CATH Superfamily 2.60.120.1000
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: waiting to be named.
FunFam 2: Collagen XI alpha 1 chain
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 19 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 |
---|---|---|
Extracellular matrix structural constituent conferring tensile strength GO:0030020
A constituent of the extracellular matrix that enables the matrix to resist longitudinal stress.
|
6 | O88207 (/RCA) O88207 (/RCA) P12107 (/RCA) P20908 (/RCA) P20908 (/RCA) Q61245 (/RCA) |
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).
|
4 | O88207 (/IPI) O88207 (/IPI) P20908 (/IPI) P20908 (/IPI) |
Heparin binding GO:0008201
Interacting selectively and non-covalently with heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
|
4 | P20908 (/IDA) P20908 (/IDA) P20909 (/IDA) Q9JI03 (/IDA) |
Heparin binding GO:0008201
Interacting selectively and non-covalently with heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
|
3 | O88207 (/ISO) O88207 (/ISO) Q61245 (/ISO) |
Integrin binding GO:0005178
Interacting selectively and non-covalently with an integrin.
|
2 | P20908 (/NAS) P20908 (/NAS) |
Extracellular matrix structural constituent GO:0005201
The action of a molecule that contributes to the structural integrity of the extracellular matrix.
|
2 | O88207 (/IDA) O88207 (/IDA) |
Extracellular matrix structural constituent conferring tensile strength GO:0030020
A constituent of the extracellular matrix that enables the matrix to resist longitudinal stress.
|
2 | P20908 (/HDA) P20908 (/HDA) |
Proteoglycan binding GO:0043394
Interacting selectively and non-covalently with a proteoglycan, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
|
2 | P20908 (/IPI) P20908 (/IPI) |
Proteoglycan binding GO:0043394
Interacting selectively and non-covalently with a proteoglycan, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Platelet-derived growth factor binding GO:0048407
Interacting selectively and non-covalently with platelet-derived growth factor.
|
2 | P20908 (/IDA) P20908 (/IDA) |
Platelet-derived growth factor binding GO:0048407
Interacting selectively and non-covalently with platelet-derived growth factor.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Extracellular matrix structural constituent GO:0005201
The action of a molecule that contributes to the structural integrity of the extracellular matrix.
|
1 | P12107 (/NAS) |
Extracellular matrix structural constituent GO:0005201
The action of a molecule that contributes to the structural integrity of the extracellular matrix.
|
1 | P20909 (/TAS) |
Heparin binding GO:0008201
Interacting selectively and non-covalently with heparin, any member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues.
|
1 | Q9IAU4 (/TAS) |
Protein binding, bridging GO:0030674
The binding activity of a molecule that brings together two or more protein molecules, or a protein and another macromolecule or complex, through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way.
|
1 | P12107 (/NAS) |
Heparan sulfate proteoglycan binding GO:0043395
Interacting selectively and non-covalently with a heparan sulfate proteoglycan, any proteoglycan containing heparan sulfate as the glycosaminoglycan carbohydrate unit.
|
1 | Q9IAU4 (/TAS) |
Extracellular matrix binding GO:0050840
Interacting selectively and non-covalently with a component of the extracellular matrix.
|
1 | P12107 (/NAS) |
Heparan sulfate binding GO:1904399
Interacting selectively and non-covalently with heparan sulfate.
|
1 | P20909 (/IDA) |
Heparan sulfate binding GO:1904399
Interacting selectively and non-covalently with heparan sulfate.
|
1 | Q61245 (/ISO) |
There are 47 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 |
---|---|---|
Cartilage morphogenesis GO:0060536
The process in which the anatomical structures of cartilage are generated and organized.
|
7 | A0ZXN1 (/IMP) D6MUD4 (/IMP) F1R5X4 (/IMP) F6NLZ6 (/IMP) I3ISS1 (/IMP) Q1LWX5 (/IMP) Q8AW17 (/IMP) |
Collagen fibril organization GO:0030199
Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix.
|
5 | O88207 (/IMP) O88207 (/IMP) P20908 (/IMP) P20908 (/IMP) Q61245 (/IMP) |
Collagen fibril organization GO:0030199
Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix.
