endoplasmic reticulum stress-induced apoptosis

intrinsic apoptotic signaling pathway induced by endoplasmic reticulum stress

apoptosis in response to endoplasmic reticulum stress

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

The series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to a stimulus indicating endoplasmic reticulum (ER) stress, and ends when the execution phase of apoptosis is triggered. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen. [GOC:mah, GOC:mtg_apoptosis, PMID:18701708]


The actin nucleation process in which actin monomers combine in the absence of any existing actin filaments; elongation of the actin oligomer formed by nucleation leads to the formation of an unbranched filament. [GOC:mah, PMID:17477841]


formin-mediated actin filament nucleation


Binding to the D- or L-enantiomer of fructose, the ketohexose arabino-hex-2-ulose. [CHEBI:28757, GOC:BHF, GOC:mah]


Binding to an RNA polymerase molecule or complex. [GOC:BHF, GOC:mah, GOC:txnOH]


Binding to a proline-rich region, i.e. a region that contains a high proportion of proline residues, in a protein. [GOC:mah]


A SNARE complex that contains cellubrevin (VAMP3), VAMP4, and syntaxin 16 (or orthologs thereof). [PMID:11839770]


SNARE complex location (Vamp3, Vamp4, Stx16)


A SNARE complex that contains cellubrevin (VAMP3), VAMP4, endobrevin (VAMP8), and syntaxin 6 (or orthologs thereof). [PMID:11839770]


SNARE complex location (Vamp3, Vamp4, Vam8, Stx6)

SNARE complex (Vamp3, Vamp4, Vam8, Stx6)


A SNARE complex that contains syntaxin 6, syntaxin 16, and Vti1a (or orthologs thereof). [PMID:11839770]


A SNARE complex that contains VAMP4, syntaxin 6, syntaxin 16, and Vti1a (or orthologs thereof). [PMID:11839770]


SNARE complex location (Vamp4, Stx6, Stx16, Vti1a)

SNARE complex (Vamp4, Stx6, Stx16, Vti1a)


A protein complex in which at least one of the proteins is a cytochrome, i.e. a heme-containing protein involved in catalysis of redox reactions. [GOC:mah]


proton-transporting V-type ATPase complex assembly

The aggregation, arrangement and bonding together of a proton-transporting V-type ATPase complex, proton-transporting two-sector ATPase complex that couples ATP hydrolysis to the transport of protons across a concentration gradient. [GOC:mah]


proton-transporting two-sector ATPase complex assembly

The aggregation, arrangement and bonding together of a proton-transporting two-sector ATPase complex, a large protein complex that catalyzes the synthesis or hydrolysis of ATP by a rotational mechanism, coupled to the transport of protons across a membrane. [GOC:mah]


vacuolar proton-transporting V-type ATPase complex assembly

The aggregation, arrangement and bonding together of a vacuolar proton-transporting V-type ATPase complex, proton-transporting two-sector ATPase complex that couples ATP hydrolysis to the transport of protons across the vacuolar membrane. [GOC:BHF, GOC:mah]


clustering of voltage gated calcium channels

clustering of voltage-dependent calcium channels

voltage-gated calcium channel clustering

clustering of voltage-gated calcium channels

The process in which voltage-gated calcium channels become localized together in high densities. [GOC:BHF, GOC:sart, PMID:18385325]


A secretory organelle that forms part of the apical complex; a small, threadlike structure located is close proximity to the subpellicular microtubules. Its contents include a rhomboid protease (PfROM1 in Plasmodium falciparum) that moves from the lateral asymmetric localization to the merozoite apical pole and the posterior pole upon release of merozoites from schizonts. [GOC:BHF, PMID:18048320]


The regulated release of the aqueous layer of the tear film from the lacrimal glands. Tears are the liquid product of a process of lacrimation to clean and lubricate the eyes. Tear fluid contains water, mucin, lipids, lysozyme, lactoferrin, lipocalin, lacritin, immunoglobulins, glucose, urea, sodium, and potassium. [GOC:rph]


The modification of a histone by the removal of a methyl group from a lysine residue. [GOC:mah]


The modification of a histone by the removal of a methyl group from an arginine residue. [GOC:mah]


The modification of histone H3 by the removal of a methyl group from arginine at position 2 of the histone. [GOC:BHF, GOC:vk]


The modification of histone H4 by the removal of a methyl group from arginine at position 3 of the histone. [GOC:BHF, GOC:vk]


Binding to a titin Z protein domain, which recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. [GOC:mah, InterPro:IPR015129]


removal of initiator methionine from protein

The protein modification process in which the translation-initiating methionine or formylmethionine residue is removed from a protein. [GOC:imk, GOC:mah]


Endocytosis of a protein that requires the substrate to be modified by ubiquitination. Several plasma membrane proteins, including cell surface permeases and some receptors, are targeted for internalization by endocytosis, and are thereafter delivered to the vacuole or lysosome, where they are degraded. [GOC:jp, GOC:mah, PMID:9409540]


Binding to a chromo shadow domain, a protein domain that is distantly related, and found in association with, the chromo domain. [GOC:BHF, GOC:vk, InterPro:IPR008251, PMID:7667093]


An inclusion body located in the cytoplasm that consists of polyhydroxyalkanoate (PHA) molecules and associated proteins, surrounded by a phospholipid monolayer; the proteins include PHA synthase, PHA depolymerase and 3HB-oligomer hydroxylase, phasins (PhaPs), which are thought to be the major structural proteins of the membrane surrounding the inclusion, and the regulator of phasin expression PhaR. [GOC:mah, PMID:15762612]


chloride-activated potassium channel activity

Enables the chloride concentration-regulatable energy-independent passage of potassium ions across a lipid bilayer down a concentration gradient. [GOC:kmv, GOC:mtg_transport]


The regulated release of glucagon from secretory granules in the A (alpha) cells of the pancreas (islets of Langerhans). [GOC:BHF, GOC:rl]


Any process that modulates the frequency, rate or extent of the regulated release of glucagon. [GOC:BHF, GOC:mah]


down-regulation of glucagon secretion
downregulation of glucagon secretion
down regulation of glucagon secretion

negative regulation of glucagon secretion

Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of glucagon. [GOC:BHF, GOC:mah]


up-regulation of glucagon secretion
up regulation of glucagon secretion
upregulation of glucagon secretion

positive regulation of glucagon secretion

Any process that activates or increases the frequency, rate or extent of the regulated release of glucagon. [GOC:BHF, GOC:mah]


Binding to fructose 6-phosphate. [GOC:mah]


mitochondrion outer membrane translocase complex assembly

mitochondrial outer membrane translocase complex assembly

The aggregation, arrangement and bonding together of a set of components to form a mitochondrial outer membrane translocase complex. [GOC:BHF, GOC:vk]


Binding to the delta subunit of the catenin complex. [GOC:rph]


The series of molecular signals initiated by a chemokine 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:mah, GOC:signaling]


regulation of chemokine-mediated signalling pathway

regulation of chemokine-mediated signaling pathway

Any process that modulates the rate, frequency or extent of a chemokine-mediated signaling pathway. [GOC:mah]


negative regulation of chemokine-mediated signalling pathway

negative regulation of chemokine-mediated signaling pathway

Any process that decreases the rate, frequency or extent of a chemokine-mediated signaling pathway. [GOC:mah]


positive regulation of chemokine-mediated signalling pathway

positive regulation of chemokine-mediated signaling pathway

Any process that increases the rate, frequency or extent of a chemokine-mediated signaling pathway. [GOC:mah]


The series of molecular signals initiated by interleukin-6 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:add, GOC:BHF, GOC:mah, GOC:signaling]


regulation of interleukin-6-mediated signalling pathway

regulation of IL-6-mediated signaling pathway

regulation of interleukin-6-mediated signaling pathway

Any process that modulates the rate, frequency or extent of an interleukin-6-mediated signaling pathway. [GOC:BHF, GOC:mah]


negative regulation of IL-6-mediated signaling pathway

negative regulation of interleukin-6-mediated signalling pathway

negative regulation of interleukin-6-mediated signaling pathway

Any process that decreases the rate, frequency or extent of an interleukin-6-mediated signaling pathway. [GOC:BHF, GOC:mah]


positive regulation of interleukin-6-mediated signalling pathway

positive regulation of IL-6-mediated signaling pathway

positive regulation of interleukin-6-mediated signaling pathway

Any process that increases the rate, frequency or extent of an interleukin-6-mediated signaling pathway. [GOC:BHF, GOC:mah]


The series of molecular signals initiated by interleukin-27 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:add, GOC:BHF, GOC:mah, GOC:signaling]


regulation of interleukin-27-mediated signalling pathway

regulation of IL27RA/IL6ST signaling pathway

regulation of IL-27-mediated signaling pathway

regulation of interleukin-27-mediated signaling pathway

Any process that modulates the rate, frequency or extent of an interleukin-27-mediated signaling pathway. [GOC:BHF, GOC:mah]


negative regulation of IL-27-mediated signaling pathway

negative regulation of IL27RA/IL6ST signaling pathway

negative regulation of interleukin-27-mediated signalling pathway

negative regulation of interleukin-27-mediated signaling pathway

Any process that decreases the rate, frequency or extent of an interleukin-27-mediated signaling pathway. [GOC:BHF, GOC:mah]


positive regulation of IL27RA/IL6ST signaling pathway

positive regulation of IL-27-mediated signaling pathway

positive regulation of interleukin-27-mediated signalling pathway

positive regulation of interleukin-27-mediated signaling pathway

Any process that increases the rate, frequency or extent of an interleukin-27-mediated signaling pathway. [GOC:BHF, GOC:mah]


ciliary neurotrophic factor receptor complex location

A protein complex that acts as a receptor for the cytokine ciliary neurotrophic factor (CNTF). In humans the receptor complex is a hexamer composed of two molecules each of CNTF and CNTFR and one molecule each of gp130 and LIFR. [GOC:BHF, GOC:mah, GOC:rl, PMID:12707266]


A bacteroid-containing symbiosome in which the bacterial component is a genetically highly reduced cyanobacterium that is photosynthetically active and incapable of an independent existence outside its host. The chromatophore functions as a photosynthetic organelle, and has been found and characterized in the amoeba Paulinella chromatophora. [GOC:expert_mm, PMID:18356055]


Either of the lipid bilayers that surround an organellar chromatophore. [GOC:mah]


Paulinella-type chromatophore inner membrane

The inner, i.e. lumen-facing, of the two lipid bilayers surrounding an organellar chromatophore. [GOC:mah]


