Binding to a GAF protein domain. [GOC:yaf, InterPro:IPR003018]


response to macrophage colony-stimulating factor stimulus

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 a macrophage colony-stimulating factor stimulus. [GOC:yaf, PMID:14687666]


cellular response to macrophage colony-stimulating factor stimulus

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 a macrophage colony-stimulating factor stimulus. [GOC:yaf, PMID:14687666]


A body present in the cytoplasm of some dinoflagellates, which is the source of bioluminescence; emits light on acidification in the presence of oxygen. [GOC:mag, GOC:pr, PMID:4501583, PMID:5642469]


sucrose catabolic process to fructose-6-phosphate and glucose-6-phosphate

The chemical reactions and pathways resulting in the breakdown of sucrose, which proceeds by phosphorylation of sucrose to form sucrose-6-phosphate. The subsequent actions of a hydrolase and a fructokinase generate fructose-6-phosphate and glucose-6-phosphate. [GOC:bf, GOC:dgf, MetaCyc:SUCUTIL-PWY]


Catalysis of the reaction: S-adenosyl-L-methionine + protein L-glutamine = S-adenosyl-L-homocysteine + protein N-methyl-L-glutamine. [GOC:imk, PMID:11847124]


protein localization in endosome
protein localisation in endosome

A process in which a protein is transported to, or maintained in, a location within an endosome. [GOC:yaf]


Division of an imaginal disc-derived leg into a series of semi-repetitive parts or segments. The Drosophila leg, for example, has nine segments, each separated from the next by a flexible joint. [GOC:bf]


The inner, i.e. lumen-facing, lipid bilayer of the cyanelle envelope; also faces the cyanelle stroma. [GOC:aa, PMID:18976493]


The outer, i.e. cytoplasm-facing, lipid bilayer of the cyanelle envelope. [GOC:aa]


cyanelle envelope lumen
cyanelle periplasm

The region between the inner and outer lipid bilayers of the cyanelle envelope; includes the peptidoglycan layer. [GOC:aa]


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 interleukin-3 stimulus. [GOC:yaf]


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 interleukin-3 stimulus. [GOC:yaf]


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 erythropoietin stimulus. Erythropoietin is a glycoprotein hormone that controls erythropoiesis. [GOC:yaf]


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 erythropoietin stimulus. [GOC:yaf]


An transient hybrid organelle formed by fusion of a late endosome with a lysosome, and in which active degradation takes place. [GOC:pde, PMID:21878991]


The lipid bilayer surrounding an endolysosome. An endolysosome is a transient hybrid organelle formed by fusion of a late endosome with a lysosome. [GOC:pde]


The volume enclosed by the membrane of an endolysosome. An endolysosome is a transient hybrid organelle formed by fusion of a late endosome with a lysosome. [GOC:pde]


The process in which the anatomical structures of a limb joint are generated and organized. A limb joint is a flexible region that separates the rigid sections of a limb to allow movement in a controlled manner. [GOC:bf]


embryonic skeletal limb joint morphogenesis

The process, occurring in the embryo, in which the anatomical structures of a skeletal limb joint are generated and organized. A skeletal limb joint is the connecting structure between the bones of a limb. [GOC:bf, Wikipedia:Joint]


protein C inhibitor-transmembrane protease serine 7 complex location

plasma serine protease inhibitor-TMPRSS7 complex location

protein C inhibitor-matriptase-3 complex location

protein C inhibitor-TMPRSS7 complex location

A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 7 (TMPRSS7); formation of the complex inhibits the serine protease activity of transmembrane protease serine 7. [GOC:ans, PMID:15853774]


protein C inhibitor-TMPRSS11E complex location

protein C inhibitor-transmembrane protease serine 11E complex location

plasma serine protease inhibitor-TMPRSS11E complex location

A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and transmembrane protease serine 11E (TMPRSS11E); formation of the complex inhibits the serine protease activity of transmembrane protease serine 11E. [GOC:ans, PMID:15328353]


protein C inhibitor-tissue-type plasminogen activator complex location

protein C inhibitor-PLAT complex location

protein C inhibitor-tPA complex location

plasma serine protease inhibitor-PLAT complex location

A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and tissue-type plasminogen activator (PLAT); formation of the complex inhibits the serine protease activity of tissue-type plasminogen activator. [GOC:ans, PMID:10340997]


protein C inhibitor-PLAU complex location

plasma serine protease inhibitor-PLAU complex location

protein C inhibitor-uPA complex location

protein C inhibitor-U-plasminogen activator complex location

protein C inhibitor-urokinase-type plasminogen activator complex location

A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and urokinase-type plasminogen activator (PLAU); formation of the complex inhibits the serine protease activity of urokinase-type plasminogen activator. [GOC:ans, PMID:10340997, PMID:3501295, PMID:8536714]


plasma serine protease inhibitor-thrombin complex location

protein C inhibitor-thrombin complex location

protein C inhibitor-coagulation factor II complex location

A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and thrombin (F2); formation of the complex inhibits the serine protease activity of thrombin. [GOC:ans, PMID:6323392]


protein C inhibitor-kallikrein-3 complex location

plasma serine protease inhibitor-KLK3 complex location

protein C inhibitor-KLK3 complex location

protein C inhibitor-prostate-specific antigen complex location

A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and prostate-specific antigen (KLK3); formation of the complex inhibits the serine protease activity of prostate-specific antigen. [GOC:ans, PMID:1725227]


SERPINA5-plasma kallikrein complex location

serpin A5-plasma kallikrein complex location

protein C inhibitor-KLKB1 complex location

plasma serine protease inhibitor-plasma kallikrein complex location

protein C inhibitor-plasma kallikrein complex location

A heterodimeric protein complex that contains protein C inhibitor (SERPINA5) and plasma kallikrein (KLK1B); formation of the complex inhibits the serine protease activity of plasma kallikrein. [GOC:ans, PMID:2844223, PMID:8536714]


capping enzyme targeting to RNA polymerase II

recruitment of guanylyltransferase to RNA polymerase II holoenzyme complex

recruitment of mRNA capping enzyme to RNA polymerase II holoenzyme complex

The process in which the guanylyltransferase enzyme responsible for adding a 7-methylguanosine cap on pre-mRNA becomes associated with the RNA polymerase II holoenzyme complex and the 5' end of a transcript. [GOC:bf, GOC:rb, PMID:10594013]


neural crest cell emigration
neural crest cell individualization

The negative regulation of cell adhesion process in which a neural crest cell physically separates from the rest of the neural tube. [CL:0000333, PMID:17076275]


Binding to a mediator complex. The mediator complex is a protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins. [GOC:yaf, PMID:18391015]


The aggregation, arrangement and bonding together of a set of components to form a mediator complex. The mediator complex is a protein complex that interacts with the carboxy-terminal domain of the largest subunit of RNA polymerase II and plays an active role in transducing the signal from a transcription factor to the transcriptional machinery. The Saccharomyces complex contains several identifiable subcomplexes: a head domain comprising Srb2, -4, and -5, Med6, -8, and -11, and Rox3 proteins; a middle domain comprising Med1, -4, and -7, Nut1 and -2, Cse2, Rgr1, Soh1, and Srb7 proteins; a tail consisting of Gal11p, Med2p, Pgd1p, and Sin4p; and a regulatory subcomplex comprising Ssn2, -3, and -8, and Srb8 proteins. Metazoan mediator complexes have similar modular structures and include homologs of yeast Srb and Med proteins. [GOC:yaf, PMID:17641689]


The process whose specific outcome is the progression of a osteoclast from its formation to the mature structure. Cell development does not include the steps involved in committing a cell to a specific fate. An osteoclast is a specialized phagocytic cell associated with the absorption and removal of the mineralized matrix of bone tissue. [CL:0000092, GOC:bf, GOC:yaf]


The negative regulation of cell adhesion process in which a cardiac neural crest cell physically separates from the rest of the neural tube. [GOC:hjd, PMID:17076275, PMID:18539270, PMID:20490374]


CD8-positive, alpha-beta T cell activation

The change in morphology and behavior of a CD8-positive, alpha-beta T cell resulting from exposure to a mitogen, cytokine, chemokine, cellular ligand, or an antigen for which it is specific. [CL:0000625, GOC:yaf]


The chemical reactions and pathways involving the polyphenol, curcumin. [PMID:21467222]


The chemical reactions and pathways resulting in the breakdown of the polyphenol, curcumin. [PMID:21467222]


Binding to a long-chain fatty acid. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. [GOC:pm, PMID:12641450]


Binding to a long-chain fatty acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. Long-chain fatty-acyl-CoAs have chain lengths of C13 or more. [GOC:krc, GOC:pm]


The removal of a malonyl group (CO-CH2-CO), from an amino acid residue within a protein or peptide. [GOC:sp, PMID:22076378]


The process of removing a malonyl group (CO-CH2-CO) from an malonylated lysine residue in a peptide or protein. [GOC:sp, PMID:22076378]


The removal of a succinyl group (CO-CH2-CH2-CO) from a residue in a peptide or protein. [GOC:sp, PMID:22076378]


The removal of a succinyl group (CO-CH2-CH2-CO) from a succinylated lysine residue in a peptide or protein. [GOC:sp, PMID:22076378]


The modification of a peptidyl-lysine residue by the addition of a succinyl group (CO-CH2-CH2-CO) to form N6-succinyl-L-lysine. [GOC:jsg, GOC:sp, PMID:21151122, RESID:AA0545]


A process in which a protein is transported to, or maintained at, the trailing edge. The trailing edge is the area of a motile cell opposite to the direction of movement. [GOC:pf, GOC:pg]


A process in which a protein is transported to, or maintained in, a uropod. A uropod is a membrane projection with related cytoskeletal components at the trailing edge of a migrating cell. [GOC:add, GOC:pf, ISBN:0781735149, PMID:12714569, PMID:12787750]


glomerular endothelial cell fenestration

A large plasma membrane-lined circular pore that perforates the flattened glomerular endothelium and, unlike those of other fenestrated capillaries, is not spanned by diaphragms; the density and size of glomerular fenestrae account, at least in part, for the high permeability of the glomerular capillary wall to water and small solutes. [GOC:cjm, MP:0011454, PMID:19129259]


protein malonyl lysine demalonylation activity

Catalysis of the reaction: protein-malonyllysine + H2O => protein-lysine + malonate. This reaction is the removal of a malonyl group (CO-CH2-CO) from a malonylated lysine residue of a protein or peptide. [GOC:sp, PMID:21908771, PMID:22076378]


