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Literature summary for 2.4.1.221 extracted from

  • Kim, M.L.; Chandrasekharan, K.; Glass, M.; Shi, S.; Stahl, M.C.; Kaspar, B.; Stanley, P.; Martin, P.T.
    O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors (2008), Mol. Cell. Neurosci., 39, 452-464.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.221

Protein Variants

Protein Variants Comment Organism
additional information deletion of Pofut1 in cultured primary myotubes and in adult skeletal muscle increases acetylcholine receptor aggregation Mus musculus
S1726A mutant protein shows no activity, loss of O-fucosylation causes a gain of function for muscle agrin such that it stimulates acetylcholine receptors, clustering and MuSK phosphorylation in cultured myotubes at levels normally only found with the neural splice form Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
-
C2C12 cell
-
 Mus musculus
-
muscle
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GDP-Fuc + biotin-DHPCTQALGNPCLNGGSCVPREATYECLCPGGFSGLHCEKG peptide of the fourth EGF domain of agrin (EGF4) is used as an acceptor substrate with biotin conjugated at the N-terminus Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
Pofut1
-
 Mus musculus
protein O-fucosyltransferase 1
-
 Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Mus musculus