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 named:
"N-Acetylglucosaminyltransferase I, Domain 2
".
FunFam 1: alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglu...
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 10 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 |
---|---|---|
Alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity GO:0003827
Catalysis of the reaction: 3-(alpha-D-mannosyl)-beta-D-mannosyl-R + UDP-N-acetyl-alpha-D-glucosamine = 3-(2-
|
4 | G5EFK6 (/IDA) P26572 (/IDA) Q60GL7 (/IDA) Q9NGK4 (/IDA) |
Alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity GO:0003827
Catalysis of the reaction: 3-(alpha-D-mannosyl)-beta-D-mannosyl-R + UDP-N-acetyl-alpha-D-glucosamine = 3-(2-
|
4 | P27115 (/ISS) P27808 (/ISS) P27808 (/ISS) Q11068 (/ISS) |
Acetylglucosaminyltransferase activity GO:0008375
Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar.
|
4 | P27808 (/IDA) P27808 (/IDA) Q60GL7 (/IDA) Q9NGK4 (/IDA) |
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
|
3 | P27115 (/ISS) P27808 (/ISS) P27808 (/ISS) |
Alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity GO:0003827
Catalysis of the reaction: 3-(alpha-D-mannosyl)-beta-D-mannosyl-R + UDP-N-acetyl-alpha-D-glucosamine = 3-(2-
|
2 | P27808 (/ISO) P27808 (/ISO) |
Acetylglucosaminyltransferase activity GO:0008375
Catalysis of the transfer of an N-acetylglucosaminyl residue from UDP-N-acetyl-glucosamine to a sugar.
|
2 | P27808 (/IMP) P27808 (/IMP) |
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
|
2 | P27808 (/ISO) P27808 (/ISO) |
Alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity GO:0003827
Catalysis of the reaction: 3-(alpha-D-mannosyl)-beta-D-mannosyl-R + UDP-N-acetyl-alpha-D-glucosamine = 3-(2-
|
1 | P26572 (/TAS) |
Protein N-acetylglucosaminyltransferase activity GO:0016262
Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + protein = UDP + 4-N-(N-acetyl-D-glucosaminyl)-protein.
|
1 | P27115 (/IDA) |
Manganese ion binding GO:0030145
Interacting selectively and non-covalently with manganese (Mn) ions.
|
1 | P26572 (/IDA) |
There are 14 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 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.
|
4 | G5EFK6 (/IDA) P27115 (/IDA) Q60GL7 (/IDA) Q9NGK4 (/IDA) |
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.
|
3 | P26572 (/IDA) Q60GL7 (/IDA) Q9NGK4 (/IDA) |
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.
|
3 | P27115 (/ISS) P27808 (/ISS) P27808 (/ISS) |
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.
|
2 | P27808 (/IMP) P27808 (/IMP) |
UDP-N-acetylglucosamine catabolic process GO:0006049
The chemical reactions and pathways resulting in the breakdown of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate.
|
2 | P27808 (/IDA) P27808 (/IDA) |
Determination of adult lifespan GO:0008340
The control of viability and duration in the adult phase of the life-cycle.
|
2 | Q60GL7 (/IMP) Q9NGK4 (/IMP) |
Adult locomotory behavior GO:0008344
Locomotory behavior in a fully developed and mature organism.
|
2 | Q60GL7 (/IMP) Q9NGK4 (/IMP) |
Mushroom body development GO:0016319
The process whose specific outcome is the progression of the mushroom body over time, from its formation to the mature structure. The mushroom body is composed of the prominent neuropil structures of the insect central brain, thought to be crucial for olfactory associated learning. These consist mainly of a bulbous calyx and tightly packaged arrays of thin parallel fibers of the Kenyon cells.
|
2 | Q60GL7 (/IMP) Q9NGK4 (/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.
|
2 | P27808 (/ISO) P27808 (/ISO) |
Encapsulation of foreign target GO:0035010
Events resulting in the formation of a multilayered cellular sheath surrounding an invader and thus preventing its development. This defense mechanism is often seen in insects in response to nematodes or parasitoids, which are too large to be phagocytosed by individual hemocytes. In some organisms the capsule is blackened due to melanization.
|
2 | Q60GL7 (/IMP) Q9NGK4 (/IMP) |
Mannose metabolic process GO:0006013
The chemical reactions and pathways involving mannose, the aldohexose manno-hexose, the C-2 epimer of glucose. The D-(+)-form is widely distributed in mannans and hemicelluloses and is of major importance in the core oligosaccharide of N-linked oligosaccharides of glycoproteins.
|
1 | P27115 (/IDA) |
Protein glycosylation GO:0006486
A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins.
|
1 | P70680 (/IMP) |
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.
|
1 | Q11068 (/ISS) |
Brain segmentation GO:0035284
Division of the brain into a series of semi-repetitive parts or segments.
|
1 | Q60GL7 (/IMP) |
There are 10 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.
|
3 | P27115 (/ISS) P27808 (/ISS) P27808 (/ISS) |
Golgi medial cisterna GO:0005797
The middle Golgi cisterna (or cisternae).
|
3 | P27115 (/IDA) Q60GL7 (/IDA) Q9NGK4 (/IDA) |
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
2 | P27808 (/ISO) P27808 (/ISO) |
Golgi medial cisterna GO:0005797
The middle Golgi cisterna (or cisternae).
|
2 | G5EFK6 (/ISS) Q11068 (/ISS) |
Perinuclear region of cytoplasm GO:0048471
Cytoplasm situated near, or occurring around, the nucleus.
|
2 | G5EFK6 (/IDA) Q11068 (/IDA) |
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
1 | P26572 (/IDA) |
Golgi membrane GO:0000139
The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
|
1 | P26572 (/TAS) |
Membrane GO:0016020
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
|
1 | P26572 (/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.
|
1 | P26572 (/HDA) |
Extracellular vesicle GO:1903561
Any vesicle that is part of the extracellular region.
|
1 | P26572 (/HDA) |