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 163: Putative ring finger protein 37
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 |
|---|---|---|
|
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
|
3 | O94941 (/IPI) Q925F4 (/IPI) Q925F4 (/IPI) |
|
Ubiquitin protein ligase binding GO:0031625
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins.
|
2 | Q925F4 (/ISO) Q925F4 (/ISO) |
|
Ubiquitin-ubiquitin ligase activity GO:0034450
Isoenergetic transfer of ubiquitin from one protein to an existing ubiquitin chain via the reaction X-ubiquitin + Y-ubiquitin -> Y-ubiquitin-ubiquitin + X, where both the X-ubiquitin and Y-ubiquitin-ubiquitin linkages are thioester bonds between the C-terminal glycine of ubiquitin and a sulfhydryl side group of a cysteine residue.
|
2 | Q925F4 (/IDA) Q925F4 (/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.
|
2 | Q925F4 (/IDA) Q925F4 (/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).
|
1 | O94941 (/IPI) |
|
Ubiquitin-ubiquitin ligase activity GO:0034450
Isoenergetic transfer of ubiquitin from one protein to an existing ubiquitin chain via the reaction X-ubiquitin + Y-ubiquitin -> Y-ubiquitin-ubiquitin + X, where both the X-ubiquitin and Y-ubiquitin-ubiquitin linkages are thioester bonds between the C-terminal glycine of ubiquitin and a sulfhydryl side group of a cysteine residue.
|
1 | O94941 (/ISS) |
There are 2 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 polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
2 | Q925F4 (/IDA) Q925F4 (/IDA) |
|
Protein polyubiquitination GO:0000209
Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
|
1 | O94941 (/ISS) |
There are 9 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 |
|---|---|---|
|
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.
|
2 | Q925F4 (/IDA) Q925F4 (/IDA) |
|
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
2 | Q925F4 (/ISO) Q925F4 (/ISO) |
|
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
2 | Q925F4 (/ISO) Q925F4 (/ISO) |
|
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
|
2 | Q925F4 (/ISO) Q925F4 (/ISO) |
|
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
|
2 | Q925F4 (/ISS) Q925F4 (/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 | O94941 (/ISS) |
|
Nucleoplasm GO:0005654
That part of the nuclear content other than the chromosomes or the nucleolus.
|
1 | O94941 (/IDA) |
|
Focal adhesion GO:0005925
Small region on the surface of a cell that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments.
|
1 | O94941 (/IDA) |
|
Nuclear body GO:0016604
Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins.
|
1 | O94941 (/IDA) |