Genes altered in major depressive disorder
Genes altered in major depressive disorder
Positive relationships between COPA and other components at different levels (count: 0)
Positive relationship network of COPA in MK4MDD
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Note:
1. The different color of the nodes denotes the level of the nodes.
Genetic/Epigenetic Locus
Protein and Other Molecule
Cell and Molecular Pathway
Neural System
Cognition and Behavior
Symptoms and Signs
Environment
MDD
2. Besides the component related relationships from literature, gene mapped protein and protein mapped gene are also shown in the network.
If the mapped gene or protein is not from literature, square node would be used instead of Circle node.
Accordingly, the relationship is marked with dot line.
2. User can drag the nodes to rearrange the layout of the network. Click the node will enter the report page of the node.
Right-click will show also the menus to link to the report page of the node and remove the node and related edges.
Hover the node will show the level of the node and hover the edge will show the evidence/description of the edge.
3. The network is generated using Cytoscape Web
Negative relationships between COPA and MDD (count: 0)
Negative relationships between COPA and other components at different levels (count: 0)
ADP-ribosylation factors (ARFs) are 20-kDa guanine nucleotid......
ADP-ribosylation factors (ARFs) are 20-kDa guanine nucleotide-binding proteins, members of the Ras GTPase superfamily that were initially recognized and purified because of their ability to stimulate the ADP-ribosyltransferase activity of the cholera toxin A subunit. We now know that they are critical components of several different vesicular trafficking pathways in all eukaryotic cells and activators of specific phospholipase Ds (PLDs) (reviewed in Refs. 13). ARF interacts with many proteins and other molecules that regulate its state of activation or are involved in its intracellular function. Arf proteins cycle between GDP-bound, inactive and GTP-bound, active forms, and the cycling is regulated by specific GEPs and GAPs. Members of the Arf GEP family can be grouped into two major subfamilies on the basis of their sequence similarities and functional differences. The high-molecular-weight Arf GEP subfamily includes yeast Sec7, Gea1, and Gea2, and mammalian BIG1/p200, BIG2, and GBF1, which all consist of 1,400 2,000 amino acid residues. Many Arf GAPs are multidomain proteins and have been found to interact with multiple signaling molecules. For instance, ASAP1 has a PH domain, ankyrin (ANK) repeats, proline-rich and Src-homology (SH) 3 domains and has been shown to bind PI(4,5)P2, Src, and Crk. PAPa/PAG3, with a similar domain structure, binds phosphoinositides, Src, Pyk, and paxillin. The GITs bind bARK, paxillin and the Rac/Cdc42 exchange factor PIX (also known as Cool). ASAP-related proteins, ARAP1, 2 and 3 have Arf GAP, Rho GAP,Ankyrin repeat, Ras-associating (RA), and five PH domains, and therefore have the potential of integrating four signaling pathways.More...
The secretory membrane system allows a cell to regulate deli......
The secretory membrane system allows a cell to regulate delivery of newly synthesized proteins, carbohydrates, and lipids to the cell surface, a necessity for growth and homeostasis. The system is made up of distinct organelles, including the endoplasmic reticulum (ER), Golgi complex, plasma membrane, and tubulovesicular transport intermediates. These organelles mediate intracellular membrane transport between themselves and the cell surface. Membrane traffic within this system flows along highly organized directional routes. Secretory cargo is synthesized and assembled in the ER and then transported to the Golgi complex for further processing and maturation. Upon arrival at the trans Golgi network (TGN), the cargo is sorted and packaged into post-Golgi carriers that move through the cytoplasm to fuse with the cell surface. This directional membrane flow is balanced by retrieval pathways that bring membrane and selected proteins back to the compartment of origin.More...
Secretory transport depends on membrane-bounded carriers to ......
Secretory transport depends on membrane-bounded carriers to move protein and lipid between intracellular compartments. The COPI coat has a central role in this process, creating a sorting domain on the membrane into which cargo proteins, destined to return to the endoplasmic reticulum (ER), concentrate. The membrane domain deforms into a coated bud, pinches off the membrane as a coated carrier, and then uncoats. Successful operation of the COPI coat system is necessary for selective retrieval of protein and lipid components back to the ER.More...
COPA related interactors from protein-protein interaction data in HPRD (count: 10)