Protein Description

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

No databases found.

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