The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:
"Trypsin-like serine proteases
".
FunFam 46285: Protease serine 2 preproprotein
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 30 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 |
|---|---|---|
|
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).
|
23 |
A0A0B6VLS7 (/ISO)
G3UXD0 (/ISO)
P00755 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P07146 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
P15946 (/ISO)
(13 more) |
|
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).
|
16 |
B5X8S0 (/IDA)
O60259 (/IDA)
P00760 (/IDA)
P00761 (/IDA)
P07478 (/IDA)
P0DJE9 (/IDA)
P15945 (/IDA)
P20151 (/IDA)
P35030 (/IDA)
P84787 (/IDA)
(6 more) |
|
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
14 |
P00755 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
P15946 (/ISO)
P15947 (/ISO)
P15948 (/ISO)
P15949 (/ISO)
(4 more) |
|
Hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides GO:0016811
Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
|
14 |
P00755 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
P15946 (/ISO)
P15947 (/ISO)
P15948 (/ISO)
P15949 (/ISO)
(4 more) |
|
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).
|
12 |
A1Z8J8 (/ISM)
A8JNS0 (/ISM)
C0HKA4 (/ISM)
P04814 (/ISM)
P15945 (/ISM)
P35004 (/ISM)
Q8IRE2 (/ISM)
Q8SYS8 (/ISM)
Q9VAG3 (/ISM)
Q9VQ98 (/ISM)
(2 more) |
|
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).
|
10 | O60259 (/IPI) P00760 (/IPI) P00763 (/IPI) P07288 (/IPI) P07478 (/IPI) P35030 (/IPI) Q92876 (/IPI) Q9H2R5 (/IPI) Q9UKR3 (/IPI) Q9Y5K2 (/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).
|
10 | P07288 (/TAS) P07477 (/TAS) P07478 (/TAS) P35030 (/TAS) P49862 (/TAS) P49863 (/TAS) Q6IE12 (/TAS) Q9H2R5 (/TAS) Q9UBX7 (/TAS) Q9Y5K2 (/TAS) |
|
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).
|
9 | P06870 (/NAS) Q07277 (/NAS) Q61754 (/NAS) Q92876 (/NAS) Q9H2R5 (/NAS) Q9P0G3 (/NAS) Q9UKQ9 (/NAS) Q9UKR0 (/NAS) Q9UKR3 (/NAS) |
|
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.
|
8 | O54854 (/IDA) P15948 (/IDA) P15949 (/IDA) P36368 (/IDA) P36369 (/IDA) Q61759 (/IDA) Q9JM71 (/IDA) Q9UKR0 (/IDA) |
|
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
7 | A0A0G2JSQ7 (/IDA) A0A0G2JX00 (/IDA) A0A0G2K6G1 (/IDA) G3V8H1 (/IDA) P00760 (/IDA) P07288 (/IDA) Q8CGR6 (/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 | O88780 (/ISS) P00763 (/ISS) P06872 (/ISS) P07146 (/ISS) Q29463 (/ISS) Q8CGR5 (/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 | P06870 (/TAS) P07288 (/TAS) P07477 (/TAS) P07478 (/TAS) P20151 (/TAS) P36376 (/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).
|
6 | A0A0B6VPC8 (/ISO) B2RVZ0 (/ISO) G3UXD0 (/ISO) Q3V2E0 (/ISO) Q9QUK9 (/ISO) Q9R0T7 (/ISO) |
|
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
5 | G3UXD0 (/ISO) P07146 (/ISO) Q3V2E0 (/ISO) Q9QUK9 (/ISO) Q9R0T7 (/ISO) |
|
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).
|
5 | P00759 (/IDA) P35030 (/IDA) P49864 (/IDA) Q7SZE2 (/IDA) Q9UKR0 (/IDA) |
|
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
4 | P00763 (/ISS) P06872 (/ISS) P07146 (/ISS) Q29463 (/ISS) |
|
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.
|
3 | A0A0B6VPC8 (/ISO) B2RVZ0 (/ISO) Q91VE3 (/ISO) |
|
Metalloendopeptidase activity GO:0004222
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions.
|
2 | P07478 (/TAS) P49862 (/TAS) |
|
Signal transducer activity, downstream of receptor GO:0005057
Conveys a signal from an upstream receptor or intracellular signal transducer, converting the signal into a form where it can ultimately trigger a change in the state or activity of a cell.
