P120-catenin
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P120-catenin
p120, and called catenin delta-1 is a protein that in humans is encoded by the CTNND1 gene. Function This gene encodes a member of the Armadillo protein family, which function in adhesion between cells and signal transduction. Multiple translation initiation codons and alternative splicing result in many different isoforms being translated. Not all of the full-length natures of the described transcript variants have been determined. Clinical significance Either loss or cytoplasmic localization of p120 is a common feature in the progression of several types of carcinoma. Interactions CTNND1 has been shown to interact with: * Beta-catenin, * CDH1, * CDH2, * Collagen, type XVII, alpha 1, * Cortactin, * FYN, * MUC1, * Nephrin, * PSEN1, * PTPN6, * PTPRJ, * PTPRM, * VE-cadherin, * YES1, and * ZBTB33 See also * Delta catenin * Catenin * CTNND2 Delta-1-catenin and Delta-2-catenin are members of a subfamily of proteins with ten Armadillo-repeats. Delta-2-cate ...
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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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Nephrin
Nephrin is a protein necessary for the proper functioning of the renal filtration barrier. The renal filtration barrier consists of fenestrated endothelial cells, the glomerular basement membrane, and the podocytes of epithelial cells. Nephrin is a transmembrane protein that is a structural component of the slit diaphragm. They are present on the tips of the podocytes as an intricate mesh and convey strong negative charges which repel protein from crossing into the Bowman's space. A defect in the gene for nephrin, NPHS1, is associated with congenital nephrotic syndrome of the Finnish type and causes massive amounts of protein to be leaked into the urine, or proteinuria. Nephrin is also required for cardiovascular development. Interactions Nephrin has been shown to interact with: * CASK, * CD2AP, * CDH3 and * CTNND1, * FYN, * KIRREL, and * NPHS2. See also * Podocyte Podocytes are cells in Bowman's capsule in the kidneys that wrap around capillaries of the glomerul ...
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CTNND2
Delta-1-catenin and Delta-2-catenin are members of a subfamily of proteins with ten Armadillo-repeats. Delta-2-catenin is expressed in the brain where it is important for normal cognitive development. Like beta-catenin and gamma-catenin, delta-catenins seem to interact with Presenilins. These catenin-presenilin interaction have implications for cadherin function and regulation of cell-to-cell adhesion. While beta-catenin acts as a transcription regulatory protein in the Wnt/TCF pathway, delta-catenin 1 has been implicated as a regulator of the NF-κB transcription factor. Palmitoylation of delta-catenin seems to coordinate activity-dependent changes in synaptic adhesion molecules, synapse structure, and receptor localizations that are involved in memory formation. References See also *Catenin *CTNND1 p120, and called catenin delta-1 is a protein that in humans is encoded by the CTNND1 gene. Function This gene encodes a member of the Armadillo protein family, which func ...
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Catenin
Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified became known as α-catenin and β-catenin. α-Catenin can bind to β-catenin and can also bind filamentous actin (F-actin). β-Catenin binds directly to the cytoplasmic tail of classical cadherins. Additional catenins such as γ-catenin and δ-catenin have been identified. The name "catenin" was originally selected ('catena' means 'chain' in Latin) because it was suspected that catenins might link cadherins to the cytoskeleton. Types * α-catenin * β-catenin *γ-catenin * δ-catenin All but α-catenin contain armadillo repeats. They exhibit a high degree of protein dynamics, alone or in complex. Function Several types of catenins work with N-cadherins to play an important role in learning and memory. Cell-cell adhesion complexes are required for simple epithelia in higher organisms to maintain structure, function and pola ...
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Delta Catenin
Delta-1-catenin and Delta-2-catenin are members of a subfamily of proteins with ten Armadillo-repeats. Delta-2-catenin is expressed in the brain where it is important for normal cognitive development. Like beta-catenin and gamma-catenin, delta-catenins seem to interact with Presenilins. These catenin-presenilin interaction have implications for cadherin function and regulation of cell-to-cell adhesion. While beta-catenin acts as a transcription regulatory protein in the Wnt/TCF pathway, delta-catenin 1 has been implicated as a regulator of the NF-κB transcription factor. Palmitoylation of delta-catenin seems to coordinate activity-dependent changes in synaptic adhesion molecules, synapse structure, and receptor localizations that are involved in memory formation. References See also *Catenin *CTNND1 p120, and called catenin delta-1 is a protein that in humans is encoded by the CTNND1 gene. Function This gene encodes a member of the Armadillo protein family, which fun ...
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ZBTB33
Transcriptional regulator Kaiso is a protein that in humans is encoded by the ''ZBTB33'' gene. This gene encodes a transcriptional regulator with bimodal DNA-binding specificity, which binds to methylated CGCG and also to the non-methylated consensus KAISO-binding site TCCTGCNA. The protein contains an N-terminal POZ/BTB domain and 3 C-terminal zinc finger motifs. It recruits the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. It may contribute to the repression of target genes of the Wnt signaling pathway, and may also activate transcription of a subset of target genes by the recruitment of catenin delta-2 (CTNND2). Its interaction with catenin delta-1 (CTNND1) inhibits binding to both methylated and non-methylated DNA. It also interacts directly with the nuclear import receptor Importin-α2 (also known as karyopherin alpha2 or RAG cohort 1), which may mediate nuclear import of this protein. Alt ...
