NothingMuch/GO-Terms huggingface dataset:
Combining with low affinity with an immunoglobulin of an IgG isotype via the Fc region, and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity.
low affinity Fc receptor activity
low affinity IgG receptor activity
Catalysis of the covalent attachment of the ubiquitin-like protein Atg8 family modifier to phosphatidylethanolamine or phosphatidylserine on a membrane.
APG8 ligase activity
Atg8 ligase activity
Atg8-like ligase activity
Catalysis of the activation of the small ubiquitin-related modifier APG12, through the formation of an ATP-dependent high-energy thiolester bond.
APG12 activating enzyme activity
Catalysis of the activation of the small ubiquitin-related modifier APG8, through the formation of an ATP-dependent high-energy thiolester bond.
APG7
APG8 activating enzyme activity
Catalysis of the initiation of the NEDD8 (RUB1) conjugation cascade.
RUB1 activating enzyme activity
Catalysis of the activation of the small ubiquitin-related modifier ISG15, through the formation of an ATP-dependent high-energy thiolester bond.
UBE1L
A thiol-dependent isopeptidase activity that cleaves ISG15 from a target protein to which it is conjugated.
ISG15-specific protease activity
Catalysis of the reaction: -C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = -C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine. An example of this reaction is the removal of ATG8 from membranes to which it is covalently linked to a phosphatidylethanolamid via its terminal glycine residue.
APG8-PE hydrolase
APG8-specific protease activity
ATG8-PE deconjugation activity
ATG8-PE hydrolase activity
Atg8-specific peptidase activity
Atg8-specific protease activity
Catalysis of the reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-3-hydroxy-L-proline + succinate + CO2.
procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating) activity
procollagen-proline,2-oxoglutarate 3-dioxygenase activity
proline,2-oxoglutarate 3-dioxygenase activity
prolyl 3-hydroxylase activity
prolyl-4-hydroxyprolyl-glycyl-peptide, 2-oxoglutarate: oxygen oxidoreductase, 3-hydroxylating activity
protocollagen proline 3-hydroxylase activity
Catalysis of the reaction: acetyl-CoA + (alpha-tubulin) L-lysine = CoA + (alpha-tubulin) N6-acetyl-L-lysine.
acetyl-CoA:alpha-tubulin-L-lysine 6-N-acetyltransferase activity
acetyl-CoA:alpha-tubulin-L-lysine N6-acetyltransferase activity
acetyl-CoA:alpha-tubulin-lysine N-acetyltransferase activity
alpha-tubulin acetylase activity
alpha-tubulin acetyltransferase activity
alpha-tubulin N-acetyltransferase activity
TAT activity
tubulin acetyltransferase activity
The cyclization of asparagine to yield an L-aspartimide (otherwise known as alpha-aminosuccinimide) residue at the C-terminus of an excised intein during protein splicing.
cyclization of asparagine, during protein splicing
The cyclization of glutamine to yield an L-glutamimide residue at the C-terminus of an excised intein during protein splicing.
cyclization of glutamine, during protein splicing
Catalysis of the reaction: 2 R-H + 2 bromide + H2O2 = 2 R-Br + 2 H2O. Enzymes with this activity often accept other halide ions as substrates, including chloride and iodide.
bromoperoxidase activity
Catalysis of the reaction: N-acyl-L-aspartate + H2O = a fatty acid anion + L-aspartate.
acetyl-aspartic deaminase activity
acylase II
aminoacylase II activity
N-acetylaspartate amidohydrolase activity
N-acyl-L-aspartate amidohydrolase activity
A multisubunit complex composed of two copies of a restriction (R) subunit, two copies of a methylation (M) subunit, and one copy of a specificity (S) subunit. This complex recognizes specific short DNA sequences (through the S subunit), and binds to them. If the recognition site is hemimethylated, the complex acts as a methyltransferase which modifies the recognition site, using S-adenosylmethionine as the methyl donor. Only the M and S subunits are required for this reaction. If the complex binds to an unmethylated recognition site, then the complex translocates the DNA bidirectionally in an ATP-dependent manner. When the translocation is stalled by impact with another complex or unusual DNA structure, the enzyme functions as an endonuclease and cleavage of the DNA will occur, hundreds or thousands of base pairs away from the recognition site. These DNA restriction systems are used by bacteria to defend against phage and other foreign DNA that may enter a cell.
