Information about Keratin 20

The Entrez Global Query Cross-Database Search System is a powerful federated search engine, or web portal that allows users to search many discrete health sciences databases at the National Center for Biotechnology Information (NCBI) website.
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Hugo is a male given name, a latinized form of the name Hugh, a German/Teutonic name meaning "Bright in Mind and Spirit".

Hugo is one of the most popular names in Europe ranking as high as #2 in France, #6 in Spain, and #7 in Belgium in 2006.
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The National Center for Biotechnology Information (NCBI) is part of the United States National Library of Medicine (NLM), a branch of the National Institutes of Health. The NCBI is located in Bethesda, Maryland and was founded in 1988.
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Swiss-Prot is a manually curated biological database of protein sequences. Swiss-Prot was created in 1986 by Amos Bairoch during his PhD and developed by the Swiss Institute of Bioinformatics and the European Bioinformatics Institute.
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locus (plural loci) is a fixed position on a chromosome, such as the position of a gene or a biomarker (genetic marker). A variant of the DNA sequence at a given locus is called an allele. The ordered list of loci known for a particular genome is called a genetic map.
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Type I keratins (or Type I cytokeratins) constitutes the Type I intermediate filaments (IFs) of the intracytoplasmatic cytoskeleton, which is present in all mammalian epithelial cells.
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Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
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Enterocyte is a type of epithelial cell of the innermost layer of the small and large intestine tissue. These cells can help break up molecules and transport them into the tissues.
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Goblet cells are glandular simple columnar epithelial cells whose sole function is to secrete mucus.

The majority of the cell's cytoplasm is occupied by mucinogen granules, except at the bottom.
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The mucous membranes (or mucosae; singular: mucosa) are linings of mostly endodermal origin, covered in epithelium, and are involved in absorption and secretion. They line various body cavities that are exposed to the external environment and internal organs.
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Proteins are large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid residues.
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Fibrous proteins, also called scleroproteins, are long filamentous protein molecules that form one of the two main classes of tertiary structure protein (the other being globular proteins). Fibrous proteins are only found in animals.
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Collagen is the main protein of connective tissue in animals and the most abundant protein in mammals, ^[1] making up about 25% of the total protein content.

Uses

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Identifiers
Symbol COL1A2
Alt. Symbols OI4

Entrez 1278
HUGO 2198
OMIM 120160

RefSeq NM_000089
UniProt P08123
Other data

Locus Chr. 7 q21.3-22.1 Type-I collagen is the most abundant collagen of the human body.
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COL1A1 (collagen, type I, alpha 1) is a human gene that is one of several genes that provide instructions for making components of collagen. Collagen is a protein that strengthens and supports many tissues in the body, including cartilage, bone, tendon, skin and the white
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Type-II collagen is the basis for articular cartilage and hyaline cartilage.

It makes up 50% of all protein in cartilage and 85-90% of collagen of articular cartilage.
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COL2A1 (collagen, type II, alpha 1 (primary osteoarthritis, spondyloepiphyseal dysplasia, congenital)) is a human gene that provides instructions for the production of the pro-alpha1(II) chain of type II collagen.
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Type-III collagen is a fibrous scleroprotein in bone and cartilage and tendon and other connective tissue; yields gelatin on boiling.

Scleroprotein is a simple protein found in horny and cartilaginous tissues and in the lens of the eye.
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Type-IV collagen is a type of collagen found primarily in the basal lamina. The C-terminus domain is not removed in post-translational processing, and the fibers link head-to-head, rather than in parallel.
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Type-V collagen is a form of fibrillar^[1] collagen associated with classical Ehlers-Danlos syndrome.

Genes

• COL5A1 , COL5A2 , COL5A3

References

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COL11A2 (collagen, type XI, alpha 2) is a human gene that is one of several genes that provide instructions for the production of type XI collagen. The COL11A2 gene produces one component of this type of collagen, called the pro-alpha2(XI) chain.
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Collagen XVII, previously called BP180, is a transmembrane protein which plays a critical role in maintaining the linkage between the intracellular and the extracellular structural elements involved in epidermal adhesion ^[1].
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Type XVIII collagen is a type of collagen which can be cleaved to form endostatin.

External links

• MeSH Collagen+Type+XVIII

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Keratins are a family of fibrous structural proteins; tough and insoluble, they form the hard but nonmineralized structures found in reptiles, birds, amphibians and mammals. They are rivaled as biological materials in toughness only by chitin.
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Cytokeratins are intermediate filament keratins found in the intracytoplasmic cytoskeleton of epithelial tissue. There are two types of cytokeratins: the low weight, acidic type I cytokeratins and the high weight, basic or neutral type II cytokeratins.
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Type I keratins (or Type I cytokeratins) constitutes the Type I intermediate filaments (IFs) of the intracytoplasmatic cytoskeleton, which is present in all mammalian epithelial cells.
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Keratin 10 is a type I cytokeratin. Mutations in the gene encoding this protein are associated with the variants of epidermolytic hyperkeratosis in which the palms and soles of the feet are unaffected.
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Keratin 12 is a keratin found expressed in corneal epithelia. Mutations in the gene encoding this protein lead to Meesmann corneal dystrophy.


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Keratin 13 is a type I cytokeratin, it is paired with keratin 4 and found in the suprabasal layers of non-cornified stratified epithelia. Mutations in the gene encoding this protein and keratin 4 have been associated with the autosomal dominant disorder White Sponge Nevus.
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Keratin 14 is a type I cytokeratin. It is usually found as a heterotetramer with two keratin 5 molecules, a type II keratin. Together they form the cytoskeleton of epithelial cells.
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