|
2 | P00756 (/IDA) P00757 (/IDA) |
|
Calcium ion binding GO:0005509
Interacting selectively and non-covalently with calcium ions (Ca2+).
|
2 | P07478 (/IDA) P35030 (/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).
|
1 | P07288 (/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 | P49862 (/IMP) |
|
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 | Q9Y5K2 (/NAS) |
|
Hydrolase activity GO:0016787
Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
|
1 | Q9UKR3 (/IDA) |
|
Hydrolase activity GO:0016787
Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
|
1 | Q8CGR6 (/ISO) |
|
Hydrolase activity GO:0016787
Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.
|
1 | Q8CGR6 (/ISS) |
|
Hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides GO:0016811
Catalysis of the hydrolysis of any non-peptide carbon-nitrogen bond in a linear amide.
|
1 | P07288 (/IMP) |
|
Protein heterodimerization activity GO:0046982
Interacting selectively and non-covalently with a nonidentical protein to form a heterodimer.
|
1 | P00760 (/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 | P00760 (/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 | P00760 (/IPI) |
There are 108 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.
|
11 |
A1Z8J8 (/ISM)
A8JNS0 (/ISM)
C0HKA4 (/ISM)
P04814 (/ISM)
P35004 (/ISM)
Q8IRE2 (/ISM)
Q8SYS8 (/ISM)
Q9VAG3 (/ISM)
Q9VQ98 (/ISM)
Q9VS86 (/ISM)
(1 more) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
8 | P00760 (/IDA) P07478 (/IDA) P15945 (/IDA) P35030 (/IDA) Q61759 (/IDA) Q9JM71 (/IDA) Q9P0G3 (/IDA) Q9UKR0 (/IDA) |
|
Response to nutrient GO:0007584
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 nutrient stimulus.
|
6 | A0A0G2JSQ7 (/IEP) A0A0G2JX00 (/IEP) A0A0G2K6G1 (/IEP) G3V8H1 (/IEP) P00762 (/IEP) P00763 (/IEP) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
5 | P00763 (/ISS) P06872 (/ISS) P07146 (/ISS) Q29463 (/ISS) Q8CGR5 (/ISS) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
5 | P35030 (/NAS) Q07277 (/NAS) Q61754 (/NAS) Q9UKR3 (/NAS) Q9Y5K2 (/NAS) |
|
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
5 | P15948 (/IDA) P15949 (/IDA) P35030 (/IDA) P36368 (/IDA) P36369 (/IDA) |
|
Positive regulation of acute inflammatory response GO:0002675
Any process that activates or increases the frequency, rate, or extent of an acute inflammatory response.
|
4 | A0A0G2JSQ7 (/IMP) A0A0G2JX00 (/IMP) A0A0G2K6G1 (/IMP) G3V8H1 (/IMP) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
4 | A0A0B6VPC8 (/ISO) B2RVZ0 (/ISO) P07146 (/ISO) Q8CGR5 (/ISO) |
|
Positive regulation of cell proliferation GO:0008284
Any process that activates or increases the rate or extent of cell proliferation.
|
4 | A0A0G2JSQ7 (/IMP) A0A0G2JX00 (/IMP) A0A0G2K6G1 (/IMP) G3V8H1 (/IMP) |
|
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
|
4 | P07477 (/TAS) P07478 (/TAS) P20151 (/TAS) P49862 (/TAS) |
|
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
|
4 | P00763 (/ISS) P06872 (/ISS) P07146 (/ISS) Q29463 (/ISS) |
|
Positive regulation of apoptotic process GO:0043065
Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
|
4 | A0A0G2JSQ7 (/IMP) A0A0G2JX00 (/IMP) A0A0G2K6G1 (/IMP) G3V8H1 (/IMP) |
|
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).
|
4 | O60259 (/TAS) Q9P0G3 (/TAS) Q9UKR0 (/TAS) Q9UKR3 (/TAS) |
|
Digestion GO:0007586
The whole of the physical, chemical, and biochemical processes carried out by multicellular organisms to break down ingested nutrients into components that may be easily absorbed and directed into metabolism.
|
3 | P00762 (/TAS) P00763 (/TAS) P35030 (/TAS) |
|
Pathogenesis GO:0009405
The set of specific processes that generate the ability of an organism to induce an abnormal, generally detrimental state in another organism.
