The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"Trypsin-like serine proteases
".
FunFam 2: Transmembrane protease serine
Please note: GO annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.
There are 34 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
9 | P00750 (/IPI) P03951 (/IPI) P08001 (/IPI) P10323 (/IPI) P23578 (/IPI) P98073 (/IPI) Q2UVH8 (/IPI) Q5S248 (/IPI) Q8BIK6 (/IPI) |
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
8 | P56677 (/IDA) P56677 (/IDA) Q5S248 (/IDA) Q86T26 (/IDA) Q8BIK6 (/IDA) Q8VHJ4 (/IDA) Q9JJI7 (/IDA) Q9Y5Y6 (/IDA) |
Amidase activity GO:0004040
Catalysis of the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3.
|
6 | P10323 (/ISS) P23578 (/ISS) P29293 (/ISS) P48038 (/ISS) P79343 (/ISS) Q9GL10 (/ISS) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
6 | P00750 (/IDA) P10323 (/IDA) P11214 (/IDA) P79343 (/IDA) Q1JRP2 (/IDA) Q28198 (/IDA) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
6 | P08001 (/ISS) P23578 (/ISS) P29293 (/ISS) P48038 (/ISS) P79343 (/ISS) Q9GL10 (/ISS) |
Mannose binding GO:0005537
Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
|
6 | P08001 (/ISS) P23578 (/ISS) P29293 (/ISS) P48038 (/ISS) P79343 (/ISS) Q9GL10 (/ISS) |
Drug binding GO:0008144
Interacting selectively and non-covalently with a drug, any naturally occurring or synthetic substance, other than a nutrient, that, when administered or applied to an organism, affects the structure or functioning of the organism; in particular, any such substance used in the diagnosis, prevention, or treatment of disease.
|
6 | P10323 (/ISS) P23578 (/ISS) P29293 (/ISS) P48038 (/ISS) P79343 (/ISS) Q9GL10 (/ISS) |
Fucose binding GO:0042806
Interacting selectively and non-covalently with fucose, the pentose 6-deoxygalactose.
|
6 | P10323 (/ISS) P23578 (/ISS) P29293 (/ISS) P48038 (/ISS) P79343 (/ISS) Q9GL10 (/ISS) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
4 | P00750 (/TAS) P03951 (/TAS) P23578 (/TAS) P29293 (/TAS) |
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
4 | Q14C59 (/ISS) Q6IE14 (/ISS) Q7RTY8 (/ISS) Q9UL52 (/ISS) |
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
3 | P56677 (/ISO) P56677 (/ISO) Q8VHK8 (/ISO) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
2 | P56677 (/EXP) P56677 (/EXP) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
2 | P11214 (/ISO) P23578 (/ISO) |
Copper ion binding GO:0005507
Interacting selectively and non-covalently with copper (Cu) ions.
|
2 | P10323 (/NAS) P79343 (/NAS) |
Drug binding GO:0008144
Interacting selectively and non-covalently with a drug, any naturally occurring or synthetic substance, other than a nutrient, that, when administered or applied to an organism, affects the structure or functioning of the organism; in particular, any such substance used in the diagnosis, prevention, or treatment of disease.
|
2 | P08001 (/IDA) Q9GL10 (/IDA) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
2 | P10323 (/NAS) P79343 (/NAS) |
Phosphoprotein binding GO:0051219
Interacting selectively and non-covalently with a phosphorylated protein.
|
2 | P00750 (/IPI) Q28198 (/IPI) |
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
1 | P10323 (/TAS) |
DNA binding GO:0003677
Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
|
1 | P10323 (/NAS) |
Amidase activity GO:0004040
Catalysis of the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3.
|
1 | Q2UVH8 (/IDA) |
Amidase activity GO:0004040
Catalysis of the reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3.
|
1 | P08001 (/IMP) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | P03951 (/NAS) |
Signaling receptor binding GO:0005102
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
|
1 | P00750 (/IPI) |
Signaling receptor binding GO:0005102
Interacting selectively and non-covalently with one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
|
1 | P11214 (/ISO) |
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
1 | P00750 (/TAS) |
Mannose binding GO:0005537
Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
|
1 | P10323 (/IDA) |
Mannose binding GO:0005537
Interacting selectively and non-covalently with mannose, a monosaccharide hexose, stereoisomeric with glucose, that occurs naturally only in polymerized forms called mannans.