Catalysis of the reaction: H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide. [GOC:sp, PMID:22076378]


A specialized cell-cell junction found between the cells of the excretory system, which provides a barrier for filtration of blood or hemolymph. [GOC:mtg_kidney_jan10, GOC:sart, PMID:18971929]


A specialized cell-cell junction found between the interdigitating foot processes of the glomerular epithelium (the podocytes) in the vertebrate kidney, which is adapted for facilitating glomerular filtration. [GOC:mtg_kidney_jan10, GOC:rph, PMID:12386277, PMID:15994232, PMID:18971929, PMID:19478094]


The aggregation, arrangement and bonding together of a set of components to form a filtration diaphragm, a specialized cell-cell junction found between the cells of the excretory system, which provides a barrier for filtration of blood or hemolymph. [GOC:mtg_kidney_jan10, PMID:18971929]


The aggregation, arrangement and bonding together of a set of components to form a nephrocyte diaphragm, a specialized cell-cell junction found between nephrocytes of the insect kidney. [GOC:mtg_kidney_jan10, GOC:sart, PMID:18971929]


The aggregation, arrangement and bonding together of a set of components to form a slit diaphragm, specialized cell-cell junction found between the interdigitating foot processes of the glomerular epithelium (the podocytes) in the vertebrate kidney, which is adapted for facilitating glomerular filtration. [GOC:mtg_kidney_jan10, GOC:rph, PMID:20633639]


muscle cell chemotaxis towards tendon cell

muscle cell chemotaxis toward tendon cell

The directed movement of a muscle cell towards a tendon cell in response to an external stimulus. Tendon cells, for example, produce positive guidance cues that attract muscle cells. [GOC:sart, PMID:19793885]


pre-synaptic periactive zone
periactive zone

A region that surrounds the active zone of the presynaptic plasma membrane, and is specialized for the control of synaptic development. [GOC:sart, PMID:10976048, PMID:18439406]


A cone-shaped structure in the head of a spermatozoon, which is formed by the coalescence of Golgi fragments following the completion of meiosis. The acroblast is situated adjacent to the acrosomal vesicle. [GOC:sart, PMID:19934220]


The covalent attachment of a fucosyl group to an acceptor molecule. [GOC:sart, PMID:19948734]


The process of transferring a fucosyl group to a serine or threonine residues in a protein acceptor molecule, to form an O-linked protein-sugar linkage. [GOC:sart, PMID:19948734]


light dependent chlorophyll biosynthetic process

light-dependent chlorophyll biosynthetic process

The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the presence of light. [GOC:yaf, PMID:12242396]


light independent chlorophyll biosynthetic process

light-independent chlorophyll biosynthetic process

The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the absence of light. [GOC:yaf, PMID:12242396, UniPathway:UPA00670]


light dependent bacteriochlorophyll biosynthetic process

light-dependent bacteriochlorophyll biosynthetic process

The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the presence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants. [GOC:yaf, PMID:12242396]


light independent bacteriochlorophyll biosynthetic process

light-independent bacteriochlorophyll biosynthetic process

The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the absence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants. [GOC:yaf, PMID:12242396, UniPathway:UPA00671]


The process of transferring a fucosyl group to an N-glycan. An N-glycan is the carbohydrate portion of an N-glycoprotein when attached to a nitrogen from asparagine or arginine side-chains. [GOC:sart, PMID:19948734]


The formation of bone or of a bony substance, or the conversion of fibrous tissue or of cartilage into bone or a bony substance, that does not require the replacement of preexisting tissues. [GO_REF:0000034]


Intramembranous ossification from the surface of a cartilage element as the perichondrium becomes a periosteum, without replacement of cartilage. [GO_REF:0000034]


Ossification that requires the replacement of a preexisting tissue prior to bone tissue formation. [GO_REF:0000034]


Ossification wherein bone tissue forms within ligamentous tissue. [GO_REF:0000034]


Ossification wherein bone tissue forms within tendonous tissue. [GO_REF:0000034]


minus-end specific microtubule depolymerization

The removal of tubulin heterodimers from the minus end of a microtubule. [GOC:sart, PMID:17452528]


purine nucleotide-sugar transmembrane transporter activity

Enables the transfer of a purine nucleotide-sugar from one side of a membrane to the other. Purine nucleotide-sugars are purine nucleotides in glycosidic linkage with a monosaccharide or monosaccharide derivative. [GOC:sart, PMID:19948734]


extracellular ammonia-gated ion channel activity

Enables the transmembrane transfer of an ion by a channel that opens when extracellular ammonia (NH3) has been bound by the channel complex or one of its constituent parts. [GOC:sart, PMID:19135896]


extracellular phenylacetaldehyde-gated ion channel activity

Enables the transmembrane transfer of an ion by a channel that opens when extracellular phenylacetaldehyde has been bound by the channel complex or one of its constituent parts. [GOC:sart, PMID:19135896]


ionotropic phenylacetaldehyde receptor activity


GDP-fucose transport into endoplasmic reticulum lumen

GDP-fucose transport across endoplasmic reticulum membrane

GDP-fucose import into endoplasmic reticulum lumen

The directed movement of GDP-fucose into the endoplasmic reticulum lumen. GDP-fucose is a substance composed of fucose in glycosidic linkage with guanosine diphosphate. [GOC:sart, PMID:3458237]


GDP-fucose transport across Golgi membrane

The directed movement of GDP-fucose into the Golgi lumen. GDP-fucose is a substance composed of fucose in glycosidic linkage with guanosine diphosphate. [GOC:sart, PMID:3458237]


positive regulation of transcription from RNA polymerase II promoter in response to iron deficiency

positive regulation of transcription from RNA polymerase II promoter in response to iron ion starvation

Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of deprivation of iron ions. [GOC:cjk]


glutathione synthetase complex
glutathione synthase complex location
glutathione synthetase complex location

A protein complex composed of two or more polypeptide subunits, and which possesses glutathione synthase activity (catalysis of the reaction: L-gamma-glutamyl-L-cysteine + ATP + glycine = ADP + glutathione + 2 H(+) + phosphate). In eukaryotes, the complex is homodimeric, in E. coli glutathione synthase exists as a tetramer, and in S. pombe the complex exists as a homodimer or a heterotetramer. [GOC:al, PMID:12734194, PMID:14990577, PMID:1958212]


D-serine catabolism
D-serine breakdown
D-serine degradation

The chemical reactions and pathways resulting in the breakdown of D-serine, the D-enantiomer of serine, i.e. (2S)-2-amino-3-hydroxypropanoic acid. [GOC:imk]


Generation of the cleavage furrow, a shallow groove in the cell surface near the old metaphase plate that marks the site of cytokinesis. This process includes the recruitment and localized activation of signals such as RhoA at the site of the future furrow to ensure that furrowing initiates at the correct site in the cell. [GOC:ans, PMID:15811947, PMID:20687468, PMID:2192590]


Advancement of the cleavage furrow from the outside of the cell inward towards the center of the cell. The cleavage furrow acts as a 'purse string' which draws tight to separate daughter cells during cytokinesis and partition the cytoplasm between the two daughter cells. The furrow ingresses until a cytoplasmic bridge is formed. [PMID:15811947, PMID:20687468]


positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:rn, PMID:14978214, PMID:18439143]


The chemical reactions and pathways resulting in the formation of phosphatidylinositol-3-phosphate, a phosphatidylinositol monophosphate carrying the phosphate group at the 3-position. [GOC:al, GOC:vw]


The multiplication or reproduction of germ cells, reproductive cells in multicellular organisms, resulting in the expansion of a cell population. [CL:0000586, GOC:kmv]


Binding to a small molecule, any low molecular weight, monomeric, non-encoded molecule. [GOC:curators, GOC:pde, GOC:pm]


OBSOLETE. Any process involved in forming the mature 3' end of a miRNA from a pre-miRNA. [GOC:sart, PMID:22055292]


miRNA 3'-end processing
miRNA 3' end terminal trimming
miRNA trimming


male germ-line stem cell population maintenance

The process by which an organism or tissue maintains a population of male germ-line stem cells. [GOC:sart, PMID:21752937]


female germ-line stem cell population maintenance

The process by which an organism or tissue maintains a population of female germ-line stem cells. [GOC:sart]


leukotriene B4 degradation
leukotriene B4 breakdown
LTB4 catabolism
leukotriene B4 catabolism

The chemical reactions and pathways resulting in the breakdown of leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents. [GOC:yaf, PMID:9799565, UniPathway:UPA00883]


The chemical reactions and pathways involving leukotriene B4, a leukotriene composed of (6Z,8E,10E,14Z)-eicosatetraenoic acid having (5S)- and (12R)-hydroxy substituents. [GOC:bf]


The chemical reactions and pathways involving Kdo2-lipid A, a lipopolysaccharide (LPS) component. [GOC:bf]


The chemical reactions and pathways resulting in the formation of Kdo2-lipid A, a lipopolysaccharide (LPS) component. [GOC:yaf, UniPathway:UPA00360]


peroxisome membrane class-1 targeting sequence binding

Binding to a class I peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane in a PEX19-dependent manner. [GOC:pm, PMID:14709540, PMID:17020786]


peroxisome membrane class-2 targeting sequence binding

Binding to a class II peroxisomal membrane targeting sequence, any of several sequences of amino acids within a protein that can act as a signal for the localization of the protein into the peroxisome membrane in a PEX19-independent manner. [GOC:pm, PMID:14709540, PMID:17020786]


undecaprenyl phosphate alpha-L-Ara4N metabolism

4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate metabolic process

4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate metabolic process

The chemical reactions and pathways involving 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N). [PMID:15695810]


