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:
"ESAT-6-like
".
FunFam 3: Alpha-(1,6)-fucosyltransferase
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 8 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 |
---|---|---|
Glycoprotein 6-alpha-L-fucosyltransferase activity GO:0008424
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-
|
12 |
P79282 (/ISS)
Q5NVB3 (/ISS)
Q659X0 (/ISS)
Q6EV76 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6NVP8 (/ISS)
(2 more) |
Glycoprotein 6-alpha-L-fucosyltransferase activity GO:0008424
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-
|
5 | Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) |
Glycoprotein 6-alpha-L-fucosyltransferase activity GO:0008424
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-
|
5 | Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) |
Alpha-(1->6)-fucosyltransferase activity GO:0046921
Catalysis of the transfer of an L-fucosyl group from GDP-beta-L-fucose to an acceptor molecule to form an alpha-(1->6) linkage.
|
3 | F1QW63 (/IMP) Q6EV75 (/IMP) Q9WTS2 (/IMP) |
Glycoprotein 6-alpha-L-fucosyltransferase activity GO:0008424
Catalysis of the reaction: N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-
|
1 | Q9WTS2 (/ISO) |
Transferase activity, transferring glycosyl groups GO:0016757
Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
|
1 | P79282 (/IDA) |
Transferase activity, transferring glycosyl groups GO:0016757
Catalysis of the transfer of a glycosyl group from one compound (donor) to another (acceptor).
|
1 | Q9WTS2 (/ISA) |
Alpha-(1->6)-fucosyltransferase activity GO:0046921
Catalysis of the transfer of an L-fucosyl group from GDP-beta-L-fucose to an acceptor molecule to form an alpha-(1->6) linkage.
|
1 | Q5ZHT6 (/ISS) |
There are 23 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 N-linked glycosylation via asparagine GO:0018279
The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
|
12 |
P79282 (/ISS)
Q5NVB3 (/ISS)
Q659X0 (/ISS)
Q6EV76 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6NVP8 (/ISS)
(2 more) |
GDP-L-fucose metabolic process GO:0046368
The chemical reactions and pathways involving GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate.
|
12 |
P79282 (/ISS)
Q5NVB3 (/ISS)
Q659X0 (/ISS)
Q6EV76 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6EV77 (/ISS)
Q6NVP8 (/ISS)
(2 more) |
In utero embryonic development GO:0001701
The process whose specific outcome is the progression of the embryo in the uterus over time, from formation of the zygote in the oviduct, to birth. An example of this process is found in Mus musculus.
|
5 | Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) |
Protein N-linked glycosylation GO:0006487
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan.
|
5 | Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) |
N-glycan processing GO:0006491
The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
|
5 | Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) |
Oligosaccharide biosynthetic process GO:0009312
The chemical reactions and pathways resulting in the formation of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
|
5 | Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) |
Protein N-linked glycosylation via asparagine GO:0018279
The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
|
5 | Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) |
L-fucose catabolic process GO:0042355
The chemical reactions and pathways resulting in the breakdown of L-fucose (6-deoxy-Lgalactose).
|
5 | Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) |
GDP-L-fucose metabolic process GO:0046368
The chemical reactions and pathways involving GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate.
|
5 | Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) |
N-glycan fucosylation GO:0036071
The process of transferring a fucosyl group to an N-glycan. An N-glycan is the carbohydrate portion of an N-glycoprotein when attached to a nitrogen from asparagine or arginine side-chains.
|
3 | F1QW63 (/IMP) Q6EV75 (/IMP) Q9WTS2 (/IMP) |
N-glycan processing GO:0006491
The conversion of N-linked glycan (N = nitrogen) structures from the initially transferred oligosaccharide to a mature form, by the actions of glycosidases and glycosyltransferases. The early processing steps are conserved and play roles in glycoprotein folding and trafficking.
|
1 | Q9WTS2 (/IMP) |
Transforming growth factor beta receptor signaling pathway GO:0007179
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
|
1 | Q9WTS2 (/IMP) |
Transforming growth factor beta receptor signaling pathway GO:0007179
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
|
1 | Q5ZHT6 (/ISS) |
Integrin-mediated signaling pathway GO:0007229
A series of molecular signals initiated by the binding of extracellular ligand to an integrin on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription.
|
1 | Q9WTS2 (/IMP) |
Respiratory gaseous exchange by respiratory system GO:0007585
The process of gaseous exchange between an organism and its environment. In plants, microorganisms, and many small animals, air or water makes direct contact with the organism's cells or tissue fluids, and the processes of diffusion supply the organism with dioxygen (O2) and remove carbon dioxide (CO2). In larger animals the efficiency of gaseous exchange is improved by specialized respiratory organs, such as lungs and gills, which are ventilated by breathing mechanisms.
|
1 | Q9WTS2 (/IMP) |
Respiratory gaseous exchange by respiratory system GO:0007585
The process of gaseous exchange between an organism and its environment. In plants, microorganisms, and many small animals, air or water makes direct contact with the organism's cells or tissue fluids, and the processes of diffusion supply the organism with dioxygen (O2) and remove carbon dioxide (CO2). In larger animals the efficiency of gaseous exchange is improved by specialized respiratory organs, such as lungs and gills, which are ventilated by breathing mechanisms.
|
1 | Q5ZHT6 (/ISS) |
Regulation of gene expression GO:0010468
Any process that modulates the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product or products (proteins or RNA). This includes the production of an RNA transcript as well as any processing to produce a mature RNA product or an mRNA or circRNA (for protein-coding genes) and the translation of that mRNA or circRNA into protein. Protein maturation is included when required to form an active form of a product from an inactive precursor form.
|
1 | Q9WTS2 (/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.
|
1 | Q9WTS2 (/IMP) |
Protein N-linked glycosylation via asparagine GO:0018279
The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
|
1 | Q9WTS2 (/ISO) |
Receptor metabolic process GO:0043112
The chemical reactions and pathways involving a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
|
1 | Q9WTS2 (/IMP) |
Receptor metabolic process GO:0043112
The chemical reactions and pathways involving a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.
|
1 | Q5ZHT6 (/ISS) |
GDP-L-fucose metabolic process GO:0046368
The chemical reactions and pathways involving GDP-L-fucose, a substance composed of L-fucose in glycosidic linkage with guanosine diphosphate.
|
1 | Q9WTS2 (/ISO) |
Regulation of cellular response to oxidative stress GO:1900407
Any process that modulates the frequency, rate or extent of cellular response to oxidative stress.
|
1 | Q9WTS2 (/IMP) |
There are 6 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 |
---|---|---|
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
10 | Q546E0 (/IDA) Q546E0 (/IDA) Q546E0 (/IDA) Q546E0 (/IDA) Q546E0 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) Q9BYC5 (/IDA) |
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
5 | Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) Q9BYC5 (/TAS) |
Golgi apparatus GO:0005794
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions.
|
5 | Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) Q9BYC5 (/NAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
5 | Q9BYC5 (/HDA) Q9BYC5 (/HDA) Q9BYC5 (/HDA) Q9BYC5 (/HDA) Q9BYC5 (/HDA) |
Extracellular exosome GO:0070062
A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.
|
5 | Q9BYC5 (/HDA) Q9BYC5 (/HDA) Q9BYC5 (/HDA) Q9BYC5 (/HDA) Q9BYC5 (/HDA) |
Cytosol GO:0005829
The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
|
1 | Q9WTS2 (/ISO) |