|
1 | P23578 (/ISO) |
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
|
1 | P23578 (/IMP) |
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
|
1 | O60235 (/TAS) |
Serine-type peptidase activity GO:0008236
Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | Q9Y5Y6 (/TAS) |
Fucose binding GO:0042806
Interacting selectively and non-covalently with fucose, the pentose 6-deoxygalactose.
|
1 | P08001 (/IDA) |
Phosphoprotein binding GO:0051219
Interacting selectively and non-covalently with a phosphorylated protein.
|
1 | P11214 (/ISO) |
Serine-type aminopeptidase activity GO:0070009
Catalysis of the hydrolysis of a peptide bond not more than three residues from the N-terminus of a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | A0A0G2K4I9 (/IDA) |
Serpin family protein binding GO:0097655
Interacting selectively and non-covalently with any member of the serpin protein family (serine protease inhibitors or classified inhibitor family I4). Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades. The majority of serpins inhibit serine proteases, but serpins that inhibit caspases and papain-like cysteine proteases have also been identified. Rarely, serpins perform a non-inhibitory function; for example, several human serpins function as hormone transporters and certain serpins function as molecular chaperones or tumor suppressors.
|
1 | Q28198 (/IPI) |
There are 72 GO terms relating to "biological process"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
9 | O60235 (/IDA) P11214 (/IDA) Q1JRP2 (/IDA) Q28198 (/IDA) Q5S248 (/IDA) Q8BIK6 (/IDA) Q8VHK8 (/IDA) Q9JJI7 (/IDA) Q9Y5Y6 (/IDA) |
Activation of adenylate cyclase activity GO:0007190
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
|
6 | P08001 (/ISS) P23578 (/ISS) P29293 (/ISS) P48038 (/ISS) P79343 (/ISS) Q9GL10 (/ISS) |
Single fertilization GO:0007338
The union of male and female gametes to form a zygote.
|
6 | P08001 (/ISS) P10323 (/ISS) P29293 (/ISS) P48038 (/ISS) P79343 (/ISS) Q9GL10 (/ISS) |
Acrosome reaction GO:0007340
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida of the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the zona pellucida.
|
6 | P08001 (/ISS) P23578 (/ISS) P29293 (/ISS) P48038 (/ISS) P79343 (/ISS) Q9GL10 (/ISS) |
Plasminogen activation GO:0031639
The process in which inactive plasminogen is processed to active plasmin. This process includes cleavage at an internal Arg-Val site to form an N-terminal A-chain and C-terminal B-chain held together by a disulfide bond, and can include further proteolytic cleavage events to remove the preactivation peptide.
|
6 | G8CXX6 (/IDA) P00750 (/IDA) P03951 (/IDA) P19637 (/IDA) Q1RLR1 (/IDA) Q28198 (/IDA) |
Acrosome reaction GO:0007340
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida of the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the zona pellucida.
|
4 | P10323 (/TAS) P23578 (/TAS) P29293 (/TAS) P79343 (/TAS) |
Epidermis development GO:0008544
The process whose specific outcome is the progression of the epidermis over time, from its formation to the mature structure. The epidermis is the outer epithelial layer of an animal, it may be a single layer that produces an extracellular material (e.g. the cuticle of arthropods) or a complex stratified squamous epithelium, as in the case of many vertebrate species.
|
4 | A1A5H5 (/IGI) A3KP13 (/IGI) A5PMY0 (/IGI) Q1RLP8 (/IGI) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
3 | P56677 (/ISO) P56677 (/ISO) Q8VHK8 (/ISO) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
3 | A0A0G2K4I9 (/TAS) P00750 (/TAS) P03951 (/TAS) |
Keratinocyte differentiation GO:0030216
The process in which a relatively unspecialized cell acquires specialized features of a keratinocyte.
|
3 | P56677 (/ISS) P56677 (/ISS) Q0IIH7 (/ISS) |
Neural tube closure GO:0001843
The last step in the formation of the neural tube, where the paired neural folds are brought together and fuse at the dorsal midline.
