Information about Plakoglobin
junction plakoglobin | |
| Identifiers | |
| Symbol | JUP |
| Alt. Symbols | CTNNG |
| Entrez | 3728 |
| HUGO | 6207 |
| OMIM | 173325 |
| RefSeq | NM_002230 |
| UniProt | P14923 |
| Other data | |
| Locus | Chr. 17 q21 |
Plakoglobin also associates with classical cadherins such as E-cadherin and in that context it was called gamma-catenin.
Plakoglobin is O-glycosylated near its N-terminal destruction box.
See also
External links
References
1: Cowin P, Kapprell HP, Franke WW, Tamkun J, Hynes RO. Plakoglobin: a protein common to different kinds of intercellular adhering junctions.Cell. 1986 Sep 26;46(7):1063-73.2: Franke WW, Goldschmidt MD, Zimbelmann R, Mueller HM, Schiller DL, Cowin P Molecular cloning and amino acid sequence of human plakoglobin, the common junctional plaque protein. Proc Natl Acad Sci U S A. 1989 Jun;86(11):4027-31.
3: Mathur M, Goodwin L, Cowin P. Interactions of the cytoplasmic domain of the desmosomal cadherin Dsg1 with plakoglobin. J Biol Chem. 1994 May 13;269(19):14075-80.
Proteins of the cytoskeleton | |
|---|---|
| Microfilaments | Actins - Actin-binding proteins - Actinin - Arp2/3 complex - Cofilin - Destrin - Gelsolin - Myosins - Profilin - Tropomodulin - Troponin (T, C, I) - Tropomyosin - Wiskott-Aldrich syndrome protein |
| Intermediate filaments | type 1 and 2 (Cytokeratin, type I, type II) - type 3 (Desmin, GFAP, Peripherin, Vimentin) - type 4 (Internexin, Nestin, Neurofilament, Synemin, Syncoilin) - type 5 (Lamin A, B) |
| Microtubules | Dyneins - Kinesins - MAPs (Tau protein, Dynamin) - Tubulins - Stathmin |
| Catenins | Alpha catenin - Beta catenin - Plakoglobin (gamma catenin) - Delta catenin |
| Nonhuman | Major sperm proteins - Prokaryotic cytoskeleton (Crescentin, FtsZ, MreB) |
| Other | APC - Dystrophin (Dystroglycan) - plakin (Desmoplakin, Plectin) - Spectrin - Talin - Utrophin - Vinculin |
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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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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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desmosome, also known as macula adherens (Latin: adhering spot), is a cell structure specialized for cell-to-cell adhesion. A type of junctional complex, they are localized spot-like adhesions randomly arranged on the lateral sides of plasma membranes.
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Cadherins are a class of type-1 transmembrane proteins. They play important roles in cell adhesion whereby they ensure cells within tissues are bound together. They are dependent on calcium (Ca2+) ions to function, hence their name.
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The desmogleins are a family of cadherins consisting of proteins DSG1 , DSG2 , DSG3 , and DSG4 . They play a role in the formation of desmosomes that join cells to one another.
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Cadherins are a class of type-1 transmembrane proteins. They play important roles in cell adhesion whereby they ensure cells within tissues are bound together. They are dependent on calcium (Ca2+) ions to function, hence their name.
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Catenins are proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified[2] became known as alpha-catenin and beta-catenin. Alpha-catenin can bind to beta-catenin and can also bind actin.
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Catenins are proteins found in complexes with cadherin cell adhesion molecules of animal cells. The first two catenins that were identified[2] became known as alpha-catenin and beta-catenin. Alpha-catenin can bind to beta-catenin and can also bind actin.
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Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. Created and updated by the United States National Library of Medicine (NLM), it is used by the MEDLINE/PubMed
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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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cytoskeleton is a cellular "scaffolding" or "skeleton" contained, as all other organelles, within the cytoplasm. It is contained in all eukaryotic cells and recent research has shown it can be present in prokaryotic cells too.
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Microfilaments are the thinnest filaments of the cytoskeleton found in the cytoplasm of all eukaryotic cells. These linear polymers of actin subunits are flexible and relatively strong, resisting buckling by multi-piconewton compressive forces and filament fracture by nanonewton
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Actin is a globular structural, 42-47 kDa protein found in many eukaryotic cells, with concentrations of over 100 μM. It is also one of the most highly conserved proteins, differing by no more than 5% in species as diverse as algae and humans.
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This is a list of actin-binding proteins in alphabetical order.
List: 0–9 A B C D E F G H I J K L M N O P Q R S T U V W x Y Z
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List: 0–9 A B C D E F G H I J K L M N O P Q R S T U V W x Y Z
References External links
0–9
- 25kDa
- 25kDa ABP from aorta p185neu
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Actinin is a microfilament protein. α-Actinin is necessary for the attachment of actin filaments to the z-line membrane, in muscle cells. The functional protein is an anti-parallel dimer, which cross-links the thin filaments in adjacent sarcomeres, and therefore coordinated
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Arp2/3 complex is a seven-subunit protein that plays a major role in the regulation of the actin cytoskeleton. It is a necessary component of the actin cytoskeleton and is therefore ubiquitous in actin cytoskeleton-containing eukaryotic cells.[1].
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Identifiers
Symbol CFL2
Entrez 1073
HUGO 1875
OMIM 601443
RefSeq NM_021914
UniProt Q9Y281
Other data
Locus Chr. 14 ADF/cofilin is a family of actin-binding proteins which disassembles actin filaments.
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Symbol CFL2
Entrez 1073
HUGO 1875
OMIM 601443
RefSeq NM_021914
UniProt Q9Y281
Other data
Locus Chr. 14 ADF/cofilin is a family of actin-binding proteins which disassembles actin filaments.
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Destrin is a protein in microfilaments.
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External links
- MeSH Destrin
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Gelsolin is an actin-binding protein that is a key regulator of actin filament assembly and disassembly. Gelsolin is one of the most potent members of the actin-severing gelsolin/villin superfamily, as it severs with nearly 100% efficiency.
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Myosins are a large family of motor proteins found in eukaryotic tissues. They are responsible for actin-based motility.
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Structure and Function
Domains
Most myosin molecules are composed of both a head and a tail domain...... Click the link for more information.
Profilin is an actin-binding protein involved in cytoskeleton dynamics. It is found in most eukaryotic cells and in mammalian cells two kinds of profilin have been discovered; Profilin I and II.
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Tropomodulin is a protein which binds and caps actin.
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Genes
- TMOD1
- TMOD2
- TMOD3
- TMOD4
External links
- MeSH Tropomodulin
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Troponin is a complex of three proteins that is integral to muscle contraction in skeletal and cardiac muscle, but not smooth muscle. Troponin is attached to the protein tropomyosin and lies within the groove between actin filaments in muscle tissue.
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Troponin T is a part of the troponin complex. It binds to tropomyosin, interlocking them to form a troponin-tropomyosin complex.
The tissue specific subtypes are:
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The tissue specific subtypes are:
- Slow skeletal troponin T1, TNNT1 (19q13.
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Troponin C is a part of the troponin complex. It binds to calcium ions to produce movement.
The tissue specific subtypes are:
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The tissue specific subtypes are:
- Slow troponin C, TNNC1 (3p21.3-p14.3, Mendelian Inheritance in Man (OMIM) 191040 )
- Fast troponin C, TNNC2 (20q12-q13.
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Troponin I is a part of the troponin complex. It binds to actin in thin myofilaments to hold the troponin-tropomyosin complex in place. The letter I is given due to its inhibitory character.
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