Paulinella-type chromatophore outer membrane

The outer, i.e. cytoplasm-facing, of the two lipid bilayers surrounding an organellar chromatophore. [GOC:mah]


Paulinella-type chromatophore intermembrane space

organellar chromatophore intermembrane space

The region between the inner and outer lipid bilayers that surround an organellar chromatophore. [GOC:mah]


A thylakoid located in an organellar chromatophore. [GOC:mah]


Paulinella-type chromatophore thylakoid lumen

organellar chromatophore thylakoid lumen

The volume enclosed by an organellar chromatophore thylakoid membrane. [GOC:mah]


Paulinella-type chromatophore thylakoid membrane

organellar chromatophore thylakoid membrane

The lipid bilayer membrane of any thylakoid within an organellar chromatophore. [GOC:mah]


Binding to the cytokine ciliary neurotrophic factor. [GOC:BHF, GOC:mah]


ciliary neurotrophic factor-mediated signalling pathway

ciliary neurotrophic factor-mediated signaling pathway

The series of molecular signals initiated by the binding of a ciliary neurotrophic factor (CNTF) to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:BHF, GOC:mah]


The progression of the Kupffer's vesicle over time from its initial formation until its mature state. The Kupffer's vesicle is a small but distinctive epithelial sac containing fluid, located midventrally posterior to the yolk cell or its extension, and transiently present during most of the segmentation period. [GOC:dgh]


type III transforming growth factor beta receptor activity

transforming growth factor beta receptor activity, type III

Combining with transforming growth factor beta to initiate a change in cell activity; facilitates ligand binding to type I and type II TGF-beta receptors. [GOC:BHF, GOC:mah, PMID:9759503]


transforming growth factor beta ligand binding to type III receptor


The process preceding formation of the peptide bond between the first two amino acids of a protein in a mitochondrion. This includes the formation of a complex of the ribosome, mRNA, and an initiation complex that contains the first aminoacyl-tRNA. [GOC:mah]


The successive addition of amino acid residues to a nascent polypeptide chain during protein biosynthesis in a mitochondrion. [GOC:mah]


The process resulting in the release of a polypeptide chain from the ribosome in a mitochondrion, usually in response to a termination codon (note that mitochondria use variants of the universal genetic code that differ between different taxa). [GOC:mah, http://mitogenome.org/index.php/Genetic_Code_of_mitochondria]


tRNA aminoacylation for mitochondrial protein translation

The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA, to be used in ribosome-mediated polypeptide synthesis in a mitochondrion. [GOC:mah]


regulation of mitochondrial protein biosynthesis

regulation of mitochondrial protein anabolism

regulation of mitochondrial protein formation

regulation of mitochondrial protein synthesis

Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA in a mitochondrion. [GOC:mah]


negative regulation of mitochondrial protein synthesis

negative regulation of mitochondrial protein anabolism

negative regulation of mitochondrial protein biosynthesis

negative regulation of mitochondrial protein formation

negative regulation of mitochondrial translation

Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA in a mitochondrion. [GOC:mah]


positive regulation of mitochondrial protein biosynthesis

positive regulation of mitochondrial protein formation

positive regulation of mitochondrial protein synthesis

positive regulation of mitochondrial protein anabolism

positive regulation of mitochondrial translation

Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA in a mitochondrion. [GOC:mah]


regulation of mitochondrial translation initiation

regulation of mitochondrial translational initiation

Any process that modulates the frequency, rate or extent of the process preceding formation of the peptide bond between the first two amino acids of a protein in a mitochondrion. [GOC:mah]


negative regulation of mitochondrial translation initiation

negative regulation of mitochondrial translational initiation

Any process that stops, prevents, or reduces the frequency, rate or extent of the process preceding formation of the peptide bond between the first two amino acids of a protein in a mitochondrion. [GOC:mah]


positive regulation of mitochondrial translation initiation

positive regulation of mitochondrial translational initiation

Any process that activates or increases the frequency, rate or extent of the process preceding formation of the peptide bond between the first two amino acids of a protein in a mitochondrion. [GOC:mah]


The chemical reactions and pathways involving beta-1,2-linked oligomannosides, which are found in fungal cell wall phosphopeptidomannan and phospholipomannan. [GOC:mah, PMID:18234669]


beta-1,2-oligomannoside anabolism
beta-1,2-oligomannoside formation
beta-1,2-oligomannoside biosynthesis
beta-1,2-oligomannoside synthesis

The chemical reactions and pathways resulting in the formation of beta-1,2-linked oligomannosides, which are found in fungal cell wall phosphopeptidomannan and phospholipomannan. [GOC:mah, PMID:18234669]


small conjugating protein-specific endopeptidase activity

ubiquitin-like protein-specific endopeptidase activity

Catalysis of the hydrolysis of peptide bonds between an alpha-carboxyl group and an alpha-amino group within a small protein such as ubiquitin or a ubiquitin-like protein (e.g. APG8, ISG15, NEDD8, SUMO). [GOC:mah]


Catalysis of the hydrolysis of peptide bonds between an alpha-carboxyl group and an alpha-amino group within the small conjugating protein SUMO. [GOC:mah]


response to UV-A radiation stimulus
response to UV-A light stimulus
response to UVA radiation stimulus
response to UVA light 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 UV-A radiation stimulus. UV-A radiation (UV-A light) spans the wavelengths 315 to 400 nm. [GOC:BHF, GOC:mah]


Evagination of a membrane to form a synaptic vesicle. [GOC:mah]


The process of coupling alanine to alanyl-tRNA in a mitochondrion, catalyzed by alanyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling arginine to arginyl-tRNA in a mitochondrion, catalyzed by arginyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling asparagine to asparaginyl-tRNA in a mitochondrion, catalyzed by asparaginyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling aspartate to aspartyl-tRNA in a mitochondrion, catalyzed by aspartyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling cysteine to cysteinyl-tRNA in a mitochondrion, catalyzed by cysteinyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling glutamine to glutaminyl-tRNA in a mitochondrion, catalyzed by glutaminyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling glutamate to glutamyl-tRNA in a mitochondrion, catalyzed by glutamyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling glycine to glycyl-tRNA in a mitochondrion, catalyzed by glycyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling histidine to histidyl-tRNA in a mitochondrion, catalyzed by histidyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling isoleucine to isoleucyl-tRNA in a mitochondrion, catalyzed by isoleucyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling leucine to leucyl-tRNA in a mitochondrion, catalyzed by leucyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling lysine to lysyl-tRNA in a mitochondrion, catalyzed by lysyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling methionine to methionyl-tRNA in a mitochondrion, catalyzed by methionyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling phenylalanine to phenylalanyl-tRNA in a mitochondrion, catalyzed by phenylalanyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling proline to prolyl-tRNA in a mitochondrion, catalyzed by prolyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling serine to seryl-tRNA in a mitochondrion, catalyzed by seryl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling threonine to threonyl-tRNA in a mitochondrion, catalyzed by threonyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The regulated release of adiponectin, a protein hormone, by adipose tissue. [GOC:BHF, GOC:rl]


Any process that modulates the frequency, rate or extent of the regulated release of adiponectin from a cell. [GOC:mah]


down regulation of adiponectin secretion

down-regulation of adiponectin secretion

negative regulation of adiponectin secretion

Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of adiponectin from a cell. [GOC:BHF, GOC:mah]


up-regulation of adiponectin secretion
upregulation of adiponectin secretion
up regulation of adiponectin secretion

positive regulation of adiponectin secretion

Any process that activates or increases the frequency, rate or extent of the regulated release of adiponectin from a cell. [GOC:BHF, GOC:mah]


The process in which calcium salts, mainly carbonated hydroxyapatite, are deposited in tooth enamel. [GOC:BHF, GOC:mah, GOC:sl, PMID:10206335, PMID:16931858, PMID:21196346]


regulation of biomineral tissue development

Any process that modulates the frequency, rate or extent of biomineral tissue development, the formation of hard tissues that consist mainly of inorganic compounds. [GOC:mah]


Any process that stops, prevents, or reduces the frequency, rate or extent of biomineral tissue development, the formation of hard tissues that consist mainly of inorganic compounds. [GOC:mah]

negative regulation of biomineral tissue development


positive regulation of biomineral tissue development

Any process that activates or increases the frequency, rate or extent of biomineral tissue development, the formation of hard tissues that consist mainly of inorganic compounds. [GOC:mah]


Any process that modulates the frequency, rate or extent of tooth mineralization, the deposition of calcium salts in tooth structures. [GOC:BHF, GOC:mah]


negative regulation of tooth mineralization

Any process that stops, prevents, or reduces the frequency, rate or extent of tooth mineralization, the deposition of calcium salts in tooth structures. [GOC:BHF, GOC:mah]


positive regulation of tooth mineralization

Any process that activates or increases the frequency, rate or extent of tooth mineralization, the deposition of calcium salts in tooth structures. [GOC:BHF, GOC:mah]


Any process that modulates the frequency, rate or extent of enamel mineralization, the deposition of calcium salts in tooth enamel. [GOC:BHF, GOC:mah]


negative regulation of enamel mineralization

Any process that stops, prevents, or reduces the frequency, rate or extent of enamel mineralization, the deposition of calcium salts in tooth enamel. [GOC:BHF, GOC:mah]


positive regulation of enamel mineralization

Any process that activates or increases the frequency, rate or extent of enamel mineralization, the deposition of calcium salts in tooth enamel. [GOC:BHF, GOC:mah]


A transcriptional repressor complex that contains the lin-9, lin-35, lin-37, lin-52, lin-53, lin-5is involved in 4-, dpl-1 and efl-1 proteins, and is involved in cell fate specification. [PMID:17075059]


The regulated release of water from a contractile vacuole to the outside of a cell by fusion of the contractile vacuole membrane with the plasma membrane. [GOC:mah, PMID:10369671]


The chemical reactions and pathways involving D-serine, the D-enantiomer of serine, i.e. (2R)-2-amino-3-hydroxypropanoic acid. [CHEBI:16523, GOC:jsg, GOC:mah]


D-serine anabolism
D-serine biosynthesis
D-serine formation
D-serine synthesis

The chemical reactions and pathways resulting in the formation of D-serine, the D-enantiomer of serine, i.e. (2R)-2-amino-3-hydroxypropanoic acid. D-serine is often formed by racemization of L-serine. [CHEBI:16523, GOC:jsg, GOC:mah]


Binding to large ribosomal subunit RNA (LSU rRNA), a constituent of the large ribosomal subunit. In S. cerevisiae, this is the 25S rRNA. [GOC:elh]


