|
ANTH Domain
The ANTH domain is a membrane binding domain that shows weak specificity for PtdIns(4,5)P2. It was found in AP180 (homologous to CALM) endocytotic accessory protein that has been implicated in the formation of clathrin-coated pits. The domain is involved in phosphatidylinositol 4,5-bisphosphate binding and is a universal adaptor for nucleation of clathrin coats. Its structure is a solenoid of 9 helices. The PtdIns(4,5)P2 binding residues are spread over several helices at the tip of the structure. The PtdIns(4,5)P2 binding sequence is Kx9Kx(K/R)(H/Y). An ANTH domain is also found in HIP1 and HIP1R, and the PtdIns(4,5)P2 binding sequence is conserved. More information is found oendocytosis.org Human proteins containing this domain HIP1; HIP1R; PICALM; SNAP91 Clathrin coat assembly protein AP180 is a protein that in humans is encoded by the ''SNAP91'' gene In biology, the word gene (from , ; "... Wilhelm Johannsen coined the word gene to describe the Mendeli ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PtdIns(4,5)P2
Phosphatidylinositol 4,5-bisphosphate or PtdIns(4,5)''P''2, also known simply as PIP2 or PI(4,5)P2, is a minor phospholipid component of cell membranes. PtdIns(4,5)''P''2 is enriched at the plasma membrane where it is a substrate for a number of important signaling proteins. PIP2 also forms lipid clusters that sort proteins. PIP2 is formed primarily by the type I phosphatidylinositol 4-phosphate 5-kinases from PI(4)P. In metazoans, PIP2 can also be formed by type II phosphatidylinositol 5-phosphate 4-kinases from PI(5)P. The fatty acids of PIP2 are variable in different species and tissues, but the most common fatty acids are stearic in position 1 and arachidonic in 2. Signaling pathways PIP2 is a part of many cellular signaling pathways, including PIP2 cycle, PI3K signalling, and PI5P metabolism. Recently, it has been found in the nucleus with unknown function. Functions Cytoskeleton dynamics near membranes PIP2 regulates the organization, polymerization, and bra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HIP1
Huntingtin-interacting protein 1 also known as HIP-1 is a protein that in humans is encoded by the HIP1 gene. Hip-1 is a protein that interacts with the huntingtin protein. It is known to contain a protein domain, domain homologous to the death effector domains (DED) found on proteins involved in apoptosis. It is believed that accumulation of high levels of the free form of this protein (free as in dissociated from the huntingtin and free to bind other key protein(s)) in the cell is one of the mechanisms by which neuron cell death is caused in Huntington's disease (via the caspase-3 route). The role of Hip-1 in caspase mediated cell death remains unclear. Discovery Huntingtin interacting protein 1 (HIP1) was first identified by Wanker et al. in 1997. Function HIP1 was found to bind to Htt in an N-terminal dependent manner, and co-localise with Htt in the CNS although the nature of this interaction with respect to was not identified. It has since been found that the CAG exp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HIP1R
Huntingtin-interacting protein 1-related protein is a protein that in humans is encoded by the ''HIP1R'' gene. References Further reading * * * * * * * * * * * * * * {{gene-12-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
PICALM
Phosphatidylinositol binding clathrin assembly protein, also known as PICALM, is a protein which in humans is encoded by the ''PICALM'' gene. Interactions PICALM has been shown to interact with CLTC. Clinical significance In humans, certain alleles of this gene have been statistically associated with an increased risk of developing late-onset Alzheimer's disease Alzheimer's disease (AD) is a neurodegeneration, neurodegenerative disease that usually starts slowly and progressively worsens. It is the cause of 60–70% of cases of dementia. The most common early symptom is difficulty in short-term me .... * References Further reading * * * * * * * * * * * * * * * * * {{gene-11-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SNAP91
Clathrin coat assembly protein AP180 is a protein that in humans is encoded by the ''SNAP91'' gene In biology, the word gene (from , ; "... Wilhelm Johannsen coined the word gene to describe the Mendelian units of heredity..." meaning ''generation'' or ''birth'' or ''gender'') can have several different meanings. The Mendelian gene is a b .... References Further reading * * * * * * * * * * * * * {{gene-6-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domains
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
