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Tripartite Motif Family
The tripartite motif family (TRIM) is a protein family. Function Many TRIM proteins are induced by interferons, which are important component of resistance to pathogens and several TRIM proteins are known to be required for the restriction of infection by lentiviruses. TRIM proteins are involved in pathogen-recognition and by regulation of transcriptional pathways in host defence. Structure The tripartite motif is always present at the N-terminus of the TRIM proteins. The TRIM motif includes the following three domains: * (1) a RING finger domain * (2) one or two B-box zinc finger domains ** when only one B-box is present, it is always a type-2 B-box ** when two B-boxes are present the type-1 B-Box always precedes the type-2 B-Box * (3) coiled coil region The C-terminus of TRIM proteins contain either: * Group 1 proteins: a C-terminal domain selected from the following list: ** NHL and IGFLMN domains, either in association or alone ** PHD domain associated with a bromodomain ** ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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TRIM33
E3 ubiquitin-protein ligase TRIM33, also known as (ectodermin homolog and tripartite motif-containing 33) is a protein encoded in the human by the gene ''TRIM33'', a member of the tripartite motif family. TRIM33 is thought to be a transcriptional corepressor. However unlike the related TRIM24 and TRIM28 proteins, few transcription factors such as SMAD4 that interact with TRIM33 have been identified. Structure The protein is a member of the tripartite motif family. This motif includes three zinc-binding domains: * RING * B-box type 1 zinc finger * B-box type 2 zinc finger and a coiled-coil region. Three alternatively spliced transcript variants for this gene have been described, however, the full-length nature of one variant has not been determined. Interactions TRIM33 has been shown to interact with TRIM24. Role in cancer ''TRIM33'' acts as a tumor suppressor gene preventing the development chronic myelomonocytic leukemia. TRIM33 regulates also the TRIM28 receptor and p ...
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TRIM29
Tripartite motif-containing protein 29 is a protein that in humans is encoded by the ''TRIM29'' gene. Function The protein encoded by this gene belongs to the TRIM protein family. It has multiple zinc finger motifs and a leucine zipper motif. It has been proposed to form homo- or heterodimers which are involved in nucleic acid binding. Thus, it may act as a transcriptional regulatory factor involved in carcinogenesis and/or differentiation. It may also function in the suppression of radiosensitivity since it is associated with ataxia–telangiectasia phenotype. Interactions TRIM29 has been shown to interact Advocates for Informed Choice, dba interACT or interACT Advocates for Intersex Youth, is a 501(c)(3) nonprofit organization using innovative strategies to advocate for the legal and human rights of children with intersex traits. The organizati ... with TRIM23 and GCC1. References Further reading

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TRIM25
Tripartite motif-containing protein 25 is a protein that in humans is encoded by the ''TRIM25'' gene. Function The protein encoded by this gene is a member of the tripartite motif (TRIM) family grouping more than 70 TRIMs. TRIM proteins primarily function as ubiquitin ligases that regulate the innate response to infection. TRIM25 localizes to the cytoplasm. The presence of potential DNA-binding and dimerization-transactivation domains suggests that this protein may act as a transcription factor, similar to several other members of the TRIM family. Expression of the gene is upregulated in response to estrogen, and it is thought to mediate estrogen actions in breast cancer as a primary response gene. Domain Architecture TRIM25 has an N-terminal RING domain, followed by a B-box type 1 domain, a B-box type 2 domain, a coiled-coil domain (CCD) and a C-terminal SPRY domain. The RING domain coordinates two zinc atoms and is essential for recruiting ubiquitin-conjugating enzymes. Th ...
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TRIM18
MID1 is a protein that belongs to the Tripartite motif family (TRIM) and is also known as TRIM18. The ''MID1'' gene is located on the short arm of the X chromosome and loss-of-function mutations in this gene are causative of the X-linked form of a rare developmental disease, Opitz G/BBB Syndrome. The ''MID1'' gene and its product The human ''MID1'' gene is located on the short arm of the X chromosome (Xp22.2) and includes 9 coding exons, spanning approximately 400 kb of the genome. Upstream to the first coding exon, the ''MID1'' gene employs alternative 5’ untranslated exons and at least five alternative promoters that drive the transcription of the gene, resulting in several ''MID1'' transcript isoforms. The ''MID1'' gene encodes a 667 amino acid protein that belongs to the TRIM family. MID1 protein consists of a conserved N-terminal tripartite module composed of a RING domain, 2 B-Box domains (B-box 1 and B-box 2) and a coiled-coil region. Within the TRIM family, MID1 belon ...
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TRIM16
Tripartite motif-containing protein 16 is a protein that in humans is encoded by the ''TRIM16'' gene. This gene was identified as an estrogen and anti-estrogen regulated gene in epithelial cells stably expressing estrogen receptor. The protein encoded by this gene contains two B box domains and a coiled-coiled region that are characteristic of the B box zinc finger protein family. The proteins of this family have been reported to be involved in a variety of biological processes including cell growth, differentiation and pathogenesis Pathogenesis is the process by which a disease or disorder develops. It can include factors which contribute not only to the onset of the disease or disorder, but also to its progression and maintenance. The word comes from Greek πάθος ''pat .... Expression of this gene was detected in most tissues. Its function, however, has not yet been determined. References Further reading