|
3 | P84787 (/IDA) P84788 (/IDA) Q7SZE2 (/IDA) |
|
Positive regulation of G-protein coupled receptor protein signaling pathway GO:0045745
Any process that activates or increases the frequency, rate or extent of G-protein coupled receptor protein signaling pathway activity.
|
3 | A0A0B6VLS7 (/ISO) Q8CGR5 (/ISO) Q91Y82 (/ISO) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
2 | P35030 (/TAS) Q6IE12 (/TAS) |
|
Memory GO:0007613
The activities involved in the mental information processing system that receives (registers), modifies, stores, and retrieves informational stimuli. The main stages involved in the formation and retrieval of memory are encoding (processing of received information by acquisition), storage (building a permanent record of received information as a result of consolidation) and retrieval (calling back the stored information and use it in a suitable way to execute a given task).
|
2 | O60259 (/ISS) O88780 (/ISS) |
|
Cell death GO:0008219
Any biological process that results in permanent cessation of all vital functions of a cell. A cell should be considered dead when any one of the following molecular or morphological criteria is met: (1) the cell has lost the integrity of its plasma membrane; (2) the cell, including its nucleus, has undergone complete fragmentation into discrete bodies (frequently referred to as apoptotic bodies). The cell corpse (or its fragments) may be engulfed by an adjacent cell in vivo, but engulfment of whole cells should not be considered a strict criteria to define cell death as, under some circumstances, live engulfed cells can be released from phagosomes (see PMID:18045538).
|
2 | O60259 (/ISS) O88780 (/ISS) |
|
Cobalamin metabolic process GO:0009235
The chemical reactions and pathways involving cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom.
|
2 | P07477 (/TAS) P35030 (/TAS) |
|
Response to wounding GO:0009611
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 damage to the organism.
|
2 | O60259 (/ISS) O88780 (/ISS) |
|
Antimicrobial humoral response GO:0019730
An immune response against microbes mediated through a body fluid. Examples of this process are seen in the antimicrobial humoral response of Drosophila melanogaster and Mus musculus.
|
2 | P07478 (/TAS) P35030 (/TAS) |
|
Negative regulation of blood coagulation GO:0030195
Any process that stops, prevents, or reduces the frequency, rate or extent of blood coagulation.
|
2 | P84787 (/IDA) P84788 (/IDA) |
|
Negative regulation of myelination GO:0031642
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
|
2 | O60259 (/ISS) O88780 (/ISS) |
|
Fibrinolysis GO:0042730
A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin.
|
2 | P84787 (/IDA) P84788 (/IDA) |
|
Neutrophil degranulation GO:0043312
The regulated exocytosis of secretory granules containing preformed mediators such as proteases, lipases, and inflammatory mediators by a neutrophil.
|
2 | P07478 (/TAS) P35030 (/TAS) |
|
Endothelial cell migration GO:0043542
The orderly movement of an endothelial cell into the extracellular matrix to form an endothelium.
|
2 | P35030 (/IMP) Q8NHM4 (/IMP) |
|
Keratinocyte proliferation GO:0043616
The multiplication or reproduction of keratinocytes, resulting in the expansion of a cell population. Keratinocytes are epidermal cells which synthesize keratin and undergo a characteristic change as they move upward from the basal layers of the epidermis to the cornified (horny) layer of the skin.
|
2 | O60259 (/ISS) O88780 (/ISS) |
|
Positive regulation of G-protein coupled receptor protein signaling pathway GO:0045745
Any process that activates or increases the frequency, rate or extent of G-protein coupled receptor protein signaling pathway activity.
|
2 | Q92876 (/IDA) Q9P0G3 (/IDA) |
|
Negative regulation of axon regeneration GO:0048681
Any process that stops, prevents, or reduces the frequency, rate or extent of axon regeneration.
|
2 | O60259 (/ISS) O88780 (/ISS) |
|
Neuron projection morphogenesis GO:0048812
The process in which the anatomical structures of a neuron projection are generated and organized. A neuron projection is any process extending from a neural cell, such as axons or dendrites.
|
2 | O60259 (/ISS) O88780 (/ISS) |
|
Regulation of synapse organization GO:0050807
Any process that modulates the physical form of a synapse, the junction between a neuron and a target (neuron, muscle, or secretory cell).
|
2 | O60259 (/ISS) O88780 (/ISS) |
|
Neuron death GO:0070997
The process of cell death in a neuron.
