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Tenascin
Tenascins are extracellular matrix glycoproteins. They are abundant in the extracellular matrix of developing vertebrate embryos and they reappear around healing wounds and in the stroma of some tumors. Types[edit] There are four members of the tenascin gene family: tenascin-C, tenascin-R, tenascin-X and tenascin-W.Tenascin-C is the founding member of the gene family
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N-terminus
The N-terminus
N-terminus
(also known as the amino-terminus, NH2-terminus, N-terminal end or amine-terminus) is the start of a protein or polypeptide referring to the free amine group (-NH2) located at the end of a polypeptide. Normally the amine group is bonded to another carboxylic group in a protein to make it a chain, but since the end of a protein has only 1 out of 2 areas chained, the free amine group is referred to the N-terminus
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EMID2
4AU2, 4AU3, 4BJ3IdentifiersAliases COL26A1, EMI6, EMID2, EMU2, SH2B, collagen type XXVI alpha 1, collagen type XXVI alpha 1 chainExternal IDs MGI: 2155345 HomoloGene: 136636 GeneCards: COL26A1 Gene
Gene
location (Human)Chr. Chromosome
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Collagen, Type I, Alpha 1
3GXE, 1Q7D, 2LLP, 3EJHIdentifiersAliases COL1A1, EDSC, OI1, OI2, OI3, OI4, collagen type I alpha 1, collagen type I alpha 1 chain, EDSARTH1External IDs OMIM: 120150 MGI: 88467 HomoloGene: 73874 GeneCards: COL1A1 Gene
Gene
location (Human)Chr. Chromosome
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COL1A2
NM_000089NM_007743RefSeq (protein)NP_000080NP_031769Location (UCSC) Chr 7: 94.39 – 94.43 Mb Chr 6: 4.5 – 4.54 Mb PubMed
PubMed
search [3] [4]WikidataView/Edit Human View/Edit Mouse Collagen
Collagen
alpha-2(I) chain is a protein that in humans is encoded by the COL1A2
COL1A2
gene.[5][6] This gene encodes one of the chains for type I collagen, the fibrillar collagen found in most connective tissues. Mutations in this gene are associated with osteogenesis imperfecta, Ehlers-Danlos syndrome, idiopathic osteoporosis, and atypical Marfan syndrome. Symptoms associated with mutations in this gene, however, tend to be less severe than mutations in the gene for alpha-1 type I collagen since alpha-2 is less abundant
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Type-II Collagen
Collagen
Collagen
/ˈkɒlədʒɪn/ is the main structural protein in the extracellular space in the various connective tissues in animal bodies. As the main component of connective tissue, it is the most abundant protein in mammals,[1] making up from 25% to 35% of the whole-body protein content. Collagen
Collagen
consists of amino acids wound together to form triple-helices to form of elongated fibrils.[2] It is mostly found in fibrous tissues such as tendons, ligaments and skin. Depending upon the degree of mineralization, collagen tissues may be rigid (bone), compliant (tendon), or have a gradient from rigid to compliant (cartilage). It is also abundant in corneas, cartilage, bones, blood vessels, the gut, intervertebral discs, and the dentin in teeth.[3] In muscle tissue, it serves as a major component of the endomysium
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Collagen, Type II, Alpha 1
1U5M, 2FSE, 2SEBIdentifiersAliases COL2A1, ANFH, AOM, COL11A3, SEDC, STL1, collagen type II alpha 1, collagen type II alpha 1 chainExternal IDs OMIM: 120140 MGI: 88452 HomoloGene: 55607 GeneCards: COL2A1 Gene
Gene
location (Human)Chr. Chromosome
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Collagen, Type III, Alpha 1
2V53, 3DMW, 4AE2, 4AEJ, 4AK3, 4GYXIdentifiersAliases COL3A1, EDS4A, collagen type III alpha 1, collagen type III alpha 1 chain, EDSVASCExternal IDs OMIM: 120180 MGI: 88453 HomoloGene: 55433 GeneCards: COL3A1 Gene
Gene
location (Human)Chr. Chromosome
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Type-V Collagen
Type-V collagen is a form of fibrillar[1] collagen associated with classical Ehlers-Danlos syndrome. It is found within the dermal/epidermal junction, placental tissues, as well as in association with tissues containing Type-I collagen.[2] Autoimmunity against type V collagen is associated with lung transplant failure.[3][4][5] Genes[edit]COL5A1, COL5A2, COL5A3References[edit]^ Wenstrup RJ, Florer JB, Brunskill EW, Bell SM, Chervoneva I, Birk DE (2004). " Type V collagen controls the initiation of collagen fibril assembly". J. Biol. Chem. 279 (51): 53331–7. doi:10.1074/jbc.M409622200. PMID 15383546.  ^ Pagon RA, Adam MP, Ardinger HH, Wallace SE, Amemiya A, Bean LJH, Bird TD, Fong CT, Mefford HC, Smith RJH, Stephens K, Malfait F, Wenstrup R, De Paepe A (1993). "Ehlers-Danlos Syndrome, Classic Type". PMID 20301422.  ^ "Studies on Collagen". www.collagencomplete.com
