Target Name: TRIM5
NCBI ID: G85363
Review Report on TRIM5 Target / Biomarker Content of Review Report on TRIM5 Target / Biomarker
TRIM5
Other Name(s): tripartite motif-containing protein 5 alpha | TRIM5alpha | tripartite motif containing 5 transcript variant iota | Tripartite motif containing 5, transcript variant alpha | RING finger protein 88 | TRIM5_HUMAN | tripartite motif containing 5 | Tripartite motif-containing protein 5 (isoform alpha) | tripartite motif containing 5 transcript variant kappa | RING-type E3 ubiquitin transferase TRIM5 | TRIM5 variant alpha | RNF88 | ring finger protein 88 | Tripartite motif-containing protein 5 | tripartite motif protein TRIM5

TRIM5: A Protein with A Tripartite Motif and Potential Drug Targets

TRIM5, or Tripartite Motif-Containing Protein 5 Alpha, is a protein that is expressed in various tissues throughout the body, including the brain, heart, and kidneys. It is characterized by the presence of a tripartite motif, which is a specific type of protein structure that is composed of three distinct regions: an N-terminus, a central 尾-sheet, and an C-terminus.

The N-terminus of TRIM5 is a 20 amino acid residue region that contains a putative N-endopeptide. The central 尾-sheet is a 30 amino acid long region that is responsible for the protein's stability and functions as a structural unit. The C- terminus is a 20 amino acid long region that contains a putative C-endopeptide.

TRIM5 is a member of the protein family known as the TRIM proteins, which are involved in various cellular processes, including cell signaling, gene regulation, and protein-protein interactions. The TRIM5 protein is unique because of its tripartite motif, which is not found in many other proteins.

The tripartite motif is a specific type of protein structure that is composed of three distinct regions: an N-terminus, a central 尾-sheet, and an C-terminus. The N-terminus is a 20 amino acid residue region that contains a putative N-endopeptide. The central 尾-sheet is a 30 amino acid long region that is responsible for the protein's stability and functions as a structural unit. The C-terminus is a 20 amino acid long region that contains a putative C-endopeptide.

TRIM5 is expressed in various tissues throughout the body, including the brain, heart, and kidneys. It is involved in various cellular processes, including cell signaling, gene regulation, and protein-protein interactions.

One of the key functions of TRIM5 is its role in cell signaling. TRIM5 is involved in the regulation of cell signaling pathways, including the insulin/IGF-1 signaling pathway, the TGF-β signaling pathway, and the Wnt signaling pathway. This suggests that TRIM5 may be a drug target that can be targeted with therapies for various diseases, including diabetes, cancer, and neurodegenerative disorders.

Another function of TRIM5 is its role in gene regulation. TRIM5 is involved in the regulation of gene expression, including the regulation of gene expression in response to various environmental and cellular stressors. This suggests that TRIM5 may be a biomarker for various diseases, including neurodegenerative disorders and chronic diseases.

TRIM5 is also involved in protein-protein interactions. TRIM5 is a member of the TRIM family, which is involved in protein-protein interactions. This suggests that TRIM5 may be a drug target that can be targeted with therapies for various diseases, including cancer and neurodegenerative disorders.

In conclusion, TRIM5 is a protein that is characterized by the presence of a tripartite motif. TRIM5 is expressed in various tissues throughout the body and is involved in various cellular processes, including cell signaling, gene regulation, and protein-protein interactions. Its unique The tripartite motif makes TRIM5 a potential drug target for various diseases. Further research is needed to fully understand the functions of TRIM5 and its potential as a drug.

Protein Name: Tripartite Motif Containing 5

Functions: Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by N-tropic murine leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian immunodeficiency virus of macaques (SIVmac), feline immunodeficiency virus (FIV), and bovine immunodeficiency virus (BIV) (PubMed:17156811). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (PubMed:25127057). Also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction (PubMed:25127057)

The "TRIM5 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about TRIM5 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

More Common Targets

TRIM50 | TRIM51 | TRIM51EP | TRIM51G | TRIM51HP | TRIM52 | TRIM53AP | TRIM54 | TRIM55 | TRIM56 | TRIM58 | TRIM59 | TRIM59-IFT80 | TRIM6 | TRIM6-TRIM34 | TRIM60 | TRIM60P15 | TRIM61 | TRIM62 | TRIM63 | TRIM64 | TRIM64B | TRIM64C | TRIM65 | TRIM66 | TRIM67 | TRIM68 | TRIM69 | TRIM7 | TRIM7-AS2 | TRIM71 | TRIM72 | TRIM73 | TRIM74 | TRIM75 | TRIM77 | TRIM8 | TRIM9 | TRIML1 | TRIML2 | TRIO | TRIOBP | TRIP10 | TRIP11 | TRIP12 | TRIP13 | TRIP4 | TRIP6 | Tripartite motif containing 78, pseudogene | TRIQK | TRIR | TRIT1 | TRL-AAG1-2 | TRL-AAG2-3 | TRL-TAG2-1 | TRMO | TRMT1 | TRMT10A | TRMT10B | TRMT10C | TRMT11 | TRMT112 | TRMT12 | TRMT13 | TRMT1L | TRMT2A | TRMT2B | TRMT44 | TRMT5 | TRMT6 | TRMT61A | TRMT61B | TRMT9B | TRMU | TRN-GTT4-1 | TRNA | tRNA splicing endonuclease complex | tRNA(Sec) complex | tRNA-splicing endonuclease complex | tRNA-splicing ligase complex | TRNAU1AP | TRNC | TRND | TRNE | TRNF | TRNG | TRNH | TRNI | TRNK | TRNL1 | TRNL2 | TRNM | TRNN | TRNP | TRNP1 | TRNQ | TRNR | TRNS1 | TRNS2 | TRNT