The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was named:
"Zinc/RING finger domain, C3HC4 (zinc finger)
".
FunFam 409: probable E3 ubiquitin-protein ligase RNF183
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 5 GO terms relating to "molecular function"
The search results have been sorted with the annotations that are found most frequently at the top of the
list. The results can be filtered by typing text into the search box at the top of the table.
| GO Term | Annotations | Evidence |
|---|---|---|
|
Protein binding GO:0005515
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
|
3 | Q8QZS5 (/IPI) Q96D59 (/IPI) Q96D59 (/IPI) |
|
Ubiquitin protein ligase activity GO:0061630
Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
|
3 | Q8QZS5 (/IMP) Q96D59 (/IMP) Q96D59 (/IMP) |
|
Ubiquitin protein ligase activity GO:0061630
Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
|
2 | Q96D59 (/IDA) Q96D59 (/IDA) |
|
Ubiquitin protein ligase activity GO:0061630
Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
|
1 | Q8QZS5 (/ISO) |
|
Ubiquitin protein ligase activity GO:0061630
Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
|
1 | Q3SWY0 (/ISS) |
There are 13 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 |
|---|---|---|
|
Protein autoubiquitination GO:0051865
The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
|
3 | Q8QZS5 (/IMP) Q96D59 (/IMP) Q96D59 (/IMP) |
|
Protein polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
2 | Q96D59 (/IDA) Q96D59 (/IDA) |
|
Protein polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
2 | Q96D59 (/IMP) Q96D59 (/IMP) |
|
Protein polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
2 | Q3SWY0 (/ISS) Q8QZS5 (/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.
|
2 | Q96D59 (/IDA) Q96D59 (/IDA) |
|
Positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway GO:1902237
Any process that activates or increases the frequency, rate or extent of an endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway.
|
2 | Q96D59 (/IMP) Q96D59 (/IMP) |
|
Protein polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
1 | Q8QZS5 (/ISO) |
|
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 | Q8QZS5 (/ISO) |
|
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 | Q3SWY0 (/ISS) |
|
Protein autoubiquitination GO:0051865
The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
|
1 | Q8QZS5 (/ISO) |
|
Protein autoubiquitination GO:0051865
The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
|
1 | Q3SWY0 (/ISS) |
|
Positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway GO:1902237
Any process that activates or increases the frequency, rate or extent of an endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway.
|
1 | Q8QZS5 (/ISO) |
|
Positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway GO:1902237
Any process that activates or increases the frequency, rate or extent of an endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway.
|
1 | Q3SWY0 (/ISS) |
There are 10 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 |
|---|---|---|
|
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
|
3 | Q3SWY0 (/ISS) Q96D59 (/ISS) Q96D59 (/ISS) |
|
Cis-Golgi network membrane GO:0033106
The lipid bilayer surrounding any of the compartments that make up the cis-Golgi network.
|
3 | Q3SWY0 (/ISS) Q96D59 (/ISS) Q96D59 (/ISS) |
|
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 | Q96D59 (/IDA) Q96D59 (/IDA) |
|
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
2 | Q96D59 (/IDA) Q96D59 (/IDA) |
|
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
|
2 | Q3SWY0 (/ISS) Q8QZS5 (/ISS) |
|
Lysosomal membrane GO:0005765
The lipid bilayer surrounding the lysosome and separating its contents from the cell cytoplasm.
|
1 | Q8QZS5 (/IDA) |
|
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 | Q8QZS5 (/ISO) |
|
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | Q8QZS5 (/IDA) |
|
Integral component of endoplasmic reticulum membrane GO:0030176
The component of the endoplasmic reticulum 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 | Q8QZS5 (/ISO) |
|
Cis-Golgi network membrane GO:0033106
The lipid bilayer surrounding any of the compartments that make up the cis-Golgi network.
|
1 | Q8QZS5 (/IDA) |