type I restriction enzyme complex
A heterodimeric enzyme complex composed of two subunits, Res and Mod, that functions as an endonuclease and cleaves DNA. Cleavage will only occur when there are two un-methylated copies of a specific recognition site in an inverse orientation on the DNA. Cleavage occurs at a specific distance away from one of the recognition sites. The Mod subunit can act alone as a methyltansferase. DNA restriction systems such as this are used by bacteria to defend against phage and other foreign DNA that may enter a cell.
type III restriction enzyme complex
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P1 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content; they contain fewer peroxisomal proteins than the other subforms.
peroxisome vesicle
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P2 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content; they are the least dense of the subforms observed.
peroxisome vesicle
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P3 peroxisomes are formed by fusion of P1 and P2 peroxisomes, and are distinguished from the other subforms on the bases of buoyant density and protein content.
peroxisome vesicle
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P4 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content.
peroxisome vesicle
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P5 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content.
peroxisome vesicle
A subform of peroxisome that corresponds to an intermediate in a peroxisome assembly pathway, which operates by conversion of peroxisomal subforms in the direction P1, P2 -> P3 -> P4 -> P5 -> P6. P6 peroxisomes are distinguished from the other subforms on the bases of buoyant density and protein content, and are equivalent to mature peroxisomes.
peroxisome vesicle
Binding to oxygen (O2).
cytochrome P450
cytochrome P450 activity
Binds to and stops, prevents or reduces the activity of aspartic-type endopeptidases.
aspartic protease inhibitor activity
The cytolytic destruction of red blood cells, with the release of intracellular hemoglobin, in the host organism by a symbiont. The host is defined as the larger of the organisms involved in a symbiotic interaction.
haemolysis in host
hemolysin activity
hemolysis by symbiont of host RBCs
hemolysis by symbiont of host red blood cells
pathogenesis
regulation of cytolysis of host cells by symbiont
The chemical reactions and pathways resulting in the breakdown of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2--4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.
ascorbate catabolic process
ascorbate catabolism
L-ascorbic acid breakdown
L-ascorbic acid catabolism
L-ascorbic acid degradation
vitamin C catabolic process
vitamin C catabolism
The chemical reactions and pathways resulting in the formation of streptomycin, a commonly used antibiotic in cell culture media; it acts only on prokaryotes and blocks transition from initiation complex to chain elongating ribosome.
streptomycin anabolism
streptomycin biosynthesis
streptomycin formation
streptomycin synthesis
Catalysis of the reaction: 1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate.
1,8-diazacyclotetradecane-2,9-dione lactamhydrolase activity
Catalysis of the reaction: N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate.
6-aminohexanoic acid oligomer hydrolase activity
N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase activity
The chemical reactions and pathways resulting in the breakdown of nylon, a polymer where the main polymer chain comprises recurring amide groups; these compounds are generally formed from combinations of diamines, diacids and amino acids.
nylon breakdown
nylon catabolism
nylon degradation
The chemical reactions and pathways resulting in the formation of diaminopimelate, both as an intermediate in lysine biosynthesis and as a component (as meso-diaminopimelate) of the peptidoglycan of Gram-negative bacterial cell walls.
diaminopimelate anabolism
diaminopimelate biosynthesis
diaminopimelate formation
diaminopimelate synthesis
The process in which an antigen-presenting cell expresses a peptide antigen of exogenous origin on its cell surface in association with an MHC class II protein complex. The peptide antigen is typically, but not always, processed from a whole protein.
antigen presentation, exogenous antigen via MHC class II
antigen presentation, exogenous peptide antigen
antigen processing, exogenous antigen via major histocompatibility complex class II
exogenous peptide antigen processing and presentation via MHC class II
A cyclin-dependent kinase activating kinase complex capable of activating cyclin-dependent kinases by threonine phosphorylation, thus regulating cell cycle progression. consists of a kinase, cyclin and optional assembly factors, in human CDK7, CCNH and MNAT1. CAK activity is itself regulated throughout the cell cycle by T-loop phosphorylation of its kinase component (CDK7 in human). Phosphorylation of serine residues during mitosis inactivates the enzyme. Also capable of CAK phosphorylating the carboxyl-terminal domain (CTD) of RNA polymerase II and other transcription activating proteins, as part of the general transcription factor TFIIH.
CAK complex
CDK-activating kinase complex
Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK).
CAK
cdk-activating kinase activity
cyclin-dependent protein kinase activating kinase, intrinsic catalyst activity
Modulation of the activity of the enzyme cyclin-dependent protein kinase activating kinase.
cyclin-dependent protein kinase activating kinase, intrinsic regulator activity
The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.
peptidyl-arginine methylation, to unsymmetrical-dimethyl arginine
Catalysis of the activation of the proteolytically processed small ubiquitin-related modifier SUMO, through the formation of an ATP-dependent high-energy thiolester bond.
