MGP Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins
MGP001196

UniProt Annotations

Entry Information
Gene NameUDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1
Protein EntryB4GT1_HUMAN
UniProt IDP15291
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative initiation; Named isoforms=2; Name=Long; Synonyms=Cell surface; IsoId=P15291-1; Sequence=Displayed; Name=Short; Synonyms=Golgi complex; IsoId=P15291-2; Sequence=VSP_018802;
Catalytic ActivityUDP-alpha-D-galactose + D-glucose = UDP + lactose.
Catalytic ActivityUDP-alpha-D-galactose + N-acetyl-beta-D- glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N- acetyl-beta-D-glucosaminylglycopeptide.
Catalytic ActivityUDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.
CofactorName=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16157350, ECO:0000269|PubMed:16497331, ECO:0000269|PubMed:19106107};
DiseaseCongenital disorder of glycosylation 2D (CDG2D) [MIM:607091]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N- glycoproteins during embryonic development, differentiation, and maintenance of cell functions. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionThe cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix.
FunctionThe Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
PathwayProtein modification; protein glycosylation.
PtmThe soluble form derives from the membrane forms by proteolytic processing.
SimilarityBelongs to the glycosyltransferase 7 family. {ECO:0000305}.
Subcellular LocationIsoform Long: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Cell membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Cell surface {ECO:0000269|PubMed:1714903}. Cell projection, filopodium {ECO:0000250|UniProtKB:P15535}. Note=Found in trans cisternae of Golgi but is mainly localized at the plasma membrane (PubMed:1714903). B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity). {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:1714903}.
Subcellular LocationIsoform Short: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Note=Found in trans cisternae of Golgi. {ECO:0000269|PubMed:1714903}.
Subcellular LocationProcessed beta-1,4-galactosyltransferase 1: Secreted. Note=Soluble form found in body fluids.
SubunitHomodimer; and heterodimer with alpha-lactalbumin to form lactose synthase. Interacts (via N-terminal cytoplasmic domain) with UBE2Q1 (via N-terminus); the interaction is direct (By similarity). {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:16157350, ECO:0000269|PubMed:16497331, ECO:0000269|PubMed:19106107, ECO:0000269|PubMed:7744867}.
Tissue SpecificityUbiquitously expressed, but at very low levels in fetal and adult brain.
Web ResourceName=Functional Glycomics Gateway - GTase; Note=Beta-1,4-galactosyltransferase 1; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_436";
Web ResourceName=GGDB; Note=GlycoGene database; URL="http://jcggdb.jp/rcmg/ggdb/Homolog?cat=symbol&symbol=B4GALT1";
  logo