pre-IC complex assembly involved in mitotic cell cycle

DNA replication preinitiation complex formation involved in mitotic cell cycle

mitotic DNA replication preinitiation complex assembly

Any DNA replication preinitiation complex assembly that is involved in mitotic cell cycle. [GO_REF:0000060, GOC:TermGenie]


DNA replication termination involved in meiotic DNA replication

Any DNA replication termination involved in meiotic cell cycle DNA replication. [GO_REF:0000060, GOC:TermGenie]


Any DNA replication termination involved in mitotic cell cycle DNA replication. [GO_REF:0000060, GOC:TermGenie]


synthesis of RNA primer involved in premeiotic DNA replication

Any synthesis of RNA primer involved in meiotic cell cycle DNA replication. [GO_REF:0000060, GOC:TermGenie]


synthesis of RNA primer involved in mitotic DNA replication

Any synthesis of RNA primer involved in mitotic cell cycle DNA replication. [GO_REF:0000060, GOC:TermGenie]


DNA strand elongation involved in premeiotic DNA replication

Any DNA strand elongation involved in meiotic cell cycle DNA replication. [GO_REF:0000060, GOC:TermGenie]


DNA strand elongation involved in mitotic DNA replication

Any DNA strand elongation involved in mitotic cell cycle DNA replication. [GO_REF:0000060, GOC:TermGenie]


nuclear pre-replicative complex assembly involved in meiotic cell cycle

pre-replicative complex assembly involved in premeiotic DNA replication

Any pre-replicative complex assembly involved in meiotic cell cycle DNA replication. [GO_REF:0000060, GOC:TermGenie]


pre-RC complex assembly involved in meiosis


pre-replicative complex assembly involved in meiosis


pre-replicative complex formation involved in meiosis


nuclear pre-replicative complex assembly involved in mitotic cell cycle

mitotic pre-replicative complex assembly

Any pre-replicative complex assembly involved in mitotic cell cycle DNA replication. [GO_REF:0000060, GOC:TermGenie]


regulation of lysine formation via aminoadipic acid

regulation of lysine biosynthetic process, aminoadipic acid pathway

regulation of lysine biosynthesis, aminoadipic pathway

regulation of lysine biosynthesis, aminoadipic acid pathway

regulation of lysine biosynthetic process, aminoadipic pathway

regulation of lysine anabolism via aminoadipic acid

regulation of lysine synthesis via aminoadipic acid

regulation of lysine biosynthetic process via aminoadipic acid

Any process that modulates the frequency, rate or extent of lysine biosynthetic process via aminoadipic acid. [GO_REF:0000058, GOC:TermGenie, PMID:8590464]


downregulation of lysine formation via aminoadipic acid

down-regulation of lysine formation via aminoadipic acid

down-regulation of lysine biosynthetic process via aminoadipic acid

downregulation of lysine biosynthetic process via aminoadipic acid

downregulation of lysine anabolism via aminoadipic acid

down regulation of lysine biosynthesis, aminoadipic pathway

negative regulation of lysine biosynthesis, aminoadipic acid pathway

down-regulation of lysine synthesis via aminoadipic acid

down regulation of lysine biosynthetic process, aminoadipic pathway

down regulation of lysine biosynthetic process, aminoadipic acid pathway

down regulation of lysine biosynthesis, aminoadipic acid pathway

down-regulation of lysine biosynthesis, aminoadipic acid pathway

downregulation of lysine synthesis via aminoadipic acid

down regulation of lysine formation via aminoadipic acid

negative regulation of lysine biosynthetic process, aminoadipic acid pathway

down regulation of lysine biosynthetic process via aminoadipic acid

down-regulation of lysine biosynthesis, aminoadipic pathway

down-regulation of lysine anabolism via aminoadipic acid

negative regulation of lysine anabolism via aminoadipic acid

down-regulation of lysine biosynthetic process, aminoadipic acid pathway

down regulation of lysine anabolism via aminoadipic acid

downregulation of lysine biosynthetic process, aminoadipic acid pathway

negative regulation of lysine biosynthetic process, aminoadipic pathway

downregulation of lysine biosynthetic process, aminoadipic pathway

down-regulation of lysine biosynthetic process, aminoadipic pathway

negative regulation of lysine synthesis via aminoadipic acid

negative regulation of lysine formation via aminoadipic acid

downregulation of lysine biosynthesis, aminoadipic acid pathway

down regulation of lysine synthesis via aminoadipic acid

negative regulation of lysine biosynthesis, aminoadipic pathway

downregulation of lysine biosynthesis, aminoadipic pathway

negative regulation of lysine biosynthetic process via aminoadipic acid

Any process that stops, prevents or reduces the frequency, rate or extent of lysine biosynthetic process via aminoadipic acid. [GO_REF:0000058, GOC:TermGenie, PMID:8590464]


inhibition of lysine anabolism via aminoadipic acid


inhibition of lysine biosynthesis, aminoadipic acid pathway


inhibition of lysine biosynthesis, aminoadipic pathway


inhibition of lysine biosynthetic process via aminoadipic acid


inhibition of lysine biosynthetic process, aminoadipic acid pathway


inhibition of lysine biosynthetic process, aminoadipic pathway


inhibition of lysine formation via aminoadipic acid


inhibition of lysine synthesis via aminoadipic acid


The aggregation, arrangement and bonding together of a set of components to form a neurofibrillary tangle. [GO_REF:0000079, GOC:sjp, GOC:TermGenie, PMID:15897157, PMID:22986780, PMID:24154541]


flame-shaped neurofibrillary tangle assembly


flame-shaped neurofibrillary tangle formation


star-shaped neurofibrillary tangle assembly


star-shaped neurofibrillary tangle formation


meiotic telomere maintenance via semi-conservative replication

Any telomere maintenance via semi-conservative replication that is involved in meiotic cell cycle. [GO_REF:0000060, GOC:TermGenie]


equal telomere replication involved in meiotic cell cycle


telomeric fork progression involved in meiotic cell cycle


telomeric replication fork progression involved in meiotic cell cycle


mitotic telomere maintenance via semi-conservative replication

Any telomere maintenance via semi-conservative replication that is involved in mitotic cell cycle. [GO_REF:0000060, GOC:TermGenie]


equal telomere replication involved in mitotic cell cycle


telomeric fork progression involved in mitotic cell cycle


telomeric replication fork progression involved in mitotic cell cycle


regulation of amyloid precursor protein breakdown

regulation of amyloid precursor protein catabolism

regulation of amyloid precursor protein degradation

regulation of amyloid precursor protein catabolic process

Any process that modulates the frequency, rate or extent of amyloid precursor protein catabolic process. [GO_REF:0000058, GOC:PARL, GOC:rl, GOC:TermGenie, PMID:24499793]


down regulation of APP catabolic process

negative regulation of amyloid precursor protein catabolism

down regulation of amyloid precursor protein breakdown

downregulation of amyloid precursor protein breakdown

negative regulation of amyloid precursor protein degradation

down-regulation of amyloid precursor protein catabolism

down regulation of amyloid precursor protein catabolic process

down regulation of amyloid precursor protein degradation

downregulation of amyloid precursor protein catabolism

down-regulation of APP catabolic process

down-regulation of amyloid precursor protein breakdown

negative regulation of amyloid precursor protein breakdown

downregulation of amyloid precursor protein catabolic process

down-regulation of amyloid precursor protein catabolic process

down-regulation of amyloid precursor protein degradation

negative regulation of APP catabolic process

down regulation of amyloid precursor protein catabolism

downregulation of amyloid precursor protein degradation

negative regulation of amyloid precursor protein catabolic process

Any process that stops, prevents or reduces the frequency, rate or extent of amyloid precursor protein catabolic process. [GO_REF:0000058, GOC:PARL, GOC:rl, GOC:TermGenie, PMID:24499793]


inhibition of amyloid precursor protein breakdown


inhibition of amyloid precursor protein catabolic process


inhibition of amyloid precursor protein catabolism


inhibition of amyloid precursor protein degradation


up-regulation of amyloid precursor protein degradation

upregulation of amyloid precursor protein degradation

upregulation of amyloid precursor protein catabolism

positive regulation of amyloid precursor protein catabolism

positive regulation of amyloid precursor protein degradation

up regulation of amyloid precursor protein catabolism

up-regulation of amyloid precursor protein catabolic process

positive regulation of amyloid precursor protein breakdown

up regulation of amyloid precursor protein breakdown

positive regulation of APP catabolic process

upregulation of amyloid precursor protein breakdown

upregulation of amyloid precursor protein catabolic process

up regulation of amyloid precursor protein catabolic process

up-regulation of amyloid precursor protein catabolism

up-regulation of amyloid precursor protein breakdown

up regulation of amyloid precursor protein degradation

positive regulation of amyloid precursor protein catabolic process

Any process that activates or increases the frequency, rate or extent of amyloid precursor protein catabolic process. [GO_REF:0000058, GOC:PARL, GOC:rl, GOC:TermGenie, PMID:24499793]


activation of amyloid precursor protein breakdown


activation of amyloid precursor protein catabolic process


activation of amyloid precursor protein catabolism


activation of amyloid precursor protein degradation


Any process that modulates the frequency, rate or extent of phospholipid efflux. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:12042316]


positive regulation of phospholipid export

positive regulation of phospholipid efflux

Any process that activates or increases the frequency, rate or extent of phospholipid efflux. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:12042316]


regulation of neurofibrillary tangle formation

regulation of neurofibrillary tangle assembly

Any process that modulates the frequency, rate or extent of neurofibrillary tangle assembly. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:15897157]


regulation of flame-shaped neurofibrillary tangle assembly


regulation of star-shaped neurofibrillary tangle assembly


regulation of star-shaped neurofibrillary tangle formation


down regulation of neurofibrillary tangle assembly

downregulation of neurofibrillary tangle assembly

down-regulation of neurofibrillary tangle assembly

downregulation of neurofibrillary tangle formation

down-regulation of neurofibrillary tangle formation

down regulation of neurofibrillary tangle formation

negative regulation of neurofibrillary tangle formation

negative regulation of neurofibrillary tangle assembly

Any process that stops, prevents or reduces the frequency, rate or extent of neurofibrillary tangle assembly. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:15897157]


