Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.198 extracted from

  • Shao, M.; Liu, Z.Z.; Wang, C.D.; Li, H.Y.; Carron, C.; Zhang, H.W.; Shi, D.L.
    Down syndrome critical region protein 5 regulates membrane localization of Wnt receptors, Dishevelled stability and convergent extension in vertebrate embryos (2009), Development, 136, 2121-2131.
    View publication on PubMed
Search for more literature for 2.4.1.198

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-glucosamine + phosphatidylinositol Xenopus laevis
-
 UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
 ?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol Danio rerio
-
 UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
 ?

Organism

Organism UniProt Comment Textmining
Danio rerio
-
-
-
Xenopus laevis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
 Xenopus laevis
-
embryo
-
 Danio rerio
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
-
 Xenopus laevis UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
 ?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
-
 Danio rerio UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
 ?

Synonyms

Synonyms Comment Organism
Down syndrome critical region protein 5 also known as Pigp, a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex Xenopus laevis
Down syndrome critical region protein 5 also known as Pigp, a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex Danio rerio
Dscr5 also known as phosphatidylinositol glycan class P (Pigp), a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex Xenopus laevis
Dscr5 also known as phosphatidylinositol glycan class P (Pigp), a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex Danio rerio
glycosylphosphatidylinositol-N-acetylglucosaminyltransferase
-
 Xenopus laevis
glycosylphosphatidylinositol-N-acetylglucosaminyltransferase
-
 Danio rerio
GPI-GnT
-
 Xenopus laevis
GPI-GnT
-
 Danio rerio
GPI-N-acetylglucosaminyltransferase
-
 Xenopus laevis
GPI-N-acetylglucosaminyltransferase
-
 Danio rerio

General Information

General Information Comment Organism
malfunction knockdown of dscr5 disrupts Knypek membrane localization and causes an enhanced Frizzled 7 receptor endocytosis in a caveolin-dependent manner, dscr5 knockdown promotes specific Dishevelled degradation by the ubiquitin-proteosome pathway, knockdown of dscr5 disrupts convergence of lateral cells and extension of dorsal cells, knockdown of dscr5 does not affect embryonic patterning Xenopus laevis
malfunction knockdown of dscr5 disrupts Knypek membrane localization and causes an enhanced Frizzled 7 receptor endocytosis in a caveolin-dependent manner, dscr5 knockdown promotes specific Dishevelled degradation by the ubiquitin-proteosome pathway, knockdown of dscr5 disrupts convergence of lateral cells and extension of dorsal cells, knockdown of dscr5 does not affect embryonic patterning Danio rerio
physiological function Dscr5 functionally interacts with Knypek/Glypican 4 and is required for its localization at the cell surface, Dscr5 interacts with the planar cell polarity pathway in convergent extension movements Xenopus laevis
physiological function Dscr5 functionally interacts with Knypek/Glypican 4 and is required for its localization at the cell surface, Dscr5 interacts with the planar cell polarity pathway in convergent extension movements Danio rerio