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:
"Peptidase S8/S53 domain
".
FunFam 1: Furin 2, isoform B
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 22 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).
|
6 | A0A044RE18 (/IDA) P09958 (/IDA) P09958 (/IDA) P26016 (/IDA) P30430 (/IDA) P30432 (/IDA) |
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).
|
5 | P09958 (/IPI) P09958 (/IPI) P23188 (/IPI) Q6UW60 (/IPI) Q6UW60 (/IPI) |
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 | O17798 (/IMP) P09958 (/IMP) P09958 (/IMP) P23377 (/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).
|
4 | P23188 (/ISS) P23377 (/ISS) P29119 (/ISS) Q28193 (/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).
|
3 | P26016 (/IGI) P30430 (/IGI) P30432 (/IGI) |
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).
|
3 | P09958 (/TAS) P09958 (/TAS) P23188 (/TAS) |
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
2 | P09958 (/IPI) P09958 (/IPI) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Serine-type endopeptidase inhibitor activity GO:0004867
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme.
|
2 | P09958 (/IDA) P09958 (/IDA) |
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.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Peptide binding GO:0042277
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Nerve growth factor binding GO:0048406
Interacting selectively and non-covalently with nerve growth factor (NGF).
|
2 | P09958 (/IDA) P09958 (/IDA) |
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
1 | P23188 (/ISO) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
1 | P23188 (/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).
|
1 | P23188 (/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).
|
1 | P51559 (/NAS) |
Serine-type endopeptidase inhibitor activity GO:0004867
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme.
|
1 | P23188 (/ISO) |
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 | O17798 (/IPI) |
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 | P23188 (/ISO) |
Peptide binding GO:0042277
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
|
1 | P23188 (/ISO) |
Nerve growth factor binding GO:0048406
Interacting selectively and non-covalently with nerve growth factor (NGF).
|
1 | P23188 (/ISO) |
There are 100 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 |
---|---|---|
Cartilage development GO:0051216
The process whose specific outcome is the progression of a cartilage element over time, from its formation to the mature structure. Cartilage elements are skeletal elements that consist of connective tissue dominated by extracellular matrix containing collagen type II and large amounts of proteoglycan, particularly chondroitin sulfate.
|
7 | A0A2R8QME4 (/IGI) A0A2R8QU31 (/IGI) B0S6Y3 (/IGI) F1QKU2 (/IGI) F1QQ43 (/IGI) Q1KHF8 (/IGI) Q1KHF9 (/IGI) |
Cartilage development GO:0051216
The process whose specific outcome is the progression of a cartilage element over time, from its formation to the mature structure. Cartilage elements are skeletal elements that consist of connective tissue dominated by extracellular matrix containing collagen type II and large amounts of proteoglycan, particularly chondroitin sulfate.
|
7 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QKU2 (/IMP) F1QQ43 (/IMP) Q1KHF8 (/IMP) Q1KHF9 (/IMP) |
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.
|
6 | P09958 (/IDA) P09958 (/IDA) P23188 (/IDA) P23377 (/IDA) Q6UW60 (/IDA) Q6UW60 (/IDA) |
Heart looping GO:0001947
The tube morphogenesis process in which the primitive heart tube loops asymmetrically. This looping brings the primitive heart chambers into alignment preceding their future integration. Heart looping begins with dextral-looping and ends when the main regional divisions of the mature heart and primordium of the great arterial trunks become established preceeding septation.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Determination of left/right asymmetry in lateral mesoderm GO:0003140
The establishment of the lateral mesoderm with respect to the left and right halves.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Heart jogging GO:0003146
The morphogenetic process in which the heart cone is displaced to the left with respect to the vector of the anterior-posterior axis.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Response to bacterium GO:0009617
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 from a bacterium.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Fin morphogenesis GO:0033334
The process in which the anatomical structures of a fin are generated and organized.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Embryonic viscerocranium morphogenesis GO:0048703
The process in which the anatomical structures of the viscerocranium are generated and organized during the embryonic phase. The viscerocranium is the part of the skull comprising the facial bones.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Cartilage morphogenesis GO:0060536
The process in which the anatomical structures of cartilage are generated and organized.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Determination of heart left/right asymmetry GO:0061371
Determination of the asymmetric location of the heart with respect to the left and right halves of the organism.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Determination of digestive tract left/right asymmetry GO:0071907
Determination of the asymmetric location of various parts of the digestive tract with respect to the left and right halves of the organism. The digestive tract is the anatomical structure through which food passes and is processed.