|
2 | A0A0B6VLS7 (/ISO) Q91Y82 (/ISO) |
|
Amelogenesis GO:0097186
The process whose specific outcome is the formation of tooth enamel, occurring in two stages: secretory stage and maturation stage.
|
2 | Q9Y5K2 (/IMP) Q9Z0M1 (/IMP) |
|
Brain renin-angiotensin system GO:0002035
The process in which an angiotensin-mediated signaling system present in the brain regulates the force with which blood passes through the circulatory system.
|
1 | P36369 (/IDA) |
|
Tissue kallikrein-kinin cascade GO:0002255
A series of reactions that takes place outside the cell initiated by the action of tissue (glandular) kallikreins on low molecular weight kininogen in response to tissue damage. Tissue kallikreins are present in glandular tissues and their fluids, such as the salivary glands, sweat glands, pancreas, and kidney. The ultimate products of the tissue kallikrein-kinin cascade include kallidin and bradykinin, agents known to induce smooth muscle contraction, vasoconstriction, and increased vascular permeability.
|
1 | P00755 (/IMP) |
|
Plasma kallikrein-kinin cascade GO:0002353
A series of reactions that takes place outside the cell occurring in response to tissue damage and initiated within blood plasma by the action of activated Factor XII (Hageman Factor) on prekallikrein to convert it to plasma kallikrein, and the subsequent reaction of plasma kallikrein with high molecular weight kininogen. The ultimate product of the plasma kallikrein-kinin cascade is bradykinin, an agent known to induce smooth muscle contraction, vasoconstriction, and increased vascular permeability.
|
1 | Q7SZE2 (/IDA) |
|
Antibacterial peptide production GO:0002778
The synthesis or release of an antibacterial peptide during an immune response, resulting in an increase in intracellular or extracellular levels.
|
1 | P07288 (/IDA) |
|
Positive regulation of antibacterial peptide production GO:0002803
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide production.
|
1 | P49862 (/IMP) |
|
Positive regulation of antibacterial peptide production GO:0002803
Any process that activates or increases the frequency, rate, or extent of antibacterial peptide production.
|
1 | Q91VE3 (/ISO) |
|
Bradykinin biosynthetic process GO:0002936
The chemical reactions and pathways resulting in the formation of the peptide hormone bradykinin.
|
1 | P00755 (/IMP) |
|
Regulation of systemic arterial blood pressure GO:0003073
The process that modulates the force with which blood travels through the systemic arterial circulatory system. The process is controlled by a balance of processes that increase pressure and decrease pressure.
|
1 | P00755 (/IMP) |
|
Left ventricular cardiac muscle tissue morphogenesis GO:0003220
The process in which the anatomical structures of left cardiac ventricle muscle are generated and organized.
|
1 | P00755 (/IMP) |
|
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | P07288 (/IMP) |
|
Small GTPase mediated signal transduction GO:0007264
Any series of molecular signals in which a small monomeric GTPase relays one or more of the signals.
|
1 | P00757 (/IDA) |
|
Central nervous system development GO:0007417
The process whose specific outcome is the progression of the central nervous system over time, from its formation to the mature structure. The central nervous system is the core nervous system that serves an integrating and coordinating function. In vertebrates it consists of the brain and spinal cord. In those invertebrates with a central nervous system it typically consists of a brain, cerebral ganglia and a nerve cord.
|
1 | Q92876 (/NAS) |
|
Memory GO:0007613
The activities involved in the mental information processing system that receives (registers), modifies, stores, and retrieves informational stimuli. The main stages involved in the formation and retrieval of memory are encoding (processing of received information by acquisition), storage (building a permanent record of received information as a result of consolidation) and retrieval (calling back the stored information and use it in a suitable way to execute a given task).
|
1 | Q61955 (/IMP) |
|
Cell death GO:0008219
Any biological process that results in permanent cessation of all vital functions of a cell. A cell should be considered dead when any one of the following molecular or morphological criteria is met: (1) the cell has lost the integrity of its plasma membrane; (2) the cell, including its nucleus, has undergone complete fragmentation into discrete bodies (frequently referred to as apoptotic bodies). The cell corpse (or its fragments) may be engulfed by an adjacent cell in vivo, but engulfment of whole cells should not be considered a strict criteria to define cell death as, under some circumstances, live engulfed cells can be released from phagosomes (see PMID:18045538).
|
1 | Q61955 (/IMP) |
|
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.
