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)
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 387: RING finger protein 26

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 6 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).
1 Q9BY78 (/IPI)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
1 Q9VIK5 (/ISM)
Zinc ion binding GO:0008270
Interacting selectively and non-covalently with zinc (Zn) ions.
1 Q9BY78 (/NAS)
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 Q9BY78 (/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 Q8BUH7 (/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 Q8BUH7 (/ISS)

There are 18 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
Endosome organization GO:0007032
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of endosomes.
1 Q9BY78 (/IDA)
Endosome organization GO:0007032
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of endosomes.
1 Q8BUH7 (/ISO)
Endosome organization GO:0007032
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of endosomes.
1 Q8BUH7 (/ISS)
Protein ubiquitination GO:0016567
The process in which one or more ubiquitin groups are added to a protein.
1 Q9BY78 (/IDA)
Protein ubiquitination GO:0016567
The process in which one or more ubiquitin groups are added to a protein.
1 Q8BUH7 (/ISO)
Protein ubiquitination GO:0016567
The process in which one or more ubiquitin groups are added to a protein.
1 Q8BUH7 (/ISS)
Regulation of type I interferon production GO:0032479
Any process that modulates the frequency, rate, or extent of interferon type I production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
1 Q9BY78 (/IDA)
Regulation of type I interferon production GO:0032479
Any process that modulates the frequency, rate, or extent of interferon type I production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
1 Q8BUH7 (/ISO)
Regulation of type I interferon production GO:0032479
Any process that modulates the frequency, rate, or extent of interferon type I production. Type I interferons include the interferon-alpha, beta, delta, episilon, zeta, kappa, tau, and omega gene families.
1 Q8BUH7 (/ISS)
Negative regulation of defense response to virus GO:0050687
Any process that stops, prevents or reduces the rate or extent of antiviral mechanisms, thereby facilitating viral replication.
1 Q9BY78 (/IDA)
Negative regulation of defense response to virus GO:0050687
Any process that stops, prevents or reduces the rate or extent of antiviral mechanisms, thereby facilitating viral replication.
1 Q8BUH7 (/ISO)
Negative regulation of defense response to virus GO:0050687
Any process that stops, prevents or reduces the rate or extent of antiviral mechanisms, thereby facilitating viral replication.
1 Q8BUH7 (/ISS)
Protein K11-linked ubiquitination GO:0070979
A protein ubiquitination process in which ubiquitin monomers are attached to a protein, and then ubiquitin polymers are formed by linkages between lysine residues at position 11 of the ubiquitin monomers. K11-linked polyubiquitination targets the substrate protein for degradation. The anaphase-promoting complex promotes the degradation of mitotic regulators by assembling K11-linked polyubiquitin chains.
1 Q9BY78 (/IDA)
Protein K11-linked ubiquitination GO:0070979
A protein ubiquitination process in which ubiquitin monomers are attached to a protein, and then ubiquitin polymers are formed by linkages between lysine residues at position 11 of the ubiquitin monomers. K11-linked polyubiquitination targets the substrate protein for degradation. The anaphase-promoting complex promotes the degradation of mitotic regulators by assembling K11-linked polyubiquitin chains.
1 Q8BUH7 (/ISO)
Protein K11-linked ubiquitination GO:0070979
A protein ubiquitination process in which ubiquitin monomers are attached to a protein, and then ubiquitin polymers are formed by linkages between lysine residues at position 11 of the ubiquitin monomers. K11-linked polyubiquitination targets the substrate protein for degradation. The anaphase-promoting complex promotes the degradation of mitotic regulators by assembling K11-linked polyubiquitin chains.
1 Q8BUH7 (/ISS)
Protein localization to perinuclear region of cytoplasm GO:1905719
A process in which a protein is transported to, or maintained in, a location within the perinuclear region of the cytoplasm.
1 Q9BY78 (/IDA)
Protein localization to perinuclear region of cytoplasm GO:1905719
A process in which a protein is transported to, or maintained in, a location within the perinuclear region of the cytoplasm.
1 Q8BUH7 (/ISO)
Protein localization to perinuclear region of cytoplasm GO:1905719
A process in which a protein is transported to, or maintained in, a location within the perinuclear region of the cytoplasm.
1 Q8BUH7 (/ISS)

There are 3 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
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
1 Q9BY78 (/IDA)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
1 Q8BUH7 (/ISO)
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
1 Q8BUH7 (/ISS)
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