down-regulation of flame-shaped neurofibrillary tangle assembly

down regulation of flame-shaped neurofibrillary tangle assembly


down-regulation of flame-shaped neurofibrillary tangle formation

down regulation of flame-shaped neurofibrillary tangle formation


down-regulation of star-shaped neurofibrillary tangle assembly

down regulation of star-shaped neurofibrillary tangle assembly


down-regulation of star-shaped neurofibrillary tangle formation

down regulation of star-shaped neurofibrillary tangle formation


downregulation of flame-shaped neurofibrillary tangle assembly


downregulation of flame-shaped neurofibrillary tangle formation


downregulation of star-shaped neurofibrillary tangle assembly


downregulation of star-shaped neurofibrillary tangle formation


inhibition of flame-shaped neurofibrillary tangle assembly


inhibition of flame-shaped neurofibrillary tangle formation


inhibition of neurofibrillary tangle assembly


inhibition of neurofibrillary tangle formation


inhibition of star-shaped neurofibrillary tangle assembly


inhibition of star-shaped neurofibrillary tangle formation


negative regulation of flame-shaped neurofibrillary tangle assembly


negative regulation of flame-shaped neurofibrillary tangle formation


negative regulation of star-shaped neurofibrillary tangle assembly


negative regulation of star-shaped neurofibrillary tangle formation


upregulation of neurofibrillary tangle assembly

up regulation of neurofibrillary tangle formation

up regulation of neurofibrillary tangle assembly

up-regulation of neurofibrillary tangle assembly

positive regulation of neurofibrillary tangle formation

upregulation of neurofibrillary tangle formation

up-regulation of neurofibrillary tangle formation

positive regulation of neurofibrillary tangle assembly

Any process that activates or increases the frequency, rate or extent of neurofibrillary tangle assembly. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:15897157]


activation of flame-shaped neurofibrillary tangle assembly


activation of flame-shaped neurofibrillary tangle formation


activation of neurofibrillary tangle assembly


activation of neurofibrillary tangle formation


activation of star-shaped neurofibrillary tangle assembly


activation of star-shaped neurofibrillary tangle formation


positive regulation of flame-shaped neurofibrillary tangle assembly


positive regulation of flame-shaped neurofibrillary tangle formation


positive regulation of star-shaped neurofibrillary tangle assembly


positive regulation of star-shaped neurofibrillary tangle formation


up-regulation of flame-shaped neurofibrillary tangle assembly

up regulation of flame-shaped neurofibrillary tangle assembly


up-regulation of flame-shaped neurofibrillary tangle formation

up regulation of flame-shaped neurofibrillary tangle formation


up-regulation of star-shaped neurofibrillary tangle assembly

up regulation of star-shaped neurofibrillary tangle assembly


up-regulation of star-shaped neurofibrillary tangle formation

up regulation of star-shaped neurofibrillary tangle formation


upregulation of flame-shaped neurofibrillary tangle assembly


upregulation of flame-shaped neurofibrillary tangle formation


upregulation of star-shaped neurofibrillary tangle assembly


upregulation of star-shaped neurofibrillary tangle formation


negative regulation of phospholipid export

negative regulation of phospholipid efflux

Any process that stops, prevents or reduces the frequency, rate or extent of phospholipid efflux. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:12042316]


regulation of lipid transport across blood brain barrier

regulation of lipid transport across blood-brain barrier

Any process that modulates the frequency, rate or extent of lipid transport across blood-brain barrier. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:24345162]


negative regulation of lipid transport across blood brain barrier

downregulation of lipid transport across blood brain barrier

down regulation of lipid transport across blood brain barrier

down-regulation of lipid transport across blood brain barrier

negative regulation of lipid transport across blood-brain barrier

Any process that stops, prevents or reduces the frequency, rate or extent of lipid transport across blood-brain barrier. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:24345162]


inhibition of lipid transport across blood brain barrier


upregulation of lipid transport across blood brain barrier

up-regulation of lipid transport across blood brain barrier

up regulation of lipid transport across blood brain barrier

positive regulation of lipid transport across blood brain barrier

positive regulation of lipid transport across blood-brain barrier

Any process that activates or increases the frequency, rate or extent of lipid transport across blood-brain barrier. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:24345162]


activation of lipid transport across blood brain barrier


upregulation of protein deubiquitinylation

upregulation of protein deubiquitylation

positive regulation of protein deubiquitinylation

up regulation of protein deubiquitination

up-regulation of protein deubiquitination

up regulation of protein deubiquitinylation

positive regulation of protein deubiquitylation

up-regulation of protein deubiquitylation

upregulation of protein deubiquitination

up regulation of protein deubiquitylation

up-regulation of protein deubiquitinylation

positive regulation of protein deubiquitination

Any process that activates or increases the frequency, rate or extent of protein deubiquitination. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22970133]


activation of protein deubiquitinylation


regulation of protein K63-linked deubiquitination

Any process that modulates the frequency, rate or extent of protein K63-linked deubiquitination. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22970133]


down-regulation of protein K63-linked deubiquitination

down regulation of protein K63-linked deubiquitination

downregulation of protein K63-linked deubiquitination

negative regulation of protein K63-linked deubiquitination

Any process that stops, prevents or reduces the frequency, rate or extent of protein K63-linked deubiquitination. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22970133]


inhibition of protein K63-linked deubiquitination


up-regulation of protein K63-linked deubiquitination

upregulation of protein K63-linked deubiquitination

up regulation of protein K63-linked deubiquitination

positive regulation of protein K63-linked deubiquitination

Any process that activates or increases the frequency, rate or extent of protein K63-linked deubiquitination. [GO_REF:0000058, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22970133]


activation of protein K63-linked deubiquitination


upregulation of Lys63-specific deubiquitinase activity

up regulation of Lys63-specific deubiquitinase activity

up-regulation of Lys63-specific deubiquitinase activity

positive regulation of Lys63-specific deubiquitinase activity

Any process that activates or increases the frequency, rate or extent of Lys63-specific deubiquitinase activity. [GO_REF:0000059, GOC:bf, GOC:PARL, GOC:TermGenie, PMID:22970133]


activation of Lys63-specific deubiquitinase activity


The disaggregation of an organelle into its constituent components. [GO_REF:0000079, GOC:TermGenie]


proteasome disassembly
proteasome degradation

The disaggregation of a proteasome complex into its constituent components. [GO_REF:0000079, GOC:TermGenie]


Any process that modulates the frequency, rate or extent of bone development. [GO_REF:0000058, GOC:mr, GOC:TermGenie, PMID:22510437]


downregulation of bone development
down regulation of bone development
down-regulation of bone development

Any process that stops, prevents or reduces the frequency, rate or extent of bone development. [GO_REF:0000058, GOC:mr, GOC:TermGenie, PMID:22510437]


up regulation of bone development
upregulation of bone development
up-regulation of bone development

Any process that activates or increases the frequency, rate or extent of bone development. [GO_REF:0000058, GOC:mr, GOC:TermGenie, PMID:22510437]


cellular response to 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one

cellular response to differentiation-inducing factor 1

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 1-(3,5-dichloro-2,6-dihydroxy-4-methoxyphenyl)hexan-1-one stimulus. [GO_REF:0000071, GOC:TermGenie, PMID:22365144]


regulation of acetylneuraminidase activity

regulation of acetylneuraminyl hydrolase activity

regulation of N-acylneuraminate glycohydrolase activity

regulation of alpha-neuraminidase activity

regulation of exo-alpha-sialidase activity

Any process that modulates the frequency, rate or extent of exo-alpha-sialidase activity. [GO_REF:0000059, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:23544079]


downregulation of acetylneuraminidase activity

downregulation of neuraminidase activity

down-regulation of acetylneuraminyl hydrolase activity

down-regulation of neuraminidase activity

negative regulation of sialidase activity

down-regulation of N-acylneuraminate glycohydrolase activity

downregulation of acetylneuraminyl hydrolase activity

downregulation of alpha-neuraminidase activity

down regulation of N-acylneuraminate glycohydrolase activity

negative regulation of acetylneuraminyl hydrolase activity

negative regulation of neuraminidase activity

down regulation of neuraminidase activity

down regulation of alpha-neuraminidase activity

downregulation of exo-alpha-sialidase activity

negative regulation of N-acylneuraminate glycohydrolase activity

downregulation of N-acylneuraminate glycohydrolase activity

negative regulation of acetylneuraminidase activity

down-regulation of alpha-neuraminidase activity

down-regulation of acetylneuraminidase activity

down regulation of exo-alpha-sialidase activity

down-regulation of exo-alpha-sialidase activity

down regulation of acetylneuraminyl hydrolase activity

negative regulation of alpha-neuraminidase activity

down regulation of acetylneuraminidase activity

negative regulation of exo-alpha-sialidase activity

Any process that stops, prevents or reduces the frequency, rate or extent of exo-alpha-sialidase activity. [GO_REF:0000059, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:23544079]


inhibition of acetylneuraminidase activity


inhibition of acetylneuraminyl hydrolase activity


inhibition of alpha-neuraminidase activity


inhibition of exo-alpha-sialidase activity


inhibition of N-acylneuraminate glycohydrolase activity


upregulation of N-acylneuraminate glycohydrolase activity

up regulation of acetylneuraminyl hydrolase activity

up regulation of N-acylneuraminate glycohydrolase activity

positive regulation of neuraminidase activity

up-regulation of acetylneuraminyl hydrolase activity

upregulation of acetylneuraminyl hydrolase activity

up-regulation of N-acylneuraminate glycohydrolase activity

positive regulation of N-acylneuraminate glycohydrolase activity

upregulation of acetylneuraminidase activity

up-regulation of acetylneuraminidase activity

positive regulation of acetylneuraminyl hydrolase activity

up-regulation of alpha-neuraminidase activity

up regulation of alpha-neuraminidase activity

positive regulation of alpha-neuraminidase activity

upregulation of alpha-neuraminidase activity

positive regulation of sialidase activity

upregulation of exo-alpha-sialidase activity

up regulation of acetylneuraminidase activity

up regulation of exo-alpha-sialidase activity

up-regulation of exo-alpha-sialidase activity

positive regulation of acetylneuraminidase activity

positive regulation of exo-alpha-sialidase activity

Any process that activates or increases the frequency, rate or extent of exo-alpha-sialidase activity. [GO_REF:0000059, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:23544079]


activation of acetylneuraminidase activity


activation of acetylneuraminyl hydrolase activity


activation of alpha-neuraminidase activity


activation of exo-alpha-sialidase activity


activation of N-acylneuraminate glycohydrolase activity


regulation of glycoprotein metabolic process

Any process that modulates the frequency, rate or extent of glycoprotein metabolic process. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:23544079]


down regulation of glycoprotein metabolic process

downregulation of glycoprotein metabolism

downregulation of glycoprotein metabolic process

down regulation of glycoprotein metabolism

negative regulation of glycoprotein metabolism

down-regulation of glycoprotein metabolism

down-regulation of glycoprotein metabolic process

negative regulation of glycoprotein metabolic process

Any process that stops, prevents or reduces the frequency, rate or extent of glycoprotein metabolic process. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:23544079]


inhibition of glycoprotein metabolic process


up regulation of glycoprotein metabolic process

up regulation of glycoprotein metabolism

up-regulation of glycoprotein metabolism

upregulation of glycoprotein metabolic process

positive regulation of glycoprotein metabolism

up-regulation of glycoprotein metabolic process

positive regulation of glycoprotein metabolic process

Any process that activates or increases the frequency, rate or extent of glycoprotein metabolic process. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:23544079]


activation of glycoprotein metabolic process


regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands

Any process that modulates the frequency, rate or extent of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands. [GO_REF:0000059, GOC:rb, GOC:TermGenie, PMID:12192046]


upregulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands

up regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands

up-regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands

positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands

Any process that activates or increases the frequency, rate or extent of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands. [GO_REF:0000059, GOC:rb, GOC:TermGenie, PMID:12192046]


activation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands


regulation of ascospore-type prospore membrane assembly

regulation of forespore membrane biosynthesis

regulation of forespore membrane formation

regulation of ascospore-type prospore membrane formation

Any process that modulates the frequency, rate or extent of formation of an ascospore-type prospore membrane. [GO_REF:0000058, GOC:TermGenie, PMID:11405625]


up regulation of forespore membrane biosynthesis

up regulation of ascospore-type prospore membrane assembly

positive regulation of forespore membrane biosynthesis

upregulation of ascospore-type prospore membrane assembly

positive regulation of ascospore-type prospore membrane assembly

up-regulation of ascospore-type prospore membrane assembly

up regulation of forespore membrane formation

upregulation of forespore membrane biosynthesis

upregulation of forespore membrane formation

up-regulation of forespore membrane formation

up-regulation of forespore membrane biosynthesis

positive regulation of forespore membrane formation

positive regulation of ascospore-type prospore membrane formation

Any process that activates or increases the frequency, rate or extent of formation of an ascospore-type prospore membrane. [GO_REF:0000058, GOC:TermGenie, PMID:11405625]


activation of ascospore-type prospore membrane assembly


activation of forespore membrane biosynthesis


activation of forespore membrane formation


regulation of RNA polymerase II regulatory region sequence-specific DNA binding

Any process that modulates the frequency, rate or extent of RNA polymerase II regulatory region sequence-specific DNA binding. [GO_REF:0000059, GOC:dph, GOC:krc, GOC:TermGenie, PMID:20026326]


downregulation of RNA polymerase II regulatory region sequence-specific DNA binding

down-regulation of RNA polymerase II regulatory region sequence-specific DNA binding

down regulation of RNA polymerase II regulatory region sequence-specific DNA binding

negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding

Any process that stops, prevents or reduces the frequency, rate or extent of RNA polymerase II regulatory region sequence-specific DNA binding. [GO_REF:0000059, GOC:dph, GOC:krc, GOC:TermGenie, PMID:20026326]


inhibition of RNA polymerase II regulatory region sequence-specific DNA binding


Any process that modulates the frequency, rate or extent of opsonization. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:22333221]


up-regulation of opsonization
up regulation of opsonization
upregulation of opsonization

Any process that activates or increases the frequency, rate or extent of opsonization. [GO_REF:0000058, GOC:BHF, GOC:rl, GOC:TermGenie, PMID:22333221]


regulation of microtubule plus-end binding

Any process that modulates the frequency, rate or extent of microtubule plus-end binding. [GO_REF:0000059, GOC:hjd, GOC:TermGenie, PMID:16148041]


downregulation of microtubule plus-end binding

down regulation of microtubule plus-end binding

down-regulation of microtubule plus-end binding

negative regulation of microtubule plus-end binding

Any process that stops, prevents or reduces the frequency, rate or extent of microtubule plus-end binding. [GO_REF:0000059, GOC:hjd, GOC:TermGenie, PMID:16148041]


inhibition of microtubule plus-end binding


up-regulation of microtubule plus-end binding

upregulation of microtubule plus-end binding

up regulation of microtubule plus-end binding

positive regulation of microtubule plus-end binding

Any process that activates or increases the frequency, rate or extent of microtubule plus-end binding. [GO_REF:0000059, GOC:hjd, GOC:TermGenie, PMID:16148041]


activation of microtubule plus-end binding


polyuridylation-dependent mRNA catabolic process

The chemical reactions and pathways resulting in the breakdown of a messenger RNA (mRNA) molecule, initiated by the enzymatic addition of a sequence of uridylyl residues (polyuridylation) at the 3' end of the target mRNA. [GOC:vw, PMID:23503588]


cell wall polysaccharide catabolic process involved in abscission

Any cell wall polysaccharide catabolic process that is involved in abscission. [GOC:TermGenie, PMID:23479623]


A protein complex that inhibits multiple events of replication initiation during one replication cycle. [GOC:bhm, PMID:21708944]


A tissue homeostatic process involved in the maintenance of an internal equilibrium within cartilage, including control of cellular proliferation and death and control of metabolic function. [GOC:hjd, PMID:21652695]


Combining with the biogenic amine 2-phenylethylamine to initiate a change in cell activity. [PMID:16878137]


Combining with the biogenic amine trimethylamine to initiate a change in cell activity. [PMID:16878137]


A protein complex that inhibits unwinding of DNA at the origin of replication and assembly of the pre-primosome. In E. coli, this complex is composed of DnaA and of the ribosomal protein L2. [GOC:bhm, PMID:21288885]


A protein complex that inactivates the function of DnaA by inhibiting the phosphorylation of DnaA-ADP to DnaA-ATP and thereby preventing multiple events of replication initiation. In E. coli, this complex is composed of DnaA and Hda. [GOC:bhm, PMID:21708944]


A protein complex that negatively regulates strand-opening at the origin of replication, thereby interfering with replication initiation. This complex is thought to be involved in the regulation of replication under oxidative stress conditions. In E. coli, this complex is composed of DnaA and Dps. [GOC:bhm, PMID:18284581]


Hda-dpo3b complex location
Hda-dpo3b complex
Hda-DnaN complex
Hda-DnaN complex location
Hda-beta clamp complex location

A protein complex involved in inactivating the function of DnaA and thereby preventing multiple events of replication initiation. In E. coli, this complex is composed of the beta clamp (DnaN) and Hda. [GOC:bhm, PMID:15150238]


Any apoptotic process in a lens fiber cell. Lens fiber cells are elongated, tightly packed cells that make up the bulk of the mature lens in a camera-type eye. [CL:0011004, GOC:hjd, PMID:11095619]


methanol-specific methylcobalamin:coenzyme M methyltransferase activity

methanol-specific methylcobalamin:CoM methyltransferase activity

methanol-specific methylcobalamin: coenzyme M methyltransferase activity

[methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase

Catalysis of the reaction: a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M = methyl-coenzyme M + a [Co(I) methanol-specific corrinoid protein] + H+. [GOC:hjd, PMID:10077852, RHEA:45208]


response to nerve growth factor stimulus

A 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 nerve growth factor stimulus. [PMID:22399805]


cellular response to nerve growth factor stimulus

A 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 nerve growth factor stimulus. [PMID:22399805, Wikipedia:Nerve_growth_factor]


The sodium-dependent hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds. [PMID:20460380]


The calcium-dependent hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds. [PMID:20460380]


positive regulation of transcription from RNA polymerase II promoter in response to reactive oxygen species

Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals. [GOC:kmv, PMID:16166371]


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

Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a superoxide stimulus. Superoxide is the anion, oxygen-, formed by addition of one electron to dioxygen (O2) or any compound containing the superoxide anion. [GOC:kmv, PMID:12869585, PMID:16166371]


A protein-DNA complex that contains an oligomer of SeqA bound to GATC sites in methylated or newly-synthesized, hemi-methylated double-stranded DNA, with preference for the latter. Binding of SeqA to hemimethylated DNA sequesters oriC, prevents re-methylation of DNA by Dam and in turn stops premature re-initiation of replication during one replication cycle. [GOC:bhm, PMID:12379844, PMID:15933720, PMID:23149570]


SeqA-hemimethylated DNA complex location


SeqA-hemimethylation dsDNA complex location


core primosome
core primosome complex location

A protein-DNA complex containing at least one DNA helicase and one primase. Can also contain associated proteins. The helicase component continues to unwind the double-stranded DNA (dsDNA) and the primase component synthesizes a RNA primer during initiation or restart of replication. [GOC:bhm, PMID:21856207]


pre-primosome complex location
preprimosome complex
preprimosome complex location
pre-priming complex location
prereplication complex location
pre-priming complex
prereplication complex
preprimosome
pre-primosome

Any of the protein-DNA complexes that contain a DNA helicase and associated protein(s) at the origin of replication, and build up to assembling the core primosome. The associated protein(s) chaperone the helicase to the DNA, and assembly of the pre-primosome is essential for the initiation or restart of replication. Pre-primosome complexes lack a primase component. [GOC:bhm, PMID:18179598, PMID:20129058, PMID:8663105]


A protein complex containing homohexameric DNA helicase DnaB, and the DNA helicase loader DnaC. The helicase loader DnaC delivers DnaB to the chromosomal origin (oriC). [GOC:bhm, PMID:20129058]


A protein-DNA complex containing the initiator protein DnaA bound to high-affinity recognition sites in the unique origin of replication, oriC. DnaA-oriC binding is the first step in assembly of a bacterial pre-replicative complex (pre-RC) and is responsible for the timely initiation of replication once per cell cycle. [GOC:bhm, PMID:19833870]


DnaA-DiaA-DNA complex
DnaA-DiaA-DNA complex location
DnaA-DiaA complex location

A protein-DNA complex containing a tetramer of DiaA attached to multiple DnaA molecule bound to oriC DNA. Regulates timely initiation of chromosomal replication during the cell cycle by stimulating assembly of DnaA-oriC complexes, conformational changes in ATP-DnaA initiation complexes, and unwinding of oriC duplex DNA. [GOC:bhm, PMID:15326179, PMID:17699754]


DnaA-HU complex location
DnaA-HU-DNA complex location
DnaA-HU-DNA complex

A protein-DNA complex containing DNA-bound DnaA attached to HU. HU is a dimer encoded by two closely related genes. Essential for the initiation of replication in bacteria; stimulates the DnaA-dependent unwinding of oriC. [GOC:bhm, PMID:18179598]


A protein-DNA complex that contains DNA in combination with a protein which binds to and bends DNA. Often plays a role in DNA compaction. [GOC:bhm, PMID:17097674]


histone-like DNA binding complex location


1-deoxy-D-xylulose 5-phosphate:thiol sulfurtransferase activity

Catalysis of the reaction: 1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-adenylate-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O. [EC:2.8.1.10, GOC:cjk, PMID:22031445, RHEA:26297]


A protein deubiquitination process in which a linear polymer of ubiquitin, formed by the amino-terminal methionine (M1) of one ubiquitin molecule and by the carboxy-terminal glycine (G76) of the next, is removed from a protein. [PMID:23708998]


The recognition and rejection of pollen of one species by cells in the stigma of another species. [PMID:21205670]


A proteasome specifically found in mammalian testis. Contains the proteasome activator PA200 in the regulatory particle, and beta1i, beta2i, beta5i and/or alpha4s in the core (20S) subunit. Beta1i, beta2i and beta5i are inducible catalytic subunits, closely related to beta1, beta2 and beta5. Alpha4s is a sperm-specific 20S subunit, but unlike other alternative 20S subunits alpha4s lies in the outer alpha-ring and lacks catalytic activity. [GOC:sp, PMID:23706739]


ribosome quality control complex location

ribosome-bound quality control complex location

A multiprotein complex that forms a stable complex with large ribosomal subunits (60S in eukaryotes and 50S in prokaryotes) containing stalled polypeptides and triggers their degradation (ribosomal quality control). In budding yeast, this complex includes Cdc48p, Rkr1p, Tae2p, Rqc1p, Npl4p and Ufd1p proteins. [GOC:rb, PMID:23178123, PMID:23232563]