|
1 | P49862 (/TAS) |
|
Fertilization GO:0009566
The union of gametes of opposite sexes during the process of sexual reproduction to form a zygote. It involves the fusion of the gametic nuclei (karyogamy) and cytoplasm (plasmogamy).
|
1 | Q9P0G3 (/IDA) |
|
Fertilization GO:0009566
The union of gametes of opposite sexes during the process of sexual reproduction to form a zygote. It involves the fusion of the gametic nuclei (karyogamy) and cytoplasm (plasmogamy).
|
1 | Q8CGR5 (/ISO) |
|
Fertilization GO:0009566
The union of gametes of opposite sexes during the process of sexual reproduction to form a zygote. It involves the fusion of the gametic nuclei (karyogamy) and cytoplasm (plasmogamy).
|
1 | Q8CGR5 (/ISS) |
|
Response to wounding GO:0009611
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 damage to the organism.
|
1 | Q61955 (/IDA) |
|
Response to wounding GO:0009611
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 damage to the organism.
|
1 | Q92876 (/NAS) |
|
Response to organic substance GO:0010033
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 organic substance stimulus.
|
1 | P00762 (/IEP) |
|
Regulation of neuron projection development GO:0010975
Any process that modulates the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites).
|
1 | O54854 (/IDA) |
|
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
|
1 | Q8CGR6 (/IDA) |
|
Negative regulation of angiogenesis GO:0016525
Any process that stops, prevents, or reduces the frequency, rate or extent of angiogenesis.
|
1 | P07288 (/NAS) |
|
Protein autoprocessing GO:0016540
Processing which a protein carries out itself. This involves actions such as the autolytic removal of residues to generate the mature form of the protein.
|
1 | Q92876 (/NAS) |
|
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
|
1 | Q9Z0M1 (/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 | Q9Z0M1 (/IMP) |
|
Positive regulation of blood coagulation GO:0030194
Any process that activates or increases the frequency, rate or extent of blood coagulation.
|
1 | P85109 (/IDA) |
|
Positive regulation of cell growth GO:0030307
Any process that activates or increases the frequency, rate, extent or direction of cell growth.
|
1 | P07478 (/TAS) |
|
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
|
1 | P07478 (/IDA) |
|
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
|
1 | P07478 (/IMP) |
|
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
|
1 | P07146 (/ISO) |
|
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
|
1 | Q92876 (/NAS) |
|
Collagen catabolic process GO:0030574
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells.
|
1 | P07478 (/TAS) |
|
Response to caffeine GO:0031000
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 caffeine stimulus. Caffeine is an alkaloid found in numerous plant species, where it acts as a natural pesticide that paralyzes and kills certain insects feeding upon them.
|
1 | P00762 (/IDA) |
|
Post-embryonic camera-type eye development GO:0031077
The process occurring during the post-embryonic phase whose specific outcome is the progression of the camera-type eye over time, from its formation to the mature structure.
|
1 | Q91036 (/TAS) |
|
Negative regulation of myelination GO:0031642
Any process that stops, prevents, or reduces the frequency, rate or extent of the formation of a myelin sheath around nerve axons.
|
1 | Q61955 (/IMP) |
|
Response to food GO:0032094
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 food stimulus; food is anything which, when taken into the body, serves to nourish or build up the tissues or to supply body heat.
|
1 | B5X8S0 (/IDA) |
|
Response to nicotine GO:0035094
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 nicotine stimulus.
|
1 | P00762 (/IDA) |
|
Tissue regeneration GO:0042246
The regrowth of lost or destroyed tissues.
|
1 | Q92876 (/NAS) |
|
Vasodilation GO:0042311
An increase in the internal diameter of blood vessels, especially arterioles or capillaries, due to relaxation of smooth muscle cells that line the vessels, and usually resulting in a decrease in blood pressure.
|
1 | P00755 (/IMP) |
|
Hormone metabolic process GO:0042445
The chemical reactions and pathways involving any hormone, naturally occurring substances secreted by specialized cells that affects the metabolism or behavior of other cells possessing functional receptors for the hormone.
|
1 | Q92876 (/NAS) |
|
Myelination GO:0042552
The process in which myelin sheaths are formed and maintained around neurons. Oligodendrocytes in the brain and spinal cord and Schwann cells in the peripheral nervous system wrap axons with compact layers of their plasma membrane. Adjacent myelin segments are separated by a non-myelinated stretch of axon called a node of Ranvier.
