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Information on EC 2.4.1.198 - phosphatidylinositol N-acetylglucosaminyltransferase
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EC Tree
2.4.1.198 phosphatidylinositol N-acetylglucosaminyltransferaseIUBMB Comments
Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). PIG-A subunit is the catalytic subunit. In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.
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Word Map
- 2.4.1.198
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paroxysmal
-
nocturnal
- hemoglobinuria
-
gpi-anchored
-
hematopoietic
-
genotoxicity
- marrow
-
x-linked
- anemia
-
aplastic
- micronucleus
-
hemolysis
-
cytometric
- granulocytes
-
micronucleated
-
intravascular
- analysis
-
n-ethyl-n-nitrosourea
- comet
-
gpi-linked
-
glycosylphosphatidylinositol-anchored
-
complement-mediated
-
pigret
-
clastogenic
-
gpi-deficient
-
mn-rets
-
gpi-aps
- eculizumab
-
myelodysplastic
- procarbazine
-
enu-treated
- 4-nitroquinoline-1-oxide
-
haemopoietic
-
immunomagnetic
-
genotoxicants
-
repeat-dose
-
enu-induced
- proaerolysin
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
pig-a, gpi-gnt, dscr5, gpi-n-acetylglucosaminyltransferase, gpi19, gpi-glcnac transferase, phosphatidylinositol n-acetylglucosaminyltransferase, gpi15, phosphatidylinositol n-acetylglucosaminyltransferase subunit a, afpig-a, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetyl-D-glucosaminyltransferase, uridine diphosphoacetylglucosamine alpha1,6-
-
-
-
-
afpig-a
Down syndrome critical region protein 5
DR437w
-
encodes an essential subunit of the yeast glycosylphosphatidylinositol N-acetylglucosaminyltransferase. The C-terminus is cytoplasmic, the N-terminus is also cytoplasmic and both transmembrane domains pass through the ER membrane. The N-terminal half (at least 60 residues) is dispensable for functions at low temperatures
Dscr5
glycosylphosphatidylinositol N-acetylglucosaminyltransferase complex
-
-
glycosylphosphatidylinositol-N-acetylglucosaminyltransferase
GPI-GlcNAc transferase
GPI-GnT
GPI-N-acetylglucosaminyltransferase
GPI-N-acetylglucosaminyltransferase complex
GPI1
GPI15
GPI19
GPI2
GPI3
PIG-A
PigA
UDP-N-acetyl-D-glucosamine:phosphatidylinositol N-acetyl-D-glucosaminyltransferase
-
-
-
-
uridine diphosphoacetylglucosamine alpha1,6-acetyl-D-glucosaminyltransferase
-
-
-
-
afpig-a
gene is the homologue of GPI3 /SPT14 /pig-A gene (encode the catalytic subunit of glycosylphosphatidylinositol-N-acetylglucoaminyltransferase complex) in Aspergillus fumigatus
afpig-a
gene is the homologue of GPI3 /SPT14 /pig-A gene (encode the catalytic subunit of glycosylphosphatidylinositol-N-acetylglucoaminyltransferase complex) in Aspergillus fumigatus
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Down syndrome critical region protein 5
-
also known as Pigp, a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex
Down syndrome critical region protein 5
-
also known as Pigp, a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex
Dscr5
-
also known as phosphatidylinositol glycan class P (Pigp), a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex
Dscr5
-
also known as phosphatidylinositol glycan class P (Pigp), a component of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex
GPI-N-acetylglucosaminyltransferase
-
-
GPI19
-
YDR437w (encodes an essential subunit of the yeast glycosylphosphatidylinositol N-acetylglucosaminyltransferase) is also called GPI19 (for glycosylphosphatidylinositol anchor 19)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:1-phosphatidyl-1D-myo-inositol 6-(N-acetyl-alpha-D-glucosaminyl)transferase
Involved in the first step of glycosylphosphatidylinositol (GPI) anchor formation in all eukaryotes. In mammalian cells, the enzyme is composed of at least five subunits (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). PIG-A subunit is the catalytic subunit. In some species, the long-chain acyl groups of the phosphatidyl group are partly replaced by long-chain alkyl or alk-1-enyl groups.
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CAS REGISTRY NUMBER
COMMENTARY
144388-35-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Halalkalibacterium halodurans
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
in alpha1-6 linkage
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
substrate specificity
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
enzyme complex
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
in alpha1-6 linkage
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
-
?
additional information
?
-
-
biosynthetic pathway and subcellular localization, overview
-
-
?
additional information
?
-
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
?
additional information
?
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
?
additional information
?
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
?
additional information
?
-
-
enzyme defect in paroxysmal nocturnal hemoglobinuria
-
-
?
additional information
?
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
?
additional information
?
-
-
biosynthetic pathway and subcellular localization, overview
-
-
?
additional information
?
-
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
-
-
?
additional information
?
-
-
glycosylphosphatidylinositol anchoring is essential for transport of cell surface proteins and enzyme deficieny leads to defective cell wall synthesis and cell death
-
-
?
additional information
?
-
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol
UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
involved in the first step of glycosylphosphatidylinositol, i.e. GPI, membrane anchor formation of surface glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + phosphatidylinositol
UDP + N-acetyl-D-glucosaminyl-phosphatidylinositol
-
-
-
-
?
additional information
?
-
-
biosynthetic pathway and subcellular localization, overview
-
-
?
additional information
?
-
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
?
additional information
?
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
?
additional information
?
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
?
additional information
?
-
-
enzyme defect in paroxysmal nocturnal hemoglobinuria
-
-
?
additional information
?
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
-
-
?
additional information
?
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H, PIG-P is absolutely required
-
-
?
additional information
?
-
-
biosynthetic pathway and subcellular localization, overview
-
-
?
additional information
?
-
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
-
-
?
additional information
?