DNA-directed RNA polymerase I complex assembly

The aggregation, arrangement and bonding together of a set of components to form the eukaryotic RNA polymerase I complex. [GOC:rb, PMID:23459708]


DNA-directed RNA polymerase II, core complex assembly

The aggregation, arrangement and bonding together of a set of components to form the eukaryotic RNA polymerase II core complex. [GOC:rb, PMID:23459708]


DNA-directed RNA polymerase III complex assembly

The aggregation, arrangement and bonding together of a set of components to form the eukaryotic RNA polymerase III complex. [GOC:rb, PMID:23459708]


B cell receptor extrinsic apoptotic signaling pathway

B cell receptor apoptotic signaling pathway

An extrinsic apoptotic signaling pathway initiated by the cross-linking of an antigen receptor on a B cell. [GOC:BHF, GOC:mtg_apoptosis, GOC:rl, PMID:15214043]


extrinsic apoptotic signaling pathway via B cell antigen receptor


extrinsic apoptotic signaling pathway via BCR


ATP-dependent RNA helicase inhibitor activity

Binds to and stops, prevents or reduces the activity of an RNA helicase. [GOC:rb, PMID:23721653]


mRNA-protein complex assembly
mRNP assembly
mRNP complex assembly

messenger ribonucleoprotein complex assembly

The aggregation, arrangement and bonding together of proteins and messenger RNA (mRNA) molecules to form a messenger ribonucleoprotein (mRNP) complex. [GOC:rb, PMID:23721653]


histone-like protein H-NS complex location

DNA-binding protein H-NS complex location

A multimer of H-NS proteins that is involved in bacterial nucleoid condensation and negative regulation of global gene expression by directly binding to promoter regions. Recognizes both structural and sequence-specific motifs in double-stranded DNA and has binding preference for bent DNA. [GOC:bhm, PMID:12592399]


L-leucine import into cell
L-leucine import across plasma membrane

The directed movement of L-leucine from outside of a cell, across the plasma membrane and into the cytosol. [GO_REF:0000075, GOC:TermGenie, PMID:23895341]


A homotetrameric protein complex consisting of a symmetrical pair of DiaA homodimers. Facilitates DnaA binding to the origin of replication during replication initiation. [GOC:bhm, PMID:17699754]


intrinsic apoptotic signaling pathway in response to osmotic stress by p53 class mediator

The series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of osmotic stress, and ends when the execution phase of apoptosis is triggered. [GOC:krc, GOC:mtg_apoptosis, PMID:16571598]


SEACIT complex
SEACIT complex location
IML1 complex location
IML1 complex
GATOR1 complex location

A GTPase-activating protein (GAP) complex that regulates TORC1 signaling by interacting with the Rag GTPase. In human, the GATOR1 complex consists of DEPDC5, NPRL2, and NPRL3. In S. cerevisiae, this complex is referred to as SEACIT and contains the Iml1p, Npr2p, and Npr3p proteins. [GOC:krc, GOC:rb, PMID:21900499, PMID:23723238, PMID:23974112, PMID:25934700, PMID:28199306, PMID:29199950]


A heterodimer GTPase complex. In S. cerevisiae, this complex contains Gtr1p and Gtr2p proteins. [GOC:rb, PMID:10388807, PMID:16143306]


molybdopterin cofactor (Moco) biosynthesis adenylyltransferase complex location

A heterodimeric protein complex which adenylates two molecules of the sulfur carrier subunit of the molybdopterin (MPT) cofactor synthase using ATP as part of molybdopterin cofactor (Moco) biosynthesis. In E. coli the subunits are MoeB and MoaD; Moco biosynthesis and its constituent molecules are evolutionarily conserved. [GOC:bhm, pmid:11713534, pmid:16669776]


epithelial cell apoptotic process involved in palatal shelf morphogenesis

An apoptotic process in a palatal shelf epithelial cell that contributes to the shaping of the palatal shelf. [GOC:dph, GOC:mtg_apoptosis, PMID:16607638]


Catalysis of the reaction: a flavonoid + 3'-phosphoadenosine-5'-phosphosulfate = sulfated flavonoid + adenosine-3',5'-diphosphate. This reaction is the transfer of a sulfate group to the hydroxyl group of a flavonoid acceptor, producing the sulfated flavonoid derivative. [PMID:23611783]


Catalysis of the reaction: linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate. [GOC:rph, RHEA:30291]


Catalysis of the reaction: R1H + R2OOH = R1OH + R2OH. [PMID:19467604]


neuronal cell projection extension
neuron protrusion extension
neuron process extension

Long distance growth of a single neuron projection involved in cellular development. A neuron projection is a prolongation or process extending from a nerve cell, e.g. an axon or dendrite. [GOC:BHF, GOC:rl, PMID:22790009]


protein localization to nuclear periphery

A process in which a protein is transported to, or maintained in, a location within the nuclear periphery. [GOC:mah, PMID:23703609]


A heterodimeric protein complex which catalyses sulfur transfer from the sulfur carrier subunit of MPT synthase to precursor Z to synthesize MPT as part of molybdopterin cofactor (Moco) biosynthesis. In E. coli the subunits are MoaE and MoaD; in human, MOCS2B and MOCS2A. Moco biosynthesis and its constituent molecules are evolutionarily conserved. [GOC:bhm, PMID:11135669, PMID:16669776, Reactome:R-HSA-947581]


molybdopterin cofactor (Moco) biosynthesis sulfurtransferase complex location


chromatin silencing at centromere outer repeat region


chromatin silencing at pericentric region


envenomation resulting in hemolysis in other organism

envenomation resulting in hemolysis in another organism

A process that begins with venom being forced into an organism by the bite or sting of another organism, and ends with hemolysis in the bitten organism. [PMID:21590705]


intrinsic apoptotic signaling pathway in response to hypoxia

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 hypoxia (lowered oxygen tension). Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. The pathway ends when the execution phase of apoptosis is triggered. [GOC:BHF, GOC:mtg_apoptosis, GOC:rl, PMID:20436456]


Suppression of the occurrence of translational errors, such as codon-anticodon mis-paring, during the process of translation of a protein using an mRNA template. [GOC:hjd, ISBN:9781936113460, PMID:21841312]


A process in which a protein is transported to, or maintained in, a location within a rhabdomere. [GOC:sart, PMID:8335687]


Binding to a talin, a family of related cytoskeletal proteins that play a role in assembly of actin filaments and migration of various cell types. [GOC:hjd, PMID:23372168]


glutamate dehydrogenase complex location

A homomeric protein complex that possesses glutamate dehydrogenase activity. This complex is evolutionarily conserved except that the number of homoprotomers per complex varies. [GOC:bhm, PMID:22393408, PMID:23412807]


dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)) complex location


glutamate dehydrogenase (NADP+) complex location


glutamic acid dehydrogenase complex location


L-glutamate dehydrogenase complex location


L-glutamate:NADP+ oxidoreductase (deaminating) complex location


L-glutamic acid dehydrogenase complex location


NAD(P)-glutamate dehydrogenase complex location


NAD(P)H-dependent glutamate dehydrogenase complex location


vascular endothelial growth factor A complex location

A homodimeric, extracellular protein complex containing two VEGF-A monomers. Binds to and activates a receptor tyrosine kinase. [GOC:bf, GOC:bhm, PMID:12207021, PMID:19658168]


A process in which a protein is transported to, or maintained in, a location at the cell tip. [PMID:22768263]


protein localization to telomeric heterochromatin

protein localisation to telomeric heterochromatin


maintenance of protein localisation to heterochromatin

maintenance of protein localization to heterochromatin

A process in which a protein is maintained in a location in telomeric heterochromatin. [PMID:21300781]


maintenance of protein location in heterochromatin


enzyme IIA-maltose transporter complex location

EIIA(Glc)-maltose transporter complex location

A protein complex consisting of the pentameric maltose transporter complex bound to two enzyme IIA (EIIA) molecules. EIIA is a component of the glucose-specific phosphotransferase system that inhibits maltose transport from the periplasm to the cytoplasm. When EIIA-bound, the maltose transporter remains in the open, inward-facing conformation, which prevents binding of maltose-loaded maltose binding protein (MBP) to the transporter. [GOC:bf, GOC:bhm, PMID:23770568]


maltose transporter inhibitor complex location


Dsc E3 ubiquitin ligase complex assembly

The aggregation, arrangement and bonding together of a set of components to form a Dsc E3 ubiquitin ligase complex, an E3 ubiquitin ligase complex localized to the ER and Golgi membrane. [GOC:mah, PMID:23760507]


A protein complex containing homohexameric DnaB helicase, and DnaG (a primase). Facilitates the unwinding of double-stranded DNA and the synthesis of RNA primer sequences during DNA replication and repair in Prokaryotes. [GOC:bhm, PMID:14557266]


A protein-DNA complex consisting of the helicase loading complex DnaB-DnaC bound to the DNA-bound DNA replication initiation protein DnaA. Essential for DNA replication initiation. [GOC:bhm, PMID:20129058]


A protein-DNA complex consisting of the helicase loading complex DnaB-DnaC, replication restart proteins DnaT, PriA and PriB, and associated DNA. Involved in the restart of DNA replication after a stalled replication fork has been repaired. [GOC:bhm, PMID:8663105]


A protein-DNA complex consisting of the helicase loading complex DnaB-DnaC, replication restart proteins DnaT, PriA and PriC, and associated DNA. Involved in the restart of DNA replication after a stalled replication fork has been repaired. [GOC:bhm, PMID:8663105]


DnaB-DnaC-Rep-PriC preprimosome
DnaB-DnaC-Rep-PriC complex location

A protein-DNA complex consisting of the helicase loading complex DnaB-DnaC, replication restart proteins Rep and PriC, and associated DNA. Involved in the restart of DNA replication after a stalled replication fork has been repaired. [GOC:bhm, PMID:19941825, PMID:8663105]


DnaB hexamer
DnaB helicase complex location

A homohexameric protein complex that possesses DNA helicase activity; functions during DNA replication and repair. [GOC:bhm, PMID:17947583]


histone deacetylase activity (H3-K4 specific)

Catalysis of the reaction: histone H3 N6-acetyl-L-lysine (position 4) + H2O = histone H3 L-lysine (position 4) + acetate. This reaction represents the removal of an acetyl group from lysine at position 4 of the histone H3 protein. [GOC:al, PMID:23771057, PMID:28450737]


