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(9Z)-hexadec-9-enoyl-CoA + [Wg]-L-serine
CoA + [Wg]-O-(9Z)-hexadec-9-enoyl-L-serine
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
(9Z)-hexadec-9-enoyl-CoA + [Wnt3]-L-serine
CoA + [Wnt3]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5a]-L-serine
CoA + [Wnt5a]-O-(9Z)-hexadec-9-enoyl-L-serine
(9Z)-hexadec-9-enoyl-CoA + [Wnt5]-L-serine
CoA + [Wnt5]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [WntWg]-L-serine
CoA + [WntWg]-O-(9Z)-hexadec-9-enoyl-L-serine
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
decanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-decanoyl-L-serine
about 30% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
dodecanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-dodecanoyl-L-serine
about 15% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
hexanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-hexanoyl-L-serine
about 20% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
octanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-octanoyl-L-serine
about 25% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
tetradecanoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-tetradecanoyl-L-serine
about 10% of the activity as compared to (9Z)-hexadec-9-enoyl-CoA. There is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
[125I]iodo-pentadecenoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-[125I]iodo-pentadecenoyl-L-serine
[125I]iodo-pentadecenoyl-CoA is a radioiodinated palmitoleate analog
-
-
?
additional information
?
-
(9Z)-hexadec-9-enoyl-CoA + [Wg]-L-serine
CoA + [Wg]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wg]-L-serine
CoA + [Wg]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt substrate from Drosophila melanogaster
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
chicken substrate, and chimeric recombinant substrate containing amino acids 1-63 from mouse Wnt1 (-EPSLQL) and amino acids 64-370 from chicken Wnt1 (LSRKQ-)
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
chick WNT1 protein, the enzyme is an O-acyl transferase for WNT1 protein, WNT1 residues 214-234 are sufficient for PORCN-dependent palmitoylation of Ser224. Substitution of Ser224 with Thr, but not Cys, is tolerated in palmitoylation and biological assays. Transiently transfection of HEK-293T cells with WNT1. WNT1 mutant S224T is accepted as substrate, while mutants S224A and S224C are inactive
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
chicken substrate, and chimeric recombinant substrate containing amino acids 1-63 from mouse Wnt1 (-EPSLQL) and amino acids 64-370 from chicken Wnt1 (LSRKQ-)
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
chicken substrate, and chimeric recombinant substrate containing amino acids 1-63 from mouse Wnt1 (-EPSLQL) and amino acids 64-370 from chicken Wnt1 (LSRKQ-)
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
chicken substrate, and substrate from Mus musculus
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of the serine corresponding to Ser209 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated in the endoplasmic reticulum and targeted to exosomes, palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus, overview
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
chicken substrate, and substrate from Mus musculus
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated by fatty acids 13-16 carbons in length at Ser209 but not at Cys77, consistent with a slow turnover rate, glycosylation is not required for Wnt3a palmitoylation, which is necessary but not sufficient for Wnt3a secretion
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a expressed in L cells
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of the serine corresponding to Ser209 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated in the endoplasmic reticulum and targeted to exosomes, palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus, overview
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
chicken substrate, and substrate from Mus musculus
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated by fatty acids 13-16 carbons in length at Ser209 but not at Cys77, consistent with a slow turnover rate, glycosylation is not required for Wnt3a palmitoylation, which is necessary but not sufficient for Wnt3a secretion
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5a]-L-serine
CoA + [Wnt5a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5a]-L-serine
CoA + [Wnt5a]-O-(9Z)-hexadec-9-enoyl-L-serine
palmitoylation of Wnt-5a at Cys104
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [WntWg]-L-serine
CoA + [WntWg]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of Wnt Wingless or Wg
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [WntWg]-L-serine
CoA + [WntWg]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of Wnt Wingless or Wg. The enzyme binds the N-terminal 24-amino acid domain (residues 83-106) of Wg
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes posttranslational modification of Wnts with palmitoleic acid. PORCN is necessary and sufficient for Wnt acylation. PORCN intimately recognizes the local structure of Wnt around the site of acylation
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
there is an increase in the catalytic activity from hexanoyl-CoA to decanoyl-CoA, after which there is an abrupt drop for dodecanoyl-CoA. Upon further increase in fatty acyl chain length, the activity stays at approximately the same level until the unsaturated palmitoleoyl-CoA, which is the best substrate
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme is an essential mediators of Wnt secretion and signaling
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
additional information
?
