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Afadin
Afadin is a protein that in humans is encoded by the ''AFDN'' gene. Function Afadin is a Ras (see HRAS; MIM 190020) target that regulates cell–cell adhesions downstream of Ras activation. It is fused with MLL (MIM 159555) in leukemias caused by t(6;11) translocations (Taya et al., 1998). upplied by OMIMref name="entrez"> Interactions Afadin has been shown to interact with: * BCR gene, * EPHB3, * F11 receptor, * HRAS and * LMO2, * PVRL1, * PVRL3, * Profilin 1, * RAP1A, * RAP1GAP, * SORBS1, * SSX2IP, * Tight junction protein 1, and * USP9X Probable ubiquitin carboxyl-terminal hydrolase FAF-X is an enzyme that in humans is encoded by the ''USP9X'' gene. Function This gene is a member of the peptidase C19 family and encodes a protein that is similar to ubiquitin-specific protease .... References Further reading * * * * * * * * * * * * * * * * * * * {{PDB Gallery, geneid=4301 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PVRL3
Nectin-3, also known as nectin cell adhesion molecule 3, is a protein that in humans is encoded by the ''NECTIN3'' gene. Nectin-3 belongs to the family of immunoglobulin(Ig)-like cellular adhesion molecules involved in Ca2+-independent cellular adhesion in several tissues during the development and was firstly isolated at the turn of 20th and 21st century. Structure and localization Nectin-3 has three splicing variants, nectin-3α, which is the biggest one, nectin-3β and the smallest variant nectin-3γ. Nectin-3α (same as the other splicing variants) is abundately expressed in testis, on slightly lower level it is also expressed in heart, brain, liver or kidney. It has been also proved that nectin-3α is together with nectin-2 localize at the junctional complex regions in small intestina absorptive epithelia. Nectin-3γ is also detectable in lung, liver and kidney. Nectin-3 is expressed not only on epithelial cells as another nectins, but there was shown that, as the on ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PVRL1
Poliovirus receptor-related 1 (PVRL1), also known as nectin-1 and CD111 (formerly herpesvirus entry mediator C, HVEC) is a human protein of the immunoglobulin superfamily (IgSF), also considered a member of the nectins. It is a membrane protein with three extracellular immunoglobulin domains, a single transmembrane helix and a cytoplasmic tail. The protein can mediate Ca2+-independent cellular adhesion further characterizing it as IgSF cell adhesion molecule (IgSF CAM). Function PVRL1 is an adhesion molecule found in a wide range of tissues where it localizes in various junctions such as the adherens junction of epithelial tissue or the chemical synapse of neurons. The cytoplasmic tail of PVRL1 can bind the protein afadin which is a scaffolding protein that binds actin. In the chemical synapse PVRL1 interacts with PVRL3 (nectin-3) and both proteins can be found in neuronal tissue already in early stages of brain development as well as in aging brains. The two proteins hav ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SORBS1
CAP/Ponsin protein, also known as Sorbin and SH3 domain-containing protein 1 is a protein that in humans is encoded by the ''SORBS1'' gene. It is part of a small family of adaptor proteins that regulate cell adhesion, growth factor signaling and cytoskeletal formation. It is mainly expressed in heart, skeletal muscle, liver, adipose tissue, and macrophages; in striated muscle tissue, it is localized to costamere structures. Structure CAP/Ponsin may exist as thirteen alternatively-spliced isoforms, ranging from 81 kDa to 142 kDa. It is part of an adaptor protein family, of which ArgBP2 and vinexin are also a part. These proteins contain a conserved sorbin homology (SOHO) domain and three SH3 domains, and CAP/Ponsin is expressed in heart, skeletal muscle, liver, adipose tissue, and macrophages. Function In muscle, CAP/Ponsin plays a role in the formation of mature costameres from focal adhesion-like contacts during assembly of the contractile apparatus, as overexpression of CA ... [...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 residue (biochemistry), residues. Proteins perform a vast array of functions within organisms, including Enzyme catalysis, catalysing metabolic reactions, DNA replication, Cell signaling, responding to stimuli, providing Cytoskeleton, structure to cells and Fibrous protein, organisms, and Intracellular transport, transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the Nucleic acid sequence, nucleotide sequence of their genes, and which usually results in protein folding into a specific Protein structure, 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 pep ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Gene
In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. 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 non-coding genes. During gene expression (the synthesis of Gene product, RNA or protein from a gene), DNA is first transcription (biology), copied into RNA. RNA can be non-coding RNA, directly functional or be the intermediate protein biosynthesis, template for the synthesis of a protein. The transmission of genes to an organism's offspring, is the basis of the inheritance of phenotypic traits from one generation to the next. These genes make up different DNA sequences, together called a genotype, that is specific to every given individual, within the gene pool of the population (biology), population of a given species. The genotype, along with environmental and developmental factors, ultimately determines the phenotype ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