|
4 | P12107 (/NAS) P20908 (/NAS) P20908 (/NAS) Q9IAU4 (/NAS) |
Skin development GO:0043588
The process whose specific outcome is the progression of the skin over time, from its formation to the mature structure. The skin is the external membranous integument of an animal. In vertebrates the skin generally consists of two layers, an outer nonsensitive and nonvascular epidermis (cuticle or skarfskin) composed of cells which are constantly growing and multiplying in the deeper, and being thrown off in the superficial layers, as well as an inner vascular dermis (cutis, corium or true skin) composed mostly of connective tissue.
|
4 | O88207 (/IMP) O88207 (/IMP) P20908 (/IMP) P20908 (/IMP) |
Heart morphogenesis GO:0003007
The developmental process in which the heart is generated and organized. The heart is a hollow, muscular organ, which, by contracting rhythmically, keeps up the circulation of the blood.
|
3 | O88207 (/IGI) O88207 (/IGI) Q61245 (/IGI) |
Collagen fibril organization GO:0030199
Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix.
|
3 | O88207 (/IGI) O88207 (/IGI) Q61245 (/IGI) |
Tendon development GO:0035989
The process whose specific outcome is the progression of a tendon over time, from its formation to the mature structure. A tendon is a fibrous, strong, connective tissue that connects muscle to bone or integument and is capable of withstanding tension. Tendons and muscles work together to exert a pulling force.
|
3 | O88207 (/IGI) O88207 (/IGI) Q61245 (/IGI) |
Tendon development GO:0035989
The process whose specific outcome is the progression of a tendon over time, from its formation to the mature structure. A tendon is a fibrous, strong, connective tissue that connects muscle to bone or integument and is capable of withstanding tension. Tendons and muscles work together to exert a pulling force.
|
3 | O88207 (/IMP) O88207 (/IMP) Q61245 (/IMP) |
Blood vessel development GO:0001568
The process whose specific outcome is the progression of a blood vessel over time, from its formation to the mature structure. The blood vessel is the vasculature carrying blood.
|
2 | O88207 (/IMP) O88207 (/IMP) |
Cell adhesion GO:0007155
The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
|
2 | P20908 (/IMP) P20908 (/IMP) |
Cell adhesion GO:0007155
The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Cell migration GO:0016477
The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.
|
2 | P20908 (/IMP) P20908 (/IMP) |
Cell migration GO:0016477
The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Extracellular matrix organization GO:0030198
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
|
2 | P20908 (/TAS) P20908 (/TAS) |
Collagen fibril organization GO:0030199
Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Collagen biosynthetic process GO:0032964
The chemical reactions and pathways resulting in the formation of collagen, any of 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 | P20908 (/IMP) P20908 (/IMP) |
Collagen biosynthetic process GO:0032964
The chemical reactions and pathways resulting in the formation of collagen, any of 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 | O88207 (/ISO) O88207 (/ISO) |
Wound healing, spreading of epidermal cells GO:0035313
The migration of an epidermal cell along or through a wound gap that contributes to the reestablishment of a continuous epidermis.
|
2 | P20908 (/IMP) P20908 (/IMP) |
Wound healing, spreading of epidermal cells GO:0035313
The migration of an epidermal cell along or through a wound gap that contributes to the reestablishment of a continuous epidermis.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Skin development GO:0043588
The process whose specific outcome is the progression of the skin over time, from its formation to the mature structure. The skin is the external membranous integument of an animal. In vertebrates the skin generally consists of two layers, an outer nonsensitive and nonvascular epidermis (cuticle or skarfskin) composed of cells which are constantly growing and multiplying in the deeper, and being thrown off in the superficial layers, as well as an inner vascular dermis (cutis, corium or true skin) composed mostly of connective tissue.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Integrin biosynthetic process GO:0045112
The chemical reactions and pathways resulting in the formation of integrins, a large family of transmembrane proteins that act as receptors for cell-adhesion molecules.
