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:
"Zinc/RING finger domain, C3HC4 (zinc finger)
".
FunFam 9: E3 ubiquitin-protein ligase RNF130
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 9 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 |
---|---|---|
Ubiquitin-protein transferase activity GO:0004842
Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.
|
4 | Q86XS8 (/IDA) Q86XS8 (/IDA) Q86XS8 (/IDA) Q86XS8 (/IDA) |
Ubiquitin-protein transferase activity GO:0004842
Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.
|
2 | Q6Y290 (/ISS) Q8VEM1 (/ISS) |
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).
|
2 | Q3U2C5 (/IPI) Q8TEB7 (/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.
|
2 | Q3U2C5 (/IDA) Q9D304 (/IDA) |
Ubiquitin-protein transferase activity GO:0004842
Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.
|
1 | Q8VEM1 (/ISO) |
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
|
1 | Q06003 (/ISM) |
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 | Q9D304 (/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 | Q06003 (/ISS) |
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 | Q8TEB7 (/TAS) |
There are 15 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 |
---|---|---|
Programmed cell death GO:0012501
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
|
5 | Q6Y290 (/ISS) Q86XS8 (/ISS) Q86XS8 (/ISS) Q86XS8 (/ISS) Q86XS8 (/ISS) |
Mesoderm formation GO:0001707
The process that gives rise to the mesoderm. This process pertains to the initial formation of the structure from unspecified parts.
|
1 | Q06003 (/IEP) |
Ubiquitin-dependent protein catabolic process GO:0006511
The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.
|
1 | Q8TEB7 (/NAS) |
Programmed cell death GO:0012501
A process which begins when a cell receives an internal or external signal and activates a series of biochemical events (signaling pathway). The process ends with the death of the cell.
|
1 | Q8VEM1 (/IMP) |
Protein ubiquitination GO:0016567
The process in which one or more ubiquitin groups are added to a protein.
|
1 | Q06003 (/IMP) |
Protein deubiquitination GO:0016579
The removal of one or more ubiquitin groups from a protein.
|
1 | Q8TEB7 (/TAS) |
Regulation of protein stability GO:0031647
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
|
1 | Q3U2C5 (/IDA) |
Regulation of protein stability GO:0031647
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
|
1 | Q8TEB7 (/IMP) |
Regulation of protein stability GO:0031647
Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
|
1 | Q9D304 (/ISO) |
Cellular response to drug GO:0035690
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 drug stimulus. A drug is a substance used in the diagnosis, treatment or prevention of a disease.
|
1 | Q3U2C5 (/IDA) |
Negative regulation of cytokine biosynthetic process GO:0042036
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of cytokines.
|
1 | Q9D304 (/IDA) |
Negative regulation of MAPK cascade GO:0043409
Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the MAPKKK cascade.
|
1 | Q3U2C5 (/IDA) |
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 | Q14B02 (/IDA) |
Protein localization to lysosome GO:0061462
A process in which a protein is transported to, or maintained in, a location within a lysosome.
|
1 | Q8TEB7 (/IC) |
Positive regulation of protein catabolic process in the vacuole GO:1904352
Any process that activates or increases the frequency, rate or extent of protein catabolic process in the vacuole.
|
1 | Q8TEB7 (/IC) |
There are 12 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 |
---|---|---|
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
4 | Q86XS8 (/IDA) Q86XS8 (/IDA) Q86XS8 (/IDA) Q86XS8 (/IDA) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
2 | Q6Y290 (/ISS) Q8VEM1 (/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.
|
1 | Q06003 (/NAS) |
Cytoplasm GO:0005737
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
|
1 | Q8VEM1 (/ISO) |
Endosome GO:0005768
A vacuole to which materials ingested by endocytosis are delivered.
|
1 | Q06003 (/IDA) |
Late endosome GO:0005770
A prelysosomal endocytic organelle differentiated from early endosomes by lower lumenal pH and different protein composition. Late endosomes are more spherical than early endosomes and are mostly juxtanuclear, being concentrated near the microtubule organizing center.
|
1 | Q9D304 (/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 | Q9D304 (/IDA) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | Q14B02 (/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 | Q9D304 (/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 | Q8TEB7 (/TAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | Q8NC42 (/HDA) |
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 | Q8VEM1 (/NAS) |