|
5 | A0A2R8QME4 (/IMP) A0A2R8QU31 (/IMP) B0S6Y3 (/IMP) F1QQ43 (/IMP) Q1KHF9 (/IMP) |
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.
|
4 | P09958 (/IMP) P09958 (/IMP) P23188 (/IMP) P23377 (/IMP) |
Positive regulation of transforming growth factor beta1 activation GO:1901394
Any process that activates or increases the frequency, rate or extent of transforming growth factor beta1 activation.
|
4 | P23188 (/ISS) P23377 (/ISS) P29119 (/ISS) Q28193 (/ISS) |
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.
|
3 | Q6UW60 (/ISS) Q6UW60 (/ISS) Q78EH2 (/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.
|
3 | Q6UW60 (/ISS) Q6UW60 (/ISS) Q78EH2 (/ISS) |
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).
|
3 | Q6UW60 (/ISS) Q6UW60 (/ISS) Q78EH2 (/ISS) |
Reproductive process GO:0022414
A biological process that directly contributes to the process of producing new individuals by one or two organisms. The new individuals inherit some proportion of their genetic material from the parent or parents.
|
3 | Q6UW60 (/ISS) Q6UW60 (/ISS) Q78EH2 (/ISS) |
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
3 | O17798 (/IMP) P09958 (/IMP) P09958 (/IMP) |
Sperm capacitation GO:0048240
A process required for sperm to reach fertilization competence. Sperm undergo an incompletely understood series of morphological and molecular maturational processes, termed capacitation, involving, among other processes, protein tyrosine phosphorylation and increased intracellular calcium.
|
3 | Q6UW60 (/ISS) Q6UW60 (/ISS) Q78EH2 (/ISS) |
Postsynaptic membrane organization GO:0001941
A process which results in the assembly, arrangement of constituent parts, or disassembly of a postsynaptic membrane, the specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft).
|
2 | P26016 (/IMP) P30430 (/IMP) |
Signal peptide processing GO:0006465
The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Signal peptide processing GO:0006465
The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Transforming growth factor beta receptor signaling pathway GO:0007179
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Synaptic target recognition GO:0008039
The process in which a neuronal cell in a multicellular organism interprets signals produced by potential target cells, with which it may form synapses.
|
2 | P26016 (/IMP) P30430 (/IMP) |
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.
|
2 | P23188 (/ISO) P29121 (/ISO) |
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.
|
2 | P29121 (/ISS) Q78EH2 (/ISS) |
Peptide hormone processing GO:0016486
The generation of a mature peptide hormone by posttranslational processing of a prohormone.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Viral life cycle GO:0019058
A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome.
|
2 | P09958 (/IEP) P09958 (/IEP) |
Viral protein processing GO:0019082
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Extracellular matrix disassembly GO:0022617
A process that results in the breakdown of the extracellular matrix.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Extracellular matrix organization GO:0030198
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
|
2 | P09958 (/TAS) P09958 (/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.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Nerve growth factor processing GO:0032455
The generation of a mature nerve growth factor (NGF) by proteolysis of a precursor.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Negative regulation of low-density lipoprotein particle receptor catabolic process GO:0032804
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Nerve growth factor production GO:0032902
The appearance of nerve growth factor (NGF) due to biosynthesis or secretion by cells in a neuron's target field, resulting in an increase in its intracellular or extracellular levels.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Negative regulation of transforming growth factor beta1 production GO:0032911
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
|
2 | P09958 (/IMP) P09958 (/IMP) |
Secretion by cell GO:0032940
The controlled release of a substance by a cell.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Regulation of protein catabolic process GO:0042176
Any process that modulates the frequency, rate or extent of 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.
|
2 | P09958 (/IMP) P09958 (/IMP) |
Peptide biosynthetic process GO:0043043
The chemical reactions and pathways resulting in the formation of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. This may include the translation of a precursor protein and its subsequent processing into a functional peptide.