ATP-dependent Holliday junction helicase activity


The modification of histone H2A by the addition of a phosphate group. [GOC:mah, PMID:23080121]


single-strand break-containing damaged DNA binding

single-strand break-containing DNA binding

Binding to damaged DNA containing single-strand breaks (SSBs). [GOC:al, PMID:21984210]


protein localisation to site of double-strand break

protein localization to double-strand break site

protein localization to site of double-strand break

Any process in which a protein is transported to, or maintained at, a region of a chromosome at which a DNA double-strand break has occurred. [GOC:mah, PMID:23080121]


A protein deubiquitination process in which a K27-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 27 of the ubiquitin monomers, is removed from a protein. [PMID:23827681]


A protein deubiquitination process in which a K33-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 33 of the ubiquitin monomers, is removed from a protein. [PMID:23827681]


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 disturbance in organismal or cellular homeostasis caused by a copper ion stimulus. [GOC:kmv, PMID:23437011]


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 disturbance in organismal or cellular homeostasis caused by a cadmium ion stimulus. [GOC:kmv]


SCF complex disassembly in response to cadmium stress

The disaggregation of the SCF ubiquitin ligase complex in response to cadmium stress. [GOC:rb, PMID:23000173]


G-protein coupled receptor catabolic process

G protein-coupled receptor catabolic process

The chemical reactions and pathways resulting in the breakdown of a G protein-coupled receptor. [PMID:12142540, PMID:23954414]


A process in which a protein is transported to, or maintained in, a location within the nucleoplasm. [GOC:mah, PMID:22918952]


phosphodiesterase decapping endonuclease activity

Catalysis of the removal of the cap from an unmethylated 5'-end capped RNA resulting in the release of the entire cap structure (GpppN) and a 5' monophosphorylated RNA. [GOC:dgf, PMID:20802481]


Binding to an EH domain of a protein. The EH stand for Eps15 homology. This was originally identified as a motif present in three copies at the NH2-termini of Eps15 and of the related molecule Eps15R. [GOC:hjd, PMID:11911876, PMID:21115825]


maltose transport complex location, core subunit

maltose transport MalFGK2 complex location

Protein complex involved in maltose transport through the plasma membrane. In E. coli, the complex is a tetramer and consists of a cytoplasmic ATPase MalK homodimer together with a heterodimeric transmembrane subunit MalF-MalG. [GOC:bhm, PMID:19250913]


IHF complex location
IHF-DNA complex location
IHFa-IHFb-DNA complex
IHF complex
IHFa-IHFb-DNA complex location

A protein-DNA complex containing IHF heterodimers (an alpha and a beta chain) bound to DNA. IHF binds to double-stranded DNA in a structure- and sequence-specific manner and bends the DNA into a nucleosome-like structure, the bacterial nucleoid. [GOC:bhm, PMID:17097674]


A protein-DNA complex that consists of HU heterodimers (an alpha and a beta chain) assembled into octamers along DNA. HU binds to double-stranded DNA in a structure- and sequence-specific manner and bends the DNA into a nucleosome-like structure. [GOC:bhm, PMID:17360520]


protein localisation to actomyosin contractile ring

protein localization to actomyosin contractile ring

A process in which a protein is transported to, or maintained at, the actomyosin contractile ring. [GOC:mah, PMID:23349808]


tRNA 3' processing in mitochondrion
tRNA 3'-end processing in mitochondria
tRNA 3' processing in mitochondria

The process in which the 3' end of a pre-tRNA molecule is converted to that of a mature tRNA in the mitochondrion. [GOC:mah, GOC:TermGenie, PMID:23928301]


acetyl-CoA biosynthetic process from pantothenate

The chemical reactions and pathways resulting in the formation of acetyl-CoA from pantothenate via phosphopantothenate and CoA. [GOC:mah, PMID:23091701]


extracellular vesicular exosome secretion

multi-vesicular body fusion with plasma membrane

The process whereby a membrane-bounded vesicle is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. [GOC:hjd, PMID:10572093, PMID:12154376, PMID:16773132, PMID:18617898]


lymphatic vascular process in circulatory system

A circulatory process that occurs at the level of the lymphatic vasculature. [PMID:21576390]


A heteromeric protein complex consisting of a multi-transmembrane spanning subunit (the light chain) and a type II glycoprotein subunit (the heavy chain) that functions to transport amino acids across a plasma membrane. [GOC:kmv, PMID:14668347]


regulation of lymphatic vascular permeability

Any process that modulates the extent to which lymphatic vessels can be pervaded by fluid. [PMID:23897233]


Any process that modulates the size of lymphatic vessels. [PMID:23897233]


regulation of collecting lymphatic vessel size


Binding to euchromatin, a dispersed and relatively uncompacted form of chromatin. [GOC:vw, PMID:22431512]


Catalysis of the reaction: acetyl-CoA + N-terminal L-serine in peptide = CoA + N-acetyl-L-serine-peptide. [GOC:al, PMID:23912279]


Catalysis of the reaction: acetyl-CoA + N-terminal L-glutamate in peptide = CoA + N-acetyl-L-glutamate-peptide. [GOC:al, PMID:23912279]


vitamin B12-transporting BtuCDF complex location

cobalamin-transporting BtuCDF complex location

Protein complex facilitating ATP-dependent cobalamin (vitamin B12) transport through inner cell membrane (periplasm to cytoplasm) in Gram-negative bacteria. In E. coli the system is composed of a periplasmic cobalamin-binding protein (BtuF), an integral membrane homodimer, BtuC, and a cytoplasmic ATP-binding homodimer BtuD. [GOC:bhm, PMID:22569249]


collecting lymphatic vessel constriction

A decrease in the diameter of collecting lymphatic vessels. [PMID:23322290]


vitamin B12 transport complex location, core subunit

vitamin B12 transport complex, core subunit

cobalamin transport complex location, core subunit

cobalamin transport complex, core subunit

Protein complex involved in cobalamin (vitamin B12) transport through the plasma membrane. In E. coli, the complex is a tetramer and consists of the cytoplasmic ATPase BtuD homodimer together with the transmembrane BtuC homodimer. [GOC:bhm, PMID:22569249]


The aggregation, arrangement and bonding together of proteins and RNA molecules to form a cytoplasmic U snRNP body. [PMID:19464282]


macrolide transmembrane transporter complex location

A bacterial transmembrane transporter complex that spans the entire cell membrane system and possesses ATP-dependent xenobiotic transport activity pumping drugs (typically antibiotics) and other toxins directly from the cytosol out of the bacterial cell. Typically, it is trimeric consisting of a inner membrane ATPase (IMP), a periplasmic membrane fusion protein (MFP) and an outer membrane factor (OMF). In E. coli, macrolide transporter complexes may consists of MacB (IMP), MacA (MFP) and TolC (OMF) or AcrB (IMP), AcrA (MFP) and TolC (OMF). Trimeric TolC is a common OMF found in many macrolide transporter complexes. [GOC:bhm, PMID:10879525, PMID:18955484, PMID:19254725]


macrolide transporter MacAB-TolC complex location

The MacAB-TolC complex is a macrolide transporter complex found in E.coli and related gram-negative bacteria. Its transport activity is specific to macrolide compounds containing 14- and 15-membered lactones. It consists of the dimeric inner membrane ATPase MacB, the hexameric, periplasmic membrane fusion protein MacA and the trimeric outer membrane factor TolC. [GOC:bhm, PMID:10879525, PMID:18955484, PMID:19254725]


ATP-dependent methionine-importing complex location

ATP-dependent methionine importing complex location

ATP-binding cassette (ABC) methionine importer complex location

methionine-importing ABC transporter complex location

ATP-dependent methionine importer complex location

An ATP-binding cassette (ABC) transporter complex that is capable of methionine-importing activity. An example is the bacterial MetNIQ methionine transporter, that consists of the dimeric ATPase subunit MetN located at the cytoplasmic side of the plasma membrane and the dimeric transmembrane subunit MetI. MetQ is regarded as the periplasmic methionine-binding chaperon subunit, and is capable of transporting methionine from the periplasm into the cytoplasm in an ATP-dependent manner. [GOC:bhm, PMID:22095702]


methionine transporter complex location, ATP-dependent

methionine transporter complex, ATP-dependent


A dimeric protein complex containing two ModE subunits. Binds directly to DNA to regulate transcription, and is involved in (positively and negatively) regulating various aspects of molybdenum metabolism. [GOC:bhm, PMID:12581638]


MsbA complex location
MsbA complex
MsbA dimer
MsbA transporter complex location

An ATP-binding cassette (ABC) transporter complex made up of a dimer of MsbA. Facilitates the export across the plasma membrane of, amongst others, lipid A and lipopolysaccharide. In contrast to most ABC transporter complexes, each chain of the homodimer contains both the transmembrane domain (TMD) and the cytoplasmic ATP-binding domain (NBD). [GOC:bhm, PMID:18024585]


A protein complex containing an alkanesulfonate monooxygenase subunit (SsuD tetramer in E.coli) and a flavin oxidoreductase subunit (SsuE dimer in E.coli). Involved in the utilization of alkanesulfonates as sulfur sources under conditions of sulfate or cysteine starvation. [GOC:bhm, PMID:16997955]


two-component alkanesulfonate monooxygenase system


alkanesulfonate monooxygenase complex location

A protein complex capable of alkanesulfonate monooxygenase activity. Involved in the utilization of alkanesulfonates as sulfur sources under conditions of sulfate or cysteine starvation, catalyzing the conversion of alkanesulfonates into aldehydes and sulfite. In E.coli the complex consists of a SsuD tetramer. [GOC:bhm, PMID:10480865, PMID:16997955]


FMN reductase complex location, NAD(P)H-dependent

FMN reductase complex, NAD(P)H-dependent

A protein complex capable of FMN reductase activity. Reduces FMN to FMNH2 in a NAD(P)H-dependent manner. In E.coli, consists of a SsuE dimer. [GOC:bhm, PMID:10480865, PMID:16997955]


flavin oxidoreductase complex location, NAD(P)H-dependent

flavin oxidoreductase complex, NAD(P)H-dependent


FMN oxidoreductase complex location, NAD(P)H-dependent

FMN oxidoreductase complex, NAD(P)H-dependent


A protein complex containing two transmembrane subunits; a MdtB dimer and one unit of MdtC. Capable of exporting substrates across the cell membrane. Involved in conferring antibiotic resistance of Gram-negative bacteria by transporting drugs across the membrane. [GOC:bhm, PMID:20038594]


oxidoreductase complex location
oxidation-reduction complex location
oxidation-reduction complex
redox complex
redox complex location

Any protein complex that possesses oxidoreductase activity. [GOC:bhm, PMID:18982432]


2-aminoethanesulfonate dioxygenase complex location

alpha-ketoglutarate-dependent taurine dioxygenase complex location

A protein complex capable of catalyzing the conversion of taurine and alpha-ketoglutarate to sulfite, aminoacetaldehyde and succinate under sulfur or cysteine starvation conditions. Its expression is repressed by the presence of sulfate or cysteine. In E. coli it is a homodimer or homotetramer of the protein TauD. [GOC:bhm, PMID:12741810]


jasmonyl-Ile conjugate hydrolase activity

Catalysis of the reaction: jasmonyl-Ile + H2O = jasmonic acid + L-isoleucine. [PMID:23943861]