4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate synthesis

undecaprenyl phosphate alpha-L-Ara4N biosynthesis

4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate formation

4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthesis

4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate anabolism

4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process

The chemical reactions and pathways resulting in the formation of 4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate, a precursor of 4-amino-4-deoxy-L-arabinose (L-Ara4N). [GOC:yaf, PMID:15695810, UniPathway:UPA00036]


cellular response to inositol starvation

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 deprivation of inositol. [GOC:al, PMID:19606215]


very long-chain fatty acyl CoA metabolic process

very long-chain fatty acyl-CoA metabolism

very long-chain fatty-acyl-CoA metabolic process

The chemical reactions and pathways involving very long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22. [GOC:pm]


medium-chain fatty acyl CoA metabolic process

medium-chain fatty-acyl-CoA metabolic process

The chemical reactions and pathways involving medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a long-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12. [GOC:pm]


very long-chain fatty-acyl-CoA breakdown

very long-chain fatty-acyl-CoA catabolism

very long-chain fatty-acyl-CoA degradation

very long-chain fatty-acyl-CoA catabolic process

The chemical reactions and pathways resulting in the breakdown of very long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A very long-chain fatty acid is a fatty acid which has a chain length greater than C22. [GOC:pm]


medium-chain fatty-acyl-CoA breakdown
medium-chain fatty-acyl-CoA catabolism
medium-chain fatty-acyl-CoA degradation

medium-chain fatty-acyl-CoA catabolic process

The chemical reactions and pathways resulting in the breakdown of medium-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A medium-chain fatty acid is a fatty acid with a chain length of between C6 and C12. [GOC:pm]


fatty-acyl-CoA catabolism
fatty-acyl-CoA degradation
fatty-acyl-CoA breakdown

The chemical reactions and pathways resulting in the breakdown of a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty-acyl group. [PMID:10578051]


long-chain fatty-acyl-CoA breakdown
long-chain fatty-acyl-CoA catabolism
long-chain fatty-acyl-CoA degradation

long-chain fatty-acyl-CoA catabolic process

The chemical reactions and pathways resulting in the breakdown of long-chain fatty-acyl-CoAs, any derivative of coenzyme A in which the sulfhydryl group is in a thioester linkage with a medium-chain fatty-acyl group. A long-chain fatty acid is a fatty acid with a chain length between C13 and C22. [GOC:pm]


A cable structure, surrounding some cell types (e.g. proximal or bronchial tubular epithelial cells), and composed of hyaluranon (HA), a ubiquitous connective tissue glycosaminoglycan. [GOC:yaf, PMID:16900089]


A process that results in the aggregation, arrangement and bonding together of a hyaluranon cable, a cable structure, surrounding some cell types (e.g. proximal or bronchial tubular epithelial cells), and composed of hyaluranon (HA), a ubiquitous connective tissue glycosaminoglycan. [GOC:yaf, PMID:16900089]


response to platelet-derived growth factor stimulus

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 a platelet-derived growth factor stimulus. [GOC:yaf]


cellular response to platelet-derived growth factor stimulus

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 a platelet-derived growth factor stimulus. [GOC:yaf]


dsDNA-dependent ATP-dependent DNA helicase activity

double-stranded DNA-dependent ATP-dependent DNA helicase activity

double-stranded DNA-dependent ATPase activity

Catalysis of the reaction: ATP + H2O = ADP + phosphate, in the presence of double-stranded DNA; drives the unwinding of a DNA helix. [GOC:kmv]


Binding to a member of the bone morphogenetic protein (BMP) family. [GOC:BHF, PMID:9660951]


histone lysine H3 K9 dimethylation
histone H3 K9 dimethylation

The modification of histone H3 by addition of two methyl groups to lysine at position 9 of the histone. [GOC:vw]


The modification of histone H3 by addition of three methyl groups to lysine at position 9 of the histone. [GOC:vw]


Binding to 3-sulfino-L-alanine (cysteine sulfinate). [GOC:al, PMID:8346915]


CatSper channel complex location
CATSPER channel
CatSper complex location
CatSper channel complex

A sperm-specific voltage-gated calcium channel that controls the intracellular calcium ion concentration and, thereby, the swimming behavior of sperm. Consists of a heteromeric tetramer surrounding a calcium ion- selective pore. May also contain additional auxiliary subunits. [GOC:sp, PMID:17478420, PMID:21224844, PMID:22354039]


PGH2 9,11-endoperoxidase
PGH2 9-,11-endoperoxide reductase

prostaglandin H2 endoperoxidase reductase activity

Catalysis of the reaction: prostaglandin H2 + NADPH + H+ -> prostaglandin F2alpha + NADP+. This reaction is the reduction of prostaglandin H2 ((5Z,13E)-(15S)-9alpha,11alpha-Epidioxy-15-hydroxyprosta-5,13-dienoate) to prostaglandin F2alpha ((5Z,13E)-(15S)-9alpha,11alpha,15-Trihydroxyprosta-5,13-dienoate). [GOC:mw, KEGG_REACTION:R02264, PMID:10622721, PMID:14979715, PMID:16475787]


NAD dependent 11-hydroxythromboxane B2 dehydrogenase activity

Catalysis of the reaction: thromboxane B2 + NAD+ = 11-dehydro-thromboxane B2 + NADH + H+. [GOC:mw, KEGG_REACTION:R05060, PMID:3461463, PMID:3823488, PMID:8200461]


12-hydroxyheptadecatrienoic acid synthase activity

Catalysis of the reaction: prostaglandin H2 = 12-hydroxyheptadecatrienoic acid (HHT) + malonaldehyde (MDA). [GOC:mw, PMID:11297515]


The orderly movement of a Schwann cell from one site to another. A Schwann cell is a glial cell that ensheathes axons of neuron in the peripheral nervous system and is necessary for their maintainance and function. [CL:0002573, PMID:20335460]


Catalysis of the reaction: L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-aspartate. [EC:2.6.1.-, GOC:pde, PMID:15606768, PMID:4149765]


The hydroxylation of peptidyl-histidine to form peptidyl-hydroxyhistidine. [GOC:reh, PMID:21251231]


Catalysis of the reaction: peptidyl L-histidine + 2-oxoglutarate + O2 = peptidyl hydroxy-L-histidine + succinate + CO2. [GOC:reh, PMID:21251231]


Catalysis of the reaction: peptidyl L-asparagine + 2-oxoglutarate + O2 = peptidyl 3-hydroxy-L-asparagine + succinate + CO2. [GOC:reh, PMID:12215170]


Catalysis of the reaction L-phenylalanine + oxaloacetate = phenylpyruvate + aspartate. [GOC:pde, PMID:15606768]


Binding to a kringle domain. Kringle domains are protein domains that fold into large loops stabilized by 3 disulfide linkages, and are important in protein-protein interactions with blood coagulation factors. [GOC:yaf, Wikipedia:Kringle_domain]


The process of regulating the proliferation and elimination of dendritic cells such that the total number of dendritic cells within a whole or part of an organism is stable over time in the absence of an outside stimulus. [CL:0000451, GOC:uh, PMID:12570827, PMID:19176316]


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 a mycotoxin stimulus. A mycotoxin is a toxic chemical substance produced by fungi. [GOC:di, PMID:20548963]


Remodeling the acyl chains of phosphatidylglycerol, through sequential deacylation and re-acylation reactions, to generate phosphatidylglycerol containing different types of fatty acid acyl chains. [GOC:mw, PMID:15485873, PMID:18458083]


Remodeling the acyl chains of phosphatidylinositol, through sequential deacylation and re-acylation reactions, to generate phosphatidylinositol containing different types of fatty acid acyl chains. [GOC:mw, PMID:18094042, PMID:18772128]


Remodeling the acyl chains of phosphatidylserine, through sequential deacylation and re-acylation reactions, to generate phosphatidylserine containing different types of fatty acid acyl chains. [GOC:mw, PMID:18287005, PMID:18458083]


Remodeling the acyl chains of phosphatidylcholine, through sequential deacylation and re-acylation reactions, to generate phosphatidylcholine containing different types of fatty acid acyl chains. [GOC:mw, PMID:18195019, PMID:18458083]


Remodeling the acyl chains of phosphatidylethanolamine, through sequential deacylation and re-acylation reactions, to generate phosphatidylethanolamine containing different types of fatty acid acyl chains. [GOC:mw, PMID:18287005, PMID:18458083]


Remodeling the acyl chains of triacylglycerol, through sequential deacylation and re-acylation reactions, to generate triacylglycerol containing different types of fatty acid acyl chains. [GOC:mw, PMID:15364929]


Remodeling the acyl chains of diacylglycerol, through sequential deacylation and re-acylation reactions, to generate diacylglycerol containing different types of fatty acid acyl chains. [GOC:mw, PMID:15364929]


Remodeling the acyl chains of an acylglycerol, through sequential deacylation and re-acylation reactions, to generate an acylglycerol containing different types of fatty acid acyl chains. [GOC:mw, PMID:15364929]


inner dynein arm complex
inner dynein arm complex location

Inner arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes. The structure of inner dynein arms is complex and may vary within the axoneme. Inner dynein arms are heteromeric, comprising 8 different heavy chains and various subunits. Inner and outer dynein arms have different functions in the generation of microtubule-based motility. [GOC:BHF, GOC:vk, PMID:19347929, PMID:2557057, PMID:7962092]


outer dynein arm complex location
outer dynein arm complex

Outer arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes. Outer dynein arms contain 2-3 heavy chains, two or more intermediate chains and a cluster of 4-8 light chains. Inner and outer dynein arms have different functions in the generation of microtubule-based motility. [GOC:BHF, GOC:vk, PMID:2557057, PMID:6218174]


The aggregation, arrangement and bonding together of a set of components to form an axonemal dynein outer arm, an outer arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes. [GOC:BHF, GOC:vk, PMID:19944400]


The aggregation, arrangement and bonding together of a set of components to form an axonemal dynein inner arm, an inner arm structure present on the outer doublet microtubules of ciliary and flagellar axonemes. [GOC:BHF, GOC:vk, PMID:19944400]


The regulated release of a melanocyte-stimulating hormone, any of a group of peptide hormones that are produced by cells in the intermediate lobe of the pituitary gland, and stimulate the production of melanin to increase pigmentation. [GOC:cjm, Wikipedia:Melanocyte-stimulating_hormone]


The regulated release of calcitonin, a peptide hormone that participates in calcium and phosphorus metabolism, from a cell. [GOC:cjm]


