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:
"Ribonuclease Inhibitor
".
FunFam 59: Chondroadherin like
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 |
---|---|---|
Collagen binding GO:0005518
Interacting selectively and non-covalently with collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
|
2 | Q6NUI6 (/IDA) Q6NUI6 (/IDA) |
Extracellular matrix structural constituent conferring compression resistance GO:0030021
A constituent of the extracellular matrix that enables the matrix to resist compressive forces; often a proteoglycan.
|
2 | Q6NUI6 (/ISS) Q6NUI6 (/ISS) |
Extracellular matrix structural constituent conferring compression resistance GO:0030021
A constituent of the extracellular matrix that enables the matrix to resist compressive forces; often a proteoglycan.
|
2 | F1SRC2 (/RCA) F1SRC2 (/RCA) |
Collagen fibril binding GO:0098633
Interacting selectively and non-covalently with a collagen fibril.
|
2 | Q6NUI6 (/IDA) Q6NUI6 (/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 | Q7SYE5 (/IPI) |
Collagen binding GO:0005518
Interacting selectively and non-covalently with collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
|
1 | E9Q7T7 (/ISO) |
Collagen binding GO:0005518
Interacting selectively and non-covalently with collagen, a group of fibrous proteins of very high tensile strength that form the main component of connective tissue in animals. Collagen is highly enriched in glycine (some regions are 33% glycine) and proline, occurring predominantly as 3-hydroxyproline (about 20%).
|
1 | E9Q7T7 (/ISS) |
Collagen fibril binding GO:0098633
Interacting selectively and non-covalently with a collagen fibril.
|
1 | E9Q7T7 (/ISO) |
Collagen fibril binding GO:0098633
Interacting selectively and non-covalently with a collagen fibril.
|
1 | E9Q7T7 (/ISS) |
There are 8 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 |
---|---|---|
Negative regulation of chondrocyte differentiation GO:0032331
Any process that stops, prevents, or reduces the frequency, rate or extent of chondrocyte differentiation.
|
2 | Q6NUI6 (/ISS) Q6NUI6 (/ISS) |
Bone development GO:0060348
The process whose specific outcome is the progression of bone over time, from its formation to the mature structure. Bone is the hard skeletal connective tissue consisting of both mineral and cellular components.
|
2 | O55226 (/IMP) O55226 (/IMP) |
Negative regulation of bone trabecula formation GO:1900155
Any process that stops, prevents or reduces the frequency, rate or extent of bone trabecula formation.
|
2 | O55226 (/IMP) O55226 (/IMP) |
Negative regulation of collagen fibril organization GO:1904027
Any process that stops, prevents or reduces the frequency, rate or extent of collagen fibril organization.
|
2 | Q6NUI6 (/IDA) Q6NUI6 (/IDA) |
Cartilage condensation GO:0001502
The condensation of mesenchymal cells that have been committed to differentiate into chondrocytes.
|
1 | O70210 (/IEP) |
Negative regulation of chondrocyte differentiation GO:0032331
Any process that stops, prevents, or reduces the frequency, rate or extent of chondrocyte differentiation.
|
1 | E9Q7T7 (/IMP) |
Negative regulation of collagen fibril organization GO:1904027
Any process that stops, prevents or reduces the frequency, rate or extent of collagen fibril organization.
|
1 | E9Q7T7 (/ISO) |
Negative regulation of collagen fibril organization GO:1904027
Any process that stops, prevents or reduces the frequency, rate or extent of collagen fibril organization.
|
1 | E9Q7T7 (/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 |
---|---|---|
Collagen-containing extracellular matrix GO:0062023
An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells.
|
3 | E9Q7T7 (/IDA) Q6NUI6 (/IDA) Q6NUI6 (/IDA) |
Extracellular matrix GO:0031012
A structure lying external to one or more cells, which provides structural support, biochemical or biomechanical cues for cells or tissues.
|
1 | O70210 (/TAS) |
Collagen-containing extracellular matrix GO:0062023
An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells.
|
1 | E9Q7T7 (/ISO) |