Binding to small ribosomal subunit RNA (SSU rRNA), a constituent of the small ribosomal subunit. In S. cerevisiae, this is the 18S rRNA. [GOC:elh]


Binding to a DNA polymerase. [GOC:BHF, GOC:mah]


The process of coupling tryptophan to tryptophanyl-tRNA in a mitochondrion, catalyzed by tryptophanyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling tyrosine to tyrosyl-tRNA in a mitochondrion, catalyzed by tyrosyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


The process of coupling valine to valyl-tRNA in a mitochondrion, catalyzed by valyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. [GOC:mah, GOC:mcc]


telosome
Pot1-Tpz1 complex location
Pot1-Tpz1 complex
shelterin complex location
shelterin complex
Pot1 complex

A nuclear telomere cap complex that is formed by the association of telomeric ssDNA- and dsDNA-binding proteins with telomeric DNA, and is involved in telomere protection and recruitment of telomerase. The complex is known to contain TERF1, TERF2, POT1, RAP1, TINF2 and ACD in mammalian cells, and Pot1, Tpz1, Rap1, Rif1, Rif2 and Taz1 in Saccharomyces. Taz1 and Rap1 (or their mammalian equivalents) form a dsDNA-binding subcomplex, Pot1 and Tpz1 form an ssDNA-binding subcomplex, and the two subcomplexes are bridged by Poz1, which acts as an effector molecule along with Ccq1. [GOC:expert_mf, GOC:mah, GOC:vw, PMID:18828880]


The chemical reactions and pathways involving kynurenine, the amino acid 3-(2-aminobenzoyl)-alanine. [CHEBI:28683, GOC:mah, GOC:rph]


Catalysis of the reaction: L-methionine R-oxide + thioredoxin = L-methionine + thioredoxin disulfide; can act on free oxidized methionine with specificity for the R enantiomer; does not act on oxidized methionine in peptide linkage. Thioredoxin disulfide is the oxidized form of thioredoxin. [GOC:mcc, PMID:17535911, PMID:19049972]


chromosome organisation involved in meiosis

chromosome organization involved in meiotic cell cycle

A process of chromosome organization that is involved in a meiotic cell cycle. [GOC:mah]


A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a synaptonemal complex. A synaptonemal complex is a proteinaceous scaffold formed between homologous chromosomes during meiosis. [GOC:mah]


The controlled breakdown of a synaptonemal complex. [GOC:mah]


growth hormone receptor complex location

A receptor complex that consists of two identical subunits and binds growth hormone. [GOC:BHF, GOC:mah, GOC:vk, PMID:11445442]


eukaryotic translation initiation factor 3 complex assembly

The aggregation, arrangement and bonding together of a set of components to form the eukaryotic translation initiation factor 3 complex. [GOC:mah]


attachment of telomeres to nuclear envelope

The meiotic cell cycle process in which physical connections are formed between telomeric heterochromatin and the nuclear envelope, facilitating bouquet formation. [GOC:jp, GOC:pr, GOC:vw, PMID:18818742]

meiotic attachment of telomere to nuclear envelope


protein localisation to chromosome, telomeric region

protein localization to chromosome, telomeric region

Any process in which a protein is transported to, or maintained at, the telomeric region of a chromosome. [GOC:BHF, GOC:mah]


establishment of protein localisation to chromosome

establishment of protein localization to chromosome

The directed movement of a protein to a specific location on a chromosome. [GOC:BHF, GOC:mah]


establishment of protein localisation to telomere

establishment of protein localization to chromosome, telomeric region

establishment of protein localization to telomere

The directed movement of a protein to a specific location in the telomeric region of a chromosome. [GOC:BHF, GOC:mah]


regulation of establishment of protein localisation

regulation of establishment of protein localization

Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location. [GOC:BHF, GOC:mah]


regulation of establishment of protein localisation to chromosome

regulation of establishment of protein localization to chromosome

Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location on a chromosome. [GOC:BHF, GOC:mah]


regulation of establishment of protein localisation to telomere

regulation of establishment of protein localization to telomere

Any process that modulates the frequency, rate or extent of the directed movement of a protein to a specific location in the telomeric region of a chromosome. [GOC:BHF, GOC:mah]


Catalysis of the reaction: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO(2). [RHEA:25593]


protein homotrimer assembly
protein homotrimer biosynthetic process
protein homotrimer formation
protein homotrimer biosynthesis

The formation of a protein homotrimer, a macromolecular structure consisting of three noncovalently associated identical subunits. [GOC:hjd]


protein heterotrimer biosynthetic process

The formation of a protein heterotrimer, a macromolecular structure consisting of three noncovalently associated subunits, of which not all are identical. [GOC:hjd]


A protein complex that is part of the chromatin remodeling machinery; the acronym stands for ASsembly of Tel, Rvb and Atm-like kinase. In Saccharomyces cerevisiae this complex includes Rvb1p, Rvb2p, Tra1p, Tel2p, Asa1p, Ttilp and Tti2p. [GOC:rb, PMID:19040720, PMID:22505622]


Clr6-LE complex
Clr6-LE complex location
Rpd3L-Expanded complex location

A protein complex that contains a histone deacetylase and is part of the chromatin remodeling machinery. In Saccharomyces cerevisiae this complex contains the Rpd3p, Sin3p, Ume1p, Pho23p, Sap30p, Sds3p, Cti6p, Rxt2p, Rxt3p, Dep1p, Ume6p, Ash1p, Dot6p, Snt1, Sif2p, Set3p, Hos2p, Tos4p and Tod6p proteins. [GOC:rb, PMID:19040720]


A histone deacetylase complex that is part of the chromatin remodeling machinery. In Saccharomyces cerevisiae this complex contains Snt2p, Ecm5p and Rpd3p. [GOC:rb, PMID:19040720]


protein amino acid poly-ADP-ribosylation

The transfer of multiple ADP-ribose residues from NAD to a protein amino acid, forming a poly(ADP-ribose) chain. [GOC:BHF, GOC:mah, GOC:rl, PMID:25043379]


protein amino acid auto-ADP-ribosylation

The ADP-ribosylation by a protein of one or more of its own amino acid residues, or residues on an identical protein. [GOC:BHF, GOC:rl]


A protein complex that contains the protein-tyrosine kinase CSK and the GTPase-activating protein (GAP)-associated p62 (GAP-A.p62); may mediate translocation of proteins, including GAP and CSK, to membrane or cytoskeletal regions upon c-Src activation. [PMID:7544435]


transcription factor TFIIIB complex assembly

The aggregation, arrangement and bonding together of a set of components to form a transcription factor TFIIIB complex. [GOC:mah]


sulphide homeostasis
sulfide homeostasis
sulphide ion homeostasis

Any process involved in the maintenance of an internal steady state of sulfide ions within an organism or cell. [GOC:mah]


cellular sulphide ion homeostasis
cellular sulphide homeostasis
cellular sulfide homeostasis

Any process involved in the maintenance of an internal steady state of sulfide ions at the level of a cell. [GOC:mah]


A sulfur oxidation process that proceeds via the reaction catalyzed by sulfur dioxygenase, and requires the presence of oxygen. [MetaCyc:SULFUROX-PWY]


sulfide oxidation, using sulfide-quinone reductase

sulphide oxidation, using sulfide:quinone oxidoreductase

sulfide oxidation, using sulfide:quinone oxidoreductase

A sulfide oxidation process that proceeds via the reaction catalyzed by sulfide:quinone oxidoreductase. [MetaCyc:P222-PWY]


sulphide oxidation, using sulfide dehydrogenase

sulfide oxidation, using sulfide dehydrogenase

A sulfide oxidation process that proceeds via the reaction catalyzed by sulfide dehydrogenase. [MetaCyc:PWY-5274]


sulphide oxidation, using sulfur dioxygenase

sulfide oxidation, using sulfur dioxygenase

A sulfide oxidation process that proceeds via the reaction catalyzed by sulfur dioxygenase. [MetaCyc:PWY-5285]


Catalysis of the reaction: hydrogen sulfide + a quinone = S0 + a hydroquinone. [MetaCyc:R17-RXN]


flavocytochrome c sulfide dehydrogenase activity

Catalysis of the reaction: hydrogen sulfide + oxidized cytochrome c = S + reduced cytochrome c. [RHEA:30223]


hydrogen sulfide:ferric ion oxidoreductase

sulfur:ferric ion oxidoreductase activity

Catalysis of the reaction: a perthiol + 4 Fe3+ + 3 H2O = sulfite + a thiol + 4 Fe2+ + 8 H+. [MetaCyc:SULFFEOXIDO-RXN]


regulation of lymphocyte apoptotic process

Any process that modulates the occurrence or rate of lymphocyte death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


programmed cell death of T cells by apoptosis

Any apoptotic process in a T cell, a type of lymphocyte whose defining characteristic is the expression of a T cell receptor complex. [CL:0000084, GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


regulation of programmed cell death of T cells by apoptosis

Any process that modulates the occurrence or rate of T cell death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


negative regulation of T lymphocyte apoptosis

negative regulation of T-lymphocyte apoptosis

negative regulation of programmed cell death of T cells by apoptosis

negative regulation of T cell apoptotic process

Any process that stops, prevents, or reduces the frequency, rate or extent of T cell death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


positive regulation of T lymphocyte apoptosis

positive regulation of programmed cell death of T cells by apoptosis

positive regulation of T-lymphocyte apoptosis

positive regulation of T cell apoptotic process

Any process that activates or increases the frequency, rate or extent of T cell death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


regulation of activation-induced cell death of T-cells

regulation of activation-induced cell death of T lymphocytes

regulation of activation-induced cell death of T-lymphocytes

regulation of activation-induced cell death of T cells

Any process that modulates the occurrence or rate of activation-induced cell death of T cells. [GOC:add, ISBN:0781765196]


regulation of activated T cell apoptosis


regulation of activation-induced cell death


downregulation of activation-induced cell death of T cells

negative regulation of activation-induced cell death of T-lymphocytes

negative regulation of activation-induced cell death of T lymphocytes

down-regulation of activation-induced cell death of T cells

negative regulation of activation-induced cell death of T-cells

down regulation of activation-induced cell death of T cells

negative regulation of activation-induced cell death of T cells

Any process that stops, prevents, or reduces the frequency, rate or extent of activation-induced cell death of T cells. [GOC:add, ISBN:0781765196]