|
2 | P09958 (/IDA) P09958 (/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.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Positive regulation of synaptic growth at neuromuscular junction GO:0045887
Any process that activates or increases the frequency, rate or extent of synaptic growth at neuromuscular junction.
|
2 | O17798 (/IGI) P51559 (/IGI) |
Regulation of lipoprotein lipase activity GO:0051004
Any process that modulates the activity of the enzyme lipoprotein lipase.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Positive regulation of membrane protein ectodomain proteolysis GO:0051044
Any process that activates or increases the frequency, rate or extent of membrane protein ectodomain peptidolysis.
|
2 | P09958 (/IC) P09958 (/IC) |
Regulation of endopeptidase activity GO:0052548
Any process that modulates the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins.
|
2 | P09958 (/IDA) P09958 (/IDA) |
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).
|
2 | P09958 (/TAS) P09958 (/TAS) |
Dibasic protein processing GO:0090472
Any protein processing achieved by the cleavage of a peptide bond after two basic amino acids within a protein.
|
2 | P09958 (/IMP) P09958 (/IMP) |
Presynaptic membrane organization GO:0097090
A process which results in the assembly, arrangement of constituent parts, or disassembly of a presynaptic membrane, including any proteins associated with the membrane, but excluding other cellular components. A presynaptic membrane is a specialized area of membrane of the axon terminal that faces the plasma membrane of the neuron or muscle fiber with which the axon terminal establishes a synaptic junction.
|
2 | P26016 (/IMP) P30430 (/IMP) |
Glutamate receptor clustering GO:0097688
The neurotransmitter-gated ion channel clustering process in which glutamate receptors are localized to distinct domains in the cell membrane.
|
2 | P26016 (/IMP) P30430 (/IMP) |
Positive regulation of transforming growth factor beta1 activation GO:1901394
Any process that activates or increases the frequency, rate or extent of transforming growth factor beta1 activation.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Signal peptide processing GO:0006465
The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell.
|
1 | P23188 (/ISO) |
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 | P29121 (/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 | P29121 (/IMP) |
Aging GO:0007568
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
|
1 | P23377 (/IEP) |
Chemosensory behavior GO:0007635
Behavior that is dependent upon the sensation of chemicals.
|
1 | P51559 (/IMP) |
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 | P29121 (/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 | P29121 (/IMP) |
Regulation of signal transduction GO:0009966
Any process that modulates the frequency, rate or extent of signal transduction.
|
1 | P23188 (/IDA) |
Gene expression GO:0010467
The process in which a gene's sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
|
1 | O17798 (/IMP) |
Peptide hormone processing GO:0016486
The generation of a mature peptide hormone by posttranslational processing of a prohormone.
|
1 | P23188 (/ISO) |
Reproductive process GO:0022414
A biological process that directly contributes to the process of producing new individuals by one or two organisms. The new individuals inherit some proportion of their genetic material from the parent or parents.
|
1 | P29121 (/IMP) |
Insulin processing GO:0030070
The formation of mature insulin by proteolysis of the precursor preproinsulin. The signal sequence is first cleaved from preproinsulin to form proinsulin; proinsulin is then cleaved to release the C peptide, leaving the A and B chains of mature insulin linked by disulfide bridges.
|
1 | O17798 (/IMP) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
1 | P23377 (/IMP) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
1 | P23188 (/ISO) |
Positive regulation of transforming growth factor beta receptor signaling pathway GO:0030511
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
|
1 | P23377 (/IMP) |
Positive regulation of transforming growth factor beta receptor signaling pathway GO:0030511
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
|
1 | P23188 (/ISO) |
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
1 | A0A044RE18 (/IDA) |
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
1 | P23188 (/ISO) |
Negative regulation of low-density lipoprotein particle receptor catabolic process GO:0032804
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
|
1 | P23188 (/ISO) |
Nerve growth factor production GO:0032902
The appearance of nerve growth factor (NGF) due to biosynthesis or secretion by cells in a neuron's target field, resulting in an increase in its intracellular or extracellular levels.
|
1 | P23188 (/ISO) |
Negative regulation of transforming growth factor beta1 production GO:0032911
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
|
1 | P23188 (/ISO) |
Secretion by cell GO:0032940
The controlled release of a substance by a cell.