|
2 | P56677 (/IGI) P56677 (/IGI) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | Q7RTY8 (/ISS) Q9UL52 (/ISS) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | P00750 (/TAS) Q9Y5Y6 (/TAS) |
Activation of adenylate cyclase activity GO:0007190
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
|
2 | P10323 (/IDA) P79343 (/IDA) |
Single fertilization GO:0007338
The union of male and female gametes to form a zygote.
|
2 | P29293 (/TAS) P79343 (/TAS) |
Penetration of zona pellucida GO:0007341
The infiltration by sperm of the zona pellucida to reach the oocyte. The process involves digestive enzymes from a modified lysosome called the acrosome, situated at the head of the sperm.
|
2 | P23578 (/IMP) P29293 (/IMP) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
2 | A0A0G2K4I9 (/IDA) P03951 (/IDA) |
Cell migration GO:0016477
The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.
|
2 | P56677 (/TAS) P56677 (/TAS) |
Keratinocyte differentiation GO:0030216
The process in which a relatively unspecialized cell acquires specialized features of a keratinocyte.
|
2 | P56677 (/ISO) P56677 (/ISO) |
Epithelial cell morphogenesis involved in placental branching GO:0060672
The change in form (cell shape and size) that occurs when a trophoblast cell elongates to contribute to the branching of the placenta.
|
2 | P56677 (/IGI) P56677 (/IGI) |
Response to hypoxia GO:0001666
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 stimulus indicating 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.
|
1 | P11214 (/IMP) |
Acrosome matrix dispersal GO:0002077
The proteolytic digestion of components in the acrosomal matrix that occurs as part of the acrosome reaction. The process can occur either in the cumulus oophorous facilitating the penetration of it by the sperm, or at the zona pellucida allowing the sperm to reach the plasma membrane of the egg where the inner acrosomal membrane of the sperm can interact with the egg plasma membrane.
|
1 | P29293 (/IMP) |
Acrosome matrix dispersal GO:0002077
The proteolytic digestion of components in the acrosomal matrix that occurs as part of the acrosome reaction. The process can occur either in the cumulus oophorous facilitating the penetration of it by the sperm, or at the zona pellucida allowing the sperm to reach the plasma membrane of the egg where the inner acrosomal membrane of the sperm can interact with the egg plasma membrane.
|
1 | P23578 (/ISO) |
Acrosome matrix dispersal GO:0002077
The proteolytic digestion of components in the acrosomal matrix that occurs as part of the acrosome reaction. The process can occur either in the cumulus oophorous facilitating the penetration of it by the sperm, or at the zona pellucida allowing the sperm to reach the plasma membrane of the egg where the inner acrosomal membrane of the sperm can interact with the egg plasma membrane.
|
1 | P10323 (/NAS) |
Cellular protein modification process GO:0006464
The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications) occurring at the level of an individual cell. Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification).
|
1 | P00750 (/TAS) |
Activation of adenylate cyclase activity GO:0007190
Any process that initiates the activity of the inactive enzyme adenylate cyclase.
|
1 | P23578 (/ISO) |
Single fertilization GO:0007338
The union of male and female gametes to form a zygote.
|
1 | P23578 (/IMP) |
Single fertilization GO:0007338
The union of male and female gametes to form a zygote.
|
1 | P79343 (/NAS) |
Binding of sperm to zona pellucida GO:0007339
The process in which the sperm binds to the zona pellucida glycoprotein layer of the egg. The process begins with the attachment of the sperm plasma membrane to the zona pellucida and includes attachment of the acrosome inner membrane to the zona pellucida after the acrosomal reaction takes place.
|
1 | P23578 (/IGI) |
Acrosome reaction GO:0007340
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida of the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the zona pellucida.
|
1 | P10323 (/IMP) |
Acrosome reaction GO:0007340
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida of the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the zona pellucida.
|
1 | P23578 (/ISO) |
Acrosome reaction GO:0007340
The discharge, by sperm, of a single, anterior secretory granule following the sperm's attachment to the zona pellucida of the oocyte. The process begins with the fusion of the outer acrosomal membrane with the sperm plasma membrane and ends with the exocytosis of the acrosomal contents into the zona pellucida.
|
1 | P79343 (/NAS) |
Penetration of zona pellucida GO:0007341
The infiltration by sperm of the zona pellucida to reach the oocyte. The process involves digestive enzymes from a modified lysosome called the acrosome, situated at the head of the sperm.