inhibition of activation-induced cell death of T cells


negative regulation of activated T cell apoptosis


negative regulation of activation-induced cell death


negative regulation of antigen-driven apoptosis


up-regulation of activation-induced cell death of T cells

upregulation of activation-induced cell death of T cells

positive regulation of activation-induced cell death of T-lymphocytes

positive regulation of activation-induced cell death of T-cells

up regulation of activation-induced cell death of T cells

positive regulation of activation-induced cell death of T lymphocytes

positive regulation of activation-induced cell death of T cells

Any process that activates or increases the frequency, rate or extent of activation-induced cell death of T cells. [GOC:add, ISBN:0781765196]


activation of activation-induced cell death of T cells


positive regulation of activated T cell apoptosis


positive regulation of activation-induced cell death


positive regulation of antigen-driven apoptosis


stimulation of activation-induced cell death of T cells


regulation of activated T lymphocyte autonomous cell death

regulation of activated T-cell autonomous cell death

regulation of activated T-lymphocyte autonomous cell death

regulation of activated T cell autonomous cell death

Any process that modulates the occurrence or rate of activated T cell autonomous cell death. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


regulation of activated cell autonomous cell death


negative regulation of activated T lymphocyte autonomous cell death

down-regulation of activated T cell autonomous cell death

negative regulation of activated T-cell autonomous cell death

negative regulation of activated T-lymphocyte autonomous cell death

downregulation of activated T cell autonomous cell death

down regulation of activated T cell autonomous cell death

negative regulation of activated T cell autonomous cell death

Any process that stops, prevents, or reduces the frequency, rate or extent of activated T cell autonomous cell death. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


inhibition of activated T cell autonomous cell death


negative regulation of activated cell autonomous cell death


upregulation of activated T cell autonomous cell death

up regulation of activated T cell autonomous cell death

positive regulation of activated T-cell autonomous cell death

positive regulation of activated T-lymphocyte autonomous cell death

up-regulation of activated T cell autonomous cell death

positive regulation of activated T lymphocyte autonomous cell death

positive regulation of activated T cell autonomous cell death

Any process that activates or increases the frequency, rate or extent of activated T cell autonomous cell death. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


activation of activated T cell autonomous cell death


positive regulation of activated cell autonomous cell death


stimulation of activated T cell autonomous cell death


Any apoptotic process in a thymocyte, an immature T cell located in the thymus. [CL:0000893, GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


regulation of thymocyte apoptotic process

Any process that modulates the occurrence or rate of thymocyte death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


negative regulation of immature T cell apoptosis


positive regulation of immature T cell apoptosis

positive regulation of thymocyte apoptosis

positive regulation of thymocyte apoptotic process

Any process that activates or increases the frequency, rate or extent of thymocyte death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


NK cell apoptosis
natural killer cell apoptosis

Any apoptotic process in a natural killer cell, a lymphocyte that can spontaneously kill a variety of target cells without prior antigenic activation. [CL:0000623, GOC:add, GOC:mtg_apoptosis, PMID:15728472]


regulation of natural killer cell apoptosis

regulation of natural killer cell apoptotic process

Any process that modulates the occurrence or rate of natural killer cell death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


down regulation of natural killer cell apoptosis

downregulation of natural killer cell apoptosis

negative regulation of NK cell apoptosis

down-regulation of natural killer cell apoptosis

negative regulation of natural killer cell apoptosis

negative regulation of natural killer cell apoptotic process

Any process that stops, prevents, or reduces the frequency, rate or extent of natural killer cell death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


inhibition of natural killer cell apoptosis


upregulation of natural killer cell apoptosis

positive regulation of natural killer cell apoptosis

up regulation of natural killer cell apoptosis

up-regulation of natural killer cell apoptosis

positive regulation of NK cell apoptosis

positive regulation of natural killer cell apoptotic process

Any process that activates or increases the frequency, rate or extent of natural killer cell death by apoptotic process. [GOC:add, GOC:mtg_apoptosis, ISBN:0781765196]


stimulation of natural killer cell apoptosis

activation of natural killer cell apoptosis


The portion of the plasma membrane surrounding a mating projection, the projection formed by unicellular fungi in response to mating pheromone. [GOC:jp]


pristanate:CoA ligase (AMP-forming)
pristanoyl-CoA ligase activity

Catalysis of the reaction: ATP + pristanate + CoA = AMP + diphosphate + pristanoyl-CoA. [GOC:pde, PMID:10198260]


The actin filament-based process in which cytoplasmic actin filaments slide past one another resulting in contraction of all or part of the cell body. [GOC:mah]


The regulated release of somatostatin from secretory granules in the D cells of the pancreas. [GOC:mah]


The regulated release of mucus by the mucosa. Mucus is a viscous slimy secretion consisting of mucins and various inorganic salts dissolved in water, with suspended epithelial cells and leukocytes. The mucosa, or mucous membrane, is the membrane covered with epithelium that lines the tubular organs of the body. Mucins are carbohydrate-rich glycoproteins that have a lubricating and protective function. [GOC:add, ISBN:068340007X, ISBN:0721662544]


Any process that modulates the frequency, rate or extent of the regulated release of mucus from a cell or a tissue. [GOC:add]


Any process that stops, prevents, or reduces the frequency, rate or extent of the regulated release of mucus from a cell or a tissue. [GOC:add]


Any process that activates or increases the frequency, rate or extent of the regulated release of mucus from a cell or a tissue. [GOC:add]


Catalysis of the hydrolysis of phosphotyrosyl groups formed as covalent intermediates (in DNA backbone breakage) between a DNA topoisomerase and DNA. [GOC:elh, PMID:16751265]


Catalysis of the hydrolysis of 5'-phosphotyrosyl groups formed as covalent intermediates (in DNA backbone breakage) between DNA topoisomerase II and DNA. [PMID:16751265]


The removal of phosphoric residues from peptidyl-O-phospho-L-serine to form peptidyl-serine. [GOC:bf]


The side of the fungal-type cell wall that is opposite to the side that faces the cell and its contents. [GOC:mah]


transcription factor TFIIIE complex location

A transcription factor complex that is involved in regulating transcription from RNA polymerase III (Pol III) promoters. TFIIIE contains a specific subset of ribosomal proteins. [GOC:jp, PMID:19116144]


A programmed necrotic cell death process which begins when a cell receives a signal (e.g. a ligand binding to a death receptor or to a Toll-like receptor), and proceeds through a series of biochemical events (signaling pathways), characterized by activation of receptor-interacting serine/threonine-protein kinase 1 and/or 3 (RIPK1/3, also called RIP1/3) and by critical dependence on mixed lineage kinase domain-like (MLKL), and which typically lead to common morphological features of necrotic cell death. The process ends when the cell has died. The process is divided into a signaling phase, and an execution phase, which is triggered by the former. [GOC:BHF, GOC:dph, GOC:mah, GOC:mtg_apoptosis, GOC:tb, PMID:18846107, PMID:20823910, PMID:21737330, PMID:21760595, PMID:21876153]


A type of programmed cell death that occurs in the epidermis, morphologically and biochemically distinct from apoptosis. It leads to the formation of corneocytes, i.e. dead keratinocytes containing an amalgam of specific proteins (e.g., keratin, loricrin, SPR and involucrin) and lipids (e.g., fatty acids and ceramides), which are necessary for the function of the cornified skin layer (mechanical resistance, elasticity, water repellence and structural stability). [GOC:krc, PMID:18846107]


A caspase-1-dependent cell death subroutine that is associated with the generation of pyrogenic mediators such as IL-1beta and IL-18. [GOC:mtg_apoptosis, PMID:18846107, PMID:21760595]


Binding to phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position. [GOC:bf, GOC:mah]


pre-mRNA retention and splicing complex location

A protein complex that is required for efficient splicing, and prevents leakage of unspliced pre-mRNAs from the nucleus (named for pre-mRNA REtention and Splicing). In Saccharomyces, the complex consists of Ist3p, Bud13p, and Pml1p. [PMID:15565172, PMID:18809678, PMID:19010333, PMID:19033360]


aerobic ammonia oxidation to nitrite via pyruvic oxime

The metabolic process in which ammonia (NH3) is oxidized to nitrite (NO2) in the presence of oxygen. Hydroxylamine is produced enzymatically, and, in the presence of pyruvate, forms pyruvic oxime in a spontaneous, non-enzymatic reaction; pyruvic oxime is then converted to nitrite. [MetaCyc:PWY-2242]


The chemical reactions and pathways involving any halogen, elements of Group VII; includes metabolism of halogen-containing compounds. [GOC:mah]


The chemical reactions and pathways by which iodide is converted to diiodine, with the concomitant loss of electrons. [GOC:mah, MetaCyc:IODIDE-PEROXIDASE-RXN]


extracellular matrix constituent secretion

The controlled release of molecules that form the extracellular matrix, including carbohydrates and glycoproteins by a cell. [GOC:mah]


Binding to a vitamin B6 compound: pyridoxal, pyridoxamine, pyridoxine, or the active form, pyridoxal phosphate. [GOC:mah]


Binding to pyridoxal, 3-hydroxy-5-(hydroxymethyl)-2-methylpyridine-4-carbaldehyde, a form of vitamin B6. [CHEBI:17310, GOC:mah]


Binding to pyridoxamine, 4-(aminomethyl)-5-(hydroxymethyl)-2-methylpyridin-3-ol, a form of vitamin B6. [CHEBI:16410, GOC:mah]


Binding to pyridoxine, 4,5-bis(hydroxymethyl)-2-methylpyridin-3-ol, a form of vitamin B6. [CHEBI:16709, GOC:mah]


4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity

Catalysis of the reaction: 5-aminoimidazole ribonucleotide + S-adenosylmethionine = 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate + 5'deoxyadenosine. [PMID:18953358]


The process whose specific outcome is the progression of a pigment cell over time, from its formation to the mature structure. Cell development does not include the steps involved in committing a cell to a pigment cell fate. [GOC:cvs]


The aggregation, arrangement and bonding together of a set of components to form an axonemal dynein complex, a dynein complex found in eukaryotic cilia and flagella, in which the motor domain heads interact with adjacent microtubules to generate a sliding force which is converted to a bending motion. [GOC:cilia, GOC:mah, PMID:19052621]


Combining with ferritin, and delivering ferritin into the cell via endocytosis. [GOC:bf, PMID:17459943, PMID:19154717]


A protein complex that binds iron and acts as a major iron storage system. Intracellular and extracellular ferritin complexes have different ratios of two types of ferritin monomer, the L (light) chain and H (heavy) chain. [GOC:mah, PMID:19154717]


A ferritin complex located in the extracellular region. Extracellular ferritin complexes contain L (light) chains but few or no H (heavy) chains. [GOC:mah, PMID:19154717]