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TRIM14
Tripartite motif-containing 14 is a protein encoded by the TRIM14 gene in the human genome. It belongs to the TRIM family of proteins which contain the TRIM motif on the N-terminus. TRIM14 lacks the RING domain within the motif and therefore it loses the function of E3 ubiquitin ligase in eukaryotic cells. Instead, the PRYSPRY domain on the C-terminus allows TRIM14 to be categorized into an evolutionarily younger group of TRIM proteins which are involved in the regulation of innate immunity. TRIM 14 is localized in both the cytoplasm and the cell nucleus. Function TRIM14 acts in cell proliferation, differentiation, morphogenesis, autophagy and in the initiation of the anti-viral immune response by innate immunity. Overexpression of TRIM14 in mouse embryonic stem cells (mESC) leads to upregulation of several genes (hsp90ab1, prr13, pu.1, tnfrsf13c (baff-r), tnfrsf13b (taci), hlx1, hbp1, junb and pdgfrb) which are involved in early stage differentiation of embryonic stem cells, in th ...
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TRIM12
Midline-2 is a protein that in humans is encoded by the ''MID2'' gene. Function 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 localizes to microtubular structures in the cytoplasm. Its function has not been identified. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Recent reports indicate the involvement of MID2 in cytokinesis .MID2 (TRIM1) ubiquitinates Sperm-associated antigen 5 (Astrin) on K409, further promoting its degradation and proper cytokinesis. In contrary, depletion of MID2 (TRIM1) stabilizes Sperm-associated antigen 5 (Astrin) whose inappropriate accumulation at the midbody triggers cytokinetic arrest, multinucleated cells, and cell death. Interactions MID2 has been shown to interact with MID1. MID2 (TRIM1) interacts with Leucine-rich repea ...
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TRIM9
Tripartite motif-containing protein 9 is a protein that in humans is encoded by the ''TRIM9'' gene. 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 localizes to cytoplasmic bodies. Its function has not been identified. Alternate splicing of this gene generates two transcript variants encoding different isoforms. Interactions TRIM9 has been shown to interact with SNAP-25 Synaptosomal-Associated Protein, 25kDa (SNAP-25) is a Target Soluble NSF (''N''-ethylmaleimide-sensitive factor) Attachment Protein Receptor ( t-SNARE) protein encoded by the ''SNAP25'' gene found on chromosome 20p12.2 in humans. SNAP-25 is a com .... References Further reading

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TRIM3
Tripartite motif-containing protein 3 is a protein that in humans is encoded by the ''TRIM3'' gene. The protein encoded by this gene is a member of the tripartite motif (TRIM) family, also called the 'RING-B-box-coiled-coil' (RBCC) subgroup of RING finger proteins. 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. This protein localizes to cytoplasmic filaments. It is similar to a rat protein which is a specific partner for the tail domain of myosin V, a class of myosins which are involved in the targeted transport of organelles. The rat protein can also interact with alpha-actinin-4. Thus it is suggested that this human protein may play a role in myosin V-mediated cargo transport. Alternatively spliced transcript variants encoding the same isoform have been identified. Interactions TRIM3 has been shown to interact with Actinin alpha 4. TRIM3 binds to and ubiquitinates Estrogen receptor alpha (ERa) leading ...
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