2.4.1.41: polypeptide N-acetylgalactosaminyltransferase
This is an abbreviated version!
For detailed information about polypeptide N-acetylgalactosaminyltransferase, go to the full flat file.
Word Map on EC 2.4.1.41
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2.4.1.41
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o-glycosylation
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mucin-type
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mucin
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glycosyltransferase
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o-glycans
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o-linked
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threonine
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gangliosides
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lectin
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calcinosis
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oligosaccharide
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metastasis
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calcification
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hyperphosphatemic
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gm2
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galactosyltransferase
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glycolipids
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1,25-dihydroxyvitamin
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phosphaturic
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gd1a
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sialyltransferase
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submaxillary
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angptl3
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mucin-like
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klotho
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hyperostosis
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muc5ac
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factor-23
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apomucin
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analysis
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drug development
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lutropin
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asn-linked
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molecular biology
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periarticular
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medicine
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o-glycoproteins
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iga1
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villosa
- 2.4.1.41
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o-glycosylation
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mucin-type
- mucin
- glycosyltransferase
- o-glycans
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o-linked
- threonine
- gangliosides
- lectin
- calcinosis
- oligosaccharide
- metastasis
- calcification
-
hyperphosphatemic
- gm2
-
galactosyltransferase
- glycolipids
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1,25-dihydroxyvitamin
-
phosphaturic
- gd1a
-
sialyltransferase
-
submaxillary
-
angptl3
-
mucin-like
- klotho
- hyperostosis
- muc5ac
-
factor-23
- apomucin
- analysis
- drug development
-
lutropin
-
asn-linked
- molecular biology
-
periarticular
- medicine
-
o-glycoproteins
- iga1
- villosa
Reaction
Synonyms
(UDP)-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein, bgibmga008904, dGalNAc-T3, Eg-ppGalNAc-T1, GalNAc transferase, GalNAc-T, GalNAc-T1, GalNAc-T11, GalNAc-T12, GalNAc-T13, GalNAc-T14, GalNAc-T16, GalNAc-T18, GalNAc-T2, GalNAc-T3, GalNAc-T4, GalNAc-T5, GalNAc-T6, GalNAc-T7, GalNAc-transferase, GalNAc-transferase T1, GalNAc-transferase T2, GalNAcT4, GALNT1, GALNT11, GALNT12, Galnt13, GALNT14, Galnt18, GALNT2, GALNT3, Galnt4, GalNT5, glycopeptide-preferring polypeptide GalNAc transferase 10, glycoprotein acetylgalactosaminyltransferase, More, N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase, N-acetylgalactosaminyltransferase, N-acetylgalactosaminyltransferase-like 1, NM_001079884, PGANT, PGANT1, PGANT2, PGANT3, PGANT4, PGANT5, PGANT6, PGANT7, PGANT8, polypeptide GalNAc transferase, polypeptide GalNAc transferase 2, polypeptide GalNAc-transferase, polypeptide GalNAc-transferase 2, polypeptide GalNAc-transferase-2, polypeptide GalNAcT, polypeptide N-acetylgalactosaminyl transferase-3, polypeptide N-acetylgalactosaminyltransferase, polypeptide N-acetylgalactosaminyltransferase 12, polypeptide N-acetylgalactosaminyltransferase 14, polypeptide N-acetylgalactosaminyltransferase 2, polypeptide N-acetylgalactosaminyltransferase 3, polypeptide N-acetylgalactosaminyltransferase 6, polypeptide N-acetylgalactosaminyltransferase-1, polypeptide-N-acetylgalactosamine transferase, polyppetide GalNAc transferase, pp-GalNAc-T13, pp-GalNAc-T15, pp-GalNAc-T2, pp-GaNTase, ppGalNAc T1, ppGalNAc T10, ppGalNAc T13, ppGalNAc T16, ppGalNAc T2, ppGalNAc T3, ppGalNAc T5, ppGalNAc T6, ppGalNAc-T, ppGalNAc-T1, ppGalNAc-T10, ppGalNAc-T12, ppGalNAc-T2, ppGalNAc-T3, ppGalNAc-T4, ppGalNAc-T5, ppGalNAc-T6, ppGalNAcT, ppGalNAcT or hT, ppGaNTase, ppGaNTase-T1, ppGaNTase-T11, ppGaNTase-T12, ppGaNTase-T3, ppGaNTase-T4, ppGaNTase-T5, ppGaNTase-T6, protein-UDP acetylgalactosaminyltransferase, UDP GalNAc:polypeptide N-acetylgalactosaminyltransferase, UDP N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyl transferase, UDP N-acetyl-alpha-Dgalactosamine:polypeptide N-acetylgalactosaminyl transferase, UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase, UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase, UDP-GalNAc polypeptide:GalNAc transferase-T2, UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase, UDP-GalNAc polypeptides:N-acetyl-alpha-galactosaminyltransferase, UDP-GalNAc transferase, UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase, UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2, UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1, UDP-GalNAc:polypeptide alphaN-acetylgalactosaminyltransferase, UDP-GalNAc:polypeptide GalNAc transferase, UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 18, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9, UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13V1, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 16, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 17, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 18, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 19, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 20, UDP-N-acetyl-alpha-D-galactosaminyltransferase, UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-6, UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1, UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T10, UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, UDP-N-acetylgalactosamine polypeptide: N-acetylgalactosaminyl-transferase, UDP-N-acetylgalactosamine-glycoprotein N-acetylgalactosaminyltransferase, UDP-N-acetylgalactosamine-protein N-acetylgalactosaminyltransferase, UDP-N-acetylgalactosamine:kappa-casein polypeptide N-acetylgalactosaminyltransferase, UDP-N-acetylgalactosamine:polypeptide N-acetyl-alpha-galactosaminyltransferase, UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase, UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase, UDP-N-alpha-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase, UDP-polypeptide N-acetylgalactosaminyl transferase, uridine diphosphate-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3, uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase, xGaltnl-1
ECTree
2.4.1.41 polypeptide N-acetylgalactosaminyltransferaseAdvanced search results
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Source Tissue on EC 2.4.1.41 - polypeptide N-acetylgalactosaminyltransferase
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SOURCE TISSUE 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SOURCE
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expression of ppGalNAc-T1, -T2, -T3, -T4, -T6 and -T9 in B-cells and IgA-bearing B cells
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isozymes ppGalNAcT-1, ppGalNAcT-2, and ppGalNAcT-3, expression patterns, overview. Expression of isozyme ppGalNAcT-1 especially in calvaria and tibia
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ascending right part, low enzyme expression, decreased activity compared to normal colon, mono-glycosylates MUC5AC peptide
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ascending right part, high enzyme expression, 2fold higher activity than in stomach
dorsal longitudinal tracheal trunks and tracheal transverse connectives at embryonic stages 15-17, loss of PGANT35A activity leads to tracheal defects at embryonic stages 15-17, altered intracellular trafficking, reduction in apical and luminal epithelial marker components, alterations in cell shape, polarity and zona adherens formation, mislocation and disfunction of septate junctions, disruption of paracellular diffusion barrier formation
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high enzyme expression in tumoral gastric tissue displaying intestinal metaplasia, increased activity compared to normal stomach, di-glycosylates MUC5AC peptide
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expression analysis of ppGalNAc-T6 in gastric mucosa, intestinal metaplasia, and gastric carcinomas, the isozyme shows a heterogeneous expression and staining pattern
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stomach fundus, 2fold lower activity than in colon, mono-glycosylates MUC5AC peptide
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ppGalNacT-1 activity is essential for O-glycosylation in germinal center (GC) B cells within the white pulp of the spleen and lymph nodes upon immunization, increased apoptosis of IgG bearing GC B cells and reduced IgG abundance in the absence of ppGalNAcT-1
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AH-66 ascites hepatoma cells, harvested 6-7 days after the intraperitoneal transfer of ascites fluid from donor rats, activity much higher than in rat liver
loss of PGANT35A activity does not alter morphology or staining patterns of epithelial marker components
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expression of ppGalNAc-T1, -T2, -T3, -T4, -T6 and -T9 in NCI-H929 IgA myeloma cells
ppGalNAc-T13 is abundantly expressed in neuroblastoma cells
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RT-PCR, expression at embryonal stage 13 in anterior mesoderm and neural crest
GALNTL5 gene expression is significantly higher in ejaculated sperm than in cauda epididymal sperm. GALNTL5 is strongly localized in the mid-piece and head of ejaculated sperm, and in the head-tail coupling apparatus and acrosome of cauda epididymal sperm. The amount of GALNTL5 protein in seminal plasma is significantly higher than in ejaculated sperm
Northern blot analysis of human tissues
additional information
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brain-specific expression of GalNAc-T9, mRNA is most abundant in cerebellum, lower levels in cerebral cortex, frontal lobe, temporal lobe and putamen
ppGalNAc-T13 is highly and restrictively expressed in brain, fetal brain, adult cerebellum and cerebral cortex, exclusively in neuronal cells
high levels of expression in cerebellum, hippocampus, thalamus, and cerebral cortex. Expression is associated with neurons, but not with glial cells
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
benign cell line HMT 3522, non-metastatic cell line BT 474, metastatic cell lines ZR75-1, T-47D, MCF-7
ppGalNAc-T1 detection in all studied breast cancer cell lines
ppGalNAc-T2 detection in all studied breast cancer cell lines
ppGalNAc-T3 nearly undetectable in breast cancer cell line HMT-3522
ppGalNAc-T4 undetectable in breast cancer cell line ZR75-1 cell
ppGalNAc-T6 nearly undetectable in breast cancer cell line HMT-3522
cloning of the pgant35A gene from embryonic cDNA library
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embryonic day 14.5, ppGaNTase-T9 is expressed relatively abundantly compared with ppGaNTase-T7, accumulation in brain
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RT-PCR, xGalnt1, -6, -7 expression throughout early and late embryonal development
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human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T1
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human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T2
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human diffuse gastric carcinoma cell line GP202, enzyme form GalNAc-T3
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human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T1