|
1 | P23578 (/IGI) |
Penetration of zona pellucida GO:0007341
The infiltration by sperm of the zona pellucida to reach the oocyte. The process involves digestive enzymes from a modified lysosome called the acrosome, situated at the head of the sperm.
|
1 | P23578 (/ISO) |
Penetration of zona pellucida GO:0007341
The infiltration by sperm of the zona pellucida to reach the oocyte. The process involves digestive enzymes from a modified lysosome called the acrosome, situated at the head of the sperm.
|
1 | P29293 (/TAS) |
Respiratory gaseous exchange by respiratory system GO:0007585
The process of gaseous exchange between an organism and its environment. In plants, microorganisms, and many small animals, air or water makes direct contact with the organism's cells or tissue fluids, and the processes of diffusion supply the organism with dioxygen (O2) and remove carbon dioxide (CO2). In larger animals the efficiency of gaseous exchange is improved by specialized respiratory organs, such as lungs and gills, which are ventilated by breathing mechanisms.
|
1 | O60235 (/TAS) |
Blood coagulation GO:0007596
The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers.
|
1 | P03951 (/NAS) |
Blood coagulation, intrinsic pathway GO:0007597
A protein activation cascade that contributes to blood coagulation and consists of the interactions among high molecular weight kininogen, prekallikrein, and factor XII that lead to the activation of clotting factor X.
|
1 | P03951 (/TAS) |
Smooth muscle cell migration GO:0014909
The orderly movement of a smooth muscle cell from one site to another, often during the development of a multicellular organism.
|
1 | P11214 (/IMP) |
Protein catabolic process GO:0030163
The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
1 | P29293 (/IMP) |
Protein catabolic process GO:0030163
The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
1 | P23578 (/ISO) |
Keratinocyte differentiation GO:0030216
The process in which a relatively unspecialized cell acquires specialized features of a keratinocyte.
|
1 | Q9Y5Y6 (/IMP) |
Plasminogen activation GO:0031639
The process in which inactive plasminogen is processed to active plasmin. This process includes cleavage at an internal Arg-Val site to form an N-terminal A-chain and C-terminal B-chain held together by a disulfide bond, and can include further proteolytic cleavage events to remove the preactivation peptide.
|
1 | P11214 (/ISO) |
Trypsinogen activation GO:0032023
The proteolytic processing of trypsinogen to the active form, trypsin.
|
1 | P98072 (/TAS) |
Positive regulation of hemocyte proliferation GO:0035208
Any process that activates or increases the rate or extent of hemocyte proliferation. Hemocytes are blood cells associated with a hemocoel (the cavity containing most of the major organs of the arthropod body) that are involved in defense and clotting of hemolymph, but not involved in transport of oxygen. An example of this process is found in Drosophila melanogaster.
|
1 | Q8IP30 (/IGI) |
Synaptic transmission, glutamatergic GO:0035249
The vesicular release of glutamate from a presynapse, across a chemical synapse, the subsequent activation of glutamate receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
|
1 | P19637 (/IMP) |
Synaptic transmission, glutamatergic GO:0035249
The vesicular release of glutamate from a presynapse, across a chemical synapse, the subsequent activation of glutamate receptors at the postsynapse of a target cell (neuron, muscle, or secretory cell) and the effects of this activation on the postsynaptic membrane potential and ionic composition of the postsynaptic cytosol. This process encompasses both spontaneous and evoked release of neurotransmitter and all parts of synaptic vesicle exocytosis. Evoked transmission starts with the arrival of an action potential at the presynapse.
|
1 | P11214 (/ISO) |
Regulation of growth GO:0040008
Any process that modulates the frequency, rate or extent of the growth of all or part of an organism so that it occurs at its proper speed, either globally or in a specific part of the organism's development.
|
1 | Q8VHJ4 (/IMP) |
Regulation of growth GO:0040008
Any process that modulates the frequency, rate or extent of the growth of all or part of an organism so that it occurs at its proper speed, either globally or in a specific part of the organism's development.
|
1 | Q8VHK8 (/ISO) |
Wound healing GO:0042060
The series of events that restore integrity to a damaged tissue, following an injury.
|
1 | P19637 (/IEP) |
Fibrinolysis GO:0042730
A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin.
