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 8: Membrane-bound transcription factor site-1 proteas...
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 8 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 |
---|---|---|
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
3 | A0A2R8Q4U2 (/ISS) Q1LWH3 (/ISS) Q6X1U1 (/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).
|
2 | Q9WTZ2 (/IDA) Q9WTZ3 (/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).
|
2 | Q14703 (/TAS) Q9WTZ2 (/TAS) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
1 | Q9WTZ2 (/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 | Q14703 (/EXP) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | Q14703 (/IMP) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | Q9WTZ2 (/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 | Q9Z2A8 (/ISS) |
There are 21 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 |
---|---|---|
Lipid metabolic process GO:0006629
The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
|
4 | A0A2R8Q4U2 (/IMP) Q1LWH3 (/IMP) Q6X1U1 (/IMP) Q9WTZ2 (/IMP) |
Liver development GO:0001889
The process whose specific outcome is the progression of the liver over time, from its formation to the mature structure. The liver is an exocrine gland which secretes bile and functions in metabolism of protein and carbohydrate and fat, synthesizes substances involved in the clotting of the blood, synthesizes vitamin A, detoxifies poisonous substances, stores glycogen, and breaks down worn-out erythrocytes.
|
3 | A0A2R8Q4U2 (/IMP) Q1LWH3 (/IMP) Q6X1U1 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
3 | Q9WTZ2 (/ISS) Q9WTZ3 (/ISS) Q9Z2A8 (/ISS) |
Lysosome organization GO:0007040
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lysosome. A lysosome is a cytoplasmic, membrane-bounded organelle that is found in most animal cells and that contains a variety of hydrolases.
|
3 | Q9WTZ2 (/ISS) Q9WTZ3 (/ISS) Q9Z2A8 (/ISS) |
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.
|
3 | A0A2R8Q4U2 (/IMP) Q1LWH3 (/IMP) Q6X1U1 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q14703 (/IMP) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q9WTZ2 (/ISO) |
Proteolysis GO:0006508
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
|
1 | Q14703 (/TAS) |
Protein import into nucleus GO:0006606
The directed movement of a protein from the cytoplasm to the nucleus.
|
1 | Q9WTZ2 (/IDA) |
Lysosome organization GO:0007040
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lysosome. A lysosome is a cytoplasmic, membrane-bounded organelle that is found in most animal cells and that contains a variety of hydrolases.
|
1 | Q14703 (/IMP) |
Lysosome organization GO:0007040
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a lysosome. A lysosome is a cytoplasmic, membrane-bounded organelle that is found in most animal cells and that contains a variety of hydrolases.
|
1 | Q9WTZ2 (/ISO) |
Endoplasmic reticulum unfolded protein response GO:0030968
The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.
|
1 | Q14703 (/TAS) |
Membrane protein intracellular domain proteolysis GO:0031293
The proteolytic cleavage of a transmembrane protein leading to the release of an intracellular domain.
|
1 | Q9Z2A8 (/IMP) |
Membrane protein intracellular domain proteolysis GO:0031293
The proteolytic cleavage of a transmembrane protein leading to the release of an intracellular domain.
|
1 | Q14703 (/ISS) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
1 | Q9Z2A8 (/IMP) |
Response to endoplasmic reticulum stress GO:0034976
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 stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.
|
1 | Q14703 (/ISS) |
Sterol regulatory element binding protein cleavage GO:0035103
The proteolytic release of a transcriptionally active sterol regulatory element binding protein (SREBP) from intracellular membranes, freeing it to move to the nucleus to upregulate transcription of target genes, in response to altered levels of one or more lipids.
|
1 | Q9VP10 (/NAS) |
ATF6-mediated unfolded protein response GO:0036500
A series of molecular signals mediated by the endoplasmic reticulum membrane stress sensor ATF6 (activating transcription factor 6). Begins with activation of ATF6 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. Under conditions of endoplasmic reticulum stress, ATF6 translocates to the Golgi where it is processed by proteases to release a cytoplasmic domain (ATF6f), which operates as a transcriptional activator of many genes required to restore folding capacity.
|
1 | Q14703 (/TAS) |
Post-translational protein modification GO:0043687
The process of covalently altering one or more amino acids in a protein after the protein has been completely translated and released from the ribosome.
|
1 | Q14703 (/TAS) |
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 | Q14703 (/TAS) |
Regulation of cholesterol biosynthetic process GO:0045540
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cholesterol.
|
1 | Q14703 (/TAS) |
There are 6 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 |
---|---|---|
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
2 | Q14703 (/TAS) Q9WTZ2 (/TAS) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
2 | Q14703 (/TAS) Q9WTZ2 (/TAS) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | Q14703 (/TAS) |
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 | Q9WTZ3 (/IDA) |
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 | Q9WTZ2 (/ISO) |
Golgi stack GO:0005795
The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
|
1 | Q9WTZ2 (/IDA) |