-
-
glycosylphosphatidylinositol anchoring is essential for transport of cell surface proteins and enzyme deficieny leads to defective cell wall synthesis and cell death
-
-
?
additional information
?
-
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
enzyme binding structure analysis, overview. The variable conformations of loop beta4-beta5 and helix alphaG correlate well with the structural flexibility required for substrate entrance to the Re side of FAD
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
-
requires cations for activity, such as Mn2+, Mg2+, K+ or Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N-ethylmaleimide
-
binding site is close or at the active site, UDP-N-acetyl-D-glucosamine protects; strong
additional information
-
GTP-bound Ras2 protein associates in vivo with enzyme complex and inhibits its activity. Ras2 associates with enzyme complex subunit Eri1
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CaRas1
localizes to the cytoplasm or endoplasmic reticulum (ER) is sufficient for GPI-GnT activation. Mutational analysis, overview
-
component 2 of dolichyl-phosphate-mannose synthase
DPM2 protein binds directly to the enzyme complex and enhances the enzyme activity, regulatory role
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
overexpression of active froms of the Ras family of proteins does not affect glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity
additional information
-
overexpression of active froms of the Ras family of proteins does not affect glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
afpig-a; Most common opportunistic fungal pathogen of human
Swissprot
brenda
GPI-GlcNAc transferase subunit P; formerly Aspergillus nidulans
UniProt
brenda
gene CaGPI19, encoding an accessory subunit of the enzyme complex
-
-
brenda
afpig-a; Most common opportunistic fungal pathogen of human
Swissprot
brenda
gene piga-1 encoding the catalytic subunit of the phosphatidylinositol N-acetylglucosaminyltransferase complex
-
-
brenda
gene CaGPI19, encoding an accessory subunit of the enzyme complex
-
-
brenda
cDNA that encode a 71-amino acid protein, which is termed PIG-Y (for phosphatidylinositlglycan-class Y). Mouse and rice homologues of PIG-Y, exhibit 79% and 25% amino acid identity with human PIG-Y, respectively. The hydropathy profile of Saccharomyces cerevisiae´s Eri1p is quite similar to PIG-Y and the amino acid identity is 22%. N-terminus and C-terminus face the cytoplasmic side.; from the human T lymphoma KT-3 cDNA library
Swissprot
brenda
at least 3 components forming the enzyme complex: GPI1, GPI2 or PIG-C, GPI3 or PIG-A
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
with paroxysmal nocturnal hemoglobinuria phenotype, i.e. PNH, obtained by Epstein-Barr immortalization of lymphocytes from PNH-patients
brenda
additional information
-
the wild-type PIGA-1 protein is solely detected in the germline, and no EGFP-tagged PIGA-1 is detected in somatic cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
major part at the cytoplasmic side of perinuclear and mitochondria-associated lamellae
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the acyl coenzyme A dehydrogenase (ACAD) family member, thus the enzyme protein folds into a beta-sheet flanked by two alpha-helical domains
malfunction
metabolism
physiological function
additional information
modeling with PigG, the acyl carrier protein, suggests a reasonable mode of interaction with PigA. The structure helps to explain the proline oxidation mechanism, in which Glu244 plays a central role by abstracting the substrate protons. It also reveals a plausible pocket for oxygen binding to the Si side of FAD
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
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
malfunction
-
depletingCaGpi19p, an accessory subunit of the enzyme complex that initiates GPI biosynthesis, specifically down-regulates ERG11, altering ergosterol levels and drug response. ERG11 down-regulation is not due to general cell wall defects or GPI deficiency. CaGPI19 mutants show increased cAMP/PKA signalling
malfunction
-
piga-1-knockout worms show 100% lethality, with decreased mitotic germline cells and abnormal eggshell formation. Cell-specific rescue of the null allele, expression of piga-1 in somatic gonads and/or in germline is sufficient for normal embryonic development and the maintenance of the germline mitotic cells. The RNAi phenotypes of each gene, including larval arrest, scrawny larvae, and germline defects, may result from N-/O-glycosylation inhibition as well as GPI-anchor inhibition
malfunction
GPI19 mutants show up-regulation of GPI2, whereas GPI2 mutants show upregulation of GPI19. GPI2 disruption leads to defective hyphal morphogenesis due to altered Ras signaling. Reintroduction of GPI2 into the GPI2 heterozygous strain can reverse the phenotypes
malfunction
-
recombinant expression of Candida albicans GPI2 subunit in a Scaccharomyces cerevisiae GPI2 subunit conditional lethal mutant cannot restore its growth defects
malfunction
Saccharomyces cerevisiae Gpi2, an accessory subunit of the enzyme catalyzing the first step of glycosylphosphatidylinositol (GPI) anchor biosynthesis, selectively complements some of the functions of its homologue in Candida albicans
malfunction
-
targeted deletion of the gene encoding GntA in A. fumigatus results in complete absence of zwitterionic glycoinositolphosphoceramide, a phenotype that can be reverted by episomal expression of GntA in the mutant
malfunction
in the CaGPI19 conditional null strain, isozyme CaGpi2 is overexpressed
malfunction
mutations in Pig-a prevent GPI-anchor synthesis resulting in loss of cell-surface GPI-linked proteins
malfunction
the strain overexpressing CaGpi2 is hyperfilamentous and also heat-shock-sensitive, a phenotype typical of hyperactive Ras mutants. When Hsp90 levels are downregulated, due to CaGpi2 overexpression, the interaction of CaRas1 with Cyr1 is promoted at the cost of its interaction with Ira2. Thus, the filamentation pathway remains turned on even at 30°C, resulting in a hyperfilamentous phenotype
malfunction
-
in the CaGPI19 conditional null strain, isozyme CaGpi2 is overexpressed
-
malfunction
-
the strain overexpressing CaGpi2 is hyperfilamentous and also heat-shock-sensitive, a phenotype typical of hyperactive Ras mutants. When Hsp90 levels are downregulated, due to CaGpi2 overexpression, the interaction of CaRas1 with Cyr1 is promoted at the cost of its interaction with Ira2. Thus, the filamentation pathway remains turned on even at 30°C, resulting in a hyperfilamentous phenotype