-
-
enzyme Porc functions on the N-terminal 24-amino acid domain (83-106) of Wg, binding of Porc with Wg is essential for its activity
-
-
?
additional information
?
-
enzyme Porc functions on the N-terminal 24-amino acid domain (83-106) of Wg, binding of Porc with Wg is essential for its activity
-
-
?
additional information
?
-
-
recombinant c-Myc-tagged substrate Wg mutants T51A, S105A, S110A, and T416A
-
-
?
additional information
?
-
recombinant c-Myc-tagged substrate Wg mutants T51A, S105A, S110A, and T416A
-
-
?
additional information
?
-
-
vertebrate Wnt1 and Wnt3a possess at least one additional site for porcupine-mediated lipid-modification, localization of Wnt proteins in the chick neural tube, overview
-
-
?
additional information
?
-
PORCN splice variants differ globally in signaling activity
-
-
?
additional information
?
-
generation of a fusion protein that is palmitoylated in a PORCN-dependent manner, overview
-
-
?
additional information
?
-
no activity with palmitoylation-defective Wnt3aS209A mutant
-
-
?
additional information
?
-
-
no activity with palmitoylation-defective Wnt3aS209A mutant
-
-
?
additional information
?
-
vertebrate Wnt1 and Wnt3a possess at least one additional site for porcupine-mediated lipid-modification
-
-
?
additional information
?
-
-
vertebrate Wnt1 and Wnt3a possess at least one additional site for porcupine-mediated lipid-modification
-
-
?
additional information
?
-
no activity with palmitoylation-defective Wnt3aS209A mutant
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
(9Z)-hexadec-9-enoyl-CoA + [Wnt3]-L-serine
CoA + [Wnt3]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5a]-L-serine
CoA + [Wnt5a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt5]-L-serine
CoA + [Wnt5]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [WntWg]-L-serine
CoA + [WntWg]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of Wnt Wingless or Wg
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
additional information
?
-
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt1]-L-serine
CoA + [Wnt1]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of the serine corresponding to Ser209 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated in the endoplasmic reticulum and targeted to exosomes, palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus, overview
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
-
the enzyme catalyzes the palmitoylation of Ser209 and Cys77 of Wnt3a expressed in L cells
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes the palmitoylation of the serine corresponding to Ser209 of Wnt3a
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt3a]-L-serine
CoA + [Wnt3a]-O-(9Z)-hexadec-9-enoyl-L-serine
Wnt3a is palmitoylated in the endoplasmic reticulum and targeted to exosomes, palmitoylated Wnt3a proteins are found throughout the cytosol and at the plasma membrane but not in the nucleus, overview
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme catalyzes posttranslational modification of Wnts with palmitoleic acid. PORCN is necessary and sufficient for Wnt acylation. PORCN intimately recognizes the local structure of Wnt around the site of acylation
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
the enzyme is an essential mediators of Wnt secretion and signaling
-
-
?
(9Z)-hexadec-9-enoyl-CoA + [Wnt]-L-serine
CoA + [Wnt]-O-(9Z)-hexadec-9-enoyl-L-serine
-
-
-
?
additional information
?
-
-
enzyme Porc functions on the N-terminal 24-amino acid domain (83-106) of Wg, binding of Porc with Wg is essential for its activity
-
-
?
additional information
?
-
enzyme Porc functions on the N-terminal 24-amino acid domain (83-106) of Wg, binding of Porc with Wg is essential for its activity
-
-
?
additional information
?
