POTEB
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POTEB
POTE ankyrin domain family, member B is a protein in humans that is encoded by the ''POTEB'' gene.(Prostate, Ovary, Testes Expressed ankyrin domain family member B).It is most likely involved in mediating protein-protein interaction via its 5 ankyrin domains. POTEB is most probably aids in intracellular signaling, but is not likely to be a secreted or nuclear protein. POTEB's function is likely to be regulated via 17 potential phosphorylation sites. There is currently no evidence to suggest that POTEB has nuclear localization signals. Gene POTEB is located at 15q11.2 on chromosome 15 in humans and is transcribed from the reverse DNA strand. POTEB is also known as POTEB3 and POTE15. The ''POTEB'' gene is 47,547 base pairs in length and is composed of 11 exons. mRNA The ''POTEB'' gene can be transcribed to create four potential mRNAs. However, only one of these mRNAs, possessing all 11 exons, is capable of being translated to the POTEB protein. The three other transcripts d ...
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POTEB Expression In Breast Cancer
POTE ankyrin domain family, member B is a protein in humans that is encoded by the ''POTEB'' gene.(Prostate, Ovary, Testes Expressed ankyrin domain family member B).It is most likely involved in mediating protein-protein interaction via its 5 ankyrin domains. POTEB is most probably aids in intracellular signaling, but is not likely to be a secreted or nuclear protein. POTEB's function is likely to be regulated via 17 potential phosphorylation sites. There is currently no evidence to suggest that POTEB has nuclear localization signals. Gene POTEB is located at 15q11.2 on chromosome 15 in humans and is transcribed from the reverse DNA strand. POTEB is also known as POTEB3 and POTE15. The ''POTEB'' gene is 47,547 base pairs in length and is composed of 11 exons. mRNA The ''POTEB'' gene can be transcribed to create four potential mRNAs. However, only one of these mRNAs, possessing all 11 exons, is capable of being translated to the POTEB protein. The three other transcripts d ...
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POTEB Schematic Diagram Updated
POTE ankyrin domain family, member B is a protein in humans that is encoded by the ''POTEB'' gene.(Prostate, Ovary, Testicle, Testes Expressed ankyrin domain family member B).It is most likely involved in mediating Protein–protein interaction, protein-protein interaction via its 5 ankyrin domains. POTEB is most probably aids in Cell signaling, intracellular signaling, but is not likely to be a secreted or nuclear protein. POTEB's function is likely to be regulated via 17 potential phosphorylation sites. There is currently no evidence to suggest that POTEB has Nuclear localization sequence, nuclear localization signals. Gene POTEB is located at 15q11.2 on Chromosome 15 (human), chromosome 15 in humans and is transcribed from the reverse DNA strand. POTEB is also known as POTEB3 and POTE15. The ''POTEB'' gene is 47,547 base pairs in length and is composed of 11 Wikipedia:Exon, exons. mRNA The ''POTEB'' gene can be Transcription (biology), transcribed to create four potentia ...
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Chromosome 15 (human)
Chromosome 15 is one of the 23 pairs of chromosomes in humans. People normally have two copies of this chromosome. Chromosome 15 spans about 102 million base pairs (the building material of DNA) and represents between 3% and 3.5% of the total DNA in cells. Chromosome 15 is an acrocentric chromosome, with a very small short arm (the "p" arm, for "petite"), which contains few protein coding genes among its 19 million base pairs. It has a larger long arm (the "q" arm) that is gene rich, spanning about 83 million base pairs. The human leukocyte antigen gene for β2-microglobulin is found on chromosome 15, as well as the FBN1 gene, coding for both fibrillin-1 (a protein critical to the proper functioning of connective tissue), and aprosin (a small protein produced from part of the transcribed FBN1 gene mRNA), which is involved in fat metabolism. Genes Number of genes The following are some of the gene count estimates of human chromosome 15. Because researchers use different approac ...
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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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Bioinformatics
Bioinformatics () is an interdisciplinary field that develops methods and software tools for understanding biological data, in particular when the data sets are large and complex. As an interdisciplinary field of science, bioinformatics combines biology, chemistry, physics, computer science, information engineering, mathematics and statistics to analyze and interpret the biological data. Bioinformatics has been used for '' in silico'' analyses of biological queries using computational and statistical techniques. Bioinformatics includes biological studies that use computer programming as part of their methodology, as well as specific analysis "pipelines" that are repeatedly used, particularly in the field of genomics. Common uses of bioinformatics include the identification of candidates genes and single nucleotide polymorphisms (SNPs). Often, such identification is made with the aim to better understand the genetic basis of disease, unique adaptations, desirable properties (e ...