EmrE multidrug transporter complex location

A transmembrane protein complex capable of transporting positively charged hydrophobic drugs across the plasma membrane thereby involved in conferring resistance to a wide range of toxic compounds (e.g. methyl viologen, ethidium bromide and acriflavine). It is commonly found in bacteria. In E. coli it forms a homodimer. [GOC:bhm, PMID:18024586]


positive regulation by symbiont of RNA levels in host

Any process in which an organism activates, maintains or increases the frequency, rate or extent of the RNA levels in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [PMID:12182338, PMID:18703740]


negative regulation by symbiont of RNA levels in host

Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of the RNA levels in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [GOC:ml, PMID:18703740]


positive regulation by symbiont of auxin levels in host

positive regulation by symbiont of IAA levels in host

positive regulation by symbiont of indole acetic acid levels in host

Any process in which an organism activates, maintains or increases the frequency, rate or extent of the indole acetic acid levels in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [GOC:ml, PMID:18056646]


positive regulation by symbiont of jasmonic acid levels in host

Any process in which an organism activates, maintains or increases the frequency, rate or extent of the jasmonic acid levels in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [GOC:ml, PMID:14617079, PMID:16553894]


positive regulation by symbiont of ethylene levels in host

Any process in which an organism activates, maintains or increases the frequency, rate or extent of the ethylene levels in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [GOC:ml, PMID:16167902]


negative regulation by symbiont of salicylic acid levels in host

Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of salicylic acid levels in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [GOC:ml, PMID:17722699, PMID:20565685]


negative regulation by symbiont of host intracellular transport

Any process in which an organism stops, prevents, or reduces the frequency, rate or extent of intracellular transport in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [PMID:22319451]


positive regulation by symbiont of host transcription

Any process in which an organism activates, maintains or increases the frequency, rate or extent of transcription in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [PMID:21994350]


negative regulation by symbiont of host phytoalexin production

suppression by symbiont of host phytoalexin production

Any process in which a symbiont stops, prevents, or reduces the frequency, rate or extent of phytoalexin production in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [PMID:21402357]


positive regulation by symbiont of abscisic acid levels in host

Any process in which an organism activates, maintains or increases the frequency, rate or extent of the abscisic acid levels in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [PMID:17304219]


Bacterial chaperonin complex consisting of a heptameric 10kDa chaperonin subunit GroES and a tetradecameric (2x7) 60kDa chaperonin subunit GroEL. The 60kDa subunit possesses ATPase activity while the holo-enzyme is responsible for the correct folding of proteins. [GOC:bhm, PMID:15313620]


bacterial chaperonin ATPase complex location


ATP-binding cassette (ABC) transporter complex ProVWX location

The ProVWX complex belongs to the family of ATP-binding cassette (ABC) transporter proteins complexes. It consists of a cytoplasmic ATPase subunit ProV, a transmembrane subunit ProW and a periplasmic binding protein ProX. It is capable of translocating a wide variety of solute (e.g. glycine betaine) across the plasma membrane and is activated under osmotic stress conditions. [GOC:bhm, PMID:23249124]


positive regulation by symbiont of cytokinin levels in host

Any process in which an organism activates, maintains or increases the frequency, rate or extent of the cytokinin levels in the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. [PMID:24124900]


beta-nicotinamide D-ribonucleotide phosphatase activity

nicotinamide mononucleotide phosphatase activity

Catalysis of the reaction: beta-nicotinamide D-ribonucleotide (NMN-) + H2O = beta-nicotinamide D-riboside (nicotinamide ribose, NmR) + phosphate. [GOC:rb, PMID:21349851, RHEA:30815]


Narrow, electron-dense part of the rhoptry that extends through the conoid at the apical tip of an apicomplexan parasite. The rhoptry neck serves as a duct through which the contents of the rhoptry are secreted after attachment to the host has been completed and at the commencement of invasion. [GOC:giardia, GOC:pr, PMID:23499754, PMID:23937520, PMID:24002067, PMID:24070999]


Binding to a histone methyltransferase enzyme. [GOC:ame, GOC:BHF, PMID:19486527]


paranodal axoglial junction maintenance
axoglial septate junction maintenance
paranodal septate maintenance

The maintenance of a paranodal junction, a highly specialized cell-cell junction found in vertebrates, which forms between a neuron and a glial cell, and has structural similarity to Drosophila septate junctions. A paranodal junction flanks the node of Ranvier in myelinated nerve, electrically isolates the myelinated from unmyelinated nerve segments, and physically separates the voltage-gated sodium channels at the node from the cluster of potassium channels underneath the myelin sheath. [GOC:pr, PMID:24011083]


sulfurtransferase complex location
sulfur transfer complex location
sulfur transfer complex

A protein complex capable of catalyzing the transfer of sulfur atoms from one compound (donor) to another (acceptor). [GOC:bhm, PMID:17350958]


iron-sulfur cluster assembly complex location

A protein complex capable of assembling an iron-sulfur (Fe-S) cluster. [GOC:bhm, PMID:17350958]


iron-sulfur cluster transfer complex location

A protein complex capable of catalyzing the transfer of an iron-sulfur (Fe-S) cluster from one compound (donor) to another (acceptor). [GOC:bhm, PMID:19810706]


stimulator of interferon genes complex location

A protein dimer containing two STING monomers. It binds cyclic purine di-nucleotides. Activation of the sting complex by 2',5'-3'-5'-cyclic GMP-AMP activates nuclear transcription factor kB (NF-kB) and interferon regulatory factor 3 (IRF3) which then induce transcription of the genes encoding type I IFN and cytokines active in the innate immune response. [GOC:bhm, PMID:22705373, PMID:23706668, PMID:23910378]


A protein complex capable of phosphomannomutase activity. [GOC:bhm, PMID:16540464]


intramolecular phosphotransferase complex location

A protein complex capable of catalyzing the transfer of a phosphate group from one position to another within a single molecule. [GOC:bhm, PMID:16540464]


A protein complex capable of catalyzing the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). [GOC:bhm, PMID:16540464]


diamine N-acetyltransferase complex location

A protein complex which is capable of diamine N-acetyltransferase activity. [GOC:bhm, PMID:8077207]


spermidine acetyltransferase complex location


proteasome core complex import into nucleus

The directed movement of the proteasome core complex (AKA core particle (CP)) from the cytoplasm into the nucleus. [GOC:dos, GOC:rb, PMID:23982732]


double-stranded DNA endodeoxyribonuclease activity

Catalysis of the hydrolysis of ester linkages within a double-stranded deoxyribonucleic acid molecule by creating internal breaks. [GOC:PG, PMID:22885404]


A heterodimeric transcription factor complex composed of the bZIP proteins atf1 and pcr1. The heterodimer binds m26 sites (homologous to CRE). [PMID:24224056]


histone threonine kinase activity (H2A-T120 specific)

histone kinase activity (H2A-T120 specific)

Catalysis of the transfer of a phosphate group to the threonine-120 residue of histone H2A. [PMID:24140421]


histone H2AT120 phosphorylation
histone H2A phosphorylation at T120

The modification of histone H2A by the addition of a phosphate group to a threonine residue at position 120 of the histone. [PMID:24140421]


mitochondrial uniporter complex location

mitochondrial uniporter holocomplex location

A calcium channel complex in the mitochondrial inner membrane capable of highly-selective calcium channel activity. Its components include the EF-hand-containing proteins mitochondrial calcium uptake 1 (MICU1) and MICU2, the pore-forming subunit mitochondrial calcium uniporter (MCU) and its paralog MCUb, and the MCU regulator EMRE. [PMID:24231807]


Binding to an RNA molecule modified by N6-methyladenosine (m6A), a modification present at internal sites of mRNAs and some non-coding RNAs. [PMID:22575960, PMID:24284625]


regulation of transcription from RNA polymerase II promoter in response to DNA damage

Any process that modulates the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of DNA damage. [PMID:15660129]


nucleotide-excision repair, DNA damage recognition complex location

A protein complex that is capable of identifying lesions in DNA, such as pyrimidine-dimers, intrastrand cross-links, and bulky adducts. The wide range of substrate specificity suggests that the repair complex recognizes distortions in the DNA helix. It subsequently recruits a nucleotide-excision repair, preincision complex. [GOC:bhm, PMID:22331906]


transcription-coupled nucleotide-excision repair, DNA damage recognition complex location

A protein complex that is capable of identifying lesions in DNA on the actively transcribed strand of the DNA duplex as well as a small subset of lesions not recognized by the general nucleotide-excision repair pathway. The wide range of substrate specificity suggests that the repair complex recognizes distortions in the DNA helix. It subsequently recruits a nucleotide-excision repair, preincision complex. [GOC:bhm, PMID:22331906]


An nuclear body involved in nuclear mRNA surveilllance. Contains at least Mmi1, or an ortholog of it, and the nuclear exosome. [GOC:al, GOC:vw, PMID:16823445, PMID:23980030, PMID:32012158]


A protein complex that contributes to the endocytic process and bud growth in yeast. It is involved in the precise timing of actin assembly during endocytosis. [GOC:bhm, PMID:19713939]


Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of leucine. [PMID:19033384]


Binding to a keratin filament, an intermediate filament composed of acidic and basic keratins (types I and II), typically expressed in epithelial cells. [GOC:krc, PMID:6170061]


A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a subsynaptic reticulum. A subsynaptic reticulum is an elaborate tubulolamellar membrane system that underlies the postsynaptic cell membrane. [PMID:21041451]


Grouping of multiple copies of a signal at a cellular location. May promote receptor clustering and alter the signal transduction response. [GOC:als, PMID:12011072, PMID:15603739]


The modification of a histone by addition of a methyl group to an glutamine residue. [PMID:24352239]


Catalysis of the reaction: S-adenosyl-L-methionine + (histone)-glutamine = S-adenosyl-L-homocysteine + (histone)-N5-methyl-glutamine. [PMID:24352239]


negative regulation of transcription from RNA polymerase II promoter by transcription factor localization involved in response to DNA damage checkpoint signaling

Any process that stops, prevents, or reduces the frequency, rate or extent of transcription from an RNA polymerase II promoter using a mechanism that involves the localization of a transcription factor and initiated in response to the DNA damage checkpoint signaling. [PMID:24006488]


The chemical reactions and pathways resulting in the breakdown of the unspliced pre-mRNA (pre-messenger RNA). [GOC:rb, PMID:22844259]


anti-Mullerian hormone signaling pathway

The series of molecular signals initiated by the binding of anti-Mullerian hormone to its receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:hjd, PMID:23624077]


