Literature summary extracted from

Abrantes, J.; Posada, D.; Guillon, P.; Esteves, P.J.; Le Pendu, J.
Widespread gene conversion of alpha-2-fucosyltransferase genes in mammals (2009), J. Mol. Evol., 69, 22-31.

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.4.1.69	Bos taurus	A4IFH1	-	-
2.4.1.69	Bos taurus	Q28113	-	-
2.4.1.69	Bos taurus	Q9TTY3	-	-
2.4.1.69	Chlorocebus sabaeus	-	-	-
2.4.1.69	Chlorocebus sabaeus	O77711	-	-
2.4.1.69	Chlorocebus sabaeus	O77712	-	-
2.4.1.69	Gorilla gorilla	O77486	-	-
2.4.1.69	Gorilla gorilla	Q9TUD4	-	-
2.4.1.69	Homo sapiens	P19526	-	-
2.4.1.69	Homo sapiens	Q10981	-	-
2.4.1.69	Homo sapiens	Q5XLR8	-	-
2.4.1.69	Hylobates agilis	Q6LA46	-	-
2.4.1.69	Hylobates lar	Q9TTC7	-	-
2.4.1.69	Macaca fascicularis	Q9N266	fragment	-
2.4.1.69	Monodelphis domestica	-	a FUT2-like gene sequence in opossum is found	-
2.4.1.69	Mus musculus	O09160	-	-
2.4.1.69	Mus musculus	P97353	-	-
2.4.1.69	Oryctolagus cuniculus	Q10979	-	-
2.4.1.69	Oryctolagus cuniculus	Q10983	-	-
2.4.1.69	Oryctolagus cuniculus	Q29505	-	-
2.4.1.69	Pan troglodytes	O77485	-	-
2.4.1.69	Pan troglodytes	Q9TUD6	-	-
2.4.1.69	Pongo pygmaeus	O77487	-	-
2.4.1.69	Pongo pygmaeus	Q6LA45	-	-
2.4.1.69	Rattus norvegicus	Q10980	-	-
2.4.1.69	Rattus norvegicus	Q10984	-	-
2.4.1.69	Rattus norvegicus	Q9WUE6	-	-
2.4.1.69	Sus scrofa	Q10982	-	-
2.4.1.69	Sus scrofa	Q29043	-	-
2.4.1.69	Xenopus tropicalis	-	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
2.4.1.69	alpha-2-fucosyltransferase	-	Chlorocebus sabaeus
2.4.1.69	alpha-2-fucosyltransferase	-	Homo sapiens
2.4.1.69	alpha-2-fucosyltransferase	-	Xenopus tropicalis
2.4.1.69	alpha-2-fucosyltransferase	-	Pongo pygmaeus
2.4.1.69	alpha-2-fucosyltransferase	-	Hylobates lar
2.4.1.69	alpha-2-fucosyltransferase	-	Hylobates agilis
2.4.1.69	alpha-2-fucosyltransferase	-	Macaca fascicularis
2.4.1.69	alpha-2-fucosyltransferase	-	Bos taurus
2.4.1.69	alpha-2-fucosyltransferase	-	Mus musculus
2.4.1.69	alpha-2-fucosyltransferase	-	Rattus norvegicus
2.4.1.69	alpha-2-fucosyltransferase	-	Sus scrofa
2.4.1.69	alpha-2-fucosyltransferase	-	Oryctolagus cuniculus
2.4.1.69	alpha-2-fucosyltransferase	-	Pan troglodytes
2.4.1.69	alpha-2-fucosyltransferase	-	Gorilla gorilla
2.4.1.69	alpha1,2fucosyltransferase	-	Chlorocebus sabaeus
2.4.1.69	alpha1,2fucosyltransferase	-	Homo sapiens
2.4.1.69	alpha1,2fucosyltransferase	-	Xenopus tropicalis
2.4.1.69	alpha1,2fucosyltransferase	-	Pongo pygmaeus
2.4.1.69	alpha1,2fucosyltransferase	-	Hylobates lar
2.4.1.69	alpha1,2fucosyltransferase	-	Hylobates agilis
2.4.1.69	alpha1,2fucosyltransferase	-	Macaca fascicularis
2.4.1.69	alpha1,2fucosyltransferase	-	Bos taurus
2.4.1.69	alpha1,2fucosyltransferase	-	Mus musculus
2.4.1.69	alpha1,2fucosyltransferase	-	Rattus norvegicus
2.4.1.69	alpha1,2fucosyltransferase	-	Sus scrofa
2.4.1.69	alpha1,2fucosyltransferase	-	Oryctolagus cuniculus