BCR Gene
The breakpoint cluster region protein (BCR) also known as renal carcinoma antigen NY-REN-26 is a protein that in humans is encoded by the ''BCR'' gene. ''BCR'' is one of the two genes in the ''BCR-ABL'' fusion protein, which is associated with the Philadelphia chromosome. Two transcript variants encoding different isoforms have been found for this gene. Function Although the BCR- ABL fusion protein has been much studied, the function of the normal BCR gene product is still not clear. The protein has serine/threonine kinase activity and is a guanine nucleotide exchange factor for the Rho family of GTPases including RhoA. Clinical significance A reciprocal translocation between chromosomes 22 and 9 produces the Philadelphia chromosome, which is often found in patients with chronic myelogenous leukemia. The chromosome 22 breakpoint for this translocation is located within the ''BCR'' gene. The translocation produces a fusion protein that is encoded by sequence from both ''BCR' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
EPHB3
Ephrin type-B receptor 3 is a protein that in humans is encoded by the ''EPHB3'' gene In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. 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: protei .... Function Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) f ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
F11 Receptor
Junctional adhesion molecule A is a protein that in humans is encoded by the ''F11R'' gene. It has also been designated as CD321 (cluster of differentiation 321). Function Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor. Multiple transcript variants encoding two different isoforms have been found for this gene. Interactions F11 receptor has been shown to interact with MLLT4, CASK and Tight junction protein 1 Tight junction protein ZO-1 also known as Zonula Occluden ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HRAS
GTPase HRas, from "Harvey Rat sarcoma virus", also known as transforming protein p21 is an enzyme that in humans is encoded by the gene. The ''HRAS'' gene is located on the short (p) arm of chromosome 11 (human), chromosome 11 at position 15.5, from base pair 522,241 to base pair 525,549. HRas is a small G protein in the Ras subfamily of the Ras superfamily of small GTPases. Once bound to Guanosine triphosphate, H-Ras will activate a Raf kinase like c-Raf, the next step in the MAPK/ERK pathway. Function GTPase HRas is involved in regulating cell division in response to growth factor stimulation. Growth factors act by binding cell surface Receptor (biochemistry), receptors that span the cell's plasma membrane. Once activated, receptors stimulate signal transduction events in the cytoplasm, a process by which proteins and second messengers relay signals from outside the cell to the cell nucleus and instructs the cell to grow or divide. The HRAS protein is a GTPase and is an earl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
LMO2
LIM domain only 2 (rhombotin-like 1), also known as LMO2, RBTNL1, RBTN2, RHOM2, LIM Domain Only Protein 2, TTG2, and T-Cell Translocation Protein 2, is a protein which in humans is encoded by the ''LMO2'' gene. Structure LMO2 is characterized as a small, cysteine-rich protein comprising two tandem LIM domains. Each LIM domain features a conserved double zinc finger motif, wherein zinc ions are coordinated by cysteine and histidine residues. These domains are critical for LMO2's primary function as a scaffolding protein facilitating protein-protein interactions within transcriptional regulatory complexes. Notably, LMO2 lacks an intrinsic DNA-binding domain; its influence on gene expression is mediated through its recruitment into multi-protein assemblies. The inter-domain linker region contributes to the protein's overall conformational dynamics, potentially modulating its interaction with diverse binding partners. The structural integrity conferred by the zinc fingers within the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Profilin 1
Profilin-1 is a protein that in humans is encoded by the ''PFN1'' gene. Structure The PFN1 protein, also known as profilin-1, is a small, monomeric protein composed of 139–140 amino acids with a molecular mass of approximately 15 kDa. Its three-dimensional structure features an antiparallel, seven-stranded β-sheet core flanked by three amphipathic α-helices—two on one side of the sheet and one on the other—forming a compact, globular fold known as the "profilin-like" fold. PFN1 contains three key functional domains: an actin-binding domain, a poly-L-proline (PLP)-binding domain, and a phosphoinositide-binding domain. These domains enable PFN1 to interact with actin monomers, polyproline-rich motifs in various cytoskeletal proteins, and phosphoinositides, respectively, facilitating its central role in actin cytoskeleton dynamics. Structural studies, including NMR and X-ray crystallography, have shown that PFN1’s binding sites for actin and PLP are distinct and flexibl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
