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YAP (protein)
YAP1 (yes-associated protein 1), also known as YAP or YAP65, is a protein that acts as a transcription coregulator that promotes transcription of genes involved in cellular proliferation and suppressing apoptotic genes. YAP1 is a component in the hippo signaling pathway which regulates organ size, regeneration, and tumorigenesis. YAP1 was first identified by virtue of its ability to associate with the SH3 domain of Yes and Src protein tyrosine kinases. ''YAP1'' is a potent oncogene, which is amplified in various human cancers. Structure Cloning of the YAP1 gene facilitated the identification of a modular protein domain, known as the WW domain. Two splice isoforms of the YAP1 gene product were initially identified, named YAP1-1 and YAP1-2, which differed by the presence of an extra 38 amino acids that encoded the WW domain. Apart from the WW domain, the modular structure of YAP1 contains a proline-rich region at the very amino terminus, which is followed by a TID (TEAD transcr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transcription Coregulator
In molecular biology and genetics, transcription coregulators are proteins that interact with transcription factors to either activate or repress the transcription of specific genes. Transcription coregulators that activate gene transcription are referred to as coactivators while those that repress are known as corepressors. The mechanism of action of transcription coregulators is to modify chromatin structure and thereby make the associated DNA more or less accessible to transcription. In humans several dozen to several hundred coregulators are known, depending on the level of confidence with which the characterisation of a protein as a coregulator can be made. One class of transcription coregulators modifies chromatin structure through covalent modification of histones. A second ATP dependent class modifies the conformation of chromatin. Histone acetyltransferases Nuclear DNA is normally tightly wrapped around histones rendering the DNA inaccessible to the general transc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Transactivation Domain
The transactivation domain or trans-activating domain (TAD) is a transcription factor scaffold domain which contains binding sites for other proteins such as transcription coregulators. These binding sites are frequently referred to as activation functions (AFs). TADs are named after their amino acid composition. These amino acids are either essential for the activity or simply the most abundant in the TAD. Transactivation by the Gal4 transcription factor is mediated by acidic amino acids, whereas hydrophobic residues in Gcn4 play a similar role. Hence, the TADs in Gal4 and Gcn4 are referred to as acidic or hydrophobic, respectively. In general we can distinguish four classes of TADs: * acidic domains (called also “acid blobs” or “negative noodles", rich in D and E amino acids, present in Gal4, Gcn4 and VP16). * glutamine-rich domains (contains multiple repetitions like "QQQXXXQQQ", present in SP1) * proline-rich domains (contains repetitions like "PPPXXXPPP" present in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Paralog
Sequence homology is the biological homology between DNA, RNA, or protein sequences, defined in terms of shared ancestry in the evolutionary history of life. Two segments of DNA can have shared ancestry because of three phenomena: either a speciation event (orthologs), or a duplication event (paralogs), or else a horizontal (or lateral) gene transfer event (xenologs). Homology among DNA, RNA, or proteins is typically inferred from their nucleotide or amino acid sequence similarity. Significant similarity is strong evidence that two sequences are related by evolutionary changes from a common ancestral sequence. Alignments of multiple sequences are used to indicate which regions of each sequence are homologous. Identity, similarity, and conservation The term "percent homology" is often used to mean "sequence similarity”, that is the percentage of identical residues (''percent identity''), or the percentage of residues conserved with similar physicochemical properties ('' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TJP2
Tight junction protein ZO-2 is a protein that in humans is encoded by the ''TJP2'' gene. Tight junction proteins (TJPs) belong to a family of membrane-associated guanylate kinase (MAGUK) homologs that are involved in the organization of epithelial and endothelial intercellular junctions. TJPs bind to the cytoplasmic C termini of junctional transmembrane proteins and link them to the actin cytoskeleton upplied by OMIM Interactions Tight junction protein 2 has been shown to interact with tight junction protein 1, band 4.1, occludin Occludin is an enzyme ( EC 1.6) that oxidizes NADH. It was first identified in epithelial cells as a 65 kDa integral plasma-membrane protein localized at the tight junctions. Together with Claudins, and zonula occludens-1 (ZO-1), occludin has be ... and USP53. References Further reading * * * * * * * * * * * * * * * * * {{PDB Gallery, geneid=9414 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TJP1
Zonula occludens-1 ZO-1, also known as Tight junction protein-1 is a 220-kD peripheral membrane protein that is encoded by the ''TJP1'' gene in humans. It belongs to the family of ''zonula occludens proteins'' (ZO-1, ZO-2, and ZO-3), which are tight junction-associated proteins and of which, ZO-1 is the first to be cloned. It was first isolated in 1986 by Stevenson and Goodenough using a monoclonal antibody raised in rodent liver to recognise a 225-kD polypeptide in whole liver homogenates and in tight junction-enriched membrane fractions. It has a role as a scaffold protein which cross-links and anchors Tight Junction (TJ) strand proteins, which are fibril-like structures within the lipid bilayer, to the actin cytoskeleton. Function This gene encodes a protein located on a cytoplasmic membrane surface of intercellular tight junctions. The encoded protein may be involved in signal transduction at cell–cell junctions. Two transcript variants encoding distinct isoforms have bee ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
AMOT
