Gene Symbol | GALNT1 |
Entrez ID | 2589 |
Uniprot ID | Q10472 |
Description | polypeptide N-acetylgalactosaminyltransferase 1 |
Chromosomal Location | chr18: 35,581,117-35,711,834 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0006493 |
protein O-linked glycosylation |
A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan. |
ISS |
BP |
GO:0016266 |
O-glycan processing |
The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form a core O-glycan structure. |
TAS |
BP |
GO:0018242 |
protein O-linked glycosylation via serine |
The glycosylation of protein via the O3 atom of peptidyl-serine, forming O3-glycosyl-L-serine; the most common forms are N-acetylgalactosaminyl, mannosyl, galactosyl, and xylosyl serine. |
IDA |
BP |
GO:0018243 |
protein O-linked glycosylation via threonine |
The glycosylation of protein via the O3 atom of peptidyl-threonine, forming O3-glycosyl-L-threonine; the most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine. |
IDA |
CC |
GO:0000139 |
Golgi membrane |
The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
TAS |
CC |
GO:0005576 |
extracellular region |
The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
IEA |
CC |
GO:0005789 |
endoplasmic reticulum membrane |
The lipid bilayer surrounding the endoplasmic reticulum. |
TAS |
CC |
GO:0005794 |
Golgi apparatus |
A compound membranous cytoplasmic organelle of eukaryotic cells, consisting of flattened, ribosome-free vesicles arranged in a more or less regular stack. The Golgi apparatus differs from the endoplasmic reticulum in often having slightly thicker membranes, appearing in sections as a characteristic shallow semicircle so that the convex side (cis or entry face) abuts the endoplasmic reticulum, secretory vesicles emerging from the concave side (trans or exit face). In vertebrate cells there is usually one such organelle, while in invertebrates and plants, where they are known usually as dictyosomes, there may be several scattered in the cytoplasm. The Golgi apparatus processes proteins produced on the ribosomes of the rough endoplasmic reticulum; such processing includes modification of the core oligosaccharides of glycoproteins, and the sorting and packaging of proteins for transport to a variety of cellular locations. Three different regions of the Golgi are now recognized both in terms of structure and function: cis, in the vicinity of the cis face, trans, in the vicinity of the trans face, and medial, lying between the cis and trans regions. |
IDA |
CC |
GO:0016020 |
membrane |
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
IDA |
CC |
GO:0016021 |
integral component of membrane |
The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
IEA |
CC |
GO:0032580 |
Golgi cisterna membrane |
The lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex. |
IEA |
CC |
GO:0048471 |
perinuclear region of cytoplasm |
Cytoplasm situated near, or occurring around, the nucleus. |
IDA |
MF |
GO:0004653 |
polypeptide N-acetylgalactosaminyltransferase activity |
Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. This reaction is the modification of serine or threonine residues in polypeptide chains by the transfer of a N-acetylgalactose from UDP-N-acetylgalactose to the hydroxyl group of the amino acid; it is the first step in O-glycan biosynthesis. |
IDA|TAS |
MF |
GO:0030145 |
manganese ion binding |
Interacting selectively and non-covalently with manganese (Mn) ions. |
IDA |
MF |
GO:0030246 |
carbohydrate binding |
Interacting selectively and non-covalently with any carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates. |
IEA |
Domain ID | Description |
---|---|
IPR000772 |
Ricin B, lectin domain |
IPR001173 |
Glycosyltransferase 2-like |
IPR029044 |
Nucleotide-diphospho-sugar transferases |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa00512 |
Mucin type O-glycan biosynthesis |
KEGG |
hsa01100 |
Metabolic pathways |
KEGG |
UMLS CUI | UMLS Term |
---|---|
C0017661 |
Iga Glomerulonephritis |
Tissue | Cell Type |
---|---|
adrenal gland |
glandular cells |
appendix |
glandular cells |
breast |
glandular cells |
bronchus |
respiratory epithelial cells |
cervix, uterine |
glandular cells |
colon |
glandular cells |
duodenum |
glandular cells |
endometrium |
glandular cells |
epididymis |
glandular cells |
esophagus |
squamous epithelial cells |
gallbladder |
glandular cells |
kidney |
cells in glomeruli |
lung |
macrophages |
lung |
pneumocytes |
nasopharynx |
respiratory epithelial cells |
parathyroid gland |
glandular cells |
placenta |
trophoblastic cells |
prostate |
glandular cells |
rectum |
glandular cells |
skin |
fibroblasts |
soft tissue |
fibroblasts |
spleen |
cells in red pulp |
stomach |
glandular cells |
testis |
Leydig cells |
thyroid gland |
glandular cells |
urinary bladder |
urothelial cells |
vagina |
squamous epithelial cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
22951915 |
Haozi et al. |
2012 |
Altered gene expression profile in cumulus cells of mature MII oocytes from patients with polycystic ovary syndrome |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
MUC1 |
4582 |
P15941 |
0.52 |
PTPRF |
5792 |
P10586 |
0.52 |
SEC23A |
10484 |
Q15436 |
0.63 |
SEC23B |
10483 |
Q15437 |
0.49 |
ELAVL1 |
1994 |
Q15717 |
0.63 |
MOV10 |
4343 |
Q9HCE1 |
0.63 |
P2RX4 |
5025 |
Q99571 |
0.63 |
NXF1 |
10482 |
Q9UBU9 |
0.63 |
NYX |
60506 |
Q9GZU5 |
0.63 |
GINM1 |
116254 |
Q9NU53 |
0.63 |