-
PORCN splice variants differ globally in signaling activity
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-((3,6-dimethyl-4-oxo-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(6-methylbenzo[d]thiazol-2-yl)acetamide
-
-
2-((3-(3-methoxyphenyl)-4-oxo-3,4,4a,6,7,7a-hexahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(6-methylbenzo[d]thiazol-2-yl)acetamide
-
-
2-((3-(4-fluorophenyl)-4-oxo-3,4,4a,6,7,7a-hexahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(6-methylbenzo[d]thiazol-2-yl)acetamide
-
-
2-((3-cyclopentyl-4-oxo-3,4-dihydroquinazolin-2-yl)thio)-N-(4-(dimethylamino)phenyl)acetamide
-
-
2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(4-(piperidin-1-yl)phenyl)acetamide
-
-
2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(4-phenylthiazol-2-yl)acetamide
-
-
2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(5-(prop-1-en-2-yl)pyridin-2-yl)acetamide
-
-
2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)-N-(5-phenylthiazol-2-yl)acetamide
-
-
2-(4-(2-methylpyridin-4-yl)phenyl)-N-(4-(pyridin-3-yl)phenyl)acetamide
i.e. C59
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(5-phenylpyridin-2-yl)acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(5-phenylpyrimidin-2-yl)acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-(6-phenylpyridin-3-yl)acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[4-(pyridin-2-yl)phenyl]acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[4-(pyridin-3-yl)phenyl]acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[4-(pyridin-4-yl)phenyl]acetamide
-
-
2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[5-(pyrimidin-5-yl)pyridin-2-yl]acetamide
-
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2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[5-(thiophen-2-yl)pyridin-2-yl]acetamide
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2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]-N-[5-(thiophen-3-yl)pyridin-2-yl]acetamide
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2-[5-methyl-6-(2-methylpyridin-4-yl)pyridin-3-yl]-N-(5-pyrazin-2-ylpyridin-2-yl)acetamide
5-((3aR,4R,6aS)-6-(4-(2-((2-((6-methylbenzo[d]thiazol-2-yl)amino)-2-oxoethyl)thio)-4-oxo-4a,6,7,7a-tetrahydrothieno[3,2-d]pyrimidin-3(4H)-yl)phenethyl)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentanoic acid
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6-oxo-N-(2-oxo-2-(thiazol-2-ylamino)ethyl)-1-phenyl-1,6-dihydropyridazine-3-carboxamide
-
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ethyl 4-(2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamido)benzoate
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N-(2-((6-methoxybenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-3-(4-methoxyphenyl)-4-oxo-3,4-dihydrophthalazine-1-carboxamide
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N-(2-((6-methoxybenzo[d]thiazol-2-yl)amino)-2-oxoethyl)-6-oxo-1-phenyl-1,6-dihydropyridine-3-carboxamide
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N-(3,3'-bipyridin-6-yl)-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
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N-(4-(dimethylamino)phenyl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
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N-(4-butylphenyl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
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N-(5-ethoxypyridin-2-yl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
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N-(6-methoxyquinolin-2-yl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
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N-(6-methylbenzo[d]thiazol-2-yl)-2-((4-oxo-3-phenyl-3,4,4a,6,7,7a-hexahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
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N-(benzo[d]thiazol-2-yl)-2-((3-ethyl-6-methyl-4-oxo-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
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N-(biphenyl-2-yl)-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
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N-(biphenyl-3-yl)-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
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N-([1,1'-biphenyl]-4-yl)-2-((4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)thio)acetamide
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N-[5-(furan-2-yl)pyridin-2-yl]-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
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N-[5-(furan-2-yl)pyrimidin-2-yl]-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
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N-[5-(furan-3-yl)pyridin-2-yl]-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
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N-[5-(furan-3-yl)pyrimidin-2-yl]-2-[(4-oxo-3-phenyl-3,4,6,7-tetrahydrothieno[3,2-d]pyrimidin-2-yl)sulfanyl]acetamide
