription factor , protooncogene
    SUBCELLULAR LOCALIZATION     intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endosome
    intracellular,nucleus,nucleoplasm,nuclear bodies
    text contained in nuclear bodies (NB) associated with the nuclear matrix
    basic FUNCTION
  • activate with MCRS1 and CHD4 ribosomal gene transcription
  • is a previously undescribed negative regulator of CD4 T cells
  • is an important negative regulator of mast cells
  • TRIM27 affects NOD2-mediated pro-inflammatory responses
  • NOD2 and TRIM27 might functionally cooperate in the nucleus
  • tripartite motif (TRIM) protein containing, positively regulating TNF-induced apoptosis
  • works as a novel E3 ligase in the PAX7-mediated degradation of MYOD1 in response to skeletal muscle atrophy
  • CELLULAR PROCESS cell life, differentiation
    nucleotide, transcription
    cell organization/biogenesis
    PHYSIOLOGICAL PROCESS
    text
  • spermatogenesis
  • differentiation of male germ cells
  • PATHWAY
    metabolism
    signaling
    a component
  • E3 RING ubiquitin ligase, MAGEL2-TRIM27, localizes to endosomes through interactions with the retromer complex
  • ubiquitin ligase activity of MAGEL2-TRIM27 is important for proper retrograde transport
  • facilitates ITGA5 recycling, an important event in tumorigenesis
  • complexing with USP7 and ubiquitination-deubiquitination cascade mediated by the TRIM27-USP7 complex plays an important role in TNF-induced apoptosis
  • ZNF446, and its associated tripartite motif protein, TRIM27, are obligate components of the ZNF165-SMAD3 complex that also support tumor cell viability
  • INTERACTION
    DNA binding to the enhancer of polycomb protein (EPC1)
    RNA
    small molecule metal binding,
  • heavy metal
  • Zn2+
  • protein
  • interacting with CHD4 (involved in transcriptional repression in the nucleus, co-localize with MCRS1 in the nucleolus and appear to activate the rRNA transcription)
  • functions to negatively regulate KCNN4 channel activity and TCR-stimulated Ca2+ influx and cytokine production in activated CD4 T cells
  • TRIM27 functions as an E3 ligase and mediates lysine 48 polyubiquitination of PI3KC2B, leading to a decrease in PI3K enzyme activity
  • is a transcriptional repressor that interacts with, and attenuates senescence induction by, the retinoblastoma-associated protein (RB1)
  • TRIM27 functions as an E3 ligase to ubiquitinate and inhibit PI3KC2B kinase activity
  • both PI3KC2B and TRIM27 play critical but opposite roles in FCER1A-stimulated activation of KCNN4, Ca2+ influx, degranulation, and cytokine production in bone marrow mast cells
  • TRIM27 is a new specific binding partner for NOD2
  • TRIM27 was identified as a major binding partner of MAGEL2 and MAGEL2-TRIM27 is likely required for endosome-to-Golgi retrograde transport
  • works as an E3 ligase in PAX7-induced degradation of MYOD1
  • SIGLEC1 suppresses antiviral innate immune response by inducing TBK1 degradation via the ubiquitin ligase TRIM27
  • cell & other
    REGULATION
    repressed by IFN-gamma and LPS
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    tumoral fusion      
    TRIM-RET fusion in thyroid cancer
    constitutional     --over  
    in Crohn disease patients
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    SystemTypeDisorderPubmed
    immunologyinflammatory 
    could be a new target for therapeutic intervention in NOD2-associated diseases
    ANIMAL & CELL MODELS
  • Trim27-/- mice are more susceptible to acute anaphylaxis