|
2 | P20908 (/IMP) P20908 (/IMP) |
Integrin biosynthetic process GO:0045112
The chemical reactions and pathways resulting in the formation of integrins, a large family of transmembrane proteins that act as receptors for cell-adhesion molecules.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Eye morphogenesis GO:0048592
The process in which the anatomical structures of the eye are generated and organized.
|
2 | P20908 (/IMP) P20908 (/IMP) |
Eye morphogenesis GO:0048592
The process in which the anatomical structures of the eye are generated and organized.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Regulation of cellular component organization GO:0051128
Any process that modulates the frequency, rate or extent of a process involved in the formation, arrangement of constituent parts, or disassembly of cell structures, including the plasma membrane and any external encapsulating structures such as the cell wall and cell envelope.
|
2 | O88207 (/IMP) O88207 (/IMP) |
Supramolecular fiber organization GO:0097435
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
|
2 | P20908 (/IMP) P20908 (/IMP) |
Supramolecular fiber organization GO:0097435
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a supramolecular fiber, a polymer consisting of an indefinite number of protein or protein complex subunits that have polymerised to form a fiber-shaped structure.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Negative regulation of endodermal cell differentiation GO:1903225
Any process that stops, prevents or reduces the frequency, rate or extent of endodermal cell differentiation.
|
2 | P20908 (/IDA) P20908 (/IDA) |
Negative regulation of endodermal cell differentiation GO:1903225
Any process that stops, prevents or reduces the frequency, rate or extent of endodermal cell differentiation.
|
2 | O88207 (/ISO) O88207 (/ISO) |
Cartilage condensation GO:0001502
The condensation of mesenchymal cells that have been committed to differentiate into chondrocytes.
|
1 | Q61245 (/IMP) |
Ossification GO:0001503
The formation of bone or of a bony substance, or the conversion of fibrous tissue or of cartilage into bone or a bony substance.
|
1 | P20909 (/IEP) |
Chondrocyte development GO:0002063
The process whose specific outcome is the progression of a chondrocyte over time, from its commitment to its mature state. Chondrocyte development does not include the steps involved in committing a chondroblast to a chondrocyte fate.
|
1 | Q61245 (/IMP) |
Proteoglycan metabolic process GO:0006029
The chemical reactions and pathways involving proteoglycans, any glycoprotein in which the carbohydrate units are glycosaminoglycans.
|
1 | Q61245 (/IMP) |
Visual perception GO:0007601
The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
|
1 | P12107 (/IMP) |
Visual perception GO:0007601
The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
|
1 | Q61245 (/ISO) |
Sensory perception of sound GO:0007605
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
|
1 | P12107 (/IMP) |
Sensory perception of sound GO:0007605
The series of events required for an organism to receive an auditory stimulus, convert it to a molecular signal, and recognize and characterize the signal. Sonic stimuli are detected in the form of vibrations and are processed to form a sound.
|
1 | Q61245 (/ISO) |
Extracellular matrix organization GO:0030198
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix.
|
1 | P12107 (/NAS) |
Collagen fibril organization GO:0030199
Any process that determines the size and arrangement of collagen fibrils within an extracellular matrix.
|
1 | P20909 (/TAS) |
Endodermal cell differentiation GO:0035987
The process in which a relatively unspecialized cell acquires the specialized features of an endoderm cell, a cell of the inner of the three germ layers of the embryo.
|
1 | P12107 (/IEP) |
Inner ear morphogenesis GO:0042472
The process in which the anatomical structures of the inner ear are generated and organized. The inner ear is the structure in vertebrates that contains the organs of balance and hearing. It consists of soft hollow sensory structures (the membranous labyrinth) containing fluid (endolymph) surrounded by fluid (perilymph) and encased in a bony cavity (the bony labyrinth). It consists of two chambers, the sacculus and utriculus, from which arise the cochlea and semicircular canals respectively.
|
1 | Q61245 (/IMP) |
Embryonic skeletal system morphogenesis GO:0048704
The process in which the anatomical structures of the skeleton are generated and organized during the embryonic phase.
|
1 | Q61245 (/IMP) |
Skeletal system morphogenesis GO:0048705
The process in which the anatomical structures of the skeleton are generated and organized.