Angiomotin (AMOT) is a protein that in humans is encoded by the ''AMOT'' gene. It belongs to the motin family of angiostatin binding proteins, which includes angiomotin, angiomotin-like 1 ( AMOTL1) and angiomotin-like 2 ( AMOTL2) characterized by coiled-coil domains at N-terminus and consensus PDZ-binding domain at the C-terminus. Angiomotin is expressed predominantly in endothelial cells of capillaries as well as angiogenic tissues such as placenta and solid tumor. Discovery Angiomotin was discovered in 2001 by screening a placenta yeast two-hybrid cDNA library for angiostatin-binding peptides, using a construct encoding the kringle domains 1-4 of angiostatin. Gene location ''AMOT'' gene is located on human chromosome X:112,021,794-112,066,354, containing 3252 nucleotides in coding sequence as 11 exons. Protein structure Two splice isoforms are known for angiomotin: p80 and p130. The alternative splicing is somewhat tissue specific. Cells expressing p130 contained more a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PTPN14
Tyrosine-protein phosphatase non-receptor type 14 is an enzyme that in humans is encoded by the ''PTPN14'' gene. Function The protein encoded by this gene is a member of the PTP family anPTPN14subfamily of tyrosine protein phosphatases. PTPs are known to be signalling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an N-terminal noncatalytic domain similar to that of band 4.1 superfamily cytoskeleton-associated proteins, which suggested the membrane or cytoskeleton localization of this protein. The specific function of this PTP has not yet been determined. Interactions PTPN14 has been shown to interact with Beta-catenin Catenin beta-1, also known as beta-catenin (β-catenin), is a protein that in humans is encoded by the ''CTNNB1'' gene. Beta-catenin is a dual function protein, involved in regulation and coordination of cell–cell adhesion and gene transcripti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
LATS2
Large tumor suppressor kinase 2 (LATS2) is an enzyme that in humans is encoded by the ''LATS2'' gene. This gene encodes a serine/threonine protein kinase belonging to the LATS tumor suppressor family and participates in the Hippo signaling pathway where it inactivates the effector proteins, YAP and WWTR1 (TAZ). The protein localizes to centrosomes during interphase and early and late metaphase. It interacts with the centrosomal proteins aurora-A and ajuba and is required for accumulation of gamma-tubulin and spindle formation at the onset of mitosis. It also interacts with a negative regulator of p53 and may function in a positive feedback loop with p53 that responds to cytoskeleton damage. Additionally, it can function as a corepressor In the field of molecular biology, a corepressor is a molecule that represses the expression of genes. In prokaryotes, corepressors are small molecules whereas in eukaryotes, corepressors are proteins. A corepressor does not directly bind to DNA ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
LATS1
Large tumor suppressor kinase 1 (LATS1) is an enzyme that in humans is encoded by the ''LATS1'' gene. It has been associated with the Hippo signaling pathway, where it phosphorylates YAP and TAZ to inactivate their function. The protein encoded by this gene is a putative serine/threonine kinase that localizes to the mitotic apparatus and complexes with cell cycle controller CDC2 kinase in early mitosis. The protein is phosphorylated in a cell-cycle dependent manner, with late prophase phosphorylation remaining through metaphase. The N-terminal region of the protein binds CDC2 to form a complex showing reduced histone H1 kinase activity, indicating a role as a negative regulator of CDC2/cyclin A. In addition, the C-terminal kinase domain binds to its own N-terminal region, suggesting potential negative regulation through interference with complex formation via intramolecular binding. Biochemical and genetic data suggest a role as a tumor suppressor. This is supported by studies in k ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
TP53BP2
Apoptosis-stimulating of p53 protein 2 (ASPP2) also known as Bcl2-binding protein (Bbp) and tumor suppressor p53-binding protein 2 (p53BP2) is a protein that in humans is encoded by the ''TP53BP2'' gene. Multiple transcript variants encoding different isoforms have been found for this gene. Nomenclature ASPP2 (amino acid residues 600 –1128) was initially identified as 53BP2 (p53-binding protein 2) in a yeast two hybrid screen using p53 as the bait. Another yeast two hybrid screening in which Bcl-2 was used as the bait gave rise to the discovery of another fragment of ASPP2 (residues 123-1128) and it was called Bbp. The full length ASPP2 (1128 amino acids) was identified later. Function ASPP2 plays a central role in regulation of apoptosis and cell growth via its interactions. ASPP2 regulates TP53 by enhancing the DNA binding and transactivation function of TP53 on the promoters of proapoptotic genes ''in vivo''. ASPP2 binds to wild-type p53 but fails to bind to mutant p53, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ErbB4
Receptor tyrosine-protein kinase erbB-4 is an enzyme that in humans is encoded by the ''ERBB4'' gene. Alternatively spliced variants that encode different protein isoforms have been described; however, not all variants have been fully characterized. Function Receptor tyrosine-protein kinase erbB-4 is a receptor tyrosine kinase that is a member of the epidermal growth factor receptor family. ERBB4 is a single-pass type I transmembrane protein with multiple furin-like cysteine rich domains, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins-2, -3 and -4, heparin-binding EGF-like growth factor and betacellulin. Ligand binding induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Clinical significance Mutations in this gene have been associat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SMAD (protein)
Smads (or SMADs) comprise a family of structurally similar proteins that are the main signal transducers for receptors of the transforming growth factor beta (TGF-B) superfamily, which are critically important for regulating cell development and growth. The abbreviation refers to the homologies to the ''Caenorhabditis elegans'' SMA ("small" worm phenotype) and MAD family ("Mothers Against Decapentaplegic") of genes in Drosophila. There are three distinct sub-types of Smads: receptor-regulated Smads ( R-Smads), common partner Smads (Co-Smads), and inhibitory Smads ( I-Smads). The eight members of the Smad family are divided among these three groups. Trimers of two receptor-regulated SMADs and one co-SMAD act as transcription factors that regulate the expression of certain genes. Sub-types The R-Smads consist of Smad1, Smad2, Smad3, Smad5 and Smad8/9, and are involved in direct signaling from the TGF-B receptor. Smad4 is the only known human Co-Smad, and has the role of partneri ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