|
1 | Q92876 (/NAS) |
|
Response to starvation GO:0042594
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 starvation stimulus, deprivation of nourishment.
|
1 | B5X8S0 (/IDA) |
|
Amyloid precursor protein metabolic process GO:0042982
The chemical reactions and pathways involving amyloid precursor protein (APP), the precursor of beta-amyloid, a glycoprotein associated with Alzheimer's disease.
|
1 | Q92876 (/NAS) |
|
Positive regulation of phosphatidylinositol 3-kinase activity GO:0043552
Any process that activates or increases the frequency, rate or extent of phosphatidylinositol 3-kinase activity.
|
1 | P00757 (/IDA) |
|
Keratinocyte proliferation GO:0043616
The multiplication or reproduction of keratinocytes, resulting in the expansion of a cell population. Keratinocytes are epidermal cells which synthesize keratin and undergo a characteristic change as they move upward from the basal layers of the epidermis to the cornified (horny) layer of the skin.
|
1 | Q61955 (/IMP) |
|
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 | B5X8S0 (/IDA) |
|
Cellular protein metabolic process GO:0044267
The chemical reactions and pathways involving a specific protein, rather than of proteins in general, occurring at the level of an individual cell. Includes cellular protein modification.
|
1 | P07288 (/TAS) |
|
Envenomation resulting in positive regulation of platelet aggregation in other organism GO:0044478
A process that begins with venom being forced into an organism by the bite or sting of another organism, and ends with the resultant activation, maintenance or an increase in the frequency, rate or extent of platelet aggregation in the bitten organism.
|
1 | P0DJE9 (/IDA) |
|
Envenomation resulting in proteolysis in other organism GO:0044481
A process that begins with venom being forced into an organism by the bite or sting of another organism, and ends with the resultant hydrolysis of proteins in of the bitten organism.
|
1 | P0DJE9 (/IDA) |
|
Envenomation resulting in fibrinogenolysis in other organism GO:0044485
The process which begins with venom being forced into an organism by the bite or sting of another organism, and ends with fibrinogenolysis, a process that degrades fibrinogen at a variety of Arg-Lys bonds, thus impairing fibrinogen clotting in the bloodstream of the bitten/stung organism.
|
1 | P0DJE9 (/IDA) |
|
Regulation of cell differentiation GO:0045595
Any process that modulates the frequency, rate or extent of cell differentiation, the process in which relatively unspecialized cells acquire specialized structural and functional features.
|
1 | Q92876 (/NAS) |
|
Negative regulation of G-protein coupled receptor protein signaling pathway GO:0045744
Any process that stops, prevents, or reduces the frequency, rate or extent of G-protein coupled receptor protein signaling pathway activity.
|
1 | Q9P0G3 (/IDA) |
|
Negative regulation of G-protein coupled receptor protein signaling pathway GO:0045744
Any process that stops, prevents, or reduces the frequency, rate or extent of G-protein coupled receptor protein signaling pathway activity.
|
1 | Q8CGR5 (/ISO) |
|
Negative regulation of G-protein coupled receptor protein signaling pathway GO:0045744
Any process that stops, prevents, or reduces the frequency, rate or extent of G-protein coupled receptor protein signaling pathway activity.
|
1 | Q8CGR5 (/ISS) |
|
Positive regulation of G-protein coupled receptor protein signaling pathway GO:0045745
Any process that activates or increases the frequency, rate or extent of G-protein coupled receptor protein signaling pathway activity.
|
1 | Q8CGR5 (/ISS) |
|
Positive regulation of cell adhesion GO:0045785
Any process that activates or increases the frequency, rate or extent of cell adhesion.
|
1 | P07478 (/TAS) |
|
Positive regulation of vasoconstriction GO:0045907
Any process that activates or increases the frequency, rate or extent of vasoconstriction.
|
1 | P07647 (/IDA) |
|
Negative regulation of axon regeneration GO:0048681
Any process that stops, prevents, or reduces the frequency, rate or extent of axon regeneration.
|
1 | Q61955 (/IMP) |
|
Epidermis morphogenesis GO:0048730
The process in which the anatomical structures of the epidermis are generated and organized. 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.
|
1 | Q9P0G3 (/IDA) |
|
Epidermis morphogenesis GO:0048730
The process in which the anatomical structures of the epidermis are generated and organized. 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.
