CATH Superfamily 2.10.220.10
Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2
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:
"Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2
".
FunFam 23: Furin, paired basic amino acid cleaving enzyme
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 11 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 |
---|---|---|
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
2 | P23188 (/ISS) P23377 (/ISS) |
Protease binding GO:0002020
Interacting selectively and non-covalently with any protease or peptidase.
|
1 | P23188 (/ISO) |
Endopeptidase activity GO:0004175
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
|
1 | P23188 (/ISO) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | P23377 (/IMP) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | P23188 (/ISO) |
Serine-type endopeptidase activity GO:0004252
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
|
1 | P23188 (/TAS) |
Serine-type endopeptidase inhibitor activity GO:0004867
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme.
|
1 | P23188 (/ISO) |
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 | P23188 (/IPI) |
Peptidase activity GO:0008233
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid.
|
1 | P23188 (/ISO) |
Peptide binding GO:0042277
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds.
|
1 | P23188 (/ISO) |
Nerve growth factor binding GO:0048406
Interacting selectively and non-covalently with nerve growth factor (NGF).
|
1 | P23188 (/ISO) |
There are 35 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 |
---|---|---|
Heart looping GO:0001947
The tube morphogenesis process in which the primitive heart tube loops asymmetrically. This looping brings the primitive heart chambers into alignment preceding their future integration. Heart looping begins with dextral-looping and ends when the main regional divisions of the mature heart and primordium of the great arterial trunks become established preceeding septation.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Determination of left/right asymmetry in lateral mesoderm GO:0003140
The establishment of the lateral mesoderm with respect to the left and right halves.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Heart jogging GO:0003146
The morphogenetic process in which the heart cone is displaced to the left with respect to the vector of the anterior-posterior axis.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Response to bacterium GO:0009617
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a bacterium.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
|
2 | P23188 (/IDA) P23377 (/IDA) |
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
|
2 | P23188 (/IMP) P23377 (/IMP) |
Fin morphogenesis GO:0033334
The process in which the anatomical structures of a fin are generated and organized.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Embryonic viscerocranium morphogenesis GO:0048703
The process in which the anatomical structures of the viscerocranium are generated and organized during the embryonic phase. The viscerocranium is the part of the skull comprising the facial bones.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
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.
|
2 | F1QQ43 (/IGI) Q1KHF9 (/IGI) |
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.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Cartilage morphogenesis GO:0060536
The process in which the anatomical structures of cartilage are generated and organized.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Determination of heart left/right asymmetry GO:0061371
Determination of the asymmetric location of the heart with respect to the left and right halves of the organism.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Determination of digestive tract left/right asymmetry GO:0071907
Determination of the asymmetric location of various parts of the digestive tract with respect to the left and right halves of the organism. The digestive tract is the anatomical structure through which food passes and is processed.
|
2 | F1QQ43 (/IMP) Q1KHF9 (/IMP) |
Positive regulation of transforming growth factor beta1 activation GO:1901394
Any process that activates or increases the frequency, rate or extent of transforming growth factor beta1 activation.
|
2 | P23188 (/ISS) P23377 (/ISS) |
Signal peptide processing GO:0006465
The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell.
|
1 | P23188 (/ISO) |
Aging GO:0007568
A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
|
1 | P23377 (/IEP) |
Regulation of signal transduction GO:0009966
Any process that modulates the frequency, rate or extent of signal transduction.
|
1 | P23188 (/IDA) |
Protein processing GO:0016485
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein.
|
1 | P23188 (/ISO) |
Peptide hormone processing GO:0016486
The generation of a mature peptide hormone by posttranslational processing of a prohormone.
|
1 | P23188 (/ISO) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
1 | P23377 (/IMP) |
Positive regulation of cell migration GO:0030335
Any process that activates or increases the frequency, rate or extent of cell migration.
|
1 | P23188 (/ISO) |
Positive regulation of transforming growth factor beta receptor signaling pathway GO:0030511
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
|
1 | P23377 (/IMP) |
Positive regulation of transforming growth factor beta receptor signaling pathway GO:0030511
Any process that activates or increases the frequency, rate or extent of TGF-beta receptor signaling pathway activity.