3-hexaprenyl-4-hydroxy-5-methoxybenzoic acid decarboxylase activity

Catalysis of the reaction: 3-hexaprenyl-4-hydroxy-5-methoxybenzoic acid -> 2-hexaprenyl-6-methoxyphenol + CO2. [GOC:mw, KEGG_REACTION:R06866, PMID:620805, PMID:7028108]


The attachment of a cell to an underlying abiotic (non-living) substrate via adhesion molecules. [GOC:di]


invasive growth in response to elevated temperature

invasive growth in response to high temperature

The growth of colonies in filamentous chains of cells as a result of an increase in temperature. [GOC:di, PMID:22365851]


invasive growth in response to temperature stimulus


A reversible switch of a cell from one cell type or form to another, at a frequency above the expected frequency for somatic mutations. Phenotypic switching involves changes in cell morphology and altered gene expression patterns. For example, Candida albicans switches from white cells to opaque cells for sexual mating. Phenotypic switching also occurs in multicellular organisms; smooth muscle cells (SMCs) exhibit phenotypic transitions to allow rapid adaption to fluctuating environmental cues. [GOC:bf, GOC:di, PMID:12443899, PMID:22406749, PMID:8456504, Wikipedia:Phenotypic_switching]


phenotypic switching in response to host

A reversible switch of a cell from one phenotype to another that occurs upon infection of a host or host cell. For example, Candida albicans switches from a unicellular form to an invasive multicellular filamentous form upon infection of host tissue. Phenotypic switching begins with changes in cell morphology and altered gene expression patterns and ends when the morphology of a population of cells has reverted back to the default state, accompanied by altered expression patterns. [GOC:di, PMID:16696644, Wikipedia:Phenotypic_switching]


filamentous growth of a population of unicellular organisms in response to heat

The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to an increase in temperature. [GOC:di, PMID:17554048]


3-methoxy-4-hydroxy-5-decaprenylbenzoic acid decarboxylase activity

Catalysis of the reaction: 3-methoxy-4-hydroxy-5-decaprenylbenzoic acid -> 2-methoxy-6-decaprenylphenol + CO2. [GOC:mw, PMID:620805, PMID:7028108]


filamentous growth of a population of unicellular organisms in response to starvation

The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to deprivation of nourishment. [GOC:di, PMID:17554048]


filamentous growth of a population of unicellular organisms in response to chemical stimulus

The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a chemical stimulus. [GOC:di, PMID:17554048]


A process that generates thiamine (vitamin B1) from derivatives of it without de novo synthesis. [PMID:15150256, PMID:16952958]


Binding to a thiosulfate, a sulfur oxide that has formula O3S2. [GOC:db, PMID:2188959]


ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor

Catalysis of the reaction: 2'-deoxyribonucleoside diphosphate + glutaredoxin disulfide + H2O -> ribonucleoside diphosphate + glutaredoxin. [EC:1.17.4.1, GOC:bf, GOC:pde, PMID:7476363]


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 a neutral pH (pH close to 7) stimulus. pH is a measure of the acidity or basicity of an aqueous solution. [GOC:di, Wikipedia:PH]


filamentous growth of a population of unicellular organisms in response to pH

The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a pH stimulus. pH is a measure of the acidity or basicity of an aqueous solution. [GOC:di, Wikipedia:PH]


filamentous growth of a population of unicellular organisms in response to neutral pH

The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a neutral pH (pH close to 7) stimulus. [GOC:di, PMID:6374461]


A developmental process, independent of morphogenetic (shape) change, that is required for an osteoclast cell to attain its fully functional state. An osteoclast is a specialized phagocytic cell associated with the absorption and removal of the mineralized matrix of bone tissue, and which typically differentiates from monocytes. [CL:0000092, GOC:pg]


filamentous growth of a population of unicellular organisms in response to biotic stimulus

The process in which a group of unicellular organisms grow in a threadlike, filamentous shape in response to a biotic (living) stimulus. [GOC:di]


A cellular protein localization process in which a protein is transported to, or maintained at, a linear element. A linear element is a proteinaceous scaffold associated with S. pombe chromosomes during meiotic prophase. [GOC:mah, PMID:19756689]


epidermal growth factor receptor ligand maturation

Any process leading to the attainment of the full functional capacity of a ligand for an epidermal growth factor receptor. The ligand is functional when it can bind to and activate an epidermal growth factor receptor. [GOC:signaling, PMID:11672524, PMID:11672525]


peptide bond cleavage involved in epidermal growth factor receptor ligand maturation


netrin receptor activity involved in positive chemotaxis

netrin receptor activity involved in chemoattraction

Combining with a netrin signal and transmitting the signal from one side of the membrane to the other to contribute to the directed movement of a motile cell towards a higher concentration of netrin. [GOC:signaling]


netrin-activated signal transduction pathway

The series of molecular signals initiated by the binding of a netrin protein to its receptor on the surface of the target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. Netrins can act as chemoattractant signals for some cells and chemorepellent signals for others. Netrins also have roles outside of cell and axon guidance. [GOC:signaling, PMID:10399919, PMID:15960985, PMID:19785719, PMID:20108323]


tumor necrosis factor receptor-associated factor signal transduction

tumor necrosis factor receptor-associated factor signaling

The intracellular process in which a signal is passed on to downstream components within the cell via a tumor necrosis factor receptor-associated factor (TRAF). TRAFs are directly or indirectly recruited to the intracellular domains of cell surface receptors, and engage other signaling proteins to transfer the signal from a cell surface receptor to other intracellular signaling components. [GOC:bf, PMID:19918944, PMID:20596822]


regulation of signaling pathway by receptor endocytosis

regulation of signal transduction by receptor internalization

Any process that modulates the frequency, rate or extent of signal transduction by the movement of a signaling receptor from the plasma membrane to the inside of the cell. Receptor internalization can have a positive or negative effect on a signaling pathway. [GOC:bf, GOC:signaling, PMID:17011816, PMID:19696798]


positive regulation of signaling pathway by receptor endocytosis

positive regulation of signal transduction by receptor internalization

Any process in which the internalization of a signaling receptor activates or increases the frequency, rate or extent of signal transduction. Receptor internalization can enhance signaling by concentrating signaling molecules in one location, or by moving a ligand-activated receptor to the location of downstream signaling proteins. Endosomes for example can serve as important intracellular signaling platforms. [GOC:bf, GOC:signaling, PMID:17908284, PMID:19696798]


negative regulation of signaling pathway by receptor endocytosis

negative regulation of signal transduction by receptor internalization

Any process in which internalization of a signaling receptor stops, prevents, or reduces the frequency, rate or extent of signal transduction. Receptor internalization can attenuate or reduce the strength of signaling by reducing the concentration of cell surface receptors available to ligands. [GOC:bf, GOC:signaling, PMID:17908284, PMID:19696798]


negative regulation of Wnt receptor signaling pathway by Wnt receptor internalization

negative regulation of Wnt-activated signaling pathway by Wnt receptor internalization

negative regulation of Wnt receptor signalling pathway by Wnt receptor internalization

negative regulation of Wnt signaling pathway by Wnt receptor internalization

Any process in which internalization of a Wnt receptor stops, prevents, or reduces the frequency, rate or extent of Wnt signal transduction. [GOC:bf, GOC:BHF, GOC:rl, PMID:17908284, PMID:19643732]


ligand-dependent internalization of Frizzled


negative regulation of Wnt receptor signaling pathway by Wnt receptor endocytosis


positive regulation of Wnt receptor signaling pathway by Wnt receptor internalization

positive regulation of Wnt receptor signalling pathway by Wnt receptor endocytosis

positive regulation of Wnt signaling pathway by Wnt receptor internalization

Any process in which internalization of a Wnt receptor activates or increases the frequency, rate or extent of the Wnt signaling pathway. [GOC:bf, GOC:signaling, PMID:17908284]


positive regulation of Wnt receptor signaling pathway by Frizzled internalization


positive regulation of Wnt receptor signaling pathway by LRP6 internalization


negative regulation of insulin receptor signalling pathway by insulin receptor internalization

negative regulation of insulin receptor signaling pathway by insulin receptor internalization

Any process in which internalization of an insulin receptor stops, prevents, or reduces the frequency, rate or extent of insulin receptor signal transduction. Internalization of insulin in association with its receptor clears insulin from the circulation and is necessary for subsequent insulin dissociation from the receptor and insulin degradation. [GOC:bf, GOC:signaling, PMID:18492485, PMID:7821727, PMID:7978876, PMID:9609114]


agonist-stimulated insulin receptor internalization


positive regulation of insulin receptor signalling pathway by insulin receptor internalization

positive regulation of insulin receptor signaling pathway by insulin receptor internalization

Any process in which internalization of an insulin receptor activates or increases the frequency, rate or extent of the insulin receptor signaling pathway. Endocytosis of activated receptors can concentrate receptors within endosomes and allow the insulin receptor to phosphorylate substrates that are spatially distinct from those accessible at the plasma membrane. [GOC:bf, GOC:signaling, PMID:9609114]


A receptor-mediated endocytosis process that results in the movement of an insulin receptor from the plasma membrane to the inside of the cell. [GOC:bf, PMID:3907718, PMID:9609114]


A receptor-mediated endocytosis process that results in the movement of a Wnt receptor from the plasma membrane to the inside of the cell. [GOC:bf, PMID:17908284]


negative regulation of Wnt receptor signaling pathway by Wnt receptor degradation

The chemical reactions and pathways resulting in the breakdown of a Wnt receptor. Internalized Wnt receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation. [GOC:BHF, GOC:rl, GOC:signaling, PMID:19643732]


The process that results in the return of a Wnt receptor to an active state at the plasma membrane. An active state is when the receptor is ready to receive a Wnt signal. Internalized Wnt receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation. [GOC:bf, GOC:signaling, PMID:19643732]


The process that results in the return of an insulin receptor to an active state at the plasma membrane. An active state is when the receptor is ready to receive an insulin signal. Internalized insulin receptors can be recycled to the plasma membrane or sorted to lysosomes for protein degradation. [GOC:bf, GOC:signaling, PMID:3907718]