|
1 | Q8CGR5 (/ISO) |
|
Epidermis morphogenesis GO:0048730
The process in which the anatomical structures of the epidermis are generated and organized. 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.
|
1 | Q8CGR5 (/ISS) |
|
Neuron projection morphogenesis GO:0048812
The process in which the anatomical structures of a neuron projection are generated and organized. A neuron projection is any process extending from a neural cell, such as axons or dendrites.
|
1 | Q61955 (/IDA) |
|
Regulation of synapse organization GO:0050807
Any process that modulates the physical form of a synapse, the junction between a neuron and a target (neuron, muscle, or secretory cell).
|
1 | Q61955 (/IMP) |
|
Synapse organization GO:0050808
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a synapse, the junction between a neuron and a target (neuron, muscle, or secretory cell).
|
1 | Q61955 (/IMP) |
|
Cardiac muscle contraction GO:0060048
Muscle contraction of cardiac muscle tissue.
|
1 | P00755 (/IMP) |
|
Seminal clot liquefaction GO:0070684
The reproductive process in which coagulated semen becomes liquid following ejaculation, allowing the progressive release of motile spermatozoa.
|
1 | Q9P0G3 (/IDA) |
|
Seminal clot liquefaction GO:0070684
The reproductive process in which coagulated semen becomes liquid following ejaculation, allowing the progressive release of motile spermatozoa.
|
1 | Q8CGR5 (/ISO) |
|
Seminal clot liquefaction GO:0070684
The reproductive process in which coagulated semen becomes liquid following ejaculation, allowing the progressive release of motile spermatozoa.
|
1 | Q8CGR5 (/ISS) |
|
Neuron death GO:0070997
The process of cell death in a neuron.
|
1 | Q92876 (/IMP) |
|
Amelogenesis GO:0097186
The process whose specific outcome is the formation of tooth enamel, occurring in two stages: secretory stage and maturation stage.
|
1 | Q9Z0M1 (/ISO) |
|
Positive regulation of cytokine production involved in inflammatory response GO:1900017
Any process that activates or increases the frequency, rate or extent of cytokine production involved in inflammatory response.
|
1 | B5X8S0 (/IMP) |
|
Positive regulation of interleukin-8 secretion GO:2000484
Any process that activates or increases the frequency, rate or extent of interleukin-8 secretion.
|
1 | B5X8S0 (/IMP) |
There are 32 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.
|
24 |
A0A0B6VLS7 (/ISO)
G3UXD0 (/ISO)
P00755 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P07146 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
P15946 (/ISO)
(14 more) |
|
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.
|
24 |
A0A0B6VPC8 (/ISO)
B2RVZ0 (/ISO)
G3UXD0 (/ISO)
P00755 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
P15946 (/ISO)
(14 more) |
|
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.
|
14 |
P00755 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
P15946 (/ISO)
P15947 (/ISO)
P15948 (/ISO)
P15949 (/ISO)
(4 more) |
|
Protein complex GO:0043234
A stable macromolecular complex composed (only) of two or more polypeptide subunits along with any covalently attached molecules (such as lipid anchors or oligosaccharide) or non-protein prosthetic groups (such as nucleotides or metal ions). Prosthetic group in this context refers to a tightly bound cofactor. The component polypeptide subunits may be identical.
|
14 |
P00755 (/ISO)
P00756 (/ISO)
P00757 (/ISO)
P04071 (/ISO)
P07628 (/ISO)
P15945 (/ISO)
P15946 (/ISO)
P15947 (/ISO)
P15948 (/ISO)
P15949 (/ISO)
(4 more) |
|
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.
|
11 |
O60259 (/TAS)
P07288 (/TAS)
P07477 (/TAS)
P07478 (/TAS)
P20151 (/TAS)
P35030 (/TAS)
P49862 (/TAS)
Q9P0G3 (/TAS)
Q9UKR0 (/TAS)
Q9UKR3 (/TAS)
(1 more) |
|
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.
|
11 |
P00762 (/IDA)
P07288 (/IDA)
P35030 (/IDA)
P36368 (/IDA)
P36369 (/IDA)
Q61759 (/IDA)
Q61955 (/IDA)
Q8CGR6 (/IDA)
Q92876 (/IDA)
Q9P0G3 (/IDA)
(1 more) |
|
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.
|
9 | B5X8S0 (/IDA) P07478 (/IDA) P0DJE9 (/IDA) P84787 (/IDA) P84788 (/IDA) P85109 (/IDA) Q7SZE2 (/IDA) Q92876 (/IDA) Q9QYN3 (/IDA) |
|
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.