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additional information
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identification, synthesis, and analysis of small molecule enzyme IWP inhibitors, i.e. inhibitors of Wnt production, structure-activity relationship, overview
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2-[5-methyl-6-(2-methylpyridin-4-yl)pyridin-3-yl]-N-(5-pyrazin-2-ylpyridin-2-yl)acetamide
i.e. LGK-974
2-[5-methyl-6-(2-methylpyridin-4-yl)pyridin-3-yl]-N-(5-pyrazin-2-ylpyridin-2-yl)acetamide
i.e. LGK-974. Directly inhibits PORCN-mediated Wnt acylation
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evolution
Drosophila Porc has an extra hydrophilic N-terminal sequence, which is not found in other Porc enzymes
evolution
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the enzyme belongs to the family of membrane-bound O-acyltransferases (MBOAT), which transfer acyl groups, such as a palmitoyl group, to substrates
evolution
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the enzyme belongs to the family of membrane-bound O-acyltransferases (MBOAT), which transfer acyl groups, such as a palmitoyl group, to substrates
evolution
the enzyme belongs to the membrane-bound O-acyltransferase family
evolution
the enzyme belongs to the membrane-bound O-acyltransferase family
evolution
the enzyme is a member of the membrane-bound O-acyl transferase (MBOAT) superfamily
evolution
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the enzyme is a member of the membrane-bound O-acyltransferase family proteins
malfunction
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compromised Porcn activity commonly results in developmental disorders including focal dermal hypoplasia (Goltz syndrome) whereas hyperactivity of Porcn is associated with cancerous cell growth. Enzyme inhibition by small molecule IWP inhibitors affect Wnt-dependent developmental processes including zebrafish posterior axis formation and kidney tubule formation
malfunction
enzyme mutation, with a 219-kb deletion in Xp11.23 in two affected females, causes focal dermal hypoplasia is an X-linked dominant disorder characterized by patchy hypoplastic skin and digital, ocular and dental malformations
malfunction
gene deletion causes embryonic lethality in mice. PORCN null cells cannot activate WNT3A, PORCN null cells do not secrete WNT3A
malfunction
mutations in gene PORCN are associated with focal dermal hypoplasia. PORCN null cells are completely incapable of autocrine Wnt signaling
malfunction
the catalytically inactive porcupine is able to act as an inhibitor of endogenous porcupine, possibly via direct competition for substrate
malfunction
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treatment with a chemical inhibitor of acyltransferases produces defective intracellular trafficking of Wingless
malfunction
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Wnt-3a with defective acylation is not transferred from the endoplasmic reticulum
metabolism
porcupine (PORCN) and Wntless (WLS) are essential mediators of Wnt secretion and signaling. PORCN and WLS form a complex. THes compete for binding to WNT1. Overexpression of PORCN promotes palmitoylation of WNT1
metabolism
the enzyme catalyzes posttranslational modification of Wnts with palmitoleic acid. This unique form of lipidation with palmitoleic acid is a vital step in the biogenesis and secretion of Wnt
physiological function
ectopic expression of porc stimulates the N-glycosylation of both endogenously and exogenously expressed protein Wingless (Wg). The enzyme binds the N-terminal 24-amino acid domain (residues 83-106) of Wg, which is highly conserved in the Wnt family and stimulates the N-glycosylation at surrounding sites. The enzyme is also necessary for the processing of Drosophila Wnt-3/5 in both embryos and cultured cells. The enzyme binds the N-terminal specific domain of the Wnt family via its C-terminnus and stimulates its posttranslational N-glycosylation by anchoring them at the endoplasmic reticulum membrane possibly through acylation, overview
physiological function
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enzyme overexpression in culture cells enhances the intracellular processing, for example, N-glycosylation, of Wingless, the Drosophila Wnt1 analogue
physiological function
Mporc binds Wnt proteins and modifies their processing, the enzyme may function as a chaperone-like molecule for Wnt, overview
physiological function
palmitoylation of Wnt-5a is important for the triggering of signalling at the cell surface level, the lipid-unmodified form of Wnt-5a cannot activate intracellular signal cascades. The palmitoylation is not essential for the secretion of Wnt-5a, but is necessary for its ability to suppress Wnt-3a-dependent T-cell factor transcriptional activity and to stimulate cell migration. Wnt-5a activates focal adhesion kinase and this activation also requires palmitoylation. Palmitoylation enables Wnt5a to induces the internalization of Fz5 and to promote cell migration by stimulating focal adhesion turnover