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Collagen, Type V, Alpha 1
1A89, 1A9AIdentifiersAliases COL5A1, EDSC, collagen type V alpha 1, collagen type V alpha 1 chain, EDSCL1External IDs OMIM: 120215 MGI: 88457 HomoloGene: 55434 GeneCards: COL5A1 Gene
Gene
location (Human)Chr. Chromosome
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COL5A2
1A9AIdentifiersAliases COL5A2, EDSC, collagen type V alpha 2, collagen type V alpha 2 chain, EDSCL2External IDs OMIM: 120190 MGI: 88458 HomoloGene: 20119 GeneCards: COL5A2 Gene
Gene
location (Human)Chr. Chromosome
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COL5A3
NM_015719NM_016919 NM_001317388RefSeq (protein)NP_056534NP_001304317 NP_058615Location (UCSC) Chr 19: 9.96 – 10.01 Mb Chr 9: 20.77 – 20.82 Mb PubMed
PubMed
search [3] [4]WikidataView/Edit Human View/Edit Mouse Collagen
Collagen
alpha-3(V) chain is a protein that in humans is encoded by the COL5A3
COL5A3
gene.[5][6] This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appears to regulate the assembly of heterotypic fibers composed of both type I and type V collagen
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COL24A1
NM_152890NM_027770 NM_001317733RefSeq (protein)NP_690850 NP_001336884NP_001304662 NP_082046Location (UCSC) n/a Chr 3: 145.29 – 145.55 Mb PubMed
PubMed
search [2] [3]WikidataView/Edit Human View/Edit MouseCollagen, type XXIV, alpha 1 is a protein that in humans is encoded by the COL24A1
COL24A1
gene.[4] Model organisms[edit] Model organisms have been used in the study of COL24A1
COL24A1
function
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FACIT Collagen
FACIT collagen (Fibril Associated Collagens with Interrupted Triple helices[1]) is a type of collagen which is also a proteoglycan.[2] FACIT collagens include collagen types IX, XII, XIV, XIX,[2] and XXI.[3][4] COL22A1
COL22A1
is also included in this class.[5] References[edit]^ GO term: FACIT collagen ^ a b FACIT - Collagens which are proteoglycnas ^ Fitzgerald J, Bateman J (2001). "A new FACIT of the collagen family: COL21A1". FEBS Lett. 505 (2): 275–80. doi:10.1016/S0014-5793(01)02754-5. PMID 11566190.  ^ Tuckwell D (2002). "Identification and analysis of collagen alpha 1(XXI), a novel member of the FACIT collagen family". Matrix Biol. 21 (1): 63–6. doi:10.1016/S0945-053X(01)00176-7. PMID 11827793.  ^ Koch, M.; Schulze, J.; Hansen, U.; Ashwodt, T.; Keene, DR.; Brunken, WJ.; Burgeson, RE.; Bruckner, P.; Bruckner-Tuderman, L. (May 2004). "A novel marker of tissue junctions, collagen XXII". J Biol Chem
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Collagen
Collagen
Collagen
/ˈkɒlədʒɪn/ is the main structural protein in the extracellular space in the various connective tissues in animal bodies. As the main component of connective tissue, it is the most abundant protein in mammals,[1] making up from 25% to 35% of the whole-body protein content. Collagen
Collagen
consists of amino acids wound together to form triple-helices to form of elongated fibrils.[2] It is mostly found in fibrous tissues such as tendons, ligaments and skin. Depending upon the degree of mineralization, collagen tissues may be rigid (bone), compliant (tendon), or have a gradient from rigid to compliant (cartilage). It is also abundant in corneas, cartilage, bones, blood vessels, the gut, intervertebral discs, and the dentin in teeth.[3] In muscle tissue, it serves as a major component of the endomysium
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Collagen, Type IX, Alpha 1
Alpha
Alpha
(uppercase Α, lowercase α; Ancient Greek: ἄλφα, álpha, modern pronunciation álfa) is the first letter of the Greek alphabet. In the system of Greek numerals, it has a value of 1. It was derived from the Phoenician and Hebrew
Hebrew
letter aleph - an ox or leader.[1] Letters that arose from alpha include the Latin
Latin
A and the Cyrillic letter А. In English, the noun "alpha" is used as a synonym for "beginning", or "first" (in a series), reflecting its Greek roots.[2]Contents1 Uses1.1 Greek1.1.1 Greek grammar1.2 Math and science 1.3 International Phonetic Alphabet2 History and symbolism2.1 Etymology 2.2 Plutarch 2.3 Alpha
Alpha
and Omega 2.4 Language3 Computer encodings 4 ReferencesUses Greek In Ancient Greek, alpha was pronounced [a] and could be either phonemically long ([a:]) or short ([a])
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