MAPK cascade involved in nutrient response signaling

A MAPK cascade that occurs as a result of deprivation of nourishment. [GOC:al, PMID:7501024]


peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity

Any peptidyl-tyrosine dephosphorylation that is involved in inactivation of protein kinase activity. [PMID:7501024]


platelet-derived growth factor complex location

A protein complex consisting of two chains of platelet-derived growth factor (PDGF) subunits. PDGF dimers bind to PDGF receptors in the plasma membrane and induce receptor dimerisation and activation. PDGFs are involved in a wide variety of signalling processes. PDGFs are found in all vertebrates where at least 2 different chains (A and B) exist. In human (and other mammals), four types of PDGF chains (A, B, C, and D) are known which form five different dimers (AA, AB, BB, CC and DD). [GOC:bhm, PMID:11331882]


response to transition metal nanoparticle

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 transition metal nanoparticle. [PMID:23150627]


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 gold nanoparticle stimulus. [PMID:23150627]


RNAP II C-terminal domain phosphoserine binding

RNA Pol II C-terminal domain phosphoserine binding

RNA polymerase II C-terminal domain phosphoserine binding

Binding to phosphorylated serine residues in the C-terminal domain of RNA polymerase II. [GOC:di, PMID:22796944]


platelet-derived growth factor receptor-ligand complex location

A tetrameric protein complex consisting of two platelet-derived growth factor (PDGF) receptor subunits and two PDGF ligand subunits. Binding of the PDGF ligand dimer to the PDGF receptor in the plasma membrane induces receptor dimerisation and activation. PDGFs are involved in a wide variety of signalling processes and are found in all vertebrates. At least two different receptor chains (A and B) and four types of ligand chains (A, B, C, and D) are known forming a wide variety of combinations of receptor-ligand complexes. [GOC:bhm, PMID:11331882]


PDGF-BB-receptor alpha-beta complex location


PDGF-CC-receptor alpha-beta complex location


PDGF-DD-receptor alpha-beta complex location


anti-Mullerian hormone receptor activity

Combining with anti-Mullerian hormone to initiate a change in cell activity. [GOC:hjd, PMID:23624077]


mitotic contractile actomyosin ring disassembly

mitotic actomyosin contractile ring disassembly

Any disaggregation of an actomyosin contractile ring into its constituent components that is involved in a mitotic cell cycle. [PMID:14602073, PMID:22891673]


Binding to a preribosome. [GOC:di, PMID:22735702]


Catalysis of the transfer of a methyl group from S-adenosyl-L-methionine to the 5'-gamma-phosphate in an RNA molecule. [GOC:al, GOC:vw, PMID:22740346]


A process in which RNA is transported to and maintained in a part of a chromosome that is organized into chromatin. [GOC:dos, GOC:mah, PMID:22582262]


efflux transmembrane transporter complex location

A protein complex that is capable of efflux transmembrane transporter activity. [GOC:dos, PMID:21556065, PMID:9417051]


The phosphorylation of a peptidyl-threonine to form peptidyl-O-phospho-L-threonine on an identical protein. For example, phosphorylation by the other kinase within a homodimer. [PMID:19357077]


A renal system process in which amino acids 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. [GOC:hjd, PMID:1526373]


Protein complex that associates with the kinetochores. [PMID:22521786]


Bub1-Bub3 complex localization to kinetochore

A cellular protein complex localization that acts on a Bub1-Bub3 complex; as a result, the complex is transported to, or maintained in, a specific location at the kinetochore. [PMID:22521786]


Binding to a cellulosome, an extracellular multi-enzyme complex containing several enzymes aligned on a non-catalytic scaffolding that functions to hydrolyze plant cell wall polysaccharides. [GOC:mengo_curators, PMID:11893054, PMID:15197390]


Bre1-Rad6 ubiquitin ligase complex location

A ubiquitin ligase complex consisting of Bre1 and Rad6 that mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. It also modulates the formation of double-strand breaks during meiosis. [GOC:bhm, PMID:19531475]


UBR1-RAD6 ubiquitin ligase complex location

A ubiquitin ligase complex consisting of UBR1 and RAD6 components. It polyubiquitinates proteins containing non-acetylated N-terminal residues causing their subsequent degradation by the proteasome as part of the Ac/N-End Rule pathway. It recognizes non-acetylated N-terminal methionine if it is followed by a hydrophobic residue. Additionally, it acts in an N-end rule independent manner as a component of a novel quality control pathway for proteins synthesized on cytosolic ribosomes. [GOC:bhm, PMID:19531475]


MUB1-RAD6-UBR2 ubiquitin ligase complex location

A ubiquitin ligase complex consisting of MUB1, RAD6 and UBR2 components. It ubiquitinates, and targets for destruction, the RPN4 transcription factor, which upregulates the proteasome genes. The binding of MUB1 may position the RPN4 ubiquitylation site proximal to the Ubiquitin-RAD6 thioester and allow the transfer of Ubiquitin from RAD6 to RPN4. One of its components, MUB1, is a short-lived protein ubiquitinated by the UBR2-RAD6 ubiquitin conjugating enzyme. [GOC:bhm, PMID:18070918]


RAD6-UBR2 ubiquitin ligase complex location

A ubiquitin ligase complex consisting of RAD6 and UBR2 components. It may act in a quality control pathway for proteins synthesized on cytosolic ribosomes. The UBR2 component lacks sequence motifs required for N-end rule degradation. [GOC:bhm, PMID:15504724]


RSP5-BUL ubiquitin ligase complex location

A ubiquitin ligase complex consisting of RSP5 and BUL components. It polyubiquinates plasma membrane transporters and permeases, required for their endocytosis and subsequent degradation in the vacuole. BUL1 or BUL2, respectively, bind to the target protein, enabling ubiquitylation by Rsp5. Phosphorylation of BUL proteins results in binding to 14-3-3 proteins, protecting the permeases from down-regulation. [GOC:bhm, PMID:9931424]


Binding to a type-I dockerin domain of a protein. Type-I dockerin domain is the binding partner of type-1 cohesin domain. [GOC:mengo_curators, PMID:23195689, PMID:24080387]


Binding to a type-II dockerin domain of a protein. Type-II dockerin domain is the binding partner of type-II cohesin domain. [GOC:mengo_curators, PMID:23195689, PMID:24080387]


Binding to a type-III dockerin domain of a protein. Type-III dockerin domain is the binding partner of type-III cohesin domain. [GOC:mengo_curators, PMID:23195689, PMID:24080387]


Binding to a type-I cohesin domain of a protein. Type-I cohesin domain is the binding partner of type-I dockerin domain. [GOC:mengo_curators, PMID:23195689, PMID:24080387]


Binding to a type-II cohesin domain of a protein. Type-II cohesin domain is the binding partner of type-II dockerin domain. [GOC:mengo_curators, PMID:23195689, PMID:24080387]


Binding to a type-III cohesin domain of a protein. Type-III cohesin domain is the binding partner of type-III dockerin domain. [GOC:mengo_curators, PMID:23195689, PMID:24080387]


cellular response to insulin-like growth factor stimulus

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin-like growth factor stimulus. [PMID:20042609]


A protein complex that consists of a phospho relay component and a MAPK cascade component. The complex is involved in signaling oxidative stress and osmostress. [PMID:24255738]


ULK1 signaling complex
ATG1 kinase complex location
autophagy-initiation complex
ULK1 complex location
autophagy-initiation complex location
ATG1-ATG13 complex location
ULK1-ATG13-FIP200 complex
ATG1 kinase complex
ULK1-ATG13-RB1CC1 complex
ATG1/ULK1 signaling complex location
Atg1p signalling complex location
ATG1/ULK1 signaling complex
ULK1-ATG13-RB1CC1 complex location
ULK complex location
ULK1-ATG13-FIP200 complex location
ULK complex
ULK1 complex
ATG1-ATG13 complex
ULK1 signaling complex location
Atg1p signalling complex
Atg1/ULK1 kinase complex location

A protein complex consisting of Atg1 (or Atg1 homologs e.g. ULK1, ULK2 in mammals) and Atg13 along with other proteins that regulate its function (e.g. Atg17 in yeast or RB1CC1(FIP200) in mammals). This complex has serine/threonine protein kinase activity and is involved in autophagosome formation. [GOC:bhm, GOC:DOS, GOC:rb, PMID:15743910, PMID:19211835, PMID:19258318, PMID:19597335, PMID:22885598]


Gin4 complex location
Gin4-septin complex location
Gin4-septin complex

A protein complex involved in septin ring formation during mitosis. In Saccharomyces cerevisiae it consists of BNI5, CDC3, CDC10, CDC11, CDC12, GIN4, NAP1 and SHS1. At least 2 GIN4 molecules are involved. [GOC:bhm, PMID:12058072]


A collagen homotrimer of alpha1(XIX) chains; type XIX collagen triple helices localize to basement membrane zones in differentiating muscle cells. [GOC:bhm, PMID:17876790]


A collagen homotrimer of alpha1(XX) chains. [GOC:bhm, PMID:17876790]


A collagen homotrimer of alpha1(XXI) chains; type XXI collagen triple helices found in the extracellular matrix component of blood vessel walls and in the cytoplasm of cultured human aortic smooth muscle. [GOC:bhm, PMID:17876790]


A collagen homotrimer of alpha1(XXII) chains; type XXII collagen triple helices acts as a cell adhesion ligand for skin epithelial cells and fibroblasts. [GOC:bhm, PMID:17876790]


A collagen homotrimer of alpha1(XXIII) chains; type XXIII collagen triple helices span the plasma membrane. [GOC:bhm, PMID:17876790]


A collagen homotrimer of alpha1(XXIV) chains; type XXIV collagen triple helices may participate in regulating type I collagen fibrillogenesis at specific anatomical locations during fetal development. [GOC:bhm, PMID:17876790]


A collagen homotrimer of alpha1(XXVI) chains. [GOC:bhm, PMID:17876790]


A collagen homotrimer of alpha1(XXVII) chains. These trimers form thin, non-striated fibrils. Type XXVII collagen triple helices play a role during the calcification of cartilage and the transition of cartilage to bone. [GOC:bhm, PMID:17876790, PMID:21421911]


A collagen homotrimer of alpha1(XXVIII) chains. [GOC:bhm, PMID:17876790]


A collagen homotrimer of alpha1(XXV) chains; type XXV collagen triple helices span the plasma membrane. [GOC:bhm, PMID:17876790]


RNA polymerase II, RPB4-RPB7 subcomplex location


A heterotetrameric protein complex involved in the sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at tRNA wobble positions. In E. coli it consists of a central IscS dimer with the two TusA protomers bound to one of the IscS units each via persulfide (-SSH) groups. [GOC:bhm, PMID:20404999]


A heterotetrameric protein complex involved in the sulfur transfer during iron-sulfur cluster assembly and in the modification of tRNA wobble positions. In E. coli it consisting of a central IscS dimer with the IscU protomers attached to one of the IscS units each via a disulfide (-SSH) group. [GOC:bhm, PMID:20404999]


A tetrameric protein complex capable of acetyltransferase activity. It can catalyze the transfer of an acetyl group from acetyl-CoA to an acceptor residue on histone H-3, histone H-4, or on polyamines. The complex is also capable of acetylating certain small basic proteins. The two Hpa2 dimers that make up the tetramer are held together by interactions between the bound acetyl-CoA molecules. [GOC:bhm, PMID:10600387]