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YES1
Proto-oncogene tyrosine-protein kinase Yes is a non-receptor tyrosine kinase A non-receptor tyrosine kinase (nRTK) is a cytosolic enzyme that is responsible for catalysing the transfer of a phosphate group from a nucleoside triphosphate donor, such as ATP, to tyrosine residues in proteins. Non-receptor tyrosine kinases a ... that in humans is encoded by the ''YES1'' gene. This gene is the cellular homolog of the Yamaguchi sarcoma virus oncogene. The encoded protein has tyrosine kinase activity and belongs to the Src family kinase, src family. This gene lies in close proximity to thymidylate synthase gene on chromosome 18, and a corresponding pseudogene has been found on chromosome 22. Interactions YES1 has been shown to Protein-protein interaction, interact with Janus kinase 2, CTNND1, RPL10 and Occludin. References Further reading * * * * * * * * * * * * * * * * External links

* {{gene-18-stub ...
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VE-cadherin
Cadherin 5, type 2 or VE-cadherin (vascular endothelial cadherin) also known as CD144 ( Cluster of Differentiation 144), is a type of cadherin. It is encoded by the human gene ''CDH5''. Function VE-cadherin is a classical cadherin from the cadherin superfamily and the gene is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. The encoded protein is a calcium-dependent cell–cell adhesion glycoprotein composed of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Functioning as a classic cadherin by imparting to cells the ability to adhere in a homophilic manner, the protein may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. Integrity of intercellular junctions is a major determinant of permeability of the endothelium, and the VE-cadheri ...
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PTPRM
Receptor-type tyrosine-protein phosphatase mu is an enzyme that in humans is encoded by the ''PTPRM'' gene. Function The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. Protein tyrosine phosphatases are protein enzymes that remove phosphate moieties from tyrosine residues on other proteins. Tyrosine kinases are enzymes that add phosphates to tyrosine residues, and are the opposing enzymes to PTPs. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. PTPs can be both cytosolic and transmembrane. Structure Transmembrane PTPs are known as receptor protein tyrosine phosphatases (RPTPs). RPTPs are single pass transmembrane proteins usually with one or two catalytic domains in their intracellular domain (the part of the protein that is inside the cell) and diverse extracellular structures (the part of the protein that i ...
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PTPRJ
Receptor-type tyrosine-protein phosphatase eta is an enzyme that in humans is encoded by the ''PTPRJ'' gene. Function The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region containing five fibronectin type III repeats, a single transmembrane region, and a single intracytoplasmic catalytic domain, and thus represents a receptor-type PTP. This PTP is present in all hematopoietic lineages, and was shown to negatively regulate T cell receptor signaling possibly through interfering with the phosphorylation of Phospholipase C Gamma 1 (PLCG1) and Linker for Activation of T Cells (LAT). This PTP was also found to dephosphorylate PDGF beta receptor, and may be involved in UV-induced signal transduction. Interactions PTPRJ has been sho ...
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PTPN6
Tyrosine-protein phosphatase non-receptor type 6, also known as Src homology region 2 domain-containing phosphatase-1 (SHP-1), is an enzyme that in humans is encoded by the ''PTPN6'' gene. Function The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. N-terminal part of this PTP contains two tandem Src homolog ( SH2) domains, which act as protein phospho-tyrosine binding domains, and mediate the interaction of this PTP with its substrates. This PTP is expressed primarily in hematopoietic cells, and functions as an important regulator of multiple signaling pathways in hematopoietic cells. This PTP has been shown to interact with, and dephosphorylate a wide spectrum of phospho-proteins involved in hematopoietic cell signaling, (e.g., the LYN-CD22-SHP-1 pathway). Multiple ...
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PSEN1
Presenilin-1 (PS-1) is a presenilin protein that in humans is encoded by the ''PSEN1'' gene. Presenilin-1 is one of the four core proteins in the gamma secretase complex, which is considered to play an important role in generation of amyloid beta (Aβ) from amyloid-beta precursor protein (APP). Accumulation of amyloid beta is associated with the onset of Alzheimer's disease. Structure Presenilin possesses a 9 transmembrane domain topology, with an extracellular C-terminus and a cytosolic N-terminus. Presenilin undergoes endo-proteolytic processing to produce ~27-28 kDa N-terminal and ~16-17 kDa C-terminal fragments in humans. Furthermore, presenilin exists in the cell mainly as a heterodimer of the C-terminal and N-terminus fragments. When presenilin 1 is overexpressed, the full length protein accumulates in an inactive form. Based on evidence that a gamma-secretase inhibitor binds to the fragments, the cleaved presenilin complex is considered to be the active form. Function ...
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