All terms in GO
| Label | Id | Description |
|---|---|---|
| fructosyltransferase activity | GO_0050738 | [Catalysis of the transfer of a fructosyl group to an acceptor molecule, typically another carbohydrate or a lipid.] |
| peptide cross-linking via S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium | GO_0050739 | [The cross-linking of a tyrosine residue to a tryptophan residue and a methionine residue to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium.] |
| PRC1 complex | GO_0035102 | [A multiprotein complex that mediates monoubiquitination of lysine residues of histone H2A (lysine-118 in Drosophila or lysine-119 in mammals). The complex is required for stable long-term maintenance of transcriptionally repressed states and is involved in chromatin remodeling.] |
| ecdysone binding | GO_0035100 | [Interacting selectively and non-covalently with 20-hydroxyecdysone (ecdysone). Ecdysone is an ecdysteroid produced by the prothoracic glands of immature insects and the ovaries of adult females, which stimulates growth and molting.] |
| sterol binding | GO_0032934 | [Interacting selectively and non-covalently with a sterol, any steroid containing a hydroxy group in the 3 position, closely related to cholestan-3-ol.] |
| FACT complex | GO_0035101 | [An abundant nuclear complex, which was originally identified in mammalian systems as a factor required for transcription elongation on chromatin templates. The FACT complex has been shown to destablilize the interaction between the H2A/H2B dimer and the H3/H4 tetramer of the nucleosome, thus reorganizing the structure of the nucleosome. In this way, the FACT complex may play a role in DNA replication and other processes that traverse the chromatin, as well as in transcription elongation. FACT is composed of two proteins that are evolutionarily conserved in all eukaryotes and homologous to mammalian Spt16 and SSRP1. In metazoans, the SSRP1 homolog contains an HMG domain; however in fungi and protists, it does not. For example, in S. cerevisiae the Pob3 protein is homologous to SSRP1, but lacks the HMG chromatin binding domain. Instead, the yFACT complex of Spt16p and Pob3p, binds to nucleosomes where multiple copies of the HMG-domain containing protein Nhp6p have already bound, but Nhp6p does not form a stable complex with the Spt16p/Pob3p heterodimer.] |
| operant conditioning | GO_0035106 | [Learning to anticipate future events on the basis of past experience with the consequences of one's own behavior.] |
| learning | GO_0007612 | [Any process in an organism in which a relatively long-lasting adaptive behavioral change occurs as the result of experience.] |
| GO_0035104 | GO_0035104 | |
| obsolete sterol regulatory element binding protein import into nucleus | GO_0035105 | [OBSOLETE. The transfer of a sterol regulatory element binding protein (SREBP) into the nucleus, across the nuclear membrane, in response to altered levels of one or more lipids. SREBPs are transcription factors that bind sterol regulatory elements (SREs), DNA motifs found in the promoters of target genes.] |
| glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity | GO_0001888 | [Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan.] |
| hepaticobiliary system development | GO_0061008 | [The progression of the hepaticobiliary system over time, from its formation to the mature structure. The hepaticobiliary system is responsible for metabolic and catabolic processing of small molecules absorbed from the blood or gut, hormones and serum proteins, detoxification, storage of glycogen, triglycerides, metals and lipid soluble vitamins and excretion of bile. Included are the synthesis of albumin, blood coagulation factors, complement, and specific binding proteins.] |
| endothelial cell morphogenesis | GO_0001886 | [The change in form (cell shape and size) that occurs during the differentiation of an endothelial cell.] |
| CARD domain binding | GO_0050700 | [Interacting selectively and non-covalently with a CARD (N-terminal caspase recruitment) domain, a protein-protein interaction domain that belongs to the death domain-fold superfamily. These protein molecule families are similar in structure with each consisting of six or seven anti-parallel alpha-helices that form highly specific homophilic interactions between signaling partners. CARD exists in the N-terminal prodomains of several caspases and in apoptosis-regulatory proteins and mediates the assembly of CARD-containing proteins that participate in activation or suppression of CARD carrying members of the caspase family.] |
| pyrimidine nucleoside binding | GO_0001884 | [Interacting selectively and non-covalently with a pyrimidine nucleoside, a compound consisting of a pyrimidine base linked either to ribose or deoxyribose.] |
| nucleoside binding | GO_0001882 | [Interacting selectively and non-covalently with a nucleoside, a compound consisting of a purine or pyrimidine nitrogenous base linked either to ribose or deoxyribose.] |
| interleukin-1 secretion | GO_0050701 | [The regulated release of interleukin-1 from a cell. Interleukin 1 is produced mainly by activated macrophages; it stimulates thymocyte proliferation by inducing interleukin 2 release and it is involved in the inflammatory response.] |
| interleukin-1 production | GO_0032612 | [The appearance of interleukin-1 due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels.] |
| interleukin-1 beta secretion | GO_0050702 | [The regulated release of interleukin 1 beta from a cell.] |
| purine nucleoside binding | GO_0001883 | [Interacting selectively and non-covalently with a purine nucleoside, a compound consisting of a purine base linked either to ribose or deoxyribose.] |