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human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T2
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human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T3
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human diffuse gastric carcinoma cell line GP220, enzyme form GalNAc-T4
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RT-PCR, expression is restricted to dorsal marginal zones at embryonal stage 20
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RT-PCR, xGalnt1, -6, -7 expression in both, dorsal and ventral marginal zones at embryonal stage 20
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
very weak signal, nearly undetectable
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
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ppGalNAcT-1 mediated O-glycosylation contributes to innate immune inflammatory response among activated endothelial cells by expression of cell surface selectin ligands on neutrophils
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
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mostly inguinal lymph nodes, not Peyers patch tissue, ppGalNAcT-1 activity regulates L-selectin ligand level in high endothelial venules that is responsible for lymph node cellularity and B- and T-cell homing
gastric cancer cell line, cDNA encoding the transferase is cloned and sequenced from a cDNA library of a human cancer cell line
GALNTL5 protein is mainly located in the theca and granulosa cells of the ovary
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
loss of PGANT35A activity does not alter morphology or staining patterns of epithelial marker components
immunohistology with a monoclonal antibody shows the expected Golgi-like localization in salivary glands
Galnt3 is the major O-glycosyltransferase expressed in the secretory cells of salivary glands
Northern analysis of eight human tissues differ clearly from that of the bovine GalNAc-transferase
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expression analysis of ppGalNAc-T6 in gastric mucosa, intestinal metaplasia, and gastric carcinomas
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RT-PCR, expression at embryonal stage 27 excluded from the central area of the mediolateral spinal cord containing proliferating neuronal precursors
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RT-PCR, expression at embryonal stage 27 in neural crest cells that migrate into heart regions, branchial arches and heart anlage
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RT-PCR, expression at embryonal stage 27 in notochord (highest in posterior regions)
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RT-PCR, expression at embryonal stage 27 in the mantle (differentiating) territory of the mediolateral spinal cord
loss of PGANT35A activity leads to diminished O-glycosylation in epithelial cells of tracheal tube as well as reduced amount of GalNAc alpha-S/T glycans at the apical cell surface
highest levels of GALNTL5 mRNA and protein occur in the uterine horn and oviductal ampulla and the lowest in the uterine cervix and oviductal infundibulum. GALNTL5 protein is mainly located in luminal and glandular epithelial cells of the uterus and oviduct
additional information
Pgant2 expresses ubiquitously in silkworm tissues and cultured cells and during development
additional information
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Pgant2 expresses ubiquitously in silkworm tissues and cultured cells and during development
additional information
expression of enzyme throughout embryonic, larval and pupal stages, in adult males and females, expression increases during larval development and continues through pupal and adult stages
additional information
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expression of enzyme throughout embryonic, larval and pupal stages, in adult males and females, expression increases during larval development and continues through pupal and adult stages
additional information
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quantitative and qualitative differences in different organs
additional information
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existence of more than one form of GalNAc-Ts which are expressed differentially in the gastrointestinal tract
additional information
tissue distribution of several ppGalNAc-transferases
additional information
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ppGalNAc-T1 is ubiquitously expressed, ppGalNAc-T13: not in glioblastoma cells and primary cultured astrocytes
additional information
ppGalNAc-T1 is ubiquitously expressed, ppGalNAc-T13: not in glioblastoma cells and primary cultured astrocytes
additional information
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no activity of GalNAc-T6 in GP202 cells and GP220 cells
additional information
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no activity of GalNAc-T6 in MKN45 cells, GP202 cells, GP220 cells, and K562
additional information
pp-GalNAc-T15 transcript is ubiquitously expressed in human tissues, very low activity in bone marrow, leukocyte, heart, liver, testis, enzyme form pp-GalNAc-T15
additional information
pp-GalNAc-T15 transcript is ubiquitously expressed in human tissues, very low activity in bone marrow, leukocyte, heart, liver, testis, enzyme form pp-GalNAc-T15
additional information
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pp-GalNAc-T15 transcript is ubiquitously expressed in human tissues, very low activity in bone marrow, leukocyte, heart, liver, testis, enzyme form pp-GalNAc-T15
additional information
Northern analysis of human organs revealed a wide expression pattern
additional information
Northern analysis of human organs revealed a wide expression pattern
additional information
Northern analysis of human organs revealed a wide expression pattern
additional information
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Northern analysis of human organs revealed a wide expression pattern
additional information
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traces of ppGaNTase-T6 in the ovary, cervix and uterus, ppGaNTase-T1 is present in all tissues examined
additional information
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quantitative and qualitative differences in different organs
additional information
traces of ppGaNTase-T6 in the ovary, cervix and uterus, ppGaNTase-T1 is present in all tissues examined