|
1 | P00750 (/TAS) |
Protein digestion GO:0044256
The whole of the physical, chemical, and biochemical processes carried out by living organisms to break down ingested proteins into components that may be easily absorbed and directed into metabolism.
|
1 | P98072 (/TAS) |
Negative regulation of proteolysis GO:0045861
Any process that stops, prevents, or reduces the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
|
1 | P00750 (/IDA) |
Negative regulation of proteolysis GO:0045861
Any process that stops, prevents, or reduces the frequency, rate or extent of the hydrolysis of a peptide bond or bonds within a protein.
|
1 | P11214 (/ISO) |
Platelet-derived growth factor receptor signaling pathway GO:0048008
The series of molecular signals generated as a consequence of a platelet-derived growth factor receptor binding to one of its physiological ligands.
|
1 | P11214 (/IDA) |
Platelet-derived growth factor receptor signaling pathway GO:0048008
The series of molecular signals generated as a consequence of a platelet-derived growth factor receptor binding to one of its physiological ligands.
|
1 | P11214 (/IMP) |
Regulation of synaptic plasticity GO:0048167
A process that modulates synaptic plasticity, the ability of synapses to change as circumstances require. They may alter function, such as increasing or decreasing their sensitivity, or they may increase or decrease in actual numbers.
|
1 | P19637 (/IEP) |
Response to steroid hormone GO:0048545
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 steroid hormone stimulus.
|
1 | P29293 (/IDA) |
Response to steroid hormone GO:0048545
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 steroid hormone stimulus.
|
1 | P23578 (/ISO) |
Cognition GO:0050890
The operation of the mind by which an organism becomes aware of objects of thought or perception; it includes the mental activities associated with thinking, learning, and memory.
|
1 | Q9UL52 (/IMP) |
Cognition GO:0050890
The operation of the mind by which an organism becomes aware of objects of thought or perception; it includes the mental activities associated with thinking, learning, and memory.
|
1 | Q5S248 (/ISO) |
Response to cAMP GO:0051591
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 cAMP (cyclic AMP, adenosine 3',5'-cyclophosphate) stimulus.
|
1 | P19637 (/IEP) |
Positive regulation of fibrinolysis GO:0051919
Any process that activates, maintains or increases the frequency, rate or extent of fibrinolysis, an ongoing process that solubilizes fibrin, resulting in the removal of small blood clots.
|
1 | P03951 (/IDA) |
Positive regulation of ovulation GO:0060279
Any process that activates or increases the frequency, rate or extent of ovulation, the release of a mature ovum/oocyte from an ovary.
|
1 | P19637 (/IMP) |
Positive regulation of ovulation GO:0060279
Any process that activates or increases the frequency, rate or extent of ovulation, the release of a mature ovum/oocyte from an ovary.
|
1 | P11214 (/ISO) |
Cornification GO:0070268
A type of programmed cell death that occurs in the epidermis, morphologically and biochemically distinct from apoptosis. It leads to the formation of corneocytes, i.e. dead keratinocytes containing an amalgam of specific proteins (e.g., keratin, loricrin, SPR and involucrin) and lipids (e.g., fatty acids and ceramides), which are necessary for the function of the cornified skin layer (mechanical resistance, elasticity, water repellence and structural stability).
|
1 | Q9Y5Y6 (/TAS) |
Response to fatty acid GO:0070542
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 fatty acid stimulus.
|
1 | P19637 (/IEP) |
Cellular response to follicle-stimulating hormone stimulus GO:0071372
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 follicle-stimulating hormone stimulus.
|
1 | P19637 (/IEP) |
Cellular response to luteinizing hormone stimulus GO:0071373
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 luteinizing hormone stimulus.
|
1 | P19637 (/IEP) |
Cellular response to dexamethasone stimulus GO:0071549
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 dexamethasone stimulus.
|
1 | P19637 (/IEP) |
Self proteolysis GO:0097264
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their own peptide bonds.
|
1 | Q1JRP2 (/IDA) |
Trans-synaptic signaling by BDNF, modulating synaptic transmission GO:0099183
Cell-cell signaling between presynapse and postsynapse, via the vesicular release and reception of brain derived neurotrophic factor (BDNF), that modulates the synaptic transmission properties of the synapse.
