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MXD1
MAD protein is a protein that in humans is encoded by the ''MXD1'' gene. MAD-MAX dimerization protein belongs to a subfamily of MAX-interacting proteins. This protein competes with MYC for binding to MAX to form a sequence-specific DNA-binding complex, acts as a transcriptional repressor (while MYC appears to function as an activator) and is a candidate tumor suppressor. Interactions MXD1 has been shown to interact with Histone deacetylase 2, SMC3 Structural maintenance of chromosomes protein 3 (SMC3) is a protein that in humans is encoded by the SMC3 gene. SMC3 is a subunit of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. Cohesi ..., MLX, SIN3A and MAX. References Further reading * * * * * * * * * * * * * * * * * External links * {{Transcription factors and intracellular receptors ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MAX (gene)
''MAX'' (also known as myc-associated factor X) is a gene that in humans encodes the MAX transcription factor. Function The protein product of ''MAX'' contains the basic helix-loop-helix and leucine zipper motifs. It is therefore included in the bHLHZ family of transcription factors. It is able to form homodimers with other MAX proteins and heterodimers with other transcription factors, including Mad, Mxl1 and Myc. The homodimers and heterodimers compete for a common DNA target site (the E-box) in a gene promoter zone. Rearrangement of dimers (e.g., Mad:Max, Max:Myc) provides a system of transcriptional regulation with greater diversity of gene targets. Max must dimerise in order to be biologically active. Transcriptionally active hetero- and homodimers involving Max can promote cell proliferation as well as apoptosis. Interactions The protein product of Max has been shown to interact with: * Myc, * MNT, * MSH2, * MXD1, * MXI1, * MYCL1, * N-Myc, * SPAG9, * TEAD1, and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Histone Deacetylase 2
Histone deacetylase 2 (HDAC2) is an enzyme that in humans is encoded by the ''HDAC2'' gene. It belongs to the histone deacetylase class of enzymes responsible for the removal of acetyl groups from lysine residues at the N-terminal region of the core histones (H2A, H2B, H3, and H4). As such, it plays an important role in gene expression by facilitating the formation of transcription repressor complexes and for this reason is often considered an important target for cancer therapy. Though the functional role of the class to which HDAC2 belongs has been carefully studied, the mechanism by which HDAC2 interacts with histone deacetylases of other classes has yet to be elucidated. HDAC2 is broadly regulated by protein kinase 2 (CK2) and protein phosphatase 1 (PP1), but biochemical analysis suggests its regulation is more complex (evinced by the coexistence of HDAC1 and HDAC2 in three distinct protein complexes). Essentially, the mechanism by which HDAC2 is regulated is still unclear b ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MLX (gene)
Max-like protein X is a protein that in humans is encoded by the ''MLX'' gene. Function The product of this gene belongs to the family of basic helix-loop-helix leucine zipper (bHLH-Zip) transcription factors. These factors form heterodimers with Mad proteins and play a role in proliferation, determination and differentiation. This gene product may act to diversify Mad family function by its restricted association with a subset of the Mad family of transcriptional repressors, namely Mad1 and Mad4. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. Interactions MLX (gene) has been shown to interact with MNT, MXD1 and MLXIPL. MLX must dimerize with MondoA or with MLXIPL (carbohydrate-responsive element-binding protein Carbohydrate-responsive element-binding protein (ChREBP) also known as MLX-interacting protein-like (MLXIPL) is a protein that in humans is encoded by the ''MLXIPL'' gene. The protein name derives from ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SIN3A
Paired amphipathic helix protein Sin3a is a protein that in humans is encoded by the ''SIN3A'' gene. Function The protein encoded by this gene is a transcriptional regulatory protein. It contains paired amphipathic helix (PAH) domains, which are important for protein-protein interactions and may mediate repression by the Mad-Max complex. Interactions SIN3A has been shown to interact with: * CABIN1 * HBP1, * HDAC1, * HDAC9, * Histone deacetylase 2, * Host cell factor C1, * IKZF1, * ING1, * KLF11, * MNT, * MXD1, * Methyl-CpG-binding domain protein 2, * Nuclear receptor co-repressor 2, * OGT, * PHF12, * Promyelocytic leukemia protein, * RBBP4, * RBBP7, * SAP130, * SAP30, * SMARCA2, * SMARCA4, * SMARCC1, * SUDS3, * TAL1, and * Zinc finger and BTB domain-containing protein 16. See also * Transcription coregulator In molecular biology and genetics, transcription coregulators are proteins that interact with transcription factors to either activate ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gene
In biology, the word gene (from , ; "...Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a basic unit of heredity and the molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protein-coding genes and noncoding genes. During gene expression, the DNA is first copied into RNA. The RNA can be directly functional or be the intermediate template for a protein that performs a function. The transmission of genes to an organism's offspring is the basis of the inheritance of phenotypic traits. These genes make up different DNA sequences called genotypes. Genotypes along with environmental and developmental factors determine what the phenotypes will be. Most biological traits are under the influence of polygenes (many different genes) as well as gen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SMC3 (gene)
Structural maintenance of chromosomes protein 3 (SMC3) is a protein that in humans is encoded by the SMC3 gene. SMC3 is a subunit of the Cohesin complex which mediates sister chromatid cohesion, homologous recombination and DNA looping. Cohesin is formed of SMC3, SMC1, RAD21 and either SA1 or SA2. In humans, SMC3 is present in all cohesin complexes whereas there are multiple paralogs for the other subunits. SMC3 is a member of the SMC protein family. Members of this family are key regulators of DNA repair, chromosome condensation and chromosome segregation. Structure and interactions The domain organisation of SMC proteins is evolutionarily conserved and is composed of an N-terminal Walker A motif, coiled-coil, "hinge", coiled-coil and a C-terminal Walker B motif. The protein folds back on itself to form a rod-shaped molecule with a heterodimerisation "hinge" domain at one end and an ABC-type ATPase "head" at the other. These globular domains are separated by a ~50 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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