Combining with the fat-cell specific hormone leptin and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:bf, GOC:signaling, PMID:9102398, Wikipedia:Leptin_receptor]


G-protein coupled olfactory receptor activity

G-protein coupled odorant receptor activity

odorant receptor activity, G-protein coupled

olfactory receptor activity, G-protein coupled

G protein-coupled olfactory receptor activity

Combining with an odorant and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex. [GOC:bf, GOC:sart, PMID:21041441]


receptor activity involved in signal transduction

Receiving a signal and transmitting it in the cell to initiate a change in cell activity. A signal is a physical entity or change in state that is used to transfer information in order to trigger a response. [GOC:bf, GOC:signaling]


receptor activity involved in receptor-mediated endocytosis

Binding specifically to a substance (cargo) to deliver it to a transport vesicle. Cargo receptors span a membrane (either the plasma membrane or a vesicle membrane), binding simultaneously to cargo molecules and coat adaptors, to efficiently recruit soluble proteins to nascent vesicles. [PMID:15239958, PMID:27903609]


Combining with the secreted glycoprotein reelin, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:bf, PMID:12827279, PMID:20223215]


reelin-mediated signal transduction pathway

The series of molecular signals initiated by the binding of reelin (a secreted glycoprotein) to a receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:bf, PMID:12827279, PMID:20223215]


apolipoprotein A-I-mediated signalling pathway

apolipoprotein A-I-mediated signaling pathway

The series of molecular signals initiated by apolipoprotein A-I binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:bf, GOC:signaling, PMID:16443932]


insulin receptor signalling pathway via phosphatidylinositol 3-kinase cascade

insulin receptor signaling pathway via phosphatidylinositol 3-kinase cascade

insulin receptor signaling pathway via PI3K cascade

An insulin receptor signaling pathway in which the signal is transmitted via the phosphatidylinositol 3-kinase cascade. [GOC:bf, GOC:signaling, PMID:19322168, PMID:20696212]


epidermal growth factor receptor signaling pathway via MAPKKK cascade

EGFR signaling pathway via MAPKKK cascade

epidermal growth factor receptor signalling pathway via MAPKKK cascade

epidermal growth factor receptor signaling pathway via MAPK cascade

An epidermal growth factor receptor signaling pathway in which the signal is transmitted via the MAPKKK cascade. [GOC:bf, GOC:signaling, PMID:21167805]


non-canonical Wnt receptor signaling pathway via MAPK cascade

non-canonical Wnt receptor signaling pathway via MAPKKK cascade

non-canonical Wnt-activated signaling pathway via MAPK cascade

non-canonical Wnt receptor signalling pathway via MAPKKK cascade

non-canonical Wnt receptor signaling pathway via MAPK signaling

non-canonical Wnt signaling pathway via MAPK cascade

The series of molecular signals initiated by a Wnt protein binding to a frizzled family receptor on the surface of a target cell, where the signal is passed on via the MAPKKK cascade. [GOC:BHF, GOC:signaling, GOC:vk, PMID:17720811]


non-canonical Wnt receptor signalling pathway via JNK cascade

non-canonical Wnt receptor signaling pathway via JNK cascade

non-canonical Wnt-activated signaling pathway via JNK cascade

non-canonical Wnt signaling pathway via JNK cascade

The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, where the signal is passed on via the JNK cascade. [GOC:BHF, GPC:rl, PMID:19137009, PMID:20032469]


termination of G-protein coupled receptor signaling pathway

termination of G-protein coupled receptor signalling pathway

termination of G protein-coupled receptor signaling pathway

The signaling process in which G protein-coupled receptor signaling is brought to an end. For example, through the action of GTPase-activating proteins (GAPs) that act to accelerate hydrolysis of GTP to GDP on G-alpha proteins, thereby terminating the transduced signal. [GOC:bf, GOC:signaling]


VEGF-VEGFR-induced endothelial cell chemotaxis

positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signalling pathway

positive regulation of endothelial cell chemotaxis by VEGF/VEGFR signaling pathway

positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway

The series of molecular signals initiated by the binding of a vascular endothelial growth factor (VEGF) to its receptor on the surface of a cell, which activates or increases the frequency, rate or extent of endothelial cell chemotaxis. [GOC:bf, GOC:BHF, GOC:rl, PMID:21245381]


vascular endothelial growth factor receptor signaling pathway involved in endothelial cell chemotaxis


VEGF-mediated chemotactic endothelial cell migration


signal transduction in absence of agonist

signal transduction in absence of ligand

The series of molecular signals initiated by the absence of a ligand or the withdrawal of a ligand from a receptor. [GOC:al, GOC:ppm, GOC:pr, PMID:15044679]


G-protein coupled receptor signaling in absence of agonist

G-protein coupled receptor signalling in absence of ligand

G-protein coupled receptor signaling in absence of ligand

G protein-coupled receptor signaling in absence of ligand

The series of molecular signals beginning with a consequence of a G protein-coupled receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex, where the G protein-coupled receptor is not bound to an agonist. [GOC:al, PMID:12402500, PMID:17629961]


basal G-protein coupled receptor signaling


Combining with the sphingolipid sphingosine-1-phosphate (S1P), and transmitting the signal across the membrane by activating an associated G-protein. [GOC:bf, PMID:12728273, Wikipedia:S1PR1]


G-protein coupled receptor dimeric complex location

G protein-coupled receptor dimeric complex location

A protein complex that contains two G protein-coupled receptors. [GOC:al, GOC:bf, PMID:10713101]


G protein-coupled receptor homodimeric complex location

G-protein coupled receptor homodimeric complex location

A protein complex that contains two G protein-coupled receptors (GPCRs) of the same subtype. Formation of a GPCR homodimer may be important for the transport of newly formed receptors to the cell surface, and the function of the receptor. [GOC:al, GOC:bf, PMID:10713101, PMID:16670762]


G-protein coupled receptor heterodimeric complex location

G protein-coupled receptor heterodimeric complex location

A protein complex that contains two G protein-coupled receptors (GPCRs) of different subtypes. Formation of a GPCR heterodimer may alter the functional property of the GPCR. [GOC:al, GOC:bf, PMID:16109836, PMID:20150590]


cross-receptor inhibition within G-protein coupled receptor heterodimer

cross-receptor inhibition within G protein-coupled receptor heterodimer

Inhibition of one protomer of a G protein-coupled receptor (GPCR) heterodimer by the associated subunit. For example, agonist activation of one cytokine receptor can prevent activation of its associated cytokine receptor subunit. [GOC:al, GOC:bf, PMID:15979374]


dimeric G-protein coupled receptor signaling pathway

dimeric G-protein coupled receptor signalling pathway

G-protein coupled receptor signaling pathway via GPCR dimer


The series of molecular signals initiated by interleukin-5 binding to its receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:signaling]


large latent transforming growth factor-beta complex location

A protein complex containing latency-associated proteins (LAPs), mature disulphide-linked dimeric TGF-beta, and latent TGF-beta binding proteins (LTBPs). TGF-beta is mostly secreted as part of the large latent complex, and must be subsequently released from the LLC in order to bind to cell surface receptors. [GOC:bf, PMID:2350783, PMID:8680476, PMID:9805445, Reactome:R-HSA-177107]


Combining with morphine (17-methyl-7,8-didehydro-4,5alpha-epoxymorphinan-3,6alpha-diol), and transmitting the signal across the membrane by activating an associated G-protein. [GOC:bf]


Combining with a dynorphin peptide, and transmitting the signal across the membrane by activating an associated G-protein. Dynorphin is any opioid peptide that is generated by cleavage of the precursor protein prodynorphin. [GOC:bf, Wikipedia:Dynorphin]


RNA polymerase II transcription factor activity, glucocorticoid-activated sequence-specific DNA binding


RNA polymerase II transcription factor activity, estrogen-activated sequence-specific DNA binding


G-protein coupled estrogen receptor activity

G protein-coupled estrogen receptor activity

Combining with estrogen and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex. [GOC:signaling, PMID:17379646, PMID:20960099]


BMP protein secretion
bone morphogenetic protein secretion

The controlled release of a member of the BMP family of proteins from a cell. [GOC:sart]


negative regulation of BMP signalling pathway by negative regulation of BMP secretion

negative regulation of BMP signaling pathway by negative regulation of bone morphogenetic protein secretion

negative regulation of BMP signaling pathway by negative regulation of BMP secretion

Any process that stops, prevents, or reduces the frequency, rate or extent of the BMP signaling pathway by stopping, preventing or reducing the frequency, rate or extent of secretion of a member of the BMP family of proteins from the signaling cell. [GOC:bf, GOC:sart, PMID:21750037]


receptor activator of nuclear factor kappa-B ligand binding

TNF-related activation-induced cytokine binding

osteoclast differentiation factor binding

tumor necrosis factor superfamily member 11 binding

tumor necrosis factor (ligand) superfamily member 11 binding

tumor necrosis factor ligand superfamily member 11 binding

Binding to tumor necrosis factor ligand superfamily member 11 (TNFSF11), a member of the tumor necrosis factor (TNF) cytokine family. [GOC:cjm]


tumor necrosis factor ligand superfamily member 11 receptor activity

Combining with a tumor necrosis factor ligand superfamily member 11 (TNFSF11) and transmitting the signal across the cell membrane to initiate a change in cell activity or function. [GOC:bf, GOC:cjm]


IKKalpha-IKKalpha protein complex location

A homodimeric protein complex containing two IkappaB kinase (IKK) alpha subunits. [GOC:bf, PMID:18626576, PMID:21173796]


nitric oxide-cGMP-mediated signalling pathway

nitric oxide-cGMP-mediated signaling pathway

Any intracellular signal transduction in which the signal is passed on within the cell by nitric oxide (NO) activating soluble guanylyl cyclase (sGC). Includes synthesis of nitric oxide, guanylyl cyclase activity, and downstream effectors that further transmit the signal within the cell following activation by cGMP. [GOC:signaling, PMID:21549190, PMID:22019632]