|
1 | P11214 (/IMP) |
There are 57 GO terms relating to "cellular component"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
GO Term | Annotations | Evidence |
---|---|---|
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
7 | A0A0G2K4I9 (/IDA) P03951 (/IDA) P11214 (/IDA) P19637 (/IDA) Q28198 (/IDA) Q2UVH8 (/IDA) Q9JJI7 (/IDA) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
4 | O60235 (/TAS) P00750 (/TAS) P03951 (/TAS) P10323 (/TAS) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
4 | Q5QSK2 (/IDA) Q5S248 (/IDA) Q86T26 (/IDA) Q8BIK6 (/IDA) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
4 | P03951 (/TAS) P56677 (/TAS) P56677 (/TAS) Q9Y5Y6 (/TAS) |
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
4 | O60235 (/TAS) P56677 (/TAS) P56677 (/TAS) Q9Y5Y6 (/TAS) |
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
|
4 | O60235 (/HDA) P00750 (/HDA) P03951 (/HDA) Q86T26 (/HDA) |
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
3 | P11214 (/ISO) P56677 (/ISO) P56677 (/ISO) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
3 | P00750 (/IDA) P11214 (/IDA) P19637 (/IDA) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
3 | Q14C59 (/ISS) Q6IE14 (/ISS) Q7RTY8 (/ISS) |
Extrinsic component of plasma membrane GO:0019897
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
|
3 | P56677 (/IDA) P56677 (/IDA) Q9JJI7 (/IDA) |
Acrosomal matrix GO:0043159
A structural framework, or 'dense core' at the interior of an acrosome. May regulate the distribution of hydrolases within the acrosome and their release during the acrosome reaction.
|
3 | P10323 (/TAS) P23578 (/TAS) P29293 (/TAS) |
Acrosomal vesicle GO:0001669
A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome.
|
2 | P23578 (/IDA) P29293 (/IDA) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
2 | P56677 (/IDA) P56677 (/IDA) |
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
2 | Q1JRP2 (/IDA) Q5S248 (/IDA) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
2 | P00750 (/IDA) Q8VHJ4 (/IDA) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
2 | P11214 (/ISO) Q8VHK8 (/ISO) |
Basolateral plasma membrane GO:0016323
The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
|
2 | P56677 (/ISO) P56677 (/ISO) |
Extrinsic component of plasma membrane GO:0019897
The component of a plasma membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
|
2 | P56677 (/ISO) P56677 (/ISO) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
2 | P08001 (/IDA) P10323 (/IDA) |
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
|
2 | P11214 (/IMP) P19637 (/IMP) |
Acrosomal vesicle GO:0001669
A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome.
|
1 | P23578 (/ISO) |
Acrosomal vesicle GO:0001669
A structure in the head of a spermatozoon that contains acid hydrolases, and is concerned with the breakdown of the outer membrane of the ovum during fertilization. It lies just beneath the plasma membrane and is derived from the lysosome.
|
1 | P29293 (/TAS) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
1 | P03951 (/NAS) |
Cell GO:0005623
The basic structural and functional unit of all organisms. Includes the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope.
|
1 | Q2UVH8 (/IDA) |
Nucleus GO:0005634
A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
|
1 | P10323 (/HDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | P11214 (/ISO) |
Golgi-associated vesicle GO:0005798
Any vesicle associated with the Golgi complex and involved in mediating transport within the Golgi or between the Golgi and other parts of the cell.
|
1 | P29293 (/IDA) |
Golgi-associated vesicle GO:0005798
Any vesicle associated with the Golgi complex and involved in mediating transport within the Golgi or between the Golgi and other parts of the cell.
|
1 | P23578 (/ISO) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
1 | Q8BZ10 (/ISO) |
Integral component of plasma membrane GO:0005887
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
1 | Q9UL52 (/ISS) |
Brush border GO:0005903
The dense covering of microvilli on the apical surface of a epithelial cells in tissues such as the intestine, kidney, and choroid plexus; the microvilli aid absorption by increasing the surface area of the cell.