physiological function
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porcupine is required for the acylation and secretion of Wnt-3a, porc-dependent acylation may regulate the processing and intracellular trafficking of Wnt, although acylation at Cys77 does not appear to be involved in these processes
physiological function
porcupine-mediated lipid-modification regulates the activity and distribution of Wnt proteins, and promotes their activity in 293T cells, porcupine is required for Wnt activity in 293T cells, and porcupine/palmitoylation regulates the activity of Wnt1 and Wnt3a in 293T cells
physiological function
porcupine-mediated lipid-modification regulates the activity and distribution of Wnt proteins, and promotes their activity in the chick neural tube, while it reduces the range of activity of Wnt1 and Wnt3a in the chick neural tube
physiological function
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porcupine-mediated lipid-modification regulates the activity and distribution of Wnt proteins, it promotes the activity of endogenous Wnt1 and Wnt3a in the chick neural tube, ectopic expression of mouse porcupine in the chick neural tube steepens the Wnt1/Wnt3a proliferation gradient, but porcupine expression restricts the Wnt activity range and distribution in the chicken neural tube, overview
physiological function
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the enzyme catalyzes the palmitoylation of Wnt proteins to enable its exit from the secretory pathway and subsequent activation of cellular responses
physiological function
the enzyme is a membrane-bound O-acyltransferase and is a key non-redundant node for the regulation of global Wnt signaling, essential regulatory role of PORCN in shaping Wnt signaling gradients. All Wnt activity absolutely requires posttranslational modification by the O-acyltransferase PORCN, whose abundance or activity modulates signaling tightly and over a large dynamic range, the enzyme activity is a key modulator of all Wnt ligand activity
physiological function
the enzyme is a membrane-bound O-acyltransferase and is a key non-redundant node for the regulation of global Wnt signaling, essential regulatory role of PORCN in shaping Wnt signaling gradients. All Wnt activity absolutely requires posttranslational modification by the O-acyltransferase PORCN, whose abundance or activity modulates signaling tightly and over a large dynamic range, the enzyme activity is a key modulator of all Wnt ligand activity
physiological function
the enzyme is critical for Wnt acylation and maintaining its hydrophobic nature, palmitoylation of the enzyme protein itself partially regulates Wnt palmitoylation and signaling, loss of palmitoylation of PORCN results in a modest increase in Wnt signaling, suggesting a negative regulatory role for PORCN Cys187 fatty acylation. Overexpression of PORCN promoted glycan processing of wild-type Wnt3a and the Ser209 (and Cys77) mutant, suggesting an additional acylation-independent role for the enzyme PORCN in maturation of Wnt3a
physiological function
the enzyme is critical for Wnt acylation and maintaining its hydrophobic nature, palmitoylation of the enzyme protein itself partially regulates Wnt palmitoylation and signaling. Overexpression of PORCN promoted glycan processing of wild-type Wnt3a and the Ser209 (and Cys77) mutant, suggesting an additional acylation-independent role for the enzyme PORCN in maturation of Wnt3a
physiological function
the enzyme is enzyme responsible for palmitoylating Wnt proteins, importance of enzyme catalyzed palmitoylation for WNT1 activity and Wnt signaling
physiological function
the enzyme is involved in secretion of Wnt proteins
physiological function
the enzyme is necessary for processing Wingless (Wg), a Drosophila Wnt (Wnt) family member. The enzyme modifies the processing of substrate Wg expressed in mammalian cells
additional information
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structure-activity relationship, overview
additional information
structure-function analysis, overview
additional information
structure-function analysis, overview
additional information
all Mporc types can substitute for Drosophila Porc, as they are able to rescue the phenotypes of Drosophila porc embryos, the enzyme modifies the processing of Drosophila Wg protein expressed in mammalian cells
additional information
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all Mporc types can substitute for Drosophila Porc, as they are able to rescue the phenotypes of Drosophila porc embryos, the enzyme modifies the processing of Drosophila Wg protein expressed in mammalian cells