2.4.1.69	alpha1,2fucosyltransferase	-	Pan troglodytes
2.4.1.69	alpha1,2fucosyltransferase	-	Gorilla gorilla
2.4.1.69	alpha2FT	-	Chlorocebus sabaeus
2.4.1.69	alpha2FT	-	Homo sapiens
2.4.1.69	alpha2FT	-	Xenopus tropicalis
2.4.1.69	alpha2FT	-	Pongo pygmaeus
2.4.1.69	alpha2FT	-	Hylobates lar
2.4.1.69	alpha2FT	-	Hylobates agilis
2.4.1.69	alpha2FT	-	Macaca fascicularis
2.4.1.69	alpha2FT	-	Bos taurus
2.4.1.69	alpha2FT	-	Mus musculus
2.4.1.69	alpha2FT	-	Rattus norvegicus
2.4.1.69	alpha2FT	-	Sus scrofa
2.4.1.69	alpha2FT	-	Oryctolagus cuniculus
2.4.1.69	alpha2FT	-	Pan troglodytes
2.4.1.69	alpha2FT	-	Gorilla gorilla
2.4.1.69	FUT1	-	Homo sapiens
2.4.1.69	FUT1	-	Xenopus tropicalis
2.4.1.69	FUT1	-	Chlorocebus sabaeus
2.4.1.69	FUT1	-	Bos taurus
2.4.1.69	FUT1	-	Mus musculus
2.4.1.69	FUT1	-	Rattus norvegicus
2.4.1.69	FUT1	-	Sus scrofa
2.4.1.69	FUT1	-	Oryctolagus cuniculus
2.4.1.69	FUT1	-	Pan troglodytes
2.4.1.69	FUT1	-	Gorilla gorilla
2.4.1.69	FUT2	-	Hylobates lar
2.4.1.69	FUT2	-	Chlorocebus sabaeus
2.4.1.69	FUT2	-	Bos taurus
2.4.1.69	FUT2	-	Rattus norvegicus
2.4.1.69	FUT2	-	Sus scrofa
2.4.1.69	FUT2	-	Oryctolagus cuniculus
2.4.1.69	FUT2	-	Pan troglodytes
2.4.1.69	FUT2	-	Pongo pygmaeus
2.4.1.69	FUT2	-	Gorilla gorilla
2.4.1.69	FUT2	-	Monodelphis domestica
2.4.1.69	FUT2	a FUT2-like gene sequence in opossum is found	Monodelphis domestica
2.4.1.69	Sec1	-	Chlorocebus sabaeus
2.4.1.69	Sec1	-	Pongo pygmaeus
2.4.1.69	Sec1	-	Homo sapiens
2.4.1.69	Sec1	-	Hylobates agilis
2.4.1.69	Sec1	-	Macaca fascicularis
2.4.1.69	Sec1	-	Bos taurus
2.4.1.69	Sec1	-	Mus musculus
2.4.1.69	Sec1	-	Rattus norvegicus
2.4.1.69	Sec1	-	Sus scrofa
2.4.1.69	Sec1	-	Oryctolagus cuniculus

General Information

EC Number	General Information	Comment	Organism
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Chlorocebus sabaeus
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Xenopus tropicalis
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Hylobates lar
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Hylobates agilis
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Macaca fascicularis
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Bos taurus
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Mus musculus
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Rattus norvegicus
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Sus scrofa
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Oryctolagus cuniculus
2.4.1.69	physiological function	Biosynthesis of cell surface glycoconjugates, which play a role in infections. For example, nonsecretors are known to be virtually resistant to infection by norovirus. Inversely, women with the nonsecretor phenotype are more prone to Escherichia coli mediated recurrent urinary tract infections than secretor women.	Gorilla gorilla