N-acyl-phosphatidylethanolamine-specific phospholipase D activity

N-acylphosphatidylethanolamine-specific phospholipase D activity

Catalysis of the release of N-acylethanolamine from N-acyl-phosphatidylethanolamine (NAPE) to generate N-acylethanolamine (NAE). [GOC:elh, PMID:14634025, PMID:15878693]


NAE metabolism
N-acylethanolamine metabolism
NAE metabolic process

The chemical reactions and pathways involving N-acylethanolamines. An N-acylethanolamine is an ethanolamine substituted at nitrogen by an acyl group. [CHEBI:52640, GOC:elh, PMID:14634025, PMID:15878693]


The chemical reactions and pathways involving N-acylphosphatidylethanolamines. An N-acylphosphatidylethanolamine is a phosphatidylethanolamine substituted at nitrogen by an acyl group. [GOC:elh, GOC:mah, PMID:14634025, PMID:15878693]


A renal system process in which water, ions, glucose and proteins are taken up from the collecting ducts, glomerulus and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures (e.g. protein absorption is observed in nephrocytes in Drosophila, see PMID:23264686). [GOC:dph, GOC:mah, GOC:yaf]


renal sodium ion reabsorption
nephron sodium ion absorption

A renal system process in which sodium ions are taken up from the collecting ducts and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures. [GOC:dph, GOC:mah]


nephron water absorption
renal water reabsorption

A renal system process in which water is taken up from the collecting ducts and proximal and distal loops of the nephron. In non-mammalian species, absorption may occur in related structures. [GOC:dph, GOC:mah]


sarcoplasmic reticulum calcium ion transport

The directed movement of calcium ions (Ca2+) into, out of or within the sarcoplasmic reticulum. [GOC:BHF, GOC:vk]


regulation of histidyl-aspartyl phosphorelay

regulation of two-component signal transduction system (phosphorelay)

regulation of phosphorelay signal transduction system

Any process that modulates the frequency, rate or extent of signal transduction via a phosphorelay signal transduction system. [GOC:mah]


negative regulation of histidyl-aspartyl phosphorelay

down-regulation of two-component signal transduction

down regulation of two-component signal transduction

downregulation of two-component signal transduction

negative regulation of two-component signal transduction system (phosphorelay)

negative regulation of phosphorelay signal transduction system

Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction via a phosphorelay signal transduction system. [GOC:mah]


inhibition of two-component signal transduction


positive regulation of histidyl-aspartyl phosphorelay

up regulation of two-component signal transduction

positive regulation of two-component signal transduction system (phosphorelay)

up-regulation of two-component signal transduction

upregulation of two-component signal transduction

positive regulation of phosphorelay signal transduction system

Any process that activates or increases the frequency, rate or extent of signal transduction via a phosphorelay signal transduction system. [GOC:mah]


stimulation of two-component signal transduction

activation of two-component signal transduction


Binding to phosphatidic acid, any of a class of glycerol phosphate in which both the remaining hydroxyl groups of the glycerol moiety are esterified with fatty acids. [CHEBI:16337, GOC:jp, ISBN:0198506732]


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 hydrogen peroxide (H2O2) stimulus. [CHEBI:16240, GOC:mah]


regulation of stress-activated protein kinase signaling pathway

regulation of stress-activated protein kinase signalling pathway

regulation of stress-activated protein kinase signaling cascade

Any process that modulates the frequency, rate or extent of signaling via a stress-activated protein kinase signaling cascade. [GOC:mah]


inhibition of stress-activated protein kinase signaling pathway


stimulation of stress-activated protein kinase signaling pathway

activation of stress-activated protein kinase signaling pathway


response to guanosine 3',5'-cyclophosphate

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 cGMP (cyclic GMP, guanosine 3',5'-cyclophosphate) stimulus. [GOC:sl]


The process in which a relatively unspecialized cell acquires specialized features of a lens fiber cell, any of the elongated, tightly packed cells that make up the bulk of the mature lens in the camera-type eye. The cytoplasm of a lens fiber cell is devoid of most intracellular organelles including the cell nucleus, and contains primarily crystallins, a group of water-soluble proteins expressed in vary large quantities. [GOC:mah, PMID:7693735]


The process whose specific outcome is the progression of a lens fiber cell over time, from its formation to the mature structure. Cell development does not include the steps involved in committing a cell to a lens fiber cell fate. A lens fiber cell is any of the elongated, tightly packed cells that make up the bulk of the mature lens in a camera-type eye. [GOC:mah, PMID:7693735]


The process in which the developmental fate of a cell becomes restricted such that it will develop into a lens fiber cell. A lens fiber cell is any of the elongated, tightly packed cells that make up the bulk of the mature lens in a camera-type eye. [GOC:mah, PMID:7693735]


lens fiber cell morphogenesis during differentiation

The process in which the structures of a lens fiber cell are generated and organized. This process occurs while the initially relatively unspecialized cell is acquiring the specialized features of a lens fiber cell. A lens fiber cell is any of the elongated, tightly packed cells that make up the bulk of the mature lens in a camera-type eye. [GOC:mah, PMID:7693735]


A protein complex that contains the protein kinase ATR and ATR-interacting protein (ATRIP) and binds single-stranded DNA; ssDNA binding affinity is increased in the presence of replication protein A. [GOC:mah, PMID:14724280]


nucleosomal methylation activator complex location

A protein complex that contains eight subunits in common with the SWI/SNF complex, plus the ATPase BRG1 (SMARCA4) and the histone methyltransferase CARM1; the complex is involved in regulating nuclear receptor-dependent transcription. [GOC:mah, PMID:14729568]


A nucleotide-excision repair complex formed by the association of the heterodimeric endonuclease XPF/ERCC4-ERCC1 (Rad1p and Rad10p in S. cerevisiae) with the RAD52 protein. [PMID:14734547]


A protein complex formed by the association of RGS6, a negative regulator of heterotrimeric G protein signaling, with the DMAP1-Dnmt1 transcriptional repressor complex; in the complex, RGS6 inhibits the transcriptional repressor activity of DMAP1. [GOC:mah, PMID:14734556]


stationary phase
G1 to G0 transition
G1/G0 transition

A cell cycle arrest process that results in arrest during G1 phase, whereupon the cell enters a specialized resting state known as G0 or quiescence. [GOC:mah, GOC:mtg_cell_cycle, ISBN:0815316194]


G1/G0 transition involved in cell differentiation

G1 to G0 transition involved in cell differentiation

A cell cycle arrest process that results in arrest during G1 phase, whereupon the cell enters G0 phase, in the context of cell differentiation. [GOC:mah, ISBN:0815316194]


A cell cycle process that modulates the rate or extent of the transition from the G0 quiescent state to the G1 phase. [GOC:mah]


positive regulation of G0 to G1 transition

A cell cycle process that activates or increases the rate or extent of the transition from the G0 quiescent state to the G1 phase. [GOC:mah]


inward rectifier potassium channel inhibitor activity

Binds to and stops, prevents, or reduces the activity of an inwardly rectifying potassium channel. [GOC:mah]


Binding to thyroxine (T4) or triiodothyronine (T3), tyrosine-based hormones produced by the thyroid gland. [GOC:rph]


very-low-density lipoprotein receptor binding

very-low-density lipoprotein particle receptor binding

Binding to a very-low-density lipoprotein receptor. [GOC:BHF, GOC:mah]


The directed movement of thyroid hormone into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:rph]


Any process involved in the maintenance of an internal steady state of triglyceride within an organism or cell. [GOC:BHF, GOC:mah]


The substitution of a selenium atom for a sulfur atom in a ribonucleotide in a tRNA molecule. [GOC:jsg, PMID:14594807]


A protein complex that contains the cell-surface protein CD20 and the Src family tyrosine kinases Lck and Fyn. [GOC:mah, PMID:7545683]


A protein complex that contains the cell-surface protein CD20 and the Src family tyrosine kinases Lck, Lyn and Fyn. [GOC:mah, PMID:7545683]


alpha6-beta4 integrin-Shc-Grb2 complex location

A protein complex that consists of an alpha6-beta4 integrin complex bound to the adaptor proteins Shc and Grb2. [PMID:7556090]


alpha6-beta4 integrin-laminin-332 complex location

alpha6-beta4 integrin-laminin 5 complex location

A protein complex that consists of an alpha6-beta4 integrin complex bound to laminin 5. [GOC:mah, PMID:7556090]


Binding to aspartate, the alpha-amino-acid anion of 2-aminobutanedioic acid that has formula C4H5NO4. [CHEBI:29995, GOC:mah]


Binding to a flap structure in DNA. A DNA flap structure is one in which a single-stranded length of DNA or RNA protrudes from a double-stranded DNA molecule. [GOC:mah, PMID:15189154]


Binding to a 3'-flap structure in DNA. A DNA flap structure is one in which a single-stranded 3'-end of DNA or RNA protrudes from a double-stranded DNA molecule. [GOC:mah, PMID:15189154]


Binding to a 5'-flap structure in DNA. A DNA flap structure is one in which a single-stranded 5'-end of DNA or RNA protrudes from a double-stranded DNA molecule. 5'-flap structures can be formed during DNA repair or lagging strand synthesis; in the latter case RNA flaps form from lagging strand RNA primers. [GOC:mah, PMID:15189154]


Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a bacterial lipopeptide stimulus. [GOC:add, PMID:12077222]