-
malfunction
-
depletingCaGpi19p, an accessory subunit of the enzyme complex that initiates GPI biosynthesis, specifically down-regulates ERG11, altering ergosterol levels and drug response. ERG11 down-regulation is not due to general cell wall defects or GPI deficiency. CaGPI19 mutants show increased cAMP/PKA signalling
-
metabolism
analysis of the regulatory function of the enzyme, overview
metabolism
the ability of Candida albicans to switch between yeast to hyphal form is a property that is primarily associated with the invasion and virulence of this human pathogenic fungus. Several glycosylphosphatidylinositol (GPI)-anchored proteins are expressed only during hyphal morphogenesis. One of the major pathways that controls hyphal morphogenesis is the Ras signaling pathway. Cross-talk between GPI anchor biosynthesis and Ras signaling occurs in Candida albicans. The first step of GPI biosynthesis is activated by Ras in Candida albicans. Activation of Ras signaling is independent of the catalytic competence of GPI-GnT
metabolism
the ability of Candida albicans to switch between yeast to hyphal form is a property that is primarily associated with the invasion and virulence of this human pathogenic fungus. Several glycosylphosphatidylinositol (GPI)-anchored proteins are expressed only during hyphal morphogenesis. One of the major pathways that controls hyphal morphogenesis is the Ras signaling pathway. Cross-talk between GPI anchor biosynthesis and Ras signaling occurs in Candida albicans. The first step of GPI biosynthesis is activated by Ras in Candida albicans. Activation of Ras signaling is independent of the catalytic competence of GPI-GnT. Possible interaction between Ras signaling and GPI-GnT in Candida albicans, detailed overview
metabolism
the enzyme is involved in the glycophosphatidylinositol (GPI) anchor synthesis pathway which is highly conserved between species
metabolism
-
the ability of Candida albicans to switch between yeast to hyphal form is a property that is primarily associated with the invasion and virulence of this human pathogenic fungus. Several glycosylphosphatidylinositol (GPI)-anchored proteins are expressed only during hyphal morphogenesis. One of the major pathways that controls hyphal morphogenesis is the Ras signaling pathway. Cross-talk between GPI anchor biosynthesis and Ras signaling occurs in Candida albicans. The first step of GPI biosynthesis is activated by Ras in Candida albicans. Activation of Ras signaling is independent of the catalytic competence of GPI-GnT. Possible interaction between Ras signaling and GPI-GnT in Candida albicans, detailed overview
-
metabolism
-
the ability of Candida albicans to switch between yeast to hyphal form is a property that is primarily associated with the invasion and virulence of this human pathogenic fungus. Several glycosylphosphatidylinositol (GPI)-anchored proteins are expressed only during hyphal morphogenesis. One of the major pathways that controls hyphal morphogenesis is the Ras signaling pathway. Cross-talk between GPI anchor biosynthesis and Ras signaling occurs in Candida albicans. The first step of GPI biosynthesis is activated by Ras in Candida albicans. Activation of Ras signaling is independent of the catalytic competence of GPI-GnT
-
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
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
physiological function
-
the enzyme is part of the enzyme complex that initiates glycosylphosphatidylinositol, GPI, biosynthesis, it catalyzes the first step of GPI anchor biosynthesis. CaGPI19 appears to be mutually regulated with ERG11
physiological function
-
the phosphatidylinositol N-acetylglucosaminyltransferase complex catalyzes the first step of GPI-anchor synthesis, which is indispensable for the germline development of the nematode Caenorhabditis elegans. GPI-anchor synthesis is indispensable for the maintenance of mitotic germline cell number
physiological function
-
Saccharomyces cerevisiae enzyme subunit Gpi2 is an accessory subunit of the enzyme that catalyzes the first step of glycosylphosphatidylinositol (GPI) anchor biosynthesis. Saccharomyces cerevisiae enzyme subunit Gpi2 subunit physically interacts with and negatively modulates Ras signaling, while enzyme subunit Gpi2 from Candida albicans is a positive modulator of Ras signaling
physiological function
the enzyme complex, GPI-N-acetylglucosaminyltransferase (GPI-GnT), is involved in the first step of GPI anchor biosynthesis in eukaryotes. Candida albicans has several glycosylphosphatidylinositol (GPI)-anchored virulence factors. Inhibiting GPI biosynthesis attenuates its virulence. Enzyme complex subunit GPI2 is essential for growth and hyphal morphogenesis and is needed for filamentation. The GPI-GnT enzyme complex accessory subunits, GPI2 and GPI19, exhibit opposite effects on ergosterol biosynthesis and Ras signaling (which determines hyphal morphogenesis), because the two subunits negatively regulate one another. GPI19 controls ergosterol biosynthesis through ERG11 levels, whereas GPI2 determines the filamentation by cross-talk with Ras1 signaling. GPI2 affects GPI anchor biosynthesis and cell wall
physiological function
-
the enzyme is involved in the initiation of zwitterionic glycoinositolphosphoceramide biosynthesis. Glycoinositolphosphoceramides (GIPCs) are complex sphingolipids that, in fungi, commonly contain an alpha-mannose residue linked at position 2 of the inositol. Several pathogenic fungi additionally synthesize zwitterionic GIPCs carrying an alpha-glucosamine residue at this position. In the human pathogen Aspergillus fumigatus, the alpha-N-acetylglucosaminyl-1,2-inositolphosphoceramide core is elongated to Manalpha1,3Manalpha1,6GlcNalpha1,2IPC, which is the most abundant glycoinositolphosphoceramide synthesized by this fungus. GntA uses UDP-N-acetylglucosamine as donor substrate to generate a glycolipid product resistant to saponification and to digestion by phosphatidylinositol-phospholipase C as expected for GlcNAcalpha1,2IPC
physiological function
the GPI-Nacetylglucosaminyltransferase (GPI-GnT) enzyme complex catalyzes the first and committing step of the pathway in Candida albicans involving transfer of N-acetylglucosamine from UDP-GlcNAc to phosphatidylinositol. Saccharomyces cerevisiae subunit Gpi2 enzyme subunit physically interacts with and negatively modulates Ras signaling, while enzyme subunit Gpi2 from Candida albicans is a positive modulator of Ras signaling. The effect of Candida albicans GPI2 subunit on sterol biosynthesis Candida albicans is independent of its interaction with the GPI-GnT enzyme complex and Ras signaling pathways