NIK/NF-kappaB signal transduction
NIK/NF-kappaB cascade

The process in which a signal is passed on to downstream components within the cell through the NIK-dependent processing and activation of NF-KappaB. Begins with activation of the NF-KappaB-inducing kinase (NIK), which in turn phosphorylates and activates IkappaB kinase alpha (IKKalpha). IKKalpha phosphorylates the NF-Kappa B2 protein (p100) leading to p100 processing and release of an active NF-KappaB (p52). [GOC:bf, GOC:mg2, GOC:signaling, GOC:vs, PMID:11239468, PMID:15140882]


noncanonical nuclear factor kappaB (NF-kappaB) pathway


protein tyrosine kinase collagen receptor activity

Combining with collagen and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity by catalysis of the reaction: ATP + a protein-L-tyrosine = ADP + a protein-L-tyrosine phosphate. [GOC:bf, GOC:uh, PMID:16626936, PMID:21568710]


collagen-activated RTK signaling pathway

collagen-activated tyrosine kinase receptor signalling pathway

collagen-activated tyrosine kinase receptor signaling pathway

The series of molecular signals initiated by collagen binding to its receptor on the surface of a target cell where the receptor possesses tyrosine kinase activity, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:bf, GOC:uh, PMID:15888913, PMID:16626936]


discoidin domain receptor signaling pathway


transmembrane collagen receptor activity

Combining with a collagen and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:bf, GOC:uh, PMID:21568710]


The series of molecular signals initiated by collagen binding to a cell surface receptor, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:bf, GOC:uh, PMID:21568710]


The phosphorylation by a protein of one or more of its own tyrosine amino acid residues, or a tyrosine residue on an identical protein. [PMID:10037737, PMID:10068444, PMID:10940390]


receptor tyrosine kinase autophosphorylation


vascular endothelial growth factor signalling pathway

vascular endothelial growth factor signaling pathway

The series of molecular signals initiated by vascular endothelial growth factor (VEGF) binding its receptor on the surface of the target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, PMID:17470632]


vascular endothelial growth factor binding

Binding to a vascular endothelial growth factor. [PMID:17470632]


VEGF-activated platelet-derived growth factor receptor signalling pathway

vascular endothelial growth factor-activated platelet-derived growth factor receptor signaling pathway

VEGF-activated platelet-derived growth factor receptor signaling pathway

The series of molecular signals initiated by vascular endothelial growth factor (VEGF) binding to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, PMID:17470632]


VEGF-activated PDGFRalpha signalling pathway

vascular endothelial growth factor-activated platelet-derived growth factor receptor-alpha signaling pathway

VEGF-activated platelet-derived growth factor receptor-alpha signalling pathway

VEGF-activated platelet-derived growth factor receptor-alpha signaling pathway

The series of molecular signals initiated by vascular endothelial growth factor (VEGF) binding to an alpha-type platelet-derived growth factor receptor (PDGFR) on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, PMID:17470632]


VEGF-activated PDGFRbeta signalling pathway

VEGF-activated platelet-derived growth factor receptor-beta signalling pathway

vascular endothelial growth factor-activated platelet-derived growth factor receptor-beta signaling pathway

VEGF-activated platelet-derived growth factor receptor-beta signaling pathway

The series of molecular signals initiated by vascular endothelial growth factor (VEGF) binding to a beta-type platelet-derived growth factor receptor (PDGFR) on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, PMID:17470632]


positive regulation of cell migration by vascular endothelial growth factor signalling pathway

positive regulation of cell migration by VEGF signaling pathway

positive regulation of cell migration by vascular endothelial growth factor signaling pathway

The series of molecular signals initiated by vascular endothelial growth factor (VEGF) binding to its receptor on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another. [GOC:bf, GOC:signaling]


positive regulation of cell migration by VEGF-activated platelet derived growth factor receptor signalling pathway

positive regulation of cell migration by VEGF/PDGFR signaling pathway

positive regulation of cell migration by VEGF-activated platelet derived growth factor receptor signaling pathway

The series of molecular signals initiated by vascular endothelial growth factor (VEGF) binding to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, which activates or increases the frequency, rate or extent of the orderly movement of a cell from one site to another. [GOC:bf, GOC:signaling, PMID:17470632]


positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signalling pathway

positive regulation of cell proliferation by VEGF/PDGFR signaling pathway

positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway

The series of molecular signals initiated by vascular endothelial growth factor (VEGF) binding to a platelet-derived growth factor receptor (PDGFR) on the surface of a cell, which activates or increases the frequency, rate or extent of cell proliferation. [GOC:signaling, PMID:17470632]


nodal signalling pathway
nodal signaling

The series of molecular signals initiated by nodal protein binding to an activin receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:BHF, GOC:vk, PMID:17287255]


The series of molecular signals initiated by the binding of the Fc portion of an immunoglobulin to an Fc receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region. [GOC:phg, Wikipedia:Fc_receptor]


The series of molecular signals initiated by the binding of the Fc portion of immunoglobulin G (IgG) to an Fc-gamma receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region. [GOC:phg, PMID:11244038]


The series of molecular signals initiated by the binding of the Fc portion of immunoglobulin E (IgE) to an Fc-epsilon receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. The Fc portion of an immunoglobulin is its C-terminal constant region. [GOC:phg, PMID:12413516, PMID:15048725]


Fc-gamma receptor signalling pathway involved in phagocytosis

Fc gamma receptor-dependent phagocytosis

Fc-gamma receptor signaling pathway involved in phagocytosis

An Fc-gamma receptor signaling pathway that contributes to the endocytic engulfment of external particulate material by phagocytes. [GOC:phg, PMID:12488490, PMID:15466916]


positive regulation of mast cell activation by Fc-epsilon receptor signalling pathway

Fc epsilon RI-dependent mast cell activation

Fc epsilon RI-mediated mast cell activation

positive regulation of mast cell activation by Fc-epsilon receptor signaling pathway

An Fc-epsilon receptor signaling pathway that results in the change in morphology and behavior of a mast cell resulting from exposure to a cytokine, chemokine, soluble factor, or to (at least in mammals) an antigen which the mast cell has specifically bound via IgE bound to Fc-epsilonRI receptors. [GOC:phg, PMID:12413516]


sequestering of BMP from receptor via BMP binding

Binding to a bone morphogenetic protein (BMP) in the extracellular region, and inhibiting BMP signaling by preventing BMP from binding to its cell surface receptor. [GOC:bf, GOC:signaling, PMID:19855014]


extracellular sequestering of bone morphogenetic protein


ActRIIB.ALK4.EGF-CFC complex formation
nodal receptor complex formation

The aggregation, arrangement and bonding together of a set of components to form a complex containing a type II activin receptor, a type I activin receptor, and a coreceptor of the EGF-CFC family (e.g. Cripto or Cryptic, in mammals). [GOC:bf, GOC:signaling, PMID:15062104]


Binding to a nodal protein, a member of the transforming growth factor-beta superfamily. [GOC:bf, PMID:20629020]


sequestering of nodal from receptor via nodal binding

Binding to a nodal protein in the extracellular region, and inhibiting nodal signaling by preventing nodal from binding to its cell surface receptor. [GOC:signaling, PMID:14570583, PMID:15062104]


activin receptor antagonist activity involved in negative regulation of nodal signalling pathway

activin receptor antagonist activity involved in negative regulation of nodal signaling pathway

Interacting with an activin receptor to reduce the action of the agonist nodal. A receptor antagonist does not initiate signaling upon binding to a receptor, but instead blocks an agonist from binding to the receptor. [GOC:signaling, PMID:15062104]


Interacting with an activin receptor complex to reduce the action of another ligand, the agonist. A receptor antagonist does not initiate signaling upon binding to a receptor, but instead blocks an agonist from binding to the receptor. [GOC:signaling, PMID:15062104]


A protein complex containing at least a type II activin receptor, a type I activin receptor, and a coreceptor (EGF-CFC protein) such as Cripto or Cryptic. Nodal receptor complexes are capable of binding a nodal protein and transducing the signal into the cell. [GOC:bf, GOC:signaling, PMID:11024047, PMID:15062104]


sequestering of TGFbeta from receptor via TGFbeta binding

Binding to a transforming growth factor-beta (TGFbeta) protein in the extracellular region, and inhibiting TGFbeta signaling by preventing TGFbeta from binding to its cell surface receptor. [GOC:bf, GOC:signaling, PMID:19855014]


extracellular sequestering of transforming growth factor-beta


chorionic gonadotropin binding
chorionic gonadotrophin binding

Binding to choriogonadotropin hormone, a heterodimer, with an alpha subunit identical to that of luteinizing hormone (LH), follicle-stimulating hormone (FSH) and thyroid-stimulating hormone (TSH), and a unique beta subunit. [GOC:BHF, GOC:rl, Wikipedia:Human_chorionic_gonadotropin]


nodal signalling pathway involved in determination of left/right asymmetry

regulation of transcription from RNA polymerase II promoter by nodal signaling pathway, involved in determination of left/right symmetry

nodal signaling pathway involved in determination of left/right asymmetry

The series of molecular signals initiated by a nodal protein binding of to an activin receptor on the surface of a target cell, which contributes to the establishment of an organism's body plan or part of an organism with respect to the left and right halves. [GOC:BHF, GOC:vk, PMID:12857784, PMID:17287255, PMID:20413706]


inhibition of appetite by leptin signaling

reduction of appetite by leptin-mediated signaling

negative regulation of appetite by leptin-mediated signalling pathway

suppression of appetite by leptin-mediated signaling pathway

negative regulation of appetite by leptin-mediated signaling pathway

The series of molecular signals initiated by leptin binding to its receptor on the surface of a cell, which reduces appetite, the desire or physical craving for food. [GOC:BHF, GOC:vk, PMID:19150989]


The series of molecular signals initiated by interleukin-2 binding to its receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling]


The series of molecular signals initiated by interleukin-7 binding to its receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling]


The series of molecular signals initiated by interleukin-8 binding to its receptor on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling]


The series of molecular signals initiated by interleukin-9 binding to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling]


The series of molecular signals initiated by interleukin-21 binding to a receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling]


chemokine (C-C motif) ligand 19 signalling pathway

chemokine (C-C motif) ligand 19 signaling pathway

The series of molecular signals initiated by the binding of the C-C chemokine CCL19 to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling, PMID:15059845]