The series of events in which a bacterial lipopeptide stimulus is received by a cell and converted into a molecular signal. [GOC:add, PMID:12077222]


adipose cell proliferation
adipocyte proliferation

The multiplication or reproduction of fat cells by cell division, resulting in the expansion of their population. A fat cell is an animal connective tissue cell specialized for the synthesis and storage of fat. [GOC:mah, GOC:sl]


brown adipose cell proliferation
brown adipocyte proliferation

The multiplication or reproduction of brown fat cells by cell division, resulting in the expansion of their population. A brown fat cell is a fat cell found the thermogenic form of adipose tissue found in newborns of many species. [CL:0000449, GOC:mah, GOC:sl]


white adipose cell proliferation
white adipocyte proliferation

The multiplication or reproduction of white fat cells by cell division, resulting in the expansion of their population. [CL:0000448, GOC:mah, GOC:sl]


regulation of adipose cell proliferation

Any process that modulates the frequency, rate or extent of fat cell proliferation. [GOC:mah, GOC:sl]


down regulation of fat cell proliferation

negative regulation of adipocyte proliferation

downregulation of fat cell proliferation

negative regulation of adipose cell proliferation

down-regulation of fat cell proliferation

negative regulation of fat cell proliferation

Any process that stops or decreases the rate or extent of fat cell proliferation. [GOC:mah, GOC:sl]


positive regulation of adipose cell proliferation

positive regulation of adipocyte proliferation

positive regulation of fat cell proliferation

Any process that activates or increases the rate or extent of fat cell proliferation. [GOC:mah, GOC:sl]


regulation of brown adipose cell proliferation

regulation of brown adipocyte proliferation

regulation of brown fat cell proliferation

Any process that modulates the frequency, rate or extent of brown fat cell proliferation. [GOC:mah, GOC:sl]


down regulation of brown fat cell proliferation

negative regulation of brown adipocyte proliferation

downregulation of brown fat cell proliferation

down-regulation of brown fat cell proliferation

negative regulation of brown adipose cell proliferation

negative regulation of brown fat cell proliferation

Any process that stops or decreases the rate or extent of brown fat cell proliferation. [GOC:mah, GOC:sl]


inhibition of brown fat cell proliferation


upregulation of brown fat cell proliferation

positive regulation of brown adipocyte proliferation

up-regulation of brown fat cell proliferation

positive regulation of brown adipose cell proliferation

up regulation of brown fat cell proliferation

positive regulation of brown fat cell proliferation

Any process that activates or increases the rate or extent of brown fat cell proliferation. [GOC:mah, GOC:sl]


stimulation of brown fat cell proliferation

activation of brown fat cell proliferation


regulation of white adipose cell proliferation

regulation of white adipocyte proliferation

regulation of white fat cell proliferation

Any process that modulates the frequency, rate or extent of white fat cell proliferation. [GOC:mah, GOC:sl]


down regulation of white fat cell proliferation

negative regulation of white adipose cell proliferation

negative regulation of white adipocyte proliferation

down-regulation of white fat cell proliferation

downregulation of white fat cell proliferation

negative regulation of white fat cell proliferation

Any process that stops or decreases the rate or extent of white fat cell proliferation. [GOC:mah, GOC:sl]


inhibition of white fat cell proliferation


positive regulation of white adipose cell proliferation

up regulation of white fat cell proliferation

upregulation of white fat cell proliferation

up-regulation of white fat cell proliferation

positive regulation of white adipocyte proliferation

positive regulation of white fat cell proliferation

Any process that activates or increases the rate or extent of white fat cell proliferation. [GOC:mah, GOC:sl]


stimulation of white fat cell proliferation

activation of white fat cell proliferation


A protein complex that contains the zinc finger transcription factor GATA1, the LIM domain protein Lmo2 (RBTN2), the basic helix-loop-helix protein TAL1 and its binding partner TCF3. The complex is involved transcriptional regulation in hematopoiesis. [PMID:7568177]


A protein complex that contains the zinc finger transcription factor GATA2, the LIM domain protein Lmo2 (RBTN2), the basic helix-loop-helix protein TAL1 and its binding partner TCF3. The complex is involved transcriptional regulation in hematopoiesis. [PMID:7568177]


SNARE complex location (STX1a, STX1b, SNAP25, RAB3a, SYT1, VAMP2, CPLX2)

SNARE complex (STX1a, STX1b, SNAP25, RAB3a, SYT1, VAMP2, CPLX2)

synaptotagmin-synaptobrevin 2-SNAP-25-syntaxin-1a-syntaxin-1b-Rab3a-complexin II complex location

A SNARE complex that contains synaptotagmin, synaptobrevin 2 (VAMP2), SNAP-25, syntaxin 1a, syntaxin1b, Rab3a, and complexin II (or orthologs thereof). [PMID:7654227]


synaptotagmin-synaptobrevin 2-SNAP-25-syntaxin-1a-syntaxin-1b-Rab3a complex location

SNARE complex (STX1a, STX1b, SNAP25, RAB3a, SYT1, VAMP2)

SNARE complex location (STX1a, STX1b, SNAP25, RAB3a, SYT1, VAMP2)

A SNARE complex that contains synaptotagmin, synaptobrevin 2 (VAMP2), SNAP-25, syntaxin 1a, syntaxin1b, and Rab3a (or orthologs thereof). [PMID:7654227]


alphav-beta3 integrin-CD47 complex location

A protein complex that consists of an alphav-beta3 integrin complex bound to CD47 (also known as IAP). [PMID:2277087, PMID:7691831]


actin polymerization-dependent cell motility

A process involved in the controlled movement of a bacterial cell powered by the continuous polymerization of actin at one pole of the cell. [GOC:mah, PMID:15773977]


migration of symbiont within host by polymerization of host actin


The process in which a relatively unspecialized cell acquires the specialized features of a hepatocyte. A hepatocyte is specialized epithelial cell that is organized into interconnected plates called lobules, and is the main structural component of the liver. [CL:0000182, PMID:7588884]


regulation of liver cell differentiation

regulation of hepatocyte differentiation

Any process that modulates the frequency, rate or extent of hepatocyte differentiation. [GOC:mah, GOC:sl]


down-regulation of hepatocyte differentiation

down regulation of hepatocyte differentiation

negative regulation of liver cell differentiation

downregulation of hepatocyte differentiation

negative regulation of hepatocyte differentiation

Any process that stops or decreases the rate or extent of hepatocyte differentiation. [GOC:mah, GOC:sl]


inhibition of hepatocyte differentiation


up regulation of hepatocyte differentiation

upregulation of hepatocyte differentiation

positive regulation of liver cell differentiation

up-regulation of hepatocyte differentiation

positive regulation of hepatocyte differentiation

Any process that activates or increases the rate or extent of hepatocyte differentiation. [GOC:mah, GOC:sl]


stimulation of hepatocyte differentiation

activation of hepatocyte differentiation


beta-catenin-TCF4 complex
beta-catenin-TCF7L2 complex location
beta-catenin-TCF4 complex location

A protein complex that contains beta-catenin and TCF7L2 (TCF4), binds to the TCF DNA motif within a promoter element, and is involved in the regulation of WNT target gene transcription. [GOC:BHF, GOC:rl, PMID:9065401, PMID:9065402]


Any process that increases heat tolerance of a cell in response to high temperatures. [GOC:jp]


extracellular signal-regulated kinase 1/2 cascade

extracellular signal-regulated kinase 1/2 (ERK1/2) cascade

An intracellular protein kinase cascade containing at least ERK1 or ERK2 (MAPKs), a MEK (a MAPKK) and a MAP3K. The cascade may involve 4 different kinases, as it can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinase in the downstream tier to transmit a signal within a cell. [GOC:add, GOC:signaling, ISBN:0121245462, ISBN:0896039986, PMID:20811974, PMID:28903453]


regulation of ERK1 and ERK2 signaling pathway

regulation of ERK1 and ERK2 signalling pathway

Any process that modulates the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. [GOC:add, ISBN:0121245462, ISBN:0896039986]


negative regulation of ERK1 and ERK2 signaling pathway

down-regulation of ERK1 and ERK2 cascade

negative regulation of ERK1 and ERK2 signalling pathway

down regulation of ERK1 and ERK2 cascade

negative regulation of ERK1 and ERK2 cascade

Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. [GOC:add, ISBN:0121245462, ISBN:0896039986]


positive regulation of ERK1 and ERK2 signalling pathway

positive regulation of ERK1 and ERK2 signaling pathway

positive regulation of ERK1 and ERK2 cascade

Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the ERK1 and ERK2 cascade. [GOC:mah]


extracellular signal-regulated kinase 5 cascade

An intracellular protein kinase cascade containing at least ERK5 (also called BMK1; a MAPK), a MEK (a MAPKK) and a MAP3K. The cascade can also contain an additional tier: the upstream MAP4K. The kinases in each tier phosphorylate and activate the kinases in the downstream tier to transmit a signal within a cell. [GOC:add, GOC:signaling, ISBN:0896039986, PMID:16376520, PMID:16880823, PMID:20811974, PMID:28903453]


regulation of ERK5 signaling pathway
regulation of BMK1 cascade
regulation of BMK cascade
regulation of MAPK7 cascade
regulation of BMK signaling pathway
regulation of BMK signalling pathway

Any process that modulates the frequency, rate or extent of signal transduction mediated by the ERK5 cascade. [GOC:add, ISBN:0121245462, ISBN:0896039986]


negative regulation of BMK signalling pathway

negative regulation of BMK signaling pathway

negative regulation of ERK5 signaling pathway

Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the ERK5 cascade. [GOC:add, ISBN:0121245462, ISBN:0896039986]


positive regulation of BMK signaling pathway

positive regulation of ERK5 signaling pathway

positive regulation of BMK signalling pathway

Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the ERK5 cascade. [GOC:mah]


Binding to high mobility group box 1 (HMBGB1). [GOC:add, PMID:18431461]


high mobility group box 1 receptor activity

Combining with high mobility group box 1 (HMBGB1) and transmitting the signal from one side of the membrane to the other to initiate a change in cell activity. [GOC:add, GOC:signaling, PMID:18431461]


endosome-plasma membrane transport vesicle

endosome to plasma membrane constitutive secretory pathway transport vesicle

endosome to plasma membrane transport vesicle

A transport vesicle that mediates transport from the endosome to the plasma membrane, and fuses with the plasma membrane to deliver lipids and membrane proteins to the plasma membrane and to release various cargo molecules, such as proteins or hormones, by exocytosis. [GOC:kad, GOC:mah, PMID:10679016, PMID:12110576]


exocytic constitutive secretory pathway transport vesicle

A transport vesicle that mediates transport from an intracellular compartment to the plasma membrane, and fuses with the plasma membrane to release various cargo molecules, such as proteins or hormones, by exocytosis. [GOC:kad, GOC:mah]


The removal of an amino group from a cytosine residue in DNA, forming a uracil residue. [GOC:mah]


The process whose specific outcome is the progression of the Harderian gland over time, from its formation to the mature structure. The Harderian gland is an anterior orbital structure usually associated with the nictitating membrane, and produces and secretes a variety of substances to the eye, depending upon the species. [GOC:hjd, PMID:16856596, PMID:7559104]


