O60512 · B4GT3_HUMAN
- ProteinBeta-1,4-galactosyltransferase 3
- GeneB4GALT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids393 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
Catalytic activity
- an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H+ + UDPThis reaction proceeds in the forward direction.
- beta-D-glucosylceramide + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H+ + UDPThis reaction proceeds in the forward direction.
- a neolactoside IV3-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer + H+ + UDPThis reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
63 μM | GlcNAc-B-S-pNP | |||||
0.084 mM | UDP-galactose | |||||
0.58 mM | benzyl-beta-D-GlcNAc | |||||
13.1 mM | D-GlcNAc |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
64.35 pmol/min/mg | towards UDP-galactose | ||||
66.25 pmol/min/mg | towards for benzyl-beta-D-GlcNAc | ||||
60.85 pmol/min/mg | towards D-GlcNAc |
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 130-134 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: PHRAR | ||||||
Binding site | 169-171 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: FNR | ||||||
Binding site | 196-197 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: VD | ||||||
Binding site | 197 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 226 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 258 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 260-263 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: GEDD | ||||||
Binding site | 291 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 291-293 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: HRG | ||||||
Binding site | 303 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi cisterna membrane | |
Cellular Component | Golgi membrane | |
Molecular Function | beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity | |
Molecular Function | galactosyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | N-acetyllactosamine synthase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | galactosylceramide biosynthetic process | |
Biological Process | glycosylation | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameBeta-1,4-galactosyltransferase 3
- EC number
- Short namesBeta-1,4-GalTase 3 ; Beta4Gal-T3; b4Gal-T3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60512
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein
Note: Trans cisternae of Golgi stack.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-10 | Cytoplasmic | ||||
Sequence: MLRRLLERPC | ||||||
Transmembrane | 11-31 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: TLALLVGSQLAVMMYLSLGGF | ||||||
Topological domain | 32-393 | Lumenal | ||||
Sequence: RSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPLSTANHTALRGSH |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 430 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080537 | 1-393 | Beta-1,4-galactosyltransferase 3 | |||
Sequence: MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSHLPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPLSTANHTALRGSH | ||||||
Glycosylation | 57 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 77↔119 | |||||
Sequence: CPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGC | ||||||
Glycosylation | 166 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 190↔209 | |||||
Sequence: CLFLHDVDLLPENDHNLYVC | ||||||
Glycosylation | 337 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 385 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in various tissues. Highest expression in placenta, prostate, testis, ovary, intestine and muscle, and in fetal brain.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 339-393 | Disordered | ||||
Sequence: TADIGTDPRGPRAPSGPRYPPGSSQAFRQEMLQRRPPARPGPLSTANHTALRGSH |
Sequence similarities
Belongs to the glycosyltransferase 7 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O60512-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length393
- Mass (Da)43,928
- Last updated2005-06-21 v2
- ChecksumCA0BF955F95ED1F4
O60512-2
- Name2
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 64 | in Ref. 2; AAC39734 | ||||
Sequence: A → R | ||||||
Sequence conflict | 112 | in Ref. 2; AAC39734 | ||||
Sequence: G → A | ||||||
Alternative sequence | VSP_014106 | 116-145 | in isoform 2 | |||
Sequence: PAGCEPRSRTAIIVPHRAREHHLRLLLYHL → PAALPPAPLLAAPAACLWHLCHPPGWKWNI | ||||||
Alternative sequence | VSP_014107 | 146-393 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 223 | in Ref. 2; AAC39734 | ||||
Sequence: K → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y12509 EMBL· GenBank· DDBJ | CAA73111.1 EMBL· GenBank· DDBJ | mRNA | ||
AF038661 EMBL· GenBank· DDBJ | AAC39734.1 EMBL· GenBank· DDBJ | mRNA | ||
AB024435 EMBL· GenBank· DDBJ | BAA75820.1 EMBL· GenBank· DDBJ | mRNA | ||
AL590714 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AK023311 EMBL· GenBank· DDBJ | BAB14520.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471121 EMBL· GenBank· DDBJ | EAW52628.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471121 EMBL· GenBank· DDBJ | EAW52629.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471121 EMBL· GenBank· DDBJ | EAW52630.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471121 EMBL· GenBank· DDBJ | EAW52631.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471121 EMBL· GenBank· DDBJ | EAW52632.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000276 EMBL· GenBank· DDBJ | AAH00276.1 EMBL· GenBank· DDBJ | mRNA | ||
BC006099 EMBL· GenBank· DDBJ | AAH06099.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009985 EMBL· GenBank· DDBJ | AAH09985.1 EMBL· GenBank· DDBJ | mRNA |