additional information
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all Mus musculus Mporc types can substitute for Drosophila Porc, as they are able to rescue the phenotypes of Drosophila porc embryos
additional information
all Mus musculus Mporc types can substitute for Drosophila Porc, as they are able to rescue the phenotypes of Drosophila porc embryos
additional information
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model for the N-glycosylation of Wnt family, overview
additional information
model for the N-glycosylation of Wnt family, overview
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C187A
site-directed mutagenesis, increase in Wnt signaling activity of about 1.5fold upon expression of PORCNC187A compared to wild-type PORCN
C375X
site-directed mutagenesis, mutations introduced in PORCN at either Cys375, Cys381 or Cys385, all situated on a predicted luminal loop projecting from transmembrane domain VII that contains the catalytic His341 residue, have detrimental effects on Wnt3a palmitoylation and signaling that are comparable to that of the catalytically dead H341A mutant
C381X
site-directed mutagenesis, mutations introduced in PORCN at either Cys375, Cys381 or Cys385, all situated on a predicted luminal loop projecting from transmembrane domain VII that contains the catalytic His341 residue, have detrimental effects on Wnt3a palmitoylation and signaling that are comparable to that of the catalytically dead H341A mutant
C385X
site-directed mutagenesis, mutations introduced in PORCN at either Cys375, Cys381 or Cys385, all situated on a predicted luminal loop projecting from transmembrane domain VII that contains the catalytic His341 residue, have detrimental effects on Wnt3a palmitoylation and signaling that are comparable to that of the catalytically dead H341A mutant
H341D
site-directed mutagenesis, catalytically inactive mutant
H341Q
site-directed mutagenesis, catalytically inactive mutant
H341A
site-directed mutagenesis, catalytically inactive mutant
H341A
site-directed mutagenesis, the mutation reduces Wnt signaling relative to wild-type PORCN
H341A
site-directed mutagenesis, catalytic active site mutant, Wnt signaling inactive mutant
additional information
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generation of three different deletion mutants of the enzyme lacking residues 1-34, 1-66, or 1-110 (DELTA34, DELTA66, and DELTA110), the mutants show affeced N-glycosylation of Wingless protein, because the mutant enzymes cannot bind to Wingless, overview
additional information
generation of three different deletion mutants of the enzyme lacking residues 1-34, 1-66, or 1-110 (DELTA34, DELTA66, and DELTA110), the mutants show affeced N-glycosylation of Wingless protein, because the mutant enzymes cannot bind to Wingless, overview
additional information
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rescue of Drosophila porc embryos by Mus musculus Mporc RNA injection
additional information
rescue of Drosophila porc embryos by Mus musculus Mporc RNA injection
additional information
identification of enzyme mutants with a 219-kb deletion in Xp11.23, heterozygous and mosaic mutations in gene PORCN, genotyping, overview
additional information
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identification of enzyme mutants with a 219-kb deletion in Xp11.23, heterozygous and mosaic mutations in gene PORCN, genotyping, overview
additional information
overexpression of HA-tagged human PORC to confirm the ability of hPORC RNAi constructs to knockdown hPORC expression
additional information
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overexpression of HA-tagged human PORC to confirm the ability of hPORC RNAi constructs to knockdown hPORC expression
additional information
the cysteine mutations might be detrimental to the enzyme's tertiary structure and its catalytic activity
additional information
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the cysteine mutations might be detrimental to the enzyme's tertiary structure and its catalytic activity
additional information
zinc finger nuclease-mediated PORCN gene deletion in HT1080 cells. Mutation or skipping of PORCN exon 9 creates cells null for PORCN catalytic activity
additional information
PORCN is deleted by adenoviral Cre-GFP excision in immortalized MEF cells, PORCN null cells cannot activate WNT3A
additional information
rescue of Drosophila melanogaster porc embryos by Mporc RNA injection
additional information
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rescue of Drosophila melanogaster porc embryos by Mporc RNA injection
additional information
the catalytically inactive porcupine is able to act as an inhibitor of endogenous porcupine, possibly via direct competition for substrate
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Kurayoshi, M.; Yamamoto, H.; Izumi, S.; Kikuchi, A.