|
1 | P23188 (/ISO) |
Protein localization to endosome GO:0036010
A process in which a protein is transported to, or maintained in, a location within an endosome.
|
1 | O17798 (/IMP) |
Collagen and cuticulin-based cuticle development GO:0040002
Synthesis and deposition of a collagen and cuticulin-based noncellular, hardened, or membranous secretion from an epithelial sheet. An example of this process is found in Caenorhabditis elegans.
|
1 | P51559 (/IMP) |
Regulation of protein catabolic process GO:0042176
Any process that modulates the frequency, rate or extent of 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 | P23188 (/ISO) |
Peptide biosynthetic process GO:0043043
The chemical reactions and pathways resulting in the formation of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. This may include the translation of a precursor protein and its subsequent processing into a functional peptide.
|
1 | P23188 (/ISO) |
R8 cell fate specification GO:0045464
The process in which a cell becomes capable of differentiating autonomously into an R8 cell in an environment that is neutral with respect to the developmental pathway; upon specification, the cell fate can be reversed.
|
1 | P30432 (/IMP) |
Regulation of low-density lipoprotein particle receptor biosynthetic process GO:0045714
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of low-density lipoprotein particle receptors.
|
1 | P23188 (/IMP) |
Sperm capacitation GO:0048240
A process required for sperm to reach fertilization competence. Sperm undergo an incompletely understood series of morphological and molecular maturational processes, termed capacitation, involving, among other processes, protein tyrosine phosphorylation and increased intracellular calcium.
|
1 | P29121 (/IDA) |
Sperm capacitation GO:0048240
A process required for sperm to reach fertilization competence. Sperm undergo an incompletely understood series of morphological and molecular maturational processes, termed capacitation, involving, among other processes, protein tyrosine phosphorylation and increased intracellular calcium.
|
1 | P29121 (/IMP) |
Dendrite morphogenesis GO:0048813
The process in which the anatomical structures of a dendrite are generated and organized.
|
1 | O17798 (/IMP) |
Regulation of dendrite morphogenesis GO:0048814
Any process that modulates the frequency, rate or extent of dendrite morphogenesis.
|
1 | O17798 (/IGI) |
Positive regulation of dendrite morphogenesis GO:0050775
Any process that activates or increases the frequency, rate or extent of dendrite morphogenesis.
|
1 | O17798 (/IGI) |
Positive regulation of dendrite morphogenesis GO:0050775
Any process that activates or increases the frequency, rate or extent of dendrite morphogenesis.
|
1 | O17798 (/IMP) |
Negative regulation of secretion GO:0051048
Any process that stops, prevents, or reduces the frequency, rate or extent of the controlled release of a substance from a cell or a tissue.
|
1 | P30432 (/IGI) |
Regulation of endopeptidase activity GO:0052548
Any process that modulates the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins.
|
1 | P23188 (/ISO) |
Cartilage morphogenesis GO:0060536
The process in which the anatomical structures of cartilage are generated and organized.
|
1 | Q1KHF9 (/IGI) |
Dendrite self-avoidance GO:0070593
The process in which dendrites recognize and avoid contact with sister dendrites from the same cell.
|
1 | O17798 (/IGI) |
Dendrite self-avoidance GO:0070593
The process in which dendrites recognize and avoid contact with sister dendrites from the same cell.
|
1 | O17798 (/IMP) |
Dibasic protein processing GO:0090472
Any protein processing achieved by the cleavage of a peptide bond after two basic amino acids within a protein.
|
1 | A0A044RE18 (/IDA) |
Dibasic protein processing GO:0090472
Any protein processing achieved by the cleavage of a peptide bond after two basic amino acids within a protein.
|
1 | P23188 (/ISO) |
Positive regulation of dendrite development GO:1900006
Any process that activates or increases the frequency, rate or extent of dendrite development.
|
1 | O17798 (/IMP) |
Positive regulation of transforming growth factor beta1 activation GO:1901394
Any process that activates or increases the frequency, rate or extent of transforming growth factor beta1 activation.
|
1 | P23188 (/ISO) |
Cellular response to salt GO:1902075
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 salt stimulus.
|
1 | P51559 (/IGI) |
Cellular response to salt GO:1902075
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 salt stimulus.