C-C chemokine receptor type 7 signaling pathway


chemokine (C-C motif) ligand 21 signalling pathway

chemokine (C-C motif) ligand 21 signaling pathway

The series of molecular signals initiated by the binding of the C-C chemokine CCL21 to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling, PMID:15059845]


C-C motif chemokine 19 receptor activity

Combining with the C-C motif chemokine 19 (CCL19) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:signaling, PMID:15059845]


C-C chemokine receptor CCR7 signalling pathway

C-C chemokine receptor CCR7 signaling pathway

The series of molecular signals initiated by a the C-C chemokine type 7 receptor on the surface of a cell binding to one of it's physiological ligands, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, PMID:15059845, PMID:15778365]


The series of molecular signals initiated by the binding of the C-C chemokine CCL19 to a C-C chemokine type 7 receptor (CCR7) on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling, PMID:15059845]


The series of molecular signals initiated by the binding of the C-C chemokine CCL21 to a C-C chemokine type 7 receptor (CCR7) on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling, PMID:15059845]


C-C motif chemokine 21 receptor activity

Combining with the C-C motif chemokine 21 (CCL21) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:signaling, PMID:15059845]


small inducible cytokine A5 receptor activity

Combining with the C-C motif chemokine 5 (CCL5) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:signaling]


toll-like receptor TLR1:TLR2 signalling pathway

toll-like receptor TLR1:TLR2 signaling pathway

The series of molecular signals initiated by a ligand binding of a heterodimeric TLR1:TLR2 complex, followed by transmission of the signal by the activated receptor, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling, PMID:17318230]


toll-like receptor TLR6:TLR2 signalling pathway

toll-like receptor TLR6:TLR2 signaling pathway

The series of molecular signals initiated by a ligand binding of a heterodimeric TLR6:TLR2 complex, followed by transmission of the signal by the activated receptor, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:nhn, GOC:signaling, PMID:17318230]


receptor tyrosine-protein kinase erbB-3 signaling pathway

The series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB3 on the surface of a cell, and ending with the regulation of a downstream cellular process, e.g. transcription. ERBB3 receptors have impaired kinase activity and rely on the kinase activity of the heterodimer partner for activation and signal transmission. [GOC:jc, PMID:16460914, Reactome:R-HSA-1247497]


Combining with a neuregulin, a member of the EGF family of growth factors, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:bf, GOC:signaling, PMID:16460914, PMID:20672328]


Binding to a neuregulin, a member of the EGF family of growth factors. [GOC:bf, GOC:signaling]


ERBB2-EGFR signalling pathway
EGFR-HER2 signaling pathway

The series of molecular signals initiated by binding of a ligand to an epidermal growth factor receptor (EGFR/ERBB1) on the surface of a cell, followed by transmission of the signal by a heterodimeric complex of ERBB2 and EGFR. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as EGFR. [GOC:signaling, PMID:16460914, Reactome:R-HSA-1963589]


HER2-HER4 signaling pathway
ERBB2-ERBB4 signalling pathway

The series of molecular signals initiated by binding of a ligand to a ERBB4 receptor on the surface of a cell, followed by transmission of the signal by a heterodimeric complex of ERBB2 and ERBB4. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB4. [GOC:signaling, PMID:16460914, Reactome:R-HSA-1963589]


HER3-HER4 signaling pathway
ERBB3-ERBB4 signalling pathway

The series of molecular signals transmitted by a heterodimeric complex of the tyrosine kinase receptors ERBB3 and ERBB4. The pathway begins with binding of a ligand to either cell surface receptor, or the dimeric receptor complex, and ends with regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, PMID:16460914, Reactome:R-HSA-1977958]


ERBB1-ERBB4 signaling pathway
ERBB4-EGFR signalling pathway
HER1-HER4 signaling pathway

The series of molecular signals transmitted by a heterodimeric complex of the tyrosine kinase receptors EGFR (epidermal growth factor receptor/ERBB1) and ERBB4. The pathway begins with binding of a ligand to either cell surface receptor, or the dimeric receptor complex, and ends with regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, PMID:16460914, Reactome:R-HSA-1977959]


ERBB4 homodimeric signaling pathway
ERBB4-ERBB4 signalling pathway
HER4-HER4 signaling pathway

The series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor ERBB4, followed by ligand-induced homodimerization of ERBB4 and transmission of the signal into the cell by the homodimeric ERBB4 complex. The pathway ends with regulation of a downstream cellular process, e.g. transcription. [GOC:signaling, PMID:16460914, Reactome:R-HSA-1250220]


EGFR-ERBB4 complex location
EGFR-ERBB4 complex
ERBB4:EGFR heterodimer
ERBB4-EGFR complex location

A heterodimeric complex between the tyrosine kinase receptors ERBB4 (also called HER4) and epidermal growth factor receptor (EGFR/ERBB1). [GOC:signaling, PMID:16460914, Reactome:R-HSA-1977956]


ERBB3-ERBB4 complex
ERBB3-ERBB4 complex location
ERBB4-ERBB3 complex location
ERBB4:ERBB3 heterodimer

A heterodimeric complex between the tyrosine kinase receptors ERBB4 (also called HER4) and ERBB3 (also called HER3). ERBB3 has impaired kinase activity so relies on the kinase activity of its heterodimer partner for activation and signal transmission. [GOC:signaling, PMID:16460914, Reactome:R-HSA-1977955]


ERBB4-ERBB4 complex location
ERBB4 homodimer

A homodimeric complex containing two monomers of the tyrosine kinase receptor ERBB4 (also called HER4). [GOC:signaling, PMID:16460914, Reactome:R-HSA-1250221]


A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated epidermal growth factor receptor (EGFR/ERBB1). ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as EGFR. [GOC:signaling, PMID:16460914, PMID:1973074, Reactome:R-HSA-1227939, Reactome:R-HSA-1963573, Reactome:R-HSA-1963589]


A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated receptor ERBB3. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB3. [GOC:signaling, PMID:16460914, PMID:8665853, Reactome:R-HSA-1247502, Reactome:R-HSA-1963573, Reactome:R-HSA-1963589]


A heterodimeric complex between the tyrosine kinase receptor ERBB2 and a ligand-activated receptor ERBB4. ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member such as ERBB4. [GOC:signaling, PMID:16460914, PMID:16978839, Reactome:R-HSA-1250224, Reactome:R-HSA-1963573, Reactome:R-HSA-1963589]


inhibition of host interferon signaling pathway by virus


inhibition of host MHC class II molecule presentation by virus


negative regulation by virus of host interferon receptor activity

downregulation by virus of host interferon receptor activity

inhibition by virus of host interferon receptor activity

inhibition of host interferon receptors by virus

down-regulation by virus of host interferon receptor activity

suppression by virus of host interferon receptor activity

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the functional activity of a host interferon receptor. [GOC:bf, GOC:sp, UniProtKB-KW:KW-1091, VZ:843]


negative regulation by virus of host protein tyrosine kinase activity

down-regulation by virus of host protein tyrosine kinase activity

inhibition by virus of host protein tyrosine kinase activity

downregulation by virus of host protein tyrosine kinase activity

suppression by virus of host protein tyrosine kinase activity

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host protein tyrosine kinase activity. [GOC:bf, GOC:sp]


downregulation by virus of host catalytic activity

negative regulation by virus of host catalytic activity

down-regulation by virus of host enzyme activity

inhibition by virus of host catalytic activity

suppression by virus of host catalytic activity

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host enzyme activity. [GOC:bf]


down-regulation by virus of host JAK-STAT cascade

downregulation by virus of host JAK-STAT cascade

negative regulation by virus of host JAK-STAT cascade

inhibition by virus of host JAK-STAT cascade

suppression by virus of host JAK-STAT cascade

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the JAK-STAT signal cascade in the host organism. [GOC:bf, GOC:sp]


suppression by virus of tyrosine phosphorylation of host STAT protein

viral inhibition of tyrosine phosphorylation of host STAT protein

negative regulation by virus of tyrosine phosphorylation of host STAT protein


regulation by virus of host catalytic activity

regulation of host catalytic activity by virus

modulation of catalytic activity of host by virus

modulation by virus of host catalytic activity

The process in which a virus effects a change in host enzyme activity. [GOC:bf, GOC:sp]


modulation by virus of protein serine/threonine phosphatase activity in host

regulation by virus of host protein serine/threonine phosphatase activity

modulation by virus of host protein serine/threonine phosphatase activity

The process in which a virus effects a change in host protein serine/threonine phosphatase activity. [GOC:bf, GOC:sp]


down-regulation by virus of host cytokine activity

downregulation by virus of host cytokine activity

inhibition by virus of host cytokine activity

negative regulation by virus of host cytokine activity

suppression by virus of host cytokine activity

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host cytokine activity. [GOC:bf, GOC:sp]


Any process in which a virus effect a change in the frequency, rate or extent of autophagy in the host. [GOC:bf, GOC:sp]