A protein complex that contains beta-glucuronidase and the carboxyl esterase egasyn; formation of the complex causes beta-glucuronidase to be retained in the endoplasmic reticulum. [PMID:7744842]


procollagen-proline 4-dioxygenase complex location, alpha(I) type

procollagen-proline, 2-oxoglutarate-4-dioxygenase complex location, alpha(I) type

procollagen-proline, 2-oxoglutarate-4-dioxygenase complex, alpha(I) type

procollagen-proline 4-dioxygenase complex, alpha(I) type

A procollagen-proline 4-dioxygenase complex that contains alpha subunits of the type I isoform; its activity is readily inhibited by poly(L-proline). [PMID:14500733, PMID:7753822]


prolyl 4-hydroxylase complex location (alpha(I)-type)

prolyl 4-hydroxylase complex (alpha(I)-type)


procollagen-proline, 2-oxoglutarate-4-dioxygenase complex location, alpha(II) type

procollagen-proline, 2-oxoglutarate-4-dioxygenase complex, alpha(II) type

procollagen-proline 4-dioxygenase complex location, alpha(II) type

procollagen-proline 4-dioxygenase complex, alpha(II) type

A procollagen-proline 4-dioxygenase complex that contains alpha subunits of the type II isoform; its activity is inhibited by poly(L-proline) only at high concentrations. [PMID:14500733, PMID:7753822]


prolyl 4-hydroxylase complex location (alpha(II)-type)

prolyl 4-hydroxylase complex (alpha(II)-type)


procollagen-proline, 2-oxoglutarate-4-dioxygenase complex, alpha(III) type

procollagen-proline 4-dioxygenase complex location, alpha(III) type

procollagen-proline, 2-oxoglutarate-4-dioxygenase complex location, alpha(III) type

procollagen-proline 4-dioxygenase complex, alpha(III) type

A procollagen-proline 4-dioxygenase complex that contains alpha subunits of the type III isoform. [PMID:14500733]


prolyl 4-hydroxylase complex location (alpha(III)-type)

prolyl 4-hydroxylase complex (alpha(III)-type)


A protein complex that couples SAGA-dependent gene expression to mRNA export at the inner side of the nuclear pore complex (NPC). The TREX-2 complex is tethered to the inner side of the NPC via the nucleoporins Nup1 and Nup60; in S. cerevisiae it contains Sac3p, Thp1p, Sem1, Sus1p and Cdc31p. [GOC:dgf, GOC:mah, PMID:17786152, PMID:19289793, PMID:28334829]


Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a lipoteichoic acid stimulus; lipoteichoic acid is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. [GOC:add, PMID:14665680, PMID:16020688]


The series of events in which a lipoteichoic acid stimulus is received by a cell and converted into a molecular signal; lipoteichoic acid is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. [GOC:add, PMID:14665680, PMID:16020688]


teichoic acid breakdown
teichoic acid degradation
teichoic acid catabolism

The chemical reactions and pathways resulting in the breakdown of teichoic acid, which is a major component of the cell wall of Gram-positive bacteria and typically consists of a polymer of glycerol-phosphate or ribitol-phosphate to which are attached glycosyl and D-alanyl ester residues. [GOC:add, PMID:14665680]


lipoteichoic acid metabolism
LTA metabolic process

The chemical reactions and pathways involving lipoteichoic acid, which is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. [GOC:add, PMID:14665680, PMID:16020688]


lipoteichoic acid synthesis
lipoteichoic acid biosynthetic process
lipoteichoic acid anabolism
LTA biosynthetic process
lipoteichoic acid biosynthesis

The chemical reactions and pathways resulting in the formation of lipoteichoic acid, which is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. [GOC:add, PMID:14665680, PMID:16020688]


lipoteichoic acid breakdown
lipoteichoic acid catabolism
lipoteichoic acid degradation

The chemical reactions and pathways resulting in the breakdown of lipoteichoic acid, which is a major component of the cell wall of gram-positive bacteria and typically consists of a chain of glycerol-phosphate repeating units linked to a glycolipid anchor. [GOC:add, PMID:14665680]


wall teichoic acid metabolism
WTA metabolic process

The chemical reactions and pathways involving wall teichoic acid, which is a major component of the cell wall of Gram-positive bacteria and typically consists of a polymer of glycerol-phosphate or ribitol-phosphate to which are attached glycosyl and D-alanyl ester residues and which is covalently linked to peptidoglycan. [GOC:add, PMID:14665680, PMID:16020688]


wall teichoic acid biosynthesis
WTA biosynthetic process
wall teichoic acid formation
wall teichoic acid anabolism
wall teichoic acid synthesis

The chemical reactions and pathways resulting in the formation of wall teichoic acid, which is a major component of the cell wall of Gram-positive bacteria and typically consists of a polymer of glycerol-phosphate or ribitol-phosphate to which are attached glycosyl and D-alanyl ester residues and which is covalently linked to peptidoglycan. [GOC:add, PMID:14665680, PMID:16020688]


wall teichoic acid degradation
wall teichoic acid catabolism
wall teichoic acid breakdown

The chemical reactions and pathways resulting in the breakdown of wall teichoic acid, which is a major component of the cell wall of Gram-positive bacteria and typically consists of a polymer of glycerol-phosphate or ribitol-phosphate to which are attached glycosyl and D-alanyl ester residues and which is covalently linked to peptidoglycan. [GOC:add, PMID:14665680]


The formation of a D-alanyl ester of teichoic acid. Alanylation of teichoic acids modulates the properties of the bacterial cell wall and modulates the inflammatory properties of the teichoic acid. [GOC:add, PMID:14665680, PMID:16020688]


oxidized nicotinamide adenine dinucleotide phosphate binding

Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. [GOC:mah]


reduced nicotinamide adenine dinucleotide phosphate binding

Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions. [GOC:mah]


NAD+ binding
NAD (oxidized) binding
oxidized NAD binding

Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. [GOC:mah]

oxidized nicotinamide adenine dinucleotide binding


reduced nicotinamide adenine dinucleotide binding

Binding to the reduced form, NADH, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. [GOC:mah]


Binding to ammonium ions (NH4+). [CHEBI:28938, GOC:ecd]


Binding to glutamine, 2,5-diamino-5-oxopentanoic acid. [CHEBI:28300, GOC:ecd]


oxidation-dependent protein degradation
oxidation-dependent proteolysis
oxidized protein catabolic process
oxidation-dependent protein breakdown
oxidation-dependent protein catabolism

oxidation-dependent protein catabolic process

The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the oxidation of one or more amino acid residues in the protein. [GOC:mah]


The chemical reactions and pathways involving carbamoyl phosphate, an intermediate in the urea cycle and other nitrogen compound metabolic pathways. [CHEBI:17672, GOC:mah, GOC:rph]


carbamoyl phosphate anabolism
carbamoyl phosphate formation
carbamyl phosphate biosynthetic process
carbamoyl phosphate synthesis
carbamoyl phosphate biosynthesis

carbamoyl phosphate biosynthetic process

The chemical reactions and pathways resulting in the formation of carbamoyl phosphate, an intermediate in the urea cycle and other nitrogen compound metabolic pathways. [CHEBI:17672, GOC:mah, GOC:rph]


common mediator SMAD binding
common-partner SMAD binding
common-mediator SMAD binding
common partner SMAD binding

Binding to a common mediator SMAD signaling protein. [GOC:BHF, GOC:vk, PMID:19114992]


Binding to an inhibitory SMAD signaling protein. [GOC:BHF, GOC:vk, PMID:19114992]


pathway-restricted SMAD binding
pathway restricted SMAD binding
receptor regulated SMAD binding
receptor-regulated SMAD binding

Binding to a receptor-regulated SMAD signaling protein. [GOC:BHF, GOC:vk, PMID:19114992]


trehalose metabolic process involved in response to stress

trehalose metabolism in response to stress

The chemical reactions and pathways involving trehalose that occur as a result of a stimulus indicating the organism is under stress. [GOC:jp, GOC:mah, PMID:9797333]


trehalose metabolic process involved in response to heat stress

trehalose metabolism in response to heat stress

The chemical reactions and pathways involving trehalose that occur as a result of a heat stimulus, a temperature stimulus above the optimal temperature for that organism. [GOC:jp, GOC:mah, PMID:9797333]


trehalose metabolic process involved in response to cold stress

trehalose metabolism in response to cold stress

The chemical reactions and pathways involving trehalose that occur as a result of a cold stimulus, a temperature stimulus below the optimal temperature for that organism. [GOC:jp, GOC:mah, PMID:9797333]


trehalose metabolic process involved in response to water deprivation

trehalose metabolism in response to water deprivation

The chemical reactions and pathways involving trehalose that occur as a result of deprivation of water. [GOC:jp, GOC:mah, PMID:9797333]


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 cold stimulus, a temperature stimulus below the optimal temperature for that organism. [GOC:jp]


DNA-dependent protein kinase complex location

DNA-dependent protein kinase, DNA-end-binding complex location

A protein complex that is involved in the repair of DNA double-strand breaks and, in mammals, V(D)J recombination events. It consists of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs) and the DNA end-binding heterodimer Ku. [GOC:mah, PMID:10854421, PMID:12235392]


non-homologous end joining complex location

nonhomologous end joining complex location

A protein complex that plays a role in DNA double-strand break repair via nonhomologous end joining. Such complexes typically contain a specialized DNA ligase (e.g. Lig4 in eukaryotes) and one or more proteins that bind to DNA ends. [GOC:mah, PMID:17072889, PMID:17938628]


A nonhomologous end joining complex that contains one or more Ku monomers and one or more DNA ligase molecules from the LigC or LigD family, and mediates nonhomologous end joining in bacteria. [GOC:mah, PMID:17938628]


A protein complex that contains DNA ligase III and XRCC1, and is involved in base excision repair. [PMID:15141024, PMID:7760816]


G-protein beta/gamma-Raf-1 complex location

A protein complex formed by the association of the serine-threonine protein kinase Raf-1 with the beta and gamma subunits of a heterotrimeric G protein. [GOC:mah, PMID:7782277]


G protein complex location (GNG2, GNB2L1, RAF1)


nucleotide-binding oligomerization domain containing signalling pathway

nucleotide-binding oligomerization domain containing signaling pathway

The series of molecular signals initiated by the binding of a ligand (such as a bacterial peptidoglycan) to a cytoplasmic nucleotide-binding oligomerization domain containing (NOD) protein receptor, and ending with regulation of a downstream cellular process. [GOC:add, PMID:17944960, PMID:18585455]


regulation of nucleotide-binding oligomerization domain containing signalling pathway

regulation of nucleotide-binding oligomerization domain containing signaling pathway

Any process that modulates the frequency, rate, or extent of a nucleotide-binding oligomerization domain containing (NOD) pathway. [GOC:add]


negative regulation of NOD signaling pathway

negative regulation of nucleotide-binding oligomerization domain containing signalling pathway

negative regulation of nucleotide-binding oligomerization domain containing signaling pathway