physiological function
hemizygous phosphatidylinositol class A (Pig-a) forms the catalytic subunit of N-acetylglucosaminyltransferase that is required for glycophosphatidylinositol (GPI) anchor biosynthesis
physiological function
of the two Candida albicans Ras proteins, CaRas1 alone activates GPI-GnT activity, and the activity is further stimulated by constitutively activated CaRas1. Of the six subunits of the GPI-N-acetylglucosaminyltransferase (GPI-GnT) that catalyze the first step of GPI biosynthesis, CaGpi2 is the key player involved in activating Ras signaling and hyphal morphogenesis. Activation of Ras signaling is independent of the catalytic competence of GPI-GnT
physiological function
-
of the two Candida albicans Ras proteins, CaRas1 alone activates GPI-GnT activity, and the activity is further stimulated by constitutively activated CaRas1. Of the six subunits of the GPI-N-acetylglucosaminyltransferase (GPI-GnT) that catalyze the first step of GPI biosynthesis, CaGpi2 is the key player involved in activating Ras signaling and hyphal morphogenesis. Activation of Ras signaling is independent of the catalytic competence of GPI-GnT
-
physiological function
-
the enzyme is part of the enzyme complex that initiates glycosylphosphatidylinositol, GPI, biosynthesis, it catalyzes the first step of GPI anchor biosynthesis. CaGPI19 appears to be mutually regulated with ERG11
-
Show AA Sequence and Transmembrane Helices (2988 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H
additional information
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H
additional information
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H
additional information
enzyme is active in a complex of at least 5 proteins, termed GPI1, PIG-P, PIG-A, PIG-C and PIG-H
additional information
-
enzyme exists as a complex of at least 3 proteins PIG-A or GPI3, PIG-C or GPI2 and GPI1, in which PIG-A, not PIG-C, is the substrate binding component
additional information
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
additional information
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
additional information
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
additional information
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
additional information
-
enzyme is active in a complex of at least 4 proteins, termed GPI1, PIG-A, PIG-C and PIG-H, in which GPI1 is absolutely essential for stabilization
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the six other components of glycosylphosphatidylinositol-N-acetylglucosaminyltransferase can form a complex without PIG-Y, but this complex does not have any detectable glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity. In PIG-A-deficient JY5 cells, PIG-Y is not coprecipitated with any other components. PIG-Y associates directly with PIG-A and indirectly with other components through the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex. Additionally, there is no detectable association between PIG-Y and any of Ras proteins
additional information
-
the six other components of glycosylphosphatidylinositol-N-acetylglucosaminyltransferase can form a complex without PIG-Y, but this complex does not have any detectable glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity. In PIG-A-deficient JY5 cells, PIG-Y is not coprecipitated with any other components. PIG-Y associates directly with PIG-A and indirectly with other components through the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex. Additionally, there is no detectable association between PIG-Y and any of Ras proteins
additional information
-
GTP-bound Ras2 protein associates in vivo with enzyme complex and inhibits its activity
additional information
the enzyme protein folds into a beta-sheet flanked by two alpha-helical domains
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
two putative N-glycosylation sites at Asn66 and Asn243. The two predicted N-glycosylation sites are located on each side of the catalytically relevant DXD motif
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant PigA in apoform and in complex with cofactor FAD or L-proline, sitting drop vapor diffusion method, mixing of 0.001 ml of 15 mg/ml protein in 100 mm NaCl and 50 mm Tris·HCl, pH 8.0, with 0.001 ml of reservoir solution containing 27% PEG 600, and 0.1 M Na-HEPES, pH 7.5, for the complex crystals FAD is added in a molar ratio of 3:1 ratio to the protein solution, and mixed with a reservoir solution containing 40% ethylene glycol and 0.1 M Na-acetate, pH 5.0; or 1.7 M (NH4)2SO4, 0.2 M NaCl, and 0.1 M sodium cacodylate, pH 6.5, for the proline-complex crystal the protein solution contains 7 mM L-proline in addition to FAD and crown ether, and the reservoir contains 1.9 M sodium malonate, pH 6.0. The Pro-Gly complex crystal is obtained by including 5 mM L-prolylglycine in the E244A protein solution, with a reservoir of 1.6 M (NH4)2SO4, 2% PEG 400, and 0.1 M citric acid, pH 4.0, X-ray diffraction structure determination and analysis at 1.3-2.55 A resolution, molecular replacement using the structure of butyryl-CoA dehydrogenase (PDB ID 4L1F) as a search model
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
afpig-a null mutant, strain CEA17 (pyrG-). This mutant shows a complete loss in glycosylphosphatidylinositol-N-acetylglucoaminyltransferase activity. None of the membrane bound glycosylphosphatidylinositol-anchored phospholipases, phosphatase, eCM33por Gl1p is found in the membrane preparation of the mutant. The mutant can grow at temperatures from 30°C to 50°C, but the growth rates are greatly inhibited. When the mutant is grown in the presence of various cell wall-disrupting agents, it is more sensitive to Calcofluor white, Congo-red, Nikkomycin Z and SDS, than the wild type. The mannoproteins and beta-glucans in mycelial cell wall of the mutant is 2.5fold and 2fold of the wild type or revertant respectively. The deletion of the afpig-a gene leads to earlier polarity, germ tube emergence and septation of mutant conidiospores in the early duplication cycles and to significant changes in developmental events and morphogenesis during conidiation. Two virulence factors, mycelial catalase Cat1 and Asp-haemolysin, are missing in the mutant, but the chitinase ChiB is found remarkably increased. After the inoculation of wild-type and mutant conidia into immunocompromised mice, early mortality is nearly identical among all groups. The remaining mice receiving the deletion mutant survived significantly longer.