Any process in which a virus activates or increases the frequency, rate or extent of autophagy in the host. [GOC:bf, GOC:sp, UniProtKB-KW:KW-1072, VZ:846]


positive regulation by virus of host autophagy


negative regulation by virus of host autophagy

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of autophagy in the host. [GOC:bf, GOC:sp, UniProtKB-KW:KW-1083, VZ:845]


suppression of host mRNA nuclear export by virus

inhibition of host mRNA nuclear export by virus

negative regulation by virus of host mRNA nuclear export

inhibition by virus of host mRNA nuclear export

suppression by virus of host mRNA export from nucleus

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of movement of mRNA from the nucleus to the cytoplasm in the host organism. [GOC:bf, GOC:sp, UniProtKB-KW:KW-1099, VZ:902]


suppression by virus of host RNA polymerase II activity

inhibition of host RNA polymerase II activity by virus

negative regulation by virus of host RNA polymerase II activity

inhibition of host RNA polymerase II by virus

suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host mRNA transcription by directly inhibiting RNA polymerase II activity. [GOC:bf, GOC:sp, PMID:25233083]


inhibition of host pre-mRNA processing by virus

inhibition of host mRNA processing by virus

inhibition by virus of host mRNA processing

negative regulation by virus of host mRNA processing

suppression by virus of host mRNA processing

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of mRNA processing in the host cell. mRNA processing is the conversion of a primary mRNA transcript into one or more mature mRNA(s) prior to translation into polypeptide. [GOC:bf, GOC:sp, UniProtKB-KW:KW-1103, VZ:903]


modulation by virus of host chromatin organisation

regulation by virus of host chromatin organization

modulation of host chromatin structure by virus

modulation by virus of host chromatin organization

Any process in which a virus effects a change in the organization of chromatin in the host. [GOC:bf, GOC:sp, PMID:11483770, PMID:16687403]


modulation of host cell apoptosis by virus

modulation by virus of host apoptotic process

Any process in which a virus modulates the frequency, rate or extent of apoptosis of infected host cells. [GOC:bf, GOC:mtg_apoptosis, GOC:sp, UniProtKB-KW:KW-1119]


negative regulation by virus of host TRAF-mediated signal transduction

suppression by virus of host tumor necrosis factor receptor-associated factor signaling

inhibition of host TRAF-mediated signal transduction by virus

suppression by virus of host TRAF-mediated signal transduction

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of TRAF-mediated signal transduction in the host. [GOC:bf, GOC:sp]


virus-induced cytoplasmic pattern recognition receptor signaling pathway

cytoplasmic pattern recognition receptor signalling pathway in response to virus

cytoplasmic pattern recognition receptor signaling pathway in response to virus

The series of molecular signals initiated by the binding of a virus or viral RNA binding to a pattern recognition receptor (PRR) located in the cytoplasm. Cytosolic PRRs such as RIG-I (DDX58) and MDA-5 (IFIH1) detect RNA synthesized during active viral replication and trigger a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. [GOC:bf, PMID:17328678, PMID:18272355, PMID:19531363]


cytoplasmic caspase-recruiting domain (CARD) helicase signaling pathway


RIG-I-like receptor (RLR) signaling pathway


retinoic acid inducible gene I signaling pathway

The series of molecular signals initiated by the binding of viral RNA to a pattern recognition receptor (PRR) RIG-1 (also known as DDX58). RIG-I is a cytoplasmic receptor that detects RNA synthesized during viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. [GOC:bf, PMID:17328678, PMID:19620789, PMID:21435580]


melanoma differentiation-associated gene 5 signaling pathway

The series of molecular signals initiated by viral RNA binding of a cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1). MDA-5 is a cytoplasmic receptor that detects RNA synthesized during viral replication and triggers a signaling pathway to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. [GOC:bf, PMID:19620789]


regulation of viral-induced cytoplasmic pattern recognition receptor signalling pathway

regulation of viral-induced cytoplasmic pattern recognition receptor signaling pathway

Any process that modulates the frequency, rate or extent of a cytoplasmic pattern recognition receptor signaling pathway in response to a virus. [GOC:bf, GOC:jl]


negative regulation of cytoplasmic pattern recognition receptor signaling pathway in response to virus

negative regulation of viral-induced cytoplasmic pattern recognition receptor signalling pathway

negative regulation of viral-induced cytoplasmic pattern recognition receptor signaling pathway

Any process that stops, prevents, or reduces the frequency, rate or extent of the series of a cytoplasmic pattern recognition receptor signaling pathway in response to a virus. [GOC:bf, GOC:jl]


regulation of melanoma differentiation-associated gene 5 signaling pathway

Any process that modulates the frequency, rate or extent of the series of molecular signals generated as a consequence of the cytoplasmic pattern recognition receptor (PRR) MDA-5 (also known as IFIH1) binding to viral RNA. [GOC:bf, GOC:jl]


negative regulation of MDA-5 signalling pathway

negative regulation of melanoma differentiation-associated gene 5 signaling pathway

negative regulation of IFIH1 signaling pathway

negative regulation of MDA5 signaling pathway

negative regulation of MDA-5 signaling pathway

Any process that stops, prevents, or reduces the frequency, rate or extent of the series of the MDA-5 signaling pathway. [GOC:bf, GOC:jl]


regulation of retinoic acid inducible gene I signaling pathway

Any process that modulates the frequency, rate or extent of the RIG-I signaling pathway. [GOC:bf, GOC:jl]


negative regulation of RIG-I signalling pathway

negative regulation of DDX58 signaling pathway

negative regulation of retinoic acid inducible gene I signaling pathway

negative regulation of RIG-I signaling pathway

Any process that stops, prevents, or reduces the frequency, rate or extent of the RIG-I signaling pathway. [GOC:bf, GOC:jl]


suppression by virus of host cytoplasmic pattern recognition receptor signaling pathway in response to virus

suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signalling pathway

suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of the host viral-induced cytoplasmic pattern recognition receptor signaling pathway. This is a mechanism by which the virus evades the host innate immune response. [GOC:bf, GOC:jl]


suppression by virus of host RIG-I-like receptor (RLR) signaling pathway


suppression by virus of host RIG-I/MDA5 signaling pathway


suppression by virus of host RIG-like helicase signaling pathway


suppression by virus of host RIG-like receptor signaling pathway


suppression by virus of host RLR signaling pathway


inhibition by virus of host DDX58 activity

suppression by virus of host RIG-I activity

suppression by virus of host RIG-I signaling pathway

suppression by virus of host RIG-I signalling pathway

suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity

Any process in which a virus stops, prevents, or reduces a host viral-induced cytoplasmic pattern recognition receptor signaling pathway by inhibiting the activity of RIG-1 (also known as DDX58). The cytoplasmic pattern recognition RIG-I recognizes viral RNA synthesized during active viral replication and signals to protect the host against viral infection, for example by inducing the expression of antiviral cytokines. [PMID:19454348, PMID:26138103]


suppression by virus of host mitochondrial antiviral-signaling protein

suppression by virus of host MAVS activity


suppression by virus of host TRAF activity

Any process in which a virus stops, prevents, or reduces the activity of a host TRAF (tumor necrosis factor receptor-associated factor) protein. TRAFs are intracellular signal transducers that lie downstream of receptors including RIG-I, MDA-5 and Toll-like receptors (TLR) and transfer the signal to other intracellular signaling components. [GOC:bf, UniProtKB-KW:KW-1110, VZ:715]


suppression by virus of host interferon regulatory factor 3

suppression by virus of host IRF3 activity


inhibition of IRF3-dependent antiviral response


Binding to RIG-I, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral RNA. [GOC:bf, PMID:21233210]


down-regulation by virus of host chemokine activity

downregulation by virus of host chemokine activity

negative regulation by virus of host chemokine activity

inhibition by virus of host chemokine activity

suppression by virus of host chemokine activity

Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of host chemokine activity. [GOC:bf, GOC:sp, UniProtKB-KW:KW-1086, VZ:813]


Combining with a Wnt protein and transmitting the signal across the plasma membrane to initiate a change in cell activity. [GOC:go_curators]


cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Binds to and stops, prevents or reduces the activity of a cysteine-type endopeptidase involved in the apoptotic process. [GOC:jl, GOC:mtg_apoptosis, PMID:14744432, Wikipedia:Caspase]


cysteine-type endopeptidase regulator activity involved in apoptotic process

Binds to and modulates the activity of a cysteine-type endopeptidase involved in the apoptotic process. [GOC:jl, GOC:mtg_apoptosis, PMID:14744432, Wikipedia:Caspase]


regulation of cysteine-type endopeptidase activity involved in apoptotic process

Any process that modulates the activity of a cysteine-type endopeptidase involved in apoptosis. [GOC:jl, GOC:mtg_apoptosis]


The component of the plasma membrane consisting of gene products and protein complexes that have some part that spans both leaflets of the membrane. [GOC:ecd]


cell wall polysaccharide catabolic process

The chemical reactions and pathways resulting in the breakdown of cell wall polysaccharides. [GOC:mengo_curators]


plant-type cell wall polysaccharide breakdown

plant-type cell wall cellulose catabolic process

The chemical reactions and pathways resulting in the breakdown of cellulose, a linear beta1-4 glucan of molecular mass 50-400 kDa with the pyranose units in the -4C1 conformation, which forms part of the cell wall. [GOC:mengo_curators]


The removal of a section of DNA from a larger DNA molecule by the making of dual incisions that flank the section to be excised. [GOC:jl]


An endocytosis process that results in the uptake of liquid material by cells from their external environment by invagination of the plasma membrane to form uncoated micropinosomes, differentiated from macropinosomes by their smaller size, on average 95 nm. [PMID:14731589, PMID:14732047]


An endocytosis process that results in the uptake of liquid material by cells from their external environment by the 'ruffling' of the cell membrane to form heterogeneously sized intracellular vesicles called macropinosomes, which can be up to 5 micrometers in size. [PMID:14732047]


A membrane-bounded, uncoated intracellular vesicle formed by the process of pinocytosis. [PMID:14731589, PMID:14732047]


A membrane-bounded, uncoated intracellular vesicle formed by the process of micropinocytosis. [PMID:14731589, PMID:14732047]


A membrane-bounded, uncoated intracellular vesicle formed by the process of macropinocytosis. [PMID:14732047]


A defense process that protects an organism from invading foreign DNA. [GO:jl, PMID:20062055]


clearance of foreign intracellular DNA by conversion of DNA cytidine to uridine


Any process that modulates the propensity of rRNA molecules to degradation. Includes processes that both stabilize and destabilize rRNAs. [GOC:jl]


envenomation resulting in hemorrhagic damage to other organism

envenomation resulting in hemorrhagic damage in another organism

A process that begins with venom being forced into an organism by the bite or sting of another organism, and ends with vascular damage and hemorrhage in the bitten organism. [PMID:10441379, PMID:20614020]


modulation of molecular function in other organism

modulation of molecular function in another organism

The process in which an organism effects a change in the function of proteins in a second organism. [GOC:jl]


modulation of voltage-gated potassium channel activity in other organism

modulation of voltage-gated potassium channel activity in another organism

Any process in which an organism effects a change in the frequency, rate or extent of the activity of a voltage-gated potassium channel in another organism. [GOC:jl]


negative regulation of voltage-gated potassium channel activity in other organism

negative regulation of voltage-gated potassium channel activity in another organism

Any process in which an organism stops, prevents or reduces the frequency, rate or extent of the activity of a voltage-gated potassium channel in another organism. [GOC:jl]