|
1 | P98073 (/TAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | P98072 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | P03951 (/NAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | P98072 (/TAS) |
Basolateral plasma membrane GO:0016323
The region of the plasma membrane that includes the basal end and sides of the cell. Often used in reference to animal polarized epithelial membranes, where the basal membrane is the part attached to the extracellular matrix, or in plant cells, where the basal membrane is defined with respect to the zygotic axis.
|
1 | Q9JJI7 (/IDA) |
Secretory granule GO:0030141
A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
|
1 | P11214 (/IDA) |
Dendrite GO:0030425
A neuron projection that has a short, tapering, morphology. Dendrites receive and integrate signals from other neurons or from sensory stimuli, and conduct nerve impulses towards the axon or the cell body. In most neurons, the impulse is conveyed from dendrites to axon via the cell body, but in some types of unipolar neuron, the impulse does not travel via the cell body.
|
1 | Q1JRP2 (/IDA) |
Protein-containing complex GO:0032991
A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
|
1 | P23578 (/ISO) |
Acrosomal matrix GO:0043159
A structural framework, or 'dense core' at the interior of an acrosome. May regulate the distribution of hydrolases within the acrosome and their release during the acrosome reaction.
|
1 | P79343 (/IDA) |
Acrosomal matrix GO:0043159
A structural framework, or 'dense core' at the interior of an acrosome. May regulate the distribution of hydrolases within the acrosome and their release during the acrosome reaction.
|
1 | P08001 (/NAS) |
Perikaryon GO:0043204
The portion of the cell soma (neuronal cell body) that excludes the nucleus.
|
1 | Q1JRP2 (/IDA) |
Apical part of cell GO:0045177
The region of a polarized cell that forms a tip or is distal to a base. For example, in a polarized epithelial cell, the apical region has an exposed surface and lies opposite to the basal lamina that separates the epithelium from other tissue.
|
1 | P11214 (/IDA) |
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
|
1 | P19637 (/IDA) |
Synapse GO:0045202
The junction between a nerve fiber of one neuron and another neuron, muscle fiber or glial cell. As the nerve fiber approaches the synapse it enlarges into a specialized structure, the presynaptic nerve ending, which contains mitochondria and synaptic vesicles. At the tip of the nerve ending is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic nerve ending secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
|
1 | P11214 (/ISO) |
Serine protease inhibitor complex GO:0097180
A heterodimeric protein complex that contains a serine protease inhibitor and a protease; formation of the complex inhibits serine protease activity.
|
1 | Q2UVH8 (/IDA) |
Schaffer collateral - CA1 synapse GO:0098685
A synapse between the Schaffer collateral axon of a CA3 pyramidal cell and a CA1 pyramidal cell.
|
1 | P11214 (/IMP) |
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
|
1 | P19637 (/IDA) |
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
|
1 | P19637 (/IMP) |
Postsynapse GO:0098794
The part of a synapse that is part of the post-synaptic cell.
|
1 | P11214 (/ISO) |
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
|
1 | P19637 (/IDA) |
Glutamatergic synapse GO:0098978
A synapse that uses glutamate as a neurotransmitter.
|
1 | P11214 (/ISO) |
Neuronal dense core vesicle GO:0098992
A dense core vesicle (granule) that is part of a neuron. These vesicles typically contain neuropeptides. They can be found in all parts of neurons, including the soma, dendrites, axonal swellings (varicosities) and synaptic terminals.
|
1 | P19637 (/IDA) |
Neuronal dense core vesicle GO:0098992
A dense core vesicle (granule) that is part of a neuron. These vesicles typically contain neuropeptides. They can be found in all parts of neurons, including the soma, dendrites, axonal swellings (varicosities) and synaptic terminals.
|
1 | P19637 (/IMP) |
Neuronal dense core vesicle GO:0098992
A dense core vesicle (granule) that is part of a neuron. These vesicles typically contain neuropeptides. They can be found in all parts of neurons, including the soma, dendrites, axonal swellings (varicosities) and synaptic terminals.
|
1 | P11214 (/ISO) |
Perisynaptic space GO:0099544
The extracellular region immediately adjacent to to a synapse.
|
1 | P19637 (/IDA) |
Perisynaptic space GO:0099544
The extracellular region immediately adjacent to to a synapse.
|
1 | P19637 (/IMP) |
Perisynaptic space GO:0099544
The extracellular region immediately adjacent to to a synapse.
|
1 | P11214 (/ISO) |