|
1 | Q61245 (/IMP) |
Detection of mechanical stimulus involved in sensory perception of sound GO:0050910
The series of events involved in the perception of sound vibration in which the vibration is received and converted into a molecular signal.
|
1 | P12107 (/IMP) |
Detection of mechanical stimulus involved in sensory perception of sound GO:0050910
The series of events involved in the perception of sound vibration in which the vibration is received and converted into a molecular signal.
|
1 | Q61245 (/ISO) |
Cartilage development GO:0051216
The process whose specific outcome is the progression of a cartilage element over time, from its formation to the mature structure. Cartilage elements are skeletal elements that consist of connective tissue dominated by extracellular matrix containing collagen type II and large amounts of proteoglycan, particularly chondroitin sulfate.
|
1 | Q61245 (/IMP) |
Ventricular cardiac muscle tissue morphogenesis GO:0055010
The process in which the anatomical structures of cardiac ventricle muscle is generated and organized.
|
1 | Q61245 (/IMP) |
There are 19 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.
|
6 | O88207 (/HDA) O88207 (/HDA) P12107 (/HDA) P20908 (/HDA) P20908 (/HDA) Q61245 (/HDA) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
3 | P12107 (/TAS) P20908 (/TAS) P20908 (/TAS) |
Collagen trimer GO:0005581
A protein complex consisting of three collagen chains assembled into a left-handed triple helix. These trimers typically assemble into higher order structures.
|
3 | O88207 (/IDA) O88207 (/IDA) Q61245 (/IDA) |
Collagen type V trimer GO:0005588
A collagen heterotrimer containing type V alpha chains;
|
3 | P20908 (/TAS) P20908 (/TAS) Q9JI03 (/TAS) |
Extracellular space GO:0005615
That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
|
3 | O88207 (/HDA) O88207 (/HDA) Q61245 (/HDA) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
3 | P12107 (/TAS) P20908 (/TAS) P20908 (/TAS) |
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.
|
3 | O88207 (/IDA) O88207 (/IDA) Q61245 (/IDA) |
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 | O88207 (/ISO) O88207 (/ISO) Q61245 (/ISO) |
Extracellular region GO:0005576
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
|
2 | P20908 (/HDA) P20908 (/HDA) |
Collagen trimer GO:0005581
A protein complex consisting of three collagen chains assembled into a left-handed triple helix. These trimers typically assemble into higher order structures.
|
2 | O88207 (/IMP) O88207 (/IMP) |
Collagen type V trimer GO:0005588
A collagen heterotrimer containing type V alpha chains;
|
2 | P20908 (/IMP) P20908 (/IMP) |
Collagen type V trimer GO:0005588
A collagen heterotrimer containing type V alpha chains;
|
2 | O88207 (/ISO) O88207 (/ISO) |
Basement membrane GO:0005604
A collagen-containing extracellular matrix consisting of a thin layer of dense material found in various animal tissues interposed between the cells and the adjacent connective tissue. It consists of the basal lamina plus an associated layer of reticulin fibers.
|
2 | O88207 (/IDA) O88207 (/IDA) |
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.
|
2 | P20908 (/IMP) P20908 (/IMP) |
Fibrillar collagen trimer GO:0005583
Any triple helical collagen trimer that forms fibrils.
|
1 | Q9IAU4 (/IDA) |
Collagen type XI trimer GO:0005592
A collagen heterotrimer containing type XI alpha chains in alpha1(XI)alpha2(XI)alpha3(XI) trimers; type XI collagen triple helices associate to form fibrils.
|
1 | P12107 (/IDA) |
Collagen type XI trimer GO:0005592
A collagen heterotrimer containing type XI alpha chains in alpha1(XI)alpha2(XI)alpha3(XI) trimers; type XI collagen triple helices associate to form fibrils.
|
1 | Q61245 (/ISO) |
Collagen type XI trimer GO:0005592
A collagen heterotrimer containing type XI alpha chains in alpha1(XI)alpha2(XI)alpha3(XI) trimers; type XI collagen triple helices associate to form fibrils.
|
1 | P12107 (/NAS) |
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 | P20909 (/IDA) |