|
9 | P06870 (/IDA) P07288 (/IDA) P07477 (/IDA) P20151 (/IDA) P35030 (/IDA) Q9P0G3 (/IDA) Q9UBX7 (/IDA) Q9UKR0 (/IDA) Q9UKR3 (/IDA) |
|
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 | O60259 (/ISS) O88780 (/ISS) P00763 (/ISS) P06872 (/ISS) P07146 (/ISS) Q29463 (/ISS) Q8CGR5 (/ISS) |
|
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.
|
6 | A0A0G2JSQ7 (/IDA) A0A0G2JX00 (/IDA) A0A0G2K6G1 (/IDA) G3V8H1 (/IDA) P06870 (/IDA) P07288 (/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.
|
5 | P00763 (/ISS) P06872 (/ISS) P07146 (/ISS) Q29463 (/ISS) Q91Y82 (/ISS) |
|
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.
|
4 | A0A0G2JSQ7 (/IDA) A0A0G2JX00 (/IDA) A0A0G2K6G1 (/IDA) G3V8H1 (/IDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
4 | O60259 (/IDA) Q61955 (/IDA) Q92876 (/IDA) Q9UKR3 (/IDA) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
4 | A0A0B6VLS7 (/ISO) Q61955 (/ISO) Q8CGR6 (/ISO) Q91Y82 (/ISO) |
|
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.
|
4 | A0A0G2JSQ7 (/IDA) A0A0G2JX00 (/IDA) A0A0G2K6G1 (/IDA) G3V8H1 (/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.
|
3 | A0A0B6VLS7 (/ISO) P07146 (/ISO) Q91Y82 (/ISO) |
|
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 | P07288 (/NAS) P07477 (/NAS) |
|
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.
|
2 | P07478 (/IMP) P49862 (/IMP) |
|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | Q8CGR6 (/ISS) Q91Y82 (/ISS) |
|
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.
|
1 | Q9UKR0 (/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 | B5X8S0 (/IDA) |
|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | C0HKA2 (/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 | Q8CGR6 (/IDA) |
|
Extracellular matrix GO:0031012
A structure lying external to one or more cells, which provides structural support for cells or tissues.
|
1 | P07478 (/TAS) |
|
Azurophil granule lumen GO:0035578
The volume enclosed by the membrane of an azurophil granule, a primary lysosomal granule found in neutrophil granulocytes that contains a wide range of hydrolytic enzymes and is released into the extracellular fluid.
|
1 | P07478 (/TAS) |
|
Protein complex GO:0043234
A stable macromolecular complex composed (only) of two or more polypeptide subunits along with any covalently attached molecules (such as lipid anchors or oligosaccharide) or non-protein prosthetic groups (such as nucleotides or metal ions). Prosthetic group in this context refers to a tightly bound cofactor. The component polypeptide subunits may be identical.
|
1 | P07288 (/IDA) |
|
Blood microparticle GO:0072562
A phospholipid microvesicle that is derived from any of several cell types, such as platelets, blood cells, endothelial cells, or others, and contains membrane receptors as well as other proteins characteristic of the parental cell. Microparticles are heterogeneous in size, and are characterized as microvesicles free of nucleic acids.
|
1 | P07477 (/IDA) |
|
Blood microparticle GO:0072562
A phospholipid microvesicle that is derived from any of several cell types, such as platelets, blood cells, endothelial cells, or others, and contains membrane receptors as well as other proteins characteristic of the parental cell. Microparticles are heterogeneous in size, and are characterized as microvesicles free of nucleic acids.
|
1 | Q792Z1 (/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 | P00760 (/IDA) |
|
Epidermal lamellar body GO:0097209
A specialized secretory organelle found in keratinocytes and involved in the formation of an impermeable, lipid-containing membrane that serves as a water barrier and is required for correct skin barrier function.
|
1 | P49862 (/IDA) |
|
Epidermal lamellar body GO:0097209
A specialized secretory organelle found in keratinocytes and involved in the formation of an impermeable, lipid-containing membrane that serves as a water barrier and is required for correct skin barrier function.
|
1 | Q91VE3 (/ISO) |
|
Tertiary granule lumen GO:1904724
Any membrane-enclosed lumen that is part of a tertiary granule.
|
1 | P35030 (/TAS) |