SMT3 activating enzyme
SUMO E1 activator enzyme
Binding to interleukin-8.
IL-8 binding
Binding to a type I interferon. Type I interferons include the interferon-alpha, beta, delta, epsilon, zeta, kappa, tau, and omega gene families.
interferon-alpha binding
interferon-alpha/beta binding
interferon-beta binding
interferon-delta binding
interferon-epsilon binding
interferon-kappa binding
interferon-omega binding
interferon-tau binding
interferon-zeta binding
type I IFN binding
Binding to type II interferon, also known as interferon-gamma.
IFN-gamma binding
IFNG binding
interferon-gamma binding
Binding to interleukin-10.
IL-10 binding
Binding to interleukin-11.
IL-11 binding
Binding to interleukin-13.
IL-13 binding
Binding to interleukin-2.
IL-2 binding
Binding to interleukin-21.
IL-21 binding
Binding to interleukin-3.
IL-3 binding
Binding to interleukin-4.
IL-4 binding
Binding to interleukin-5.
IL-5 binding
Binding to interleukin-6.
IL-6 binding
Binding to interleukin-7.
IL-7 binding
Binding to interleukin-9.
IL-9 binding
The chemical reactions and pathways resulting in the breakdown of pteridine, pyrazino(2,3-dipyrimidine), the parent structure of pterins and the pteroyl group.
pteridine breakdown
pteridine catabolism
pteridine degradation
The space between a symbiont plasma membrane and the symbiont-containing vacuole membrane.
parasitophorous vacuolar space
symbiont-containing vacuole space
Tubular network of extensions from the symbiont-containing vacuole membrane that protrude into the host cytoplasm.
parasitophorous vacuolar membrane network
symbiont-containing vacuole membrane network
tubulovesicular network
Any process in which a symbiont organism modulates the frequency, rate or extent of erythrocyte aggregation in its host organism, e.g. the binding of parasite-infected erythrocytes to uninfected erythrocytes.
modulation by symbiont of host erythrocyte aggregation
rosetting
That part of the plasma membrane found in the ciliary pocket (also called flagellar pocket).
cilial pocket membrane
cilium pocket membrane
flagellar pocket membrane
Vacuole within a parasite used for digestion of the host cell cytoplasm. An example of this component is found in the Apicomplexa.
digestive vacuole
The directed movement of hemoglobin into a cell by receptor-mediated endocytosis.
endocytic hemoglobin import
haemoglobin uptake
hemoglobin uptake
An electron dense ring at the most anterior position of the apical complex, from which the conoid fibers originate; formed during an invasive life cycle stage of an apicomplexan parasite.
anterior polar ring of apical complex
upper polar ring of apical complex
An electron dense ring at the most posterior position of the apical complex, from which the subpellicular microtubules originate; formed during an invasive life cycle stage of an apicomplexan parasite.
lower polar ring of apical complex
posterior polar ring of apical complex
preconoidal ring of apical complex
A process by which a symbiont evades the host adaptive immune response by changing antigenic determinants on the symbiont surface that are exposed to host antibodies.
surface antigen variation
The adherence of symbiont-infected erythrocytes to microvascular endothelium via symbiont proteins embedded in the membrane of the erythrocyte.
cytoadherence to microvasculature, mediated by parasite protein
cytoadherence to microvasculature, mediated by symbiont protein
heterophilic cell adhesion involved in cytoadherence to microvasculature, mediated by parasite protein
parasite-protein-mediated cytoadherence to microvasculature
symbiont-protein-mediated cytoadherence to microvasculature
A disk-like structure that appears at the periphery of a red blood cell infected by an apicomplexan parasite, characterized by a translucent lumen and an electron-dense coat of variable thickness; often appears to be tethered to the host cell membrane by fibrous connections with the erythrocyte cytoskeleton.
Maurers cleft
Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring.
haem binding
The formation of the median and lateral hinge points in the neural folds. These are created by apical constriction and basal expansion of the underlying neural cells. The median hinge point extends for the entire length of the neural tube, and the lateral hinge points do not form in the spinal cord region of the neural tube.
neural fold furrowing
The process in which neuroepithelial cells in the ventral neural tube acquire specialized structural and/or functional features of radial glial cells. Radial cell precursors differentiate into both neuronal cell types and mature radial glial cells. Mature radial glial cells regulate the axon growth and pathfinding processes that occur during white matter patterning of the developing spinal cord. Differentiation includes the processes involved in commitment of a cell to a specific fate.
radial glial cell differentiation in spinal cord
The process whose specific outcome is the progression of the ammon gyrus over time, from its formation to the mature structure. The ammon gyrus, often subdivided into the CA1 and CA3 regions, is one of the two interlocking gyri of the hippocampus that is rich in large pyramidal neurons.
