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Symbol TRIM5 contributors: mct - updated : 19-03-2020
HGNC name tripartite motif-containing 5
HGNC id 16276
Location 11p15.4      Physical location : 5.684.424 - 5.706.339
Synonym name
  • tripartite motif protein TRIM
  • RING finger protein 88
  • tripartite motif-containing protein 5 alpha
  • tripartite motif-containing protein 5
  • Synonym symbol(s) RNF88, TRIM5alpha, rNF88alpha
    EC.number 6.3.2.-/
    TYPE functioning gene
    SPECIAL FEATURE component of a cluster
    text clustered with TRIM6, TRIM21, TRIM22, TRIM34, and a TRIM pseudogene
    STRUCTURE 94.20 kb     8 Exon(s)
    10 Kb 5' upstream gene genomic sequence study
    regulatory sequence Promoter
    text structure a putative interferon-stimulated response element (ISRE)
    MAPPING cloned Y linked N status confirmed
    Map pter - D11S1760 - D11S4124 - TRIM5 - D11S1338 - D11S1323 - cen
    TRANSCRIPTS type messenger
    identificationnb exonstypebpproduct
    ProteinkDaAAspecific expressionYearPubmed
    8 splicing 3363 56.2 493 - 2018 30282803
  • isoform alpha
  • acts during the early postentry stages of the retroviral life cycle to block infection by a broad range of retroviruses, disrupting reverse transcription and integration
  • 7 splicing 3624 39.9 347 - 2018 30282803
  • isoform gamma
  • 8 splicing 1994 37.5 326 - 2018 30282803
  • isoform delta
  • interacting with BTBD1 and BTBD2
  • exhibiting ubiquitylation in the presence of UBCH5B, dependent on the presence of zinc-coordinating cysteines in the RING domain
       expressed in (based on citations)
    SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
    Cardiovascularvessel   moderately
    Digestivemouth   moderately
    Endocrinethyroid   moderately
    Lymphoid/Immunethymus   predominantly
    Reproductivefemale systemuterus  highly
    Urinarybladder   highly
    cell lineage
    cell lines
    at STAGE
  • a N terminal RING-type zinc finger
  • a B box-type zinc finger (type 2)
  • a C terminal B30.2/SPRY domain
    interspecies ortholog to TRIM5, Pan troglodytes
    ortholog to Trim5, Mus musculus
    ortholog to Trim5, Rattus norvegicus
    intraspecies paralog to TRIM6, TRIM34
  • TRIM/RBCC family
  • B box family
  • CATEGORY enzyme , immunity/defense
    SUBCELLULAR LOCALIZATION     intracellular
  • cytoplasmic bodies
  • ability of TRIM5 to shuttle into and out of the nucleus
  • basic FUNCTION
  • may act as an E3 ubiquitin ligase
  • potent inhibitor of infection by diverse retroviruses, modestly inhibits HIV1 strain carrying a mutation in the cyclophilin binding loop (Zhang 2006)
  • is an intrinsic immunity factor against HIV-1 infection, and arginine at 437 aa in SPRY domain for the late restriction is species-specific
  • a single amino acid substitution of the human immunodeficiency virus type 1 capsid protein affects viral sensitivity to TRIM5
  • promotes innate immune signalling and that this activity is amplified by retroviral infection and interaction with the capsid lattice
  • retrovirus restriction factor TRIM5 blocks post-entry infection of retroviruses in a species-specific manner
  • novel function for TRIM5 as a pattern recognition receptor in innate immune recognition
  • TRIM5 blocks retroviral replication after cell entry, and species-specific differences in its activity are determined by sequence variations within the C-terminal B30.2/PRYSPRY domain
  • importance of TRIM5 recruitment to the Plasma membrane for TRIM5-mediated innate immune sensing and restriction of retroviral infection
  • specific cytoskeleton structures involved in TRIM5 innate antiretroviral defenses
  • TRIM5 acts as a selective autophagy receptor, and delivered its cognate cytosolic target, a viral capsid protein, for autophagic degradation
  • is an antiviral factor that can greatly limit HIV-1 infection
  • is an interferon-inducible retroviral restriction factor that prevents infection by inducing the abortive disassembly of capsid cores recognized by its C-terminal PRY/SPRY domain
  • in the absence of a restriction-sensitive virus, TRIM5 is degraded by both proteasomal and autophagic degradation pathways
  • link between TRIM5 and components of the autophagosome
  • is a RING domain E3 ubiquitin ligase with potent antiretroviral function
  • TRIM5 initiates innate immune signaling and orchestrates disassembly of the viral particle
  • is an interferon inducible restriction factor which contributes to intrinsic defense against HIV infection by targeting the HIV capsid protein CA
  • CELLULAR PROCESS protein, ubiquitin dependent proteolysis
    PHYSIOLOGICAL PROCESS immunity/defense
    a component
    small molecule metal binding,
  • Zn2+
  • protein
  • unique function of TRIM5 is dependent on its association with the E2 ubiquitin-conjugating enzyme complex UBE2N-UBE2V1 and subsequent activation of the MAP3K7 complex and downstream genes involved in innate immune responses
  • TRIM5 is a SUMO1 and SUMO2 substrate, and SUMO machinery is involved in TRIM5-mediated retroviral restriction
  • MAP1LC3B binds to TRIM5 via the alpha-helical coiled-coil region
  • cell & other
    induced by interferons
    corresponding disease(s)
    Susceptibility to risk of HIV-1 infection
    Variant & Polymorphism SNP
  • polymorphism may influence susceptibility to HIV1 infection (Javanbakht 2006)
  • TRIM5 H43Y polymorphism is associated with a decreased risk of HIV-1 infection in the homozygote comparison and recessive model
  • Candidate gene
    Therapy target
    introduction of two aminoacid substitutions, R332G and R355G, in the TRIM5 domain responsible for retroviral capsid recognition leads to efficient HIV-1 restriction upon stable over-expression