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Triple-negative Breast Cancer
Triple-negative breast cancer (TNBC) is any breast cancer that lacks or show low levels of estrogen receptor (ER), progesterone receptor (PR) and human epidermal growth factor receptor 2 (HER2) overexpression and/or gene amplification (i.e. the tumor is negative on all three tests giving the name ''triple-negative''). Triple-negative is sometimes used as a surrogate term for basal-like. Triple-negative breast cancer comprises 15–20% of all breast cancer cases and affects more young women or women with a mutation in the BRCA1 gene than other breast cancers. Triple-negative breast cancers comprise a very heterogeneous group of cancers. TNBC is the most challenging breast cancer type to treat. Hormone therapy that is used for other breast cancers does not work for TNBC. In its early stages, the cancer is typically treated through surgery, radiation and chemotherapy. In later stages where surgery is not possible or the cancer has spread from the initial localised area, treatment i ...
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Embryonic Stem Cell
Embryonic stem cells (ESCs) are pluripotent stem cells derived from the inner cell mass of a blastocyst, an early-stage pre- implantation embryo. Human embryos reach the blastocyst stage 4–5 days post fertilization, at which time they consist of 50–150 cells. Isolating the inner cell mass (embryoblast) using immunosurgery results in destruction of the blastocyst, a process which raises ethical issues, including whether or not embryos at the pre-implantation stage have the same moral considerations as embryos in the post-implantation stage of development. Researchers are currently focusing heavily on the therapeutic potential of embryonic stem cells, with clinical use being the goal for many laboratories. Potential uses include the treatment of diabetes and heart disease. The cells are being studied to be used as clinical therapies, models of genetic disorders, and cellular/DNA repair. However, adverse effects in the research and clinical processes such as tumors and unw ...
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Myristoylation
Myristoylation is a lipidation modification where a myristoyl group, derived from myristic acid, is covalently attached by an amide bond to the alpha-amino group of an N-terminus, N-terminal glycine residue. Myristic acid is a 14-carbon saturated fatty acid (14:0) with the systematic name of ''n''-Tetradecanoic acid. This modification can be added either co-translationally or Posttranslational modification, post-translationally. N-myristoyltransferase 1, N-myristoyltransferase (NMT) catalyzes the myristic acid addition reaction in the cytoplasm of cells. This lipidation event is the most found type of fatty acylation and is common among many organisms including animals, plants, fungi, protozoans and viruses. Myristoylation allows for weak protein–protein and protein–lipid interactions and plays an essential role in membrane targeting, protein–protein interactions and functions widely in a variety of signal transduction pathways. Discovery In 1982, Koiti Titani's lab id ...
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Protein Secondary Structure
Protein secondary structure is the three dimensional form of ''local segments'' of proteins. The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well. Secondary structure elements typically spontaneously form as an intermediate before the protein folds into its three dimensional tertiary structure. Secondary structure is formally defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen atoms in the peptide backbone. Secondary structure may alternatively be defined based on the regular pattern of backbone dihedral angles in a particular region of the Ramachandran plot regardless of whether it has the correct hydrogen bonds. The concept of secondary structure was first introduced by Kaj Ulrik Linderstrøm-Lang at Stanford in 1952. Other types of biopolymers such as nucleic acids also possess characteristic secondary structures. Types The most common secondary structures ...
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Tyrosine
-Tyrosine or tyrosine (symbol Tyr or Y) or 4-hydroxyphenylalanine is one of the 20 standard amino acids that are used by cells to synthesize proteins. It is a non-essential amino acid with a polar side group. The word "tyrosine" is from the Greek ''tyrós'', meaning ''cheese'', as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. It is called tyrosyl when referred to as a functional group or side chain. While tyrosine is generally classified as a Hydrophobe, hydrophobic amino acid, it is more hydrophilic than phenylalanine. It is Genetic code, encoded by the Genetic code#Codons, codons UAC and UAU in messenger RNA. Functions Aside from being a proteinogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. It occurs in proteins that are part of signal transduction processes and functions as a receiver of phosphate groups that are transferred by way of protein kinases. Phosphorylation of the hyd ...
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Threonine
Threonine (symbol Thr or T) is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated −NH form under biological conditions), a carboxyl group (which is in the deprotonated −COO− form under biological conditions), and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as ''E. coli''. It is encoded by all the codons starting AC (ACU, ACC, ACA, and ACG). Threonine sidechains are often hydrogen bonded; the most common small motifs formed are based on interactions with serine: ST turns, ST motifs (often at the beginning of alpha helices) and ST staples (usually at the middle of alpha helices). Modifications The threonine residue is susceptible to numerous posttranslational modifications. The hydroxyl side-chain can unde ...
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Serine
Serine (symbol Ser or S) is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated − form under biological conditions), a carboxyl group (which is in the deprotonated − form under biological conditions), and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal physiological circumstances, making it a nonessential amino acid. It is encoded by the codons UCU, UCC, UCA, UCG, AGU and AGC. Occurrence This compound is one of the naturally occurring proteinogenic amino acids. Only the L-stereoisomer appears naturally in proteins. It is not essential to the human diet, since it is synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865 by Emil Cramer. Its name is derived from the Latin for silk, ''sericum''. Serine's structure was estab ...
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