A type-I transmembrane protein complex located in the endoplasmic reticulum (ER) consisting of an IRE1-IRE1 dimer, which forms in response to the accumulation of unfolded protein in the ER. The dimeric complex has endoribonuclease (RNase) activity and evokes the unfolded protein response (UPR) by cleaving an intron of a mRNA coding for the transcription factor HAC1 in yeast or XBP1 in mammals; the complex cleaves a single phosphodiester bond in each of two RNA hairpins (with non-specific base paired stems and loops of consensus sequence CNCNNGN, where N is any base) to remove an intervening intron from the target transcript. [GOC:bf, GOC:bhm, PMID:18191223, PMID:25437541]


mitotic checkpoint complex, CDC20-MAD2 subcomplex location

A protein complex involved in the spindle checkpoint, preventing the activation of the anaphase-promoting complex until all chromosomes are correctly attached in a bipolar fashion to the mitotic spindle. In budding yeast this complex consists of Mad2p and Cdc20p, and in mammalian cells it consists of MAD2 and CDC20. [GOC:bhm, PMID:15879521]


A protein complex that acts as a two-component GTPase-activating protein for Tem1 GTPase, thus regulating a signal transduction cascade, called the mitotic exit network (MEN), which is required for mitotic exit and cytokinesis. Bub2/Bfa1 keeps Tem1 inactive until the spindle is properly oriented, thus inhibiting MEN activation. [GOC:bhm, PMID:16449187]


process resulting in tolerance to alcohol


process resulting in tolerance to butan-1-ol


process resulting in tolerance to isobutanol


A laminin complex composed of alpha4, beta2 and gamma3 polypeptide chains. [GOC:bhm, GOC:dph, PMID:15979864, PMID:17453709]


A laminin complex composed of alpha5, beta2 and gamma2 polypeptide chains. [GOC:bhm, GOC:dph, PMID:15979864, PMID:17453709]


A laminin complex composed of alpha5, beta2 and gamma3 polypeptide chains. [GOC:bhm, PMID:17453709]


A homotrimeric or homopentameric glycoprotein that functions at the interface of the cell membrane and the extracellular matrix through its interactions with proteins and proteoglycans, such as collagens, integrins and fibronectin, to regulate matrix structure and cellular behaviour. [GOC:bhm, PMID:18193164]


A region of facultative heterochromatin formed dynamically at specific loci in response to environmental signals, independently of RNAi. [PMID:22144463, PMID:24210919]


A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a secondary cell septum following nuclear division. [PMID:22891259]


A heterodimeric protein complex consisting of BID and BCL-xl, members of the Bcl-2 family of anti- and proapoptotic regulators. [GOC:bhm, PMID:14634621]


gap junction-mediated intercellular transport

The movement of substances between cells via gap junctions. A gap junction is a fine cytoplasmic channel, found in animal cells, that connects the cytoplasm of one cell to that of an adjacent cell, allowing ions and other molecules to pass freely between the two cells. [GOC:hjd, PMID:14506308, PMID:23261543, Wikipedia:Gap_junction]


A protein complex facilitating glucose transport into, out of or within a cell, or between cells. [GOC:bhm, PMID:15449578]


A protein complex facilitating transport of molecules (proteins, small molecules, nucleic acids) into, out of or within a cell, or between cells. [GOC:bhm, PMID:15449578]


BRE1 E3 ubiquitin ligase complex location

BRE1 E3 ubiquitin-protein ligase complex location

A homodimeric protein complex composed of the E3 ubiquitin-protein ligase BRE1. Plays a role in regulating association of RNA polymerase II with active genes. [GOC:bhm, PMID:19531475]


Fused-Smurf ubiquitin ligase complex location

A ubiquitin ligase complex. In D. melanogaster, it regulates ubiquitination and proteolysis of the BMP receptor Thickveins in cystoblasts, potentially by controlling Tkv ubiquitination and degradation. [GOC:bhm, PMID:21145463]


activated SUMO-E1 ligase complex location

A protein complex consisting of a SUMO protein bound to a SUMO activating enzyme complex. Activation by the E1 complex and linkage to the E2 enzyme UBE2I is required for the formation of covalent bonds between SUMO and its ultimate target proteins. [GOC:bhm, PMID:15660128]


L-methionine salvage from methionine sulphoxide

The generation of L-methionine from methionine sulphoxide. [PMID:24118096]


methionine salvage from methionine sulphoxide


A protein complex consisting of a SUMO (small ubiquitin-related modifier) protein bound to a SUMO-conjugating E2 ligase. Sumoylation of the E2 ligase is an intermediate step required for the formation of covalent bonds between a SUMO protein and its ultimate protein target. SUMO is transferred to the E2 ligase by a SUMO-activating E1 enzyme. Sumoylation of the target protein is either facilitated directly by the sumoylated E2 ligase or aided by an optional E3 ligase. [GOC:bhm, PMID:18691969]


An actin-rich cytoskeletal network located beneath the microvilli of the apical plasma membrane of polarized epithelial cells. In addition to actin filaments, the terminal web may contain actin-binding proteins, myosin motor proteins, and intermediate filaments. The terminal web can function as a contractile structure that influences the spatial distribution of microvilli as well as the development and morphogenesis of tissues containing polarized epithelial cells. [GOC:kmv, PMID:19437512, PMID:24677443, PMID:7511618, Wikipedia:Terminal_web]


xylanolytic complex location
xylanolytic complex

A multifunctional supermolecular complex, containing several proteins with hemicellulase activity. Functions to hydrolyze hemicellulose. [GOC:mengo_curators, PMID:16769147]


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 disturbance in organismal or cellular homeostasis caused by a zinc ion stimulus. [GOC:kmv, pmid:17888400]


PKM2-SAICAR protein kinase complex location


PKM2 pyruvate kinase complex location
PKM2 homotetramer

A protein complex capable of pyruvate kinase activity. PKM2 only exists as homotetramer when bound to beta-d-fructofuranose 1,6-bisphosphate (CHEBI:28013). [GOC:bhm, PMID:24606918]


Catalysis of the reaction: butanal + NADH + H+ => n-butanol + NAD+. [GOC:mengo_curators, PMID:1999395, RHEA:33199]


process resulting in tolerance to organic substance


process resulting in tolerance to ketone


process resulting in tolerance to alkane


Kir2 inward rectifier potassium channel complex location

A inward rectifier potassium channel complex. Homo- or heterotetramer composed of subunits of the eukaryotic Kir2 protein family. Plays a key role in maintaining the correct resting potential in eukaryotic cells. [GOC:bhm, PMID:16834334]


os penis development
penile bone development
penis bone development

The reproductive developmental process whose specific outcome is the progression of the baculum over time, from its formation to the mature structure. [GOC:sl, PMID:21471296]


An extracellular matrix consisting of a densely packed organomineral assembly in which the mineral phase represents the majority of the material by weight. [GOC:jh2, PMID:15994301]


upstream stimulatory factor complex location

A protein complex capable of sequence-specific DNA binding RNA polymerase II transcription factor activity through binding to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3'). Found in a variety of viral and cellular promoters. [GOC:bhm, PMID:8576131]


lipid transport across blood brain barrier

lipid transport across blood-brain barrier

The directed movement of lipid molecules passing through the blood-brain barrier. [GOC:sjp, PMID:24345162]


K48-specific deubiquitinase activity
K48-specific deubiquitinating activity

Hydrolysis of Lys48-linked ubiquitin unit(s) from a ubiquitinated protein. [GOC:bf, GOC:PARL, PMID:22970133]


regulation of Wnt-activated signaling pathway involved in digestive tract morphogenesis


regulation of termination of RNA polymerase II transcription, polyadenylation-coupled


negative regulation of termination of RNA polymerase II transcription, polyadenylation-coupled


positive regulation of termination of RNA polymerase II transcription, polyadenylation-coupled


ditrans, polycis-undecaprenyl-phosphate mannosyltransferase activity

Catalysis of the reaction: ditrans,octacis-undecaprenyl phosphate + GDP-alpha-D-mannose = D-mannosyl undecaprenyl phosphate+ GDP. [GOC:curators]


The cell cycle process by which a cell in G2 phase commits to M phase. [GOC:jl, GOC:mtg_cell_cycle]


The directed movement of a ceramide 1-phosphate into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:TermGenie, PMID:23863933]


inhibition of fusion of autophagosome with lysosome


The process in which the anatomical structure of a cranial ganglion is generated and organized. [GOC:dph]


regulation of flame-shaped neurofibrillary tangle formation


Merging of two or more vacuoles, or of vacuoles and vesicles within a cell to form a single larger vacuole. [GOC:pr, GOC:vw, Wikipedia:Vacuole]


A xylanase activity that acts on one of the ends of a xylan polymer which does not contain side chains. [GOC:jh2, ISBN:81-7736-269-0, PMID:16535010]


Centriole assembly in which a centriole arises de novo, rather than by replication from an existing centriole. This process may occur via different mechanisms. Examples include the deuterosome pathway in multicilated epithelial animal cells and formation of centrioles during parthenogenesis in some insects. [GOC:cilia, PMID:25047614, PMID:25291643]


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 stimulus from a virus. [GOC:dos]


regulation of DNA replication origin binding

Any process that modulates the frequency, rate or extent of DNA replication origin binding. [GO_REF:0000059, GOC:TermGenie, PMID:11850415]


positive regulation of tau-protein kinase I activity


A network of extracellular fibrillar structures containing granule proteins, chromatin fibers and DNA that are released by neutrophils as part of the host defense response. Extracellular release of antimicrobial proteins such as neutrophil elastase, cathepsin G and histones can bind, disarm, and kill microbes independent of phagocytosis and the fibrillar nature of these structures may target these effects locally by preventing diffusion of these proteins outside the target site.


A multi-organism process in which a virus is a participant. The other participant is the host. Includes infection of a host cell, replication of the viral genome, and assembly of progeny virus particles. In some cases the viral genetic material may integrate into the host genome and only subsequently, under particular circumstances, 'complete' its life cycle. [GOC:bf, GOC:jl, GOC:mah]


An old term for glycolysis. Often it is used to describe anaerobic glucose catabolism that includes the further conversion of PYRUVIC ACID to LACTIC ACID or ETHANOL.


A double-membrane-bounded compartment that engulfs endogenous cellular material as well as invading microorganisms to target them to the lytic vacuole/lysosome for degradation as part of macroautophagy. [GOC:autophagy, ISBN:0198547684, PMID:11099404]


Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus. [GOC:jl]


aromatic amino acid decarboxylase activity

Catalysis of the reaction: L-amino acid + H+ = R-H + CO2. [EC:4.1.1.28]

aromatic L-amino acid decarboxylase activity


Catalysis of the reaction: L-phenylalanine = phenylethylamine + CO2. [EC:4.1.1.53, MetaCyc:PHENYLALANINE-DECARBOXYLASE-RXN]


Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interleukin-21 stimulus. [GOC:BHF, GOC:mah]