Ammon\'s horn development
cornu ammonis development
The regionalization process that gives rise to the midbrain-hindbrain boundary. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
isthmus biosynthesis
isthmus formation
MHB biosynthesis
MHB formation
midbrain-hindbrain boundary biosynthesis
midbrain-hindbrain boundary formation
The process that contributes to the act of creating the structural organization of the midbrain-hindbrain boundary structure. The midbrain-hindbrain domain of the embryonic brain is comprised of the mesencephalic vesicle and the first rhombencephalic vesicle at early somitogenesis stages. An organizing center at the boundary patterns the midbrain and hindbrain primordia of the neural plate.
isthmus structural organization
MHB structural organization
midbrain-hindbrain boundary structural organisation
The process that contributes to the act of creating the structural organization of the cerebellum. This process pertains to the physical shaping of a rudimentary structure. The cerebellum is the portion of the brain in the back of the head between the cerebrum and the pons. The cerebellum controls balance for walking and standing, modulates the force and range of movement and is involved in the learning of motor skills.
cerebellum structural organisation
The process that contributes to the act of creating the structural organization of the central nervous system structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain, spinal cord and spinal nerves. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
central nervous system structural organisation
The process that gives rise to the abducens nerve. This process pertains to the initial formation of a structure from unspecified parts. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
CN VI biosynthesis
CN VI formation
The process that contributes to the act of creating the structural organization of the abducens nerve. This process pertains to the physical shaping of a rudimentary structure. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
abducens nerve structural organisation
CN VI structural organization
A developmental process, independent of morphogenetic (shape) change, that is required for the abducens nerve to attain its fully functional state. The motor function of the abducens nerve is to contract the lateral rectus which results in abduction of the eye.
CN VI maturation
A developmental process, independent of morphogenetic (shape) change, that is required for the accessory nerve to attain its fully functional state. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
CN XI maturation
spinal accessory nerve maturation
The process that gives rise to the accessory nerve. This process pertains to the initial formation of a structure from unspecified parts. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
CN XI biosynthesis
CN XI formation
The process that contributes to the act of creating the structural organization of the accessory nerve This process pertains to the physical shaping of a rudimentary structure. The spinal branch of this motor nerve innervates the trapezius and the sternocleidomastoid muscles. The cranial branch joins the vagus nerve and innervates the same targets as the vagus nerve.
accessory nerve structural organisation
CN XI structural organization
The process that gives rise to the facial nerve. This process pertains to the initial formation of a structure from unspecified parts. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial ophthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
CN VII biosynthesis
CN VII formation
The process that contributes to the act of creating the structural organization of the facial nerve. This process pertains to the physical shaping of a rudimentary structure. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial ophthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
CN VII structural organization
facial nerve structural organisation
A developmental process, independent of morphogenetic (shape) change, that is required for the facial nerve to attain its fully functional state. This sensory and motor nerve supplies the muscles of facial expression and the expression and taste at the anterior two-thirds of the tongue. The principal branches are the superficial ophthalmic, buccal, palatine and hyomandibular. The main trunk synapses within pterygopalatine ganglion in the parotid gland and this ganglion then gives of nerve branches which supply the lacrimal gland and the mucous secreting glands of the nasal and oral cavities.
CN VII maturation
A developmental process, independent of morphogenetic (shape) change, that is required for the glossopharyngeal nerve to attain its fully functional state. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
CN IX maturation
The process that gives rise to the glossopharyngeal nerve. This process pertains to the initial formation of a structure from unspecified parts. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
CN IX biosynthesis
CN IX formation
The process that contributes to the act of creating the structural organization of the glossopharyngeal nerve. This process pertains to the physical shaping of a rudimentary structure. Various sensory and motor branches of the glossopharyngeal nerve supply nerve connections to the pharynx and back of the tongue. The branchial motor component contains motor fibers that innervate muscles that elevate the pharynx and larynx, and the tympanic branch supplies parasympathetic fibers to the otic ganglion.
CN IX structural organization
glossopharyngeal nerve structural organisation