All terms in GO
| Label | Id | Description |
|---|---|---|
| regulation of glutamate metabolic process | GO_2000211 | [Any process that modulates the frequency, rate or extent of glutamate metabolic process.] |
| serine protease inhibitor complex | GO_0097180 | [A heterodimeric protein complex that contains a serine protease inhibitor and a protease; formation of the complex inhibits serine protease activity.] |
| positive regulation of glutamate metabolic process | GO_2000213 | [Any process that activates or increases the frequency, rate or extent of glutamate metabolic process.] |
| arteriole smooth muscle contraction | GO_0014830 | [A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. This process occurs in the arteriole. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. The arteriole is the smallest division of the artery located between the muscular arteries and the capillaries.] |
| protein C inhibitor-coagulation factor V complex | GO_0097181 | [A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor V (F5); formation of the complex inhibits the serine protease activity of coagulation factor V.] |
| positive regulation of anoikis | GO_2000210 | [Any process that activates or increases the frequency, rate or extent of anoikis.] |
| protein C inhibitor-coagulation factor Xa complex | GO_0097182 | [A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor Xa (F10); formation of the complex inhibits the serine protease activity of coagulation factor Xa.] |
| protein C inhibitor-coagulation factor XI complex | GO_0097183 | [A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and coagulation factor XI (F11); formation of the complex inhibits the serine protease activity of coagulation factor XI.] |
| response to azide | GO_0097184 | [Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an azide stimulus.] |
| cellular response to azide | GO_0097185 | [Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an azide stimulus.] |
| cellular response to inorganic substance | GO_0071241 | [Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an inorganic substance stimulus.] |
| amelogenesis | GO_0097186 | [The process whose specific outcome is the formation of tooth enamel, occurring in two stages: secretory stage and maturation stage.] |
| odontogenesis of dentin-containing tooth | GO_0042475 | [The process whose specific outcome is the progression of a dentin-containing tooth over time, from its formation to the mature structure. A dentin-containing tooth is a hard, bony organ borne on the jaw or other bone of a vertebrate, and is composed mainly of dentin, a dense calcified substance, covered by a layer of enamel.] |
| dentinogenesis | GO_0097187 | [The process whose specific outcome is the formation of dentin, the mineralized tissue that constitutes the major bulk of teeth. Dentin may be one of three types: primary dentin, secondary dentin, and tertiary dentin.] |
| dentin mineralization | GO_0097188 | [The process in which calcium salts are deposited into the calcareous tooth structure known as dentin.] |
| apoptotic body | GO_0097189 | [A vesicle containing parts of a dying cell. Apoptotic bodies can be formed during the execution phase of the apoptotic process, when the cell's cytoskeleton breaks up and causes the membrane to bulge outward. These bulges may separate from the cell, taking a portion of cytoplasm with them, to become apoptotic bodies. These are then engulfed by phagocytic cells, and their components recycled. Apoptotic bodies may range in size from 0.8 to 5um.] |
| GO_0000129 | GO_0000129 | |
| SAGA complex | GO_0000124 | [A SAGA-type histone acetyltransferase complex that contains Spt8 (in budding yeast) or a homolog thereof; additional polypeptides include Spt group, consisting of Spt7, Spt3, and Spt20/Ada5, which interact with the TATA-binding protein (TBP); the Ada group, consisting of Ada1, Ada2, Ada3, Ada4/Gcn5, and Ada5/Spt20, which is functionally linked to the nucleosomal HAT activity; Tra1, an ATM/PI-3 kinase-related protein that targets DNA-bound activators for recruitment to promoters; the TBP-associated factor (TAF) proteins, consisting of Taf5, Taf6, Taf9, Taf10, and Taf12, which mediate nucleosomal HAT activity and are thought to help recruit the basal transcription machinery; the ubiquitin specifc protease Ubp-8.] |
| SAGA-type complex | GO_0070461 | [A histone acetyltransferase complex that acetylates nucleosomal H3 and H2B and is required for the expression of a subset of Pol II-transcribed genes. The budding yeast complex includes the acetyltransferase Gcn5p, several proteins of the Spt and Ada families, and several TBP-associate proteins (TAFs); analogous complexes in other species have analogous compositions, and usually contain homologs of the yeast proteins.] |
| DUBm complex | GO_0071819 | [A protein complex that forms part of SAGA-type complexes SAGA and SLIK, and mediates deubiquitination of histone H2B. In S. cerevisiae, the DUBm consists of the proteins Ubp8p, Sgf11p, Sus1p, and Sgf73p.] |