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Protein

Beta-1,4-galactosyltransferase 1

Gene

B4GALT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The 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.
The 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.

Catalytic activityi

UDP-alpha-D-galactose + D-glucose = UDP + lactose.
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide.
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.

Cofactori