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Tripartite Motif Containing 5 Proteins (TRIM5)

The protein encoded by TRIM5 is a member of the tripartite motif (TRIM) family. Additionally we are shipping TRIM5 Antibodies (153) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
TRIM5 85363 Q9C035
Mouse TRIM5 TRIM5 667823  
Rat TRIM5 TRIM5 308906  
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Top TRIM5 Proteins at

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Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
HOST_Escherichia coli (E. coli) Human His tag   50 μg Log in to see 5 Days
HOST_Escherichia coli (E. coli) Human His tag   10 μg Log in to see 11 Days
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
Yeast Pan paniscus His tag   1 mg Log in to see 56 to 66 Days
Yeast Pongo pygmaeus His tag   1 mg Log in to see 56 to 66 Days
Yeast Pongo abelii His tag   1 mg Log in to see 56 to 66 Days
Yeast Pan troglodytes His tag   1 mg Log in to see 56 to 66 Days
Yeast Saguinus oedipus His tag   1 mg Log in to see 56 to 66 Days
Yeast Primates His tag   1 mg Log in to see 56 to 66 Days

TRIM5 Proteins by Origin and Source

Origin Expressed in Conjugate
Human ,

More Proteins for Tripartite Motif Containing 5 (TRIM5) Interaction Partners

Rabbit Tripartite Motif Containing 5 (TRIM5) interaction partners

  1. The Sylvilagus TRIM5 alpha was 91% identical to the Oryctolagus protein.

Human Tripartite Motif Containing 5 (TRIM5) interaction partners

  1. Collectively, these results are consistent with observations that the turnover of TRIM5alpha proteins is sensitive to autophagy inhibition; however, the data presented here do not support observations that the inhibition of autophagy abrogates retroviral restriction by TRIM5 proteins.

  2. This meta-analysis indicates that TRIM5alpha H43Y polymorphism is associated with a decreased risk of HIV-1 infection in the homozygote comparison and recessive model.

  3. higher-order oligomerization of TRIM5alpha, which is promoted by the interaction with the retroviral capsid, enhances the E3 Ub ligase activity of TRIM5alpha and contributes to its antiretroviral function.

  4. TRIM5alpha requires Ube2W to anchor Lys63-linked ubiquitin chains and restrict reverse transcription.

  5. co-immunoprecipitation experiments demonstrate that IE1CORE binds via the coiled-coil domain to PML (show PML Proteins) and also interacts with TRIM5alpha

  6. TRIM5alpha variations influence transduction efficiency with lentiviral vectors in both human and rhesus CD34 (show CD34 Proteins)(+) cells in vitro and in vivo.

  7. TRIM5 acts as a selective autophagy receptor. Based on direct sequence-specific recognition, TRIM5 delivered its cognate cytosolic target, a viral capsid protein, for autophagic degradation. Thus, our study establishes that TRIMs can function both as regulators of autophagy and as autophagic cargo receptors, and reveals a basis for selective autophagy in mammalian cells.

  8. TRIM5alpha and TRIM22 (show TRIM22 Proteins) have differential transcriptional regulation and distinct anti-HIV roles according to infection phase.

  9. In conclusion, association with microtubules and the translocation activity of dynein motor complexes are required to achieve efficient retrovirus restriction by TRIM5alpha.

  10. Data report that markers in two TRIMs, TRIM5 and TRIM22 (show TRIM22 Proteins) and a marker in BST2 (show BST2 Proteins), associated statistically with the risk of getting MS.

Rhesus Monkey Tripartite Motif Containing 5 (TRIM5) interaction partners

  1. Mutations in gag and pol are associated with escape of HIV-1 from rhTrim5alpha.

  2. These studies provide direct evidence that ubiquitin conjugation to rhTRIM5alpha-containing complexes is required for inhibition of HIV-1 Reverse Transcription and Capsid Destabilization.

  3. These results confirm that the SUMO machinery is involved in TRIM5alpha-mediated retroviral restriction, and demonstrate that TRIM5alpha is a SUMO 1 (show SUMO1 Proteins) and SUMO 2 (show SUMO2 Proteins) substrate.

  4. These data show that there could be some distinct HIV-1 capsid patterns to confer significant resistance to rhesus TRIM5-alpha.

  5. Authors found that TRIM5alpha restriction significantly delayed disease progression and improved the survival rate of simian immunodeficiency virus-infected macaques.

  6. Analysis of TRIM genotype revealed a potential role for TRIM in disease development in the central nervous system. 5 of 5 animals with the permissive TRIM5alpha genotype (TRIMQ/Q) progressed to Simian Immunodeficiency Virus Encephalitis. In contrast, 2 animals with the restrictive TRIM5alpha genotype (TRIMTFP/TFP) did not show neurologic signs, nor did they develop SIVE.

  7. Rhesus TRIM5alpha acts as an autophagic receptor to restrict HIV-1 through autophagic degradation.

  8. In conclusion, the TRIM5alpha sumoylation site appears to modulate the E3 ubiquitin ligase activities of the adjacent RING domain, promoting K63-linked ubiquitin chains at the expense of auto-ubiquitylation which is probably K48-linked.

  9. The antiparallel organization of the NtD regions of Fv1 and Trim5alpha dimers correctly positions C-terminal specificity and N-terminal effector domains and facilitates stable binding to adjacent capsid hexamers in viral cores.

  10. Taken together, it is likely that rhTRIM5alpha cytoplasmic bodies are involved in recruiting components of the ubiquitin-proteasome system to coordinate proteasomal destruction of a viral or cellular protein(s) during restriction of HIV-1.

Chimpanzee Tripartite Motif Containing 5 (TRIM5) interaction partners

  1. TRIM5alpha protein functionally resembled human TRIM5alpha, potently restricting infection by N-tropic murine leukemia virus (N-MLV) and moderately restricting human immunodeficiency virus type 1 (HIV-1) infection

  2. SPRY domain of TRIM5alpha showed higher nonsynon/synonymous substitution ratios than the non-SPRY domain, indicating that the adaptive evolution of TRIM5alpha might be a strategy developed in defending retrovirus infection during primate evolution.

TRIM5 Protein Profile

Protein Summary

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein forms homo-oligomers via the coilel-coil region and localizes to cytoplasmic bodies. It appears to function as a E3 ubiquitin-ligase and ubiqutinates itself to regulate its subcellular localization. It may play a role in retroviral restriction. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene.

Gene names and symbols associated with TRIM5

  • tripartite motif-containing 5 (TRIM5)
  • tripartite motif containing 5 (TRIM5)
  • tripartite motif-containing 5 (Trim5)
  • EG667823 protein
  • Gm8833 protein
  • RGD1304579 protein
  • RNF88 protein
  • TRIM5 protein
  • TRIM5alpha protein

Protein level used designations for TRIM5

tripartite motif-containing 5 , TRIM5alpha , tripartite motif-containing 5 alpha , tripartite motif-containing protein 5 , tri-partite motif protein 5 , ring finger protein 88 , tripartite motif containing 5 transcript variant iota , tripartite motif containing 5 transcript variant kappa , tripartite motif protein TRIM5 , tripartite motif-containing protein 5 isoform alpha , TRIM5 alpha

100126072 Oryctolagus cuniculus
100126714 Papio anubis
100302544 Felis catus
85363 Homo sapiens
574288 Macaca mulatta
100984455 Pan paniscus
100137088 Pongo abelii
503563 Pan troglodytes
667823 Mus musculus
308906 Rattus norvegicus
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