|
1 | P51559 (/IMP) |
Regulation of dendrite extension GO:1903859
Any process that modulates the frequency, rate or extent of dendrite extension.
|
1 | O17798 (/IGI) |
Positive regulation of dendrite extension GO:1903861
Any process that activates or increases the frequency, rate or extent of dendrite extension.
|
1 | O17798 (/IMP) |
Negative regulation of dauer entry GO:1905910
Any process that stops, prevents or reduces the frequency, rate or extent of dauer entry.
|
1 | O17798 (/IGI) |
Negative regulation of protein localization to cell surface GO:2000009
Any process that stops, prevents, or reduces the frequency, rate or extent of protein localization to the cell surface.
|
1 | O17798 (/IMP) |
Regulation of neuron migration GO:2001222
Any process that modulates the frequency, rate or extent of neuron migration.
|
1 | O17798 (/IMP) |
There are 37 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 |
---|---|---|
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.
|
3 | Q6UW60 (/ISS) Q6UW60 (/ISS) Q78EH2 (/ISS) |
Acrosomal membrane GO:0002080
The membrane that surrounds the acrosomal lumen. The acrosome is a special type of lysosome 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.
|
3 | Q6UW60 (/ISS) Q6UW60 (/ISS) Q78EH2 (/ISS) |
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 | P09958 (/TAS) P09958 (/TAS) P23188 (/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.
|
3 | P23377 (/IDA) P26016 (/IDA) P30430 (/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 | P26016 (/ISS) P30430 (/ISS) P30432 (/ISS) |
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
2 | P09958 (/IMP) P09958 (/IMP) |
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
2 | P09958 (/IGI) P09958 (/IGI) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | P23188 (/TAS) P29121 (/TAS) |
Golgi lumen GO:0005796
The volume enclosed by the membranes of any cisterna or subcompartment of the Golgi apparatus, including the cis- and trans-Golgi networks.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Trans-Golgi network GO:0005802
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
|
2 | P09958 (/IDA) P09958 (/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.
|
2 | P09958 (/TAS) P09958 (/TAS) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
2 | P09958 (/HDA) P09958 (/HDA) |
Trans-Golgi network transport vesicle GO:0030140
A vesicle that mediates transport between the trans-Golgi network and other parts of the cell.
|
2 | P09958 (/IDA) P09958 (/IDA) |
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
|
2 | P09958 (/IDA) P09958 (/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.
|
2 | P09958 (/HDA) P09958 (/HDA) |
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
1 | P23188 (/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 | P29121 (/IDA) |
Acrosomal membrane GO:0002080
The membrane that surrounds the acrosomal lumen. The acrosome is a special type of lysosome 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.
|
1 | P29121 (/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 | P51559 (/IDA) |
Early endosome GO:0005769
A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways.
|
1 | P23188 (/TAS) |
Endoplasmic reticulum GO:0005783
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
|
1 | P23188 (/ISO) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | P23377 (/IDA) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | P23188 (/ISO) |
Golgi apparatus GO:0005794
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
|
1 | B1AMG5 (/IDA) |
Trans-Golgi network GO:0005802
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
|
1 | P23188 (/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 | P23188 (/ISO) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
1 | P23188 (/ISO) |
Trans-Golgi network transport vesicle membrane GO:0012510
The lipid bilayer surrounding a vesicle transporting substances between the trans-Golgi network and other parts of the cell.
|
1 | P23188 (/TAS) |
Integral component of membrane GO:0016021
The component of a 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 | P51559 (/NAS) |
Integral component of membrane GO:0016021
The component of a 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 | P23188 (/TAS) |
Trans-Golgi network transport vesicle GO:0030140
A vesicle that mediates transport between the trans-Golgi network and other parts of the cell.
|
1 | P23188 (/ISO) |
Golgi cisterna GO:0031985
Any of the thin, flattened membrane-bounded compartments that form the central portion of the Golgi complex.
|
1 | P23377 (/IDA) |
Golgi cisterna GO:0031985
Any of the thin, flattened membrane-bounded compartments that form the central portion of the Golgi complex.
|
1 | P23188 (/ISO) |
Neuronal cell body GO:0043025
The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites.
|
1 | O17798 (/IDA) |
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
|
1 | P23188 (/ISO) |