Any process that stops, prevents, or reduces the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing (NOD) pathway. [GOC:add]


positive regulation of nucleotide-binding oligomerization domain containing signalling pathway

positive regulation of NOD signaling pathway

positive regulation of nucleotide-binding oligomerization domain containing signaling pathway

Any process that activates or increases the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing (NOD) pathway. [GOC:add]


nucleotide-binding oligomerization domain containing 1 signalling pathway

nucleotide-binding oligomerization domain containing 1 signaling pathway

The series of molecular signals initiated by the binding of a ligand (such as a bacterial peptidoglycan) to a cytoplasmic nucleotide-binding oligomerization domain containing 1 (NOD1) protein receptor, and ending with regulation of a downstream cellular process. [GOC:add, PMID:17944960, PMID:18585455]


regulation of nucleotide-binding oligomerization domain containing 1 signalling pathway

regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway

Any process that modulates the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 1 (NOD1) pathway. [GOC:add]


negative regulation of nucleotide-binding oligomerization domain containing 1 signalling pathway

negative regulation of NOD1 signaling pathway

negative regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway

Any process that stops, prevents, or reduces the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 1 (NOD1) pathway. [GOC:add]


positive regulation of NOD1 signaling pathway

positive regulation of nucleotide-binding oligomerization domain containing 1 signalling pathway

positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway

Any process that activates or increases the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 1 (NOD1) pathway. [GOC:add]


nucleotide-binding oligomerization domain containing 2 signalling pathway

nucleotide-binding oligomerization domain containing 2 signaling pathway

The series of molecular signals initiated by the binding of a ligand (such as a bacterial peptidoglycan) to a cytoplasmic nucleotide-binding oligomerization domain containing 2 (NOD2) protein receptor, and ending with regulation of a downstream cellular process. [GOC:add, PMID:17944960, PMID:18585455]


regulation of nucleotide-binding oligomerization domain containing 2 signalling pathway

regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway

Any process that modulates the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 2 (NOD2) pathway. [GOC:add]


negative regulation of nucleotide-binding oligomerization domain containing 2 signalling pathway

negative regulation of NOD2 signaling pathway

negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway

Any process that stops, prevents, or reduces the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 2 (NOD2) pathway. [GOC:add]


positive regulation of nucleotide-binding oligomerization domain containing 2 signalling pathway

positive regulation of NOD2 signaling pathway

positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway

Any process that activates or increases the frequency, rate, or extent of the nucleotide-binding oligomerization domain containing 2 (NOD2) pathway. [GOC:add]


A protein complex that contains the epidermal growth factor receptor (EGFR) and the adaptor protein Shc, and is involved in linking EGFR activation to the p21-Ras pathway. [GOC:mah, PMID:7798267]


Shc-Egfr complex location, EGF stimulated


A protein complex that contains the epidermal growth factor receptor (EGFR) and Grb2, and is involved in linking EGFR activation to the p21-Ras pathway. [GOC:mah, PMID:7798267]


Grb2-Egfr complex location, EGF stimulated


A protein complex that contains Grb2 and the adaptor protein Shc, and is involved in linking epidermal growth factor receptor (EGFR) activation to the p21-Ras pathway. [GOC:mah, PMID:7798267]


Grb2-Shc complex location, EGF stimulated


A transcriptional repressor complex that contains a heterodimer of the bHLH-ZIP proteins Mad and Max, plus mSin3A, a homolog of the yeast Sin3p. [PMID:7889570]


A transcriptional repressor complex that contains a heterodimer of the bHLH-ZIP proteins Mad and Max, plus mSin3B, a homolog of the yeast Sin3p. [PMID:7889570]


G-protein beta/gamma-Btk complex location

A protein complex formed by the association of the Bruton tyrosine protein kinase Btk, which is implicated in mammalian X-linked immunodeficiencies, with the beta and gamma subunits of a heterotrimeric G protein. [GOC:mah, PMID:7972043]


G protein complex location (BTK, GNG1, GNG2)


G protein complex location (Btk, Gng2, Gnb1)


alphaIIb-beta3 integrin complex location

integrin alphaIIb-beta3 complex location

An integrin complex that comprises one alphaIIb subunit and one beta3 subunit. [PMID:12297042]


A transcriptional repressor complex that consists of a heterodimer of the bHLH-ZIP proteins Mad and Max. [PMID:8224841]


The multiplication or reproduction of oligodendrocyte progenitor cells by cell division, resulting in the expansion of their population. Oligodendrocyte progenitors give rise to oligodendrocytes, which form the insulating myelin sheath of axons in the central nervous system. [GOC:mah, GOC:sl, PMID:15504915]


regulation of oligodendrocyte precursor proliferation

regulation of oligodendrocyte progenitor proliferation

Any process that modulates the frequency, rate or extent of oligodendrocyte progenitor proliferation. [GOC:mah, GOC:sl]


negative regulation of oligodendrocyte precursor proliferation

negative regulation of oligodendrocyte progenitor proliferation

Any process that stops or decreases the rate or extent of oligodendrocyte progenitor proliferation. [GOC:mah, GOC:sl]


positive regulation of oligodendrocyte precursor proliferation

positive regulation of oligodendrocyte progenitor proliferation

Any process that activates or increases the rate or extent of oligodendrocyte progenitor proliferation. [GOC:mah, GOC:sl]


Catalysis of the reaction: S-adenosyl-L-methionine + laricitrin = S-adenosyl-L-homocysteine + syringetin. [RHEA:25633]


transcription factor B (SIII) complex location

transcription elongation factor SIII complex location

A transcription elongation factor complex that suppresses RNA polymerase II pausing, and may act by promoting proper alignment of the 3'-end of nascent transcripts with the polymerase catalytic site. Consists of a transcriptionally active Elongin A subunit (about 100 kDa) and two smaller Elongin B (about 18 kDa) and Elongin C (about 15 kDa) subunits. [PMID:12676794]


interleukin4-interleukin-4 receptor complex location

A protein complex that is formed by the association of a heterodimeric interleukin-4 receptor complex with an interleukin-4 molecule. [GOC:mah, PMID:10358772]


positive regulation of ergosterol biosynthesis

up regulation of ergosterol biosynthetic process

positive regulation of ergosterol anabolism

positive regulation of ergosterol formation

upregulation of ergosterol biosynthetic process

up-regulation of ergosterol biosynthetic process

positive regulation of ergosterol synthesis

positive regulation of ergosterol biosynthetic process

Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of ergosterol. [GOC:mah]


stimulation of ergosterol biosynthetic process

activation of ergosterol biosynthetic process


regulation of heme biosynthesis
regulation of haem biosynthetic process
regulation of haem biosynthesis
regulation of heme anabolism
regulation of heme synthesis
regulation of heme formation

Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of heme. [GOC:mah]


down-regulation of heme biosynthetic process

downregulation of heme biosynthetic process

down regulation of heme biosynthetic process

negative regulation of heme biosynthesis

negative regulation of haem biosynthetic process

negative regulation of heme biosynthetic process

Any process that decreases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of heme. [GOC:mah]


positive regulation of heme biosynthesis

positive regulation of haem biosynthetic process

upregulation of heme biosynthetic process

up regulation of heme biosynthetic process

up-regulation of heme biosynthetic process

positive regulation of heme biosynthetic process

Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of heme. [GOC:mah]


stimulation of heme biosynthetic process


Catalysis of the reaction: galactose-1-phosphate + H2O = galactose + phosphate. [GOC:mah]


Catalysis of the reaction: D-galactose-1-phosphate + H2O = D-galactose + phosphate. [GOC:mah, PMID:9462881]


cellular detoxification of nitrogenous compound

cellular detoxification of nitrogen compound

Any cellular process that reduces or removes the toxicity of nitrogenous compounds which are dangerous or toxic. This includes the aerobic conversion of toxic compounds to harmless substances. [GOC:mah]


The regulated release of prolactin, a peptide hormone that stimulates lactation, from secretory granules in the anterior pituitary. [GOC:mah, ISBN:0198506732]


thyroid stimulating hormone secretion
TSH secretion

The regulated release of thyroid-stimulating hormone, a peptide hormone that stimulates the activity of the thyroid gland, from secretory granules in the anterior pituitary. [GOC:mah, ISBN:0198506732]


SAGA family complex
SAGA family complex location
SAGA-type complex location

A histone acetyltransferase complex that acetylates nucleosomal histones H2B, H3, or H4 and is required for the expression of a subset of Pol II-transcribed genes. This complex includes the acetyltransferases GCN5/KAT2A or PCAF/KAT2B, several proteins of the ADA, SGF and SPT families, and several TBP-associate proteins (TAFs). [GOC:mah, PMID:10637607, PMID:17337012]


plus-end specific microtubule depolymerization

The removal of tubulin heterodimers from the plus end of a microtubule. [GOC:krc, PMID:16906145, PMID:16906148]


Catalysis of the reaction: ATP + H2O = ADP + phosphate. This reaction requires the presence of a tubulin dimer to accelerate release of ADP and phosphate. [GOC:mah, PMID:16906148]


alphav-beta3 integrin-collagen alpha3(VI) complex location

A protein complex that consists of an alphav-beta3 integrin complex bound to the alpha3 chain of type VI collagen; the integrin binds most strongly to unfolded collagen. [PMID:8387021]


alpha1-beta1 integrin-alpha3(VI) complex location

A protein complex that consists of an alpha1-beta1 integrin complex bound to a type VI collagen triple helix containing an alpha3(VI) chain. [PMID:8387021]


alpha2-beta1 integrin-alpha3(VI) complex location

A protein complex that consists of an alpha2-beta1 integrin complex bound to a type VI collagen triple helix containing an alpha3(VI) chain. [PMID:8387021]


RC-1 complex location (recombination complex 1)

A protein complex that contains DNA ligase III, DNA polymerase epsilon, a 5'-3' exonuclease, and the SMC1 and SMC2 proteins, and is involved in recombinational repair of deletions and gaps in DNA. [PMID:8392064, PMID:8670910]


plasma membrane electron transport chain

A respiratory chain located in the plasma membrane of a cell; made up of the protein complexes that form the electron transport system (the respiratory chain), associated with the plasma membrane. The respiratory chain complexes transfer electrons from an electron donor to an electron acceptor and are associated with a proton pump to create a transmembrane electrochemical gradient. [GOC:curators, GOC:imk, GOC:mah, ISBN:0198547684]


regulation of myometrial smooth muscle contraction

regulation of uterine smooth muscle contraction

Any process that modulates the frequency, rate or extent of uterine smooth muscle contraction. [GOC:go_curators]