|
1 | P23188 (/ISO) |
Zymogen activation GO:0031638
The proteolytic processing of an inactive enzyme to an active form.
|
1 | P23188 (/ISO) |
Negative regulation of low-density lipoprotein particle receptor catabolic process GO:0032804
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors.
|
1 | P23188 (/ISO) |
Nerve growth factor production GO:0032902
The appearance of nerve growth factor (NGF) due to biosynthesis or secretion by cells in a neuron's target field, resulting in an increase in its intracellular or extracellular levels.
|
1 | P23188 (/ISO) |
Negative regulation of transforming growth factor beta1 production GO:0032911
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1.
|
1 | P23188 (/ISO) |
Secretion by cell GO:0032940
The controlled release of a substance by a cell.
|
1 | P23188 (/ISO) |
Regulation of protein catabolic process GO:0042176
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
|
1 | P23188 (/ISO) |
Peptide biosynthetic process GO:0043043
The chemical reactions and pathways resulting in the formation of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. This may include the translation of a precursor protein and its subsequent processing into a functional peptide.
|
1 | P23188 (/ISO) |
Regulation of low-density lipoprotein particle receptor biosynthetic process GO:0045714
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of low-density lipoprotein particle receptors.
|
1 | P23188 (/IMP) |
Regulation of endopeptidase activity GO:0052548
Any process that modulates the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins.
|
1 | P23188 (/ISO) |
Cartilage morphogenesis GO:0060536
The process in which the anatomical structures of cartilage are generated and organized.
|
1 | Q1KHF9 (/IGI) |
Dibasic protein processing GO:0090472
Any protein processing achieved by the cleavage of a peptide bond after two basic amino acids within a protein.
|
1 | P23188 (/ISO) |
Positive regulation of transforming growth factor beta1 activation GO:1901394
Any process that activates or increases the frequency, rate or extent of transforming growth factor beta1 activation.
|
1 | P23188 (/ISO) |
There are 17 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 |
---|---|---|
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
1 | P23188 (/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.
|
1 | P23188 (/TAS) |
Early endosome GO:0005769
A membrane-bounded organelle that receives incoming material from primary endocytic vesicles that have been generated by clathrin-dependent and clathrin-independent endocytosis; vesicles fuse with the early endosome to deliver cargo for sorting into recycling or degradation pathways.
|
1 | P23188 (/TAS) |
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 | P23188 (/ISO) |
Endoplasmic reticulum lumen GO:0005788
The volume enclosed by the membranes of the endoplasmic reticulum.
|
1 | P23188 (/TAS) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | P23377 (/IDA) |
Endoplasmic reticulum membrane GO:0005789
The lipid bilayer surrounding the endoplasmic reticulum.
|
1 | P23188 (/ISO) |
Trans-Golgi network GO:0005802
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination.
|
1 | P23188 (/ISO) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
1 | P23377 (/IDA) |
Plasma membrane GO:0005886
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
|
1 | P23188 (/ISO) |
Cell surface GO:0009986
The external part of the cell wall and/or plasma membrane.
|
1 | P23188 (/ISO) |
Trans-Golgi network transport vesicle membrane GO:0012510
The lipid bilayer surrounding a vesicle transporting substances between the trans-Golgi network and other parts of the cell.
|
1 | P23188 (/TAS) |
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 | P23188 (/TAS) |
Trans-Golgi network transport vesicle GO:0030140
A vesicle that mediates transport between the trans-Golgi network and other parts of the cell.
|
1 | P23188 (/ISO) |
Golgi cisterna GO:0031985
Any of the thin, flattened membrane-bounded compartments that form the central portion of the Golgi complex.
|
1 | P23377 (/IDA) |
Golgi cisterna GO:0031985
Any of the thin, flattened membrane-bounded compartments that form the central portion of the Golgi complex.
|
1 | P23188 (/ISO) |
Membrane raft GO:0045121
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions.
|
1 | P23188 (/ISO) |