Post-translational palmitoylation and glycosylation of Wnt-5a are necessary for its signalling
Biochem. J.
402
515-523
2007
Homo sapiens (Q9H237)
brenda
Takada, R.; Satomi, Y.; Kurata, T.; Ueno, N.; Norioka, S.; Kondoh, H.; Takao, T.; Takada, S.
Monounsaturated fatty acid modification of Wnt p+rotein: its role in Wnt secretion
Dev. Cell
11
791-801
2006
Drosophila melanogaster, Mus musculus
brenda
Galli, L.; Barnes, T.; Secrest, S.; Kadowaki, T.; Burrus, L.
Porcupine-mediated lipid-modification regulates the activity and distribution of Wnt proteins in the chick neural tube
Development
134
3339-3348
2007
Gallus gallus, Homo sapiens (Q9H237), Homo sapiens, Mus musculus (Q9JJJ7)
brenda
Tanaka, K.; Okabayashi, K.; Asashima, M.; Perrimon, N.; Kadowaki, T.
The evolutionarily conserved porcupine family is involved in the processing of the Wnt family
Eur. J. Biochem.
267
4300-4311
2000
Drosophila melanogaster, Drosophila melanogaster (Q9VWV9), Caenorhabditis elegans (Q22329), Homo sapiens (Q9H237), Xenopus laevis (Q9I935), Mus musculus (Q9JJJ7), Mus musculus
brenda
Miranda, M.; Galli, L.M.; Enriquez, M.; Szabo, L.A.; Gao, X.; Hannoush, R.N.; Burrus, L.W.
Identification of the WNT1 residues required for palmitoylation by Porcupine
FEBS Lett.
588
4815-4824
2014
Homo sapiens (Q9H237)
brenda
Proffitt, K.D.; Virshup, D.M.
Precise regulation of porcupine activity is required for physiological Wnt signaling
J. Biol. Chem.
287
34167-34178
2012
Homo sapiens (Q9H237), Mus musculus (Q9JJJ7)
brenda
Wang, X.; Moon, J.; Dodge, M.E.; Pan, X.; Zhang, L.; Hanson, J.M.; Tuladhar, R.; Ma, Z.; Shi, H.; Williams, N.S.; Amatruda, J.F.; Carroll, T.J.; Lum, L.; Chen, C.
The development of highly potent inhibitors for porcupine
J. Med. Chem.
56
2700-2704
2013
Danio rerio
brenda
Gao, X.; Hannoush, R.N.
Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine
Nat. Chem. Biol.
10
61-68
2014
Homo sapiens (Q9H237), Homo sapiens, Mus musculus (Q9JJJ7)
brenda
Wang, X.; Reid Sutton, V.; Omar Peraza-Llanes, J.; Yu, Z.; Rosetta, R.; Kou, Y.C.; Eble, T.N.; Patel, A.; Thaller, C.; Fang, P.; Van den Veyver, I.B.
Mutations in X-linked PORCN, a putative regulator of Wnt signaling, cause focal dermal hypoplasia
Nat. Genet.
39
836-838
2007
Homo sapiens (Q9H237), Homo sapiens
brenda
Galli, L.M.; Zebarjadi, N.; Li, L.; Lingappa, V.R.; Burrus, L.W.
Divergent effects of porcupine and Wntless on WNT1 trafficking, secretion, and signaling
Exp. Cell Res.
347
171-183
2016
Mus musculus (Q9JJJ7)
brenda
Asciolla, J.J.; Miele, M.M.; Hendrickson, R.C.; Resh, M.D.
An in vitro fatty acylation assay reveals a mechanism for Wnt recognition by the acyltransferase porcupine
J. Biol. Chem.
292
13507-13513
2017
Mus musculus (Q9JJJ7)
brenda
Lee, C.J.; Rana, M.S.; Bae, C.; Li, Y.; Banerjee, A.
In vitro reconstitution of Wnt acylation reveals structural determinants of substrate recognition by the acyltransferase human porcupine
J. Biol. Chem.
294
231-245
2019
Homo sapiens (Q9H237), Homo sapiens
brenda