additional information
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afpig-a null mutant, strain CEA17 (pyrG-). This mutant shows a complete loss in glycosylphosphatidylinositol-N-acetylglucoaminyltransferase activity. None of the membrane bound glycosylphosphatidylinositol-anchored phospholipases, phosphatase, eCM33por Gl1p is found in the membrane preparation of the mutant. The mutant can grow at temperatures from 30°C to 50°C, but the growth rates are greatly inhibited. When the mutant is grown in the presence of various cell wall-disrupting agents, it is more sensitive to Calcofluor white, Congo-red, Nikkomycin Z and SDS, than the wild type. The mannoproteins and beta-glucans in mycelial cell wall of the mutant is 2.5fold and 2fold of the wild type or revertant respectively. The deletion of the afpig-a gene leads to earlier polarity, germ tube emergence and septation of mutant conidiospores in the early duplication cycles and to significant changes in developmental events and morphogenesis during conidiation. Two virulence factors, mycelial catalase Cat1 and Asp-haemolysin, are missing in the mutant, but the chitinase ChiB is found remarkably increased. After the inoculation of wild-type and mutant conidia into immunocompromised mice, early mortality is nearly identical among all groups. The remaining mice receiving the deletion mutant survived significantly longer.
additional information
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afpig-a null mutant, strain CEA17 (pyrG-). This mutant shows a complete loss in glycosylphosphatidylinositol-N-acetylglucoaminyltransferase activity. None of the membrane bound glycosylphosphatidylinositol-anchored phospholipases, phosphatase, eCM33por Gl1p is found in the membrane preparation of the mutant. The mutant can grow at temperatures from 30°C to 50°C, but the growth rates are greatly inhibited. When the mutant is grown in the presence of various cell wall-disrupting agents, it is more sensitive to Calcofluor white, Congo-red, Nikkomycin Z and SDS, than the wild type. The mannoproteins and beta-glucans in mycelial cell wall of the mutant is 2.5fold and 2fold of the wild type or revertant respectively. The deletion of the afpig-a gene leads to earlier polarity, germ tube emergence and septation of mutant conidiospores in the early duplication cycles and to significant changes in developmental events and morphogenesis during conidiation. Two virulence factors, mycelial catalase Cat1 and Asp-haemolysin, are missing in the mutant, but the chitinase ChiB is found remarkably increased. After the inoculation of wild-type and mutant conidia into immunocompromised mice, early mortality is nearly identical among all groups. The remaining mice receiving the deletion mutant survived significantly longer.
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additional information
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the RNAi phenotypes of each gene, including larval arrest, scrawny larvae, and germline defects, may result from N-/O-glycosylation inhibition as well as GPI-anchor inhibition
additional information
generation of single knock-out of gene GPI2 and double knockout mutants of genes GPI1 and GPI119 from Cancdida albicans strain BWP17, microsomes generated from GPI2 mutants exhibited lower GPI-GnT activity as compared with CAI4, phenotypes, overview
additional information
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generation of single knock-out of gene GPI2 and double knockout mutants of genes GPI1 and GPI119 from Cancdida albicans strain BWP17, microsomes generated from GPI2 mutants exhibited lower GPI-GnT activity as compared with CAI4, phenotypes, overview
additional information
recombinant expression of Candida albicans GPI2 subunit in a Saccharomyces cerevisiae GPI2 subunit conditional lethal mutant cannot restore its growth defects. In mutants where CaGPI19 is downregulated, a downregulation of CaGPI2 is unable to restore CaERG11 levels, suggesting that CaGpi19, rather than CaGpi2 is the major partner in the cross-talk with CaErg11
additional information
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recombinant expression of Candida albicans GPI2 subunit in a Saccharomyces cerevisiae GPI2 subunit conditional lethal mutant cannot restore its growth defects. In mutants where CaGPI19 is downregulated, a downregulation of CaGPI2 is unable to restore CaERG11 levels, suggesting that CaGpi19, rather than CaGpi2 is the major partner in the cross-talk with CaErg11
additional information
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analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). CaGpi2 overexpression results in Hsp90 down-regulation, which is reflected in a decrease in transcript levels as well as in Hsp90 activity. Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). CaGpi2 overexpression results in Hsp90 down-regulation, which is reflected in a decrease in transcript levels as well as in Hsp90 activity. Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). CaGpi2 overexpression results in Hsp90 down-regulation, which is reflected in a decrease in transcript levels as well as in Hsp90 activity. Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). CaGpi2 overexpression results in Hsp90 down-regulation, which is reflected in a decrease in transcript levels as well as in Hsp90 activity. Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). CaGpi2 overexpression results in Hsp90 down-regulation, which is reflected in a decrease in transcript levels as well as in Hsp90 activity. Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
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analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
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analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
additional information
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analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
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additional information
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analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
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additional information
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analysis of enzyme-deficient WY-ZY4 strain (BWP17- Caras1/Caras2 mutant). CaGpi2 overexpression results in Hsp90 down-regulation, which is reflected in a decrease in transcript levels as well as in Hsp90 activity. Depletion of CaGpi2 can perhaps reduce the levels of CaRas1 available at the PM for signaling in the cAMP/PKA pathway for hyphal morphogenesis. Generation of revertant strains for all GPI-GnT subunits are created in their respective heterozygous strains
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additional information
disruption of the genes in F9 cells via homologous recombination, causing a severe but not complete defect in the generation of glycosylphosphatidylinositol-anchored proteins, highly reduced activity in vivo, no activity in vitro, decrease in GPI1 also caused decrease of PIG-C and PIG-H
additional information
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disruption of the genes in F9 cells via homologous recombination, causing a severe but not complete defect in the generation of glycosylphosphatidylinositol-anchored proteins, highly reduced activity in vivo, no activity in vitro, decrease in GPI1 also caused decrease of PIG-C and PIG-H
additional information
GPI anchor deficiency is most often caused by mutation in the Pig-a gene, thus measuring GPI anchor deficiency is considered to be almost equivalent to measuring Pig-a mutation. Development and validation of an in vitro Pig-a assay in L5178Y mouse lymphoma cells, method optimization, overview. Antibodies against GPI-linked CD90.2 and stably expressed CD45 are used to determine GPI-status by flow cytometry, antibody concentration and incubation times are optimized. The optimum phenotypic expression period is 8 days. Application of the in vitro Pig-a assay to a selection of well-validated genotoxic and non-genotoxic compounds. EMS, N-ethyl-N-nitrosourea, and 4-nitroquinoline-N-oxide dose dependently increase the numbers of GPI(-) cells, while etoposide, mitomycin C, and a bacterial-specific mutagen do not dependently increase the numbers of GPI(-) cells
additional information
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GPI anchor deficiency is most often caused by mutation in the Pig-a gene, thus measuring GPI anchor deficiency is considered to be almost equivalent to measuring Pig-a mutation. Development and validation of an in vitro Pig-a assay in L5178Y mouse lymphoma cells, method optimization, overview. Antibodies against GPI-linked CD90.2 and stably expressed CD45 are used to determine GPI-status by flow cytometry, antibody concentration and incubation times are optimized. The optimum phenotypic expression period is 8 days. Application of the in vitro Pig-a assay to a selection of well-validated genotoxic and non-genotoxic compounds. EMS, N-ethyl-N-nitrosourea, and 4-nitroquinoline-N-oxide dose dependently increase the numbers of GPI(-) cells, while etoposide, mitomycin C, and a bacterial-specific mutagen do not dependently increase the numbers of GPI(-) cells
additional information
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subunit eri1 deletion mutant, displays growth arrest at 37°C and cell wall defect at permissive temperature, defect is suppressed by increased UDP-GlcNAc levels. Mutant also accumulates chitin and is deficient in maturation of glucosamine phosphatidyl-inositol anchor proteins in the ER
additional information
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a gpi19 deletion allele that lacks nearly the entire coding sequence in the EG123 strain background confirmed the lethality of this mutation
additional information
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a set of temperature-sensitive gpi19 allels is created using error-prone PCR. All of the gpi19 alleles, with the exception of gpi19-4, are osmotically remedial. The gpi19 mutants are hypersensitive to zymolyase treatment. The least severely impaired alleles of gpi19 (gpi19-1 and gpi19-2) are suppressed for their growth defects at restrictive temperature by either GFA1 overexpression or exogenous glucosamine. The gpi19 mutants display weak filamentation phenotypes and invasive growth, which is enhanced by the inclusion of sorbitol in the medium to suppress their growth defects.
additional information
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Saccharomyces cerevisiae Gpi2, an accessory subunit of the enzyme catalyzing the first step of glycosylphosphatidylinositol (GPI) anchor biosynthesis, selectively complements some of the functions of its homologue in Candida albicans
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of GPI1 by overexpression of PIG-A in JY5 cells and isolation of the complex by affinity chromatography
recombinant FLAG-tagged and His-tagged PIG-A from human B lymphoblastoid JY5 cells and from Escherichia coli
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of FLAG-tagged PIG-C, GST-tagged PIG-A and PIG-H with and without mGPI1 in the mGPI1-deficient F9 cells
expressed in Daudi cells. Daudi cells have no PIG-Y transcritpt. PIG-Y cDNA restores the surface expression of CD59, DAF and CD48, but an empty vector does not. glycosylphosphatidylinositol-N-acetylglucosaminyltransferase activity is also restored
expression of FLAG-tagged and His-tagged PIG-A in PIG-A-deficient human B lymphoblastoid JY5 cells and in Escherichia coli, complementation in JY5 cells
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expression of PIG-A/GPI3 and PIG-C/GPI2 as FLAG-tagged fusion proteins in yeast, expression of FLAG-tagged PIG-A/GPI3 in Escherichia coli
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expression of PIG-P in enzyme deficient mouse mutant T cell line can complement and restore the enzyme activity
gene GPI1, recombinant expression in the GPI-GnT heterozygous WY-ZY4 mutant strain, RT-PCR enzyme expression analysis
gene GPI15, recombinant expression in the GPI-GnT heterozygous WY-ZY4 mutant strain, phenotype, RT-PCR enzyme expression analysis
gene GPI19, recombinant expression in the GPI-GnT heterozygous WY-ZY4 mutant strain, RT-PCR enzyme expression analysis
gene GPI2 encodes for one of the six accessory subunits of the GPI-N-acetylglucosaminyltransferase complex
gene GPI2, recombinant expression in the GPI-GnT heterozygous WY-ZY4 mutant strain, phenotype, RT-PCR enzyme expression analysis
gene GPI3, recombinant expression in the GPI-GnT heterozygous WY-ZY4 mutant strain, RT-PCR enzyme expression analysis
gene gtA, functional recombinant expression of FLAG-tagged GntA enzyme in Saccharomyces cerevisiae
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gene pigA, recombinant expression of codon-optimmized gene encoding the C-terminally His6-tagged wild-type and mutant enzymes with TEV protease cleavage site in Escherichia coli strain BL21(DE3)
genes involved in GPI-anchor synthesis in Caenorhabditis elegans, overview. Isolation and analysis of piga-1-knockout allele tm2939
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hGPI1, DNA sequence determination, coexpression as GST-tagged protein in human B lymphoblastoid JY25 or JY5 cells with the other three GST- or FLAG-tagged protein of the active protein complex
mGPI1, DNA sequence determination, expression in embryonal carcinoma F9 cells
overexpression of FLAG- and GST-double tagged PIG-A in human B lymphoblastoid JY5 cells
gene GPI2 encodes for one of the six accessory subunits of the GPI-N-acetylglucosaminyltransferase complex
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gene GPI2 encodes for one of the six accessory subunits of the GPI-N-acetylglucosaminyltransferase complex
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
downregulation of ERG11 downregulates CaGPI19 and GPI biosynthesis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
Halalkalibacterium halodurans
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PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
analysis
-
PIGA proteins possess characteristic motifs that can be used for identifying PIG-A proteins from newly sequenced genomes. Statistical as well as phylogenetic analysis demonstrates that PIG-A proteins evolved from glycosyltransferases, PIG-A proteins from archaeabacteria and primitive eukaryotes are closer to bacterial GT4 glycosyltransferases than to eukaryotic PIG-A proteins and should be classified as such rather than as 'true' PIG-A protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Doering, T.L.; Masterson, W.J.; Englund, P.T.; Hart, G.W.
Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine
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Trypanosoma brucei
brenda
Milne, K.G.; Ferguson, M.A.J.; Masterson, W.J.
Inhibition of the GlcNAc transferase of the glycosylphosphatidylinositol anchor biosynthesis in African trypanosomes
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Trypanosoma brucei
brenda
Hillmen, P.; Bessler, M.; Mason, P.J.; Watkins, W.M.; Luzzatto, L.
Specific defect in N-acetylglucosamine incorporation in the biosynthesis of the glycosylphosphatidylinositol anchor in cloned cell lines from patients with paroxysmal nocturnal hemoglobinuria
Proc. Natl. Acad. Sci. USA
90
5272-5276
1993
Homo sapiens
brenda
Takano, D.; Kishimoto, T.; Hayakawa, T.; Mitsui, T.; Hori, H.
Activity of phosphatidylinositol/UDP-GlcNAc:GlcNAc transferase in midgut tissue of Bombyx mori
Niigata Daigaku Nogakubu Kenkyu Hokoku
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Bombyx mori
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brenda
Watanabe, R.; Inoue, N.; Westfall, B.; Taron, C.H.; Orlean, P.; Takeda, J.; Kinoshita, T.
The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1
EMBO J.
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Saccharomyces cerevisiae, Homo sapiens, Homo sapiens (Q9BRB3)
brenda
Hong, Y.; Oshihi, K.; Watanabe, R.; Endo, Y.; Maeda, Y.; Kinoshita, T.
GPI1 stabilizes an enzyme essential in the first step of glycosylphosphatidylinositol biosynthesis
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Homo sapiens, Mus musculus (Q9QYT7), Mus musculus
brenda
Vidugiriene, J.; Sharma, D.K.; Smith, T.K.; Baumann, N.A.; Menon, A.K.
Segregation of glycosylphosphatidylinositol biosynthetic reactions in a subcompartment of the endoplasmic reticulum
J. Biol. Chem.
274
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Cricetulus griseus, Mus musculus
-
brenda
Watanabe, R.; Murakami, Y.; Marmor, M.; Inoue, N.; Maeda, Y.; Hino, J.; Kangawa, K.; Julius, M.; Kinoshita, T.
Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2
EMBO J.
19
4402-4411
2000
Homo sapiens, Homo sapiens (P57054), Homo sapiens (Q9BRB3), Mus musculus (Q9JHG1)
brenda
Kostova, Z.; Rancour, D.M.; Menon, A.K.; Orlean, P.
Photoaffinity labelling with P3-(4-azidoanilido)uridine 5'-triphosphate identifies Gpi3p as the UDP-GlcNAc-binding subunit of the enzyme that catalyses formation of GlcNAc-phosphatidylinositol, the first glycolipid intermediate in glycosylphosphatidylinositol synthesis
Biochem. J.
350
815-822
2000
Saccharomyces cerevisiae, Saccharomyces cerevisiae XM37-10c
-
brenda
Tiede, A.; Nischan, C.; Schubert, J.; Schmidt, R.
Characterization of the enzymatic complex for the first step in glycosylphosphatidylinositol biosynthesis
Int. J. Biochem. Cell Biol.
32
339-250
2000
Homo sapiens
brenda
Sobering, A.K.; Watanabe, R.; Romeo, M.J.; Yan, B.C.; Specht, C.A.; Orlean, P.; Riezman, H.; Levin, D.E.
Yeast Ras regulates the complex that catalyzes the first step in GPI-anchor biosynthesis at the ER
Cell
117
637-648
2004
Saccharomyces cerevisiae
brenda
Newman, H.A.; Romeo, M.J.; Lewis, S.E.; Yan, B.C.; Orlean, P.; Levin, D.E.
Gpi19, the Saccharomyces cerevisiae homologue of mammalian PIG-P, is a subunit of the initial enzyme for glycosylphosphatidylinositol anchor biosynthesis
Eukaryot. Cell
4
1801-1807
2005
Saccharomyces cerevisiae
brenda
Murakami, Y.; Siripanyaphinyo, U.; Hong, Y.; Tashima, Y.; Maeda, Y.; Kinoshita, T.
The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component
Mol. Biol. Cell
16
5236-5246
2005
Homo sapiens (Q3MUY2), Homo sapiens
brenda
Li, H.; Zhou, H.; Luo, Y.; Ouyang, H.; Hu, H.; Jin, C.
Glycosylphosphatidylinositol (GPI) anchor is required in Aspergillus fumigatus for morphogenesis and virulence
Mol. Microbiol.
64
1014-1027
2007
Aspergillus fumigatus (Q6Q2B4), Aspergillus fumigatus, Aspergillus fumigatus YJ-407 (Q6Q2B4)
brenda
Oswal, N.; Sahni, N.S.; Bhattacharya, A.; Komath, S.S.; Muthuswami, R.
Unique motifs identify PIG-A proteins from glycosyltransferases of the GT4 family
BMC Evol. Biol.
8
168
2008
Actinobacillus succinogenes, Aeropyrum pernix, Alkaliphilus metalliredigens, Arabidopsis thaliana, Bacteroides thetaiotaomicron, Caenorhabditis elegans, Candida albicans, Clostridium beijerinckii, Clostridium tetani, Cryptosporidium parvum, Cutibacterium acnes, Desulfitobacterium hafniense, Dictyostelium discoideum, Drosophila melanogaster, Entamoeba histolytica, Giardia intestinalis, Halalkalibacterium halodurans, Homo sapiens, Leishmania major, Methanosarcina acetivorans, Methanosarcina barkeri, Methanothermobacter thermautotrophicus, Mycobacterium sp., Oryza sativa, Paramecium tetraurelia, Plasmodium falciparum, Pyrococcus furiosus, Rattus norvegicus, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Thermoplasma acidophilum, Trypanosoma brucei, [Mannheimia] succiniciproducens
brenda
Pilsyk, S.; Paszewski, A.
The Aspergillus nidulans pigP gene encodes a subunit of GPI-N-acetylglucosaminyltransferase which influences filamentation and protein secretion
Curr. Genet.
55
301-309
2009
Aspergillus nidulans (Q5AUG0), Aspergillus nidulans
brenda
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
Development
136
2121-2131
2009
Danio rerio, Xenopus laevis
brenda
Victoria, G.S.; Yadav, B.; Hauhnar, L.; Jain, P.; Bhatnagar, S.; Komath, S.S.
Mutual co-regulation between GPI-N-acetylglucosaminyltransferase and ergosterol biosynthesis in Candida albicans
Biochem. J.
443
619-625
2012
Candida albicans, Candida albicans BWP17
brenda
Murata, D.; Nomura, K.H.; Dejima, K.; Mizuguchi, S.; Kawasaki, N.; Matsuishi-Nakajima, Y.; Ito, S.; Gengyo-Ando, K.; Kage-Nakadai, E.; Mitani, S.; Nomura, K.
GPI-anchor synthesis is indispensable for the germline development of the nematode Caenorhabditis elegans
Mol. Biol. Cell
23
982-995
2012
Caenorhabditis elegans
brenda
Engel, J.; Schmalhorst, P.S.; Krueger, A.T.; Mueller, C.T.; Buettner, F.F.; Routier, F.H.
Characterization of an N-acetylglucosaminyltransferase involved in Aspergillus fumigatus zwitterionic glycoinositolphosphoceramide biosynthesis
Glycobiology
25
1423-1430
2015
Aspergillus fumigatus
brenda
Yadav, A.; Singh, S.L.; Yadav, B.; Komath, S.S.
Saccharomyces cerevisiae Gpi2, an accessory subunit of the enzyme catalyzing the first step of glycosylphosphatidylinositol (GPI) anchor biosynthesis, selectively complements some of the functions of its homolog in Candida albicans
Glycoconj. J.
31
497-507
2014
Candida albicans (Q5A6L6), Candida albicans, Saccharomyces cerevisiae
brenda
Yadav, B.; Bhatnagar, S.; Ahmad, M.F.; Jain, P.; Pratyusha, V.A.; Kumar, P.; Komath, S.S.
First step of glycosylphosphatidylinositol (GPI) biosynthesis cross-talks with ergosterol biosynthesis and Ras signaling in Candida albicans
J. Biol. Chem.
289
3365-3382
2014
Candida albicans (Q5A6L6), Candida albicans
brenda
David, R.; Talbot, E.; Allen, B.; Wilson, A.; Arshad, U.; Doherty, A.
The development of an in vitro Pig-a assay in L5178Y cells
Arch. Toxicol.
92
1609-1623
2018
Mus musculus (Q64323), Mus musculus
brenda
Lee, C.C.; Ko, T.P.; Chen, C.T.; Chan, Y.T.; Lo, S.Y.; Chang, J.Y.; Chen, Y.W.; Chung, T.F.; Hsieh, H.J.; Hsiao, C.D.; Wang, A.H.
Crystal structure of PigA a prolyl thioester-oxidizing enzyme in prodigiosin biosynthesis
ChemBioChem
20
193-202
2019
Serratia marcescens (Q5W254)
brenda
Jain, P.; Sethi, S.C.; Pratyusha, V.A.; Garai, P.; Naqvi, N.; Singh, S.; Pawar, K.; Puri, N.; Komath, S.S.
Ras signaling activates glycosylphosphatidylinositol (GPI) anchor biosynthesis via the GPI-N-acetylglucosaminyltransferase (GPI-GnT) in Candida albicans
J. Biol. Chem.
293
12222-12238
2018
Candida albicans, Candida albicans (A0A1D8PHD4), Candida albicans (A0A1D8PKB8), Candida albicans (Q5A6L6), Candida albicans (Q5A9D6), Candida albicans ATCC MYA-2876, Candida albicans ATCC MYA-2876 (A0A1D8PHD4), Candida albicans ATCC MYA-2876 (A0A1D8PKB8), Candida albicans ATCC MYA-2876 (Q5A6L6), Candida albicans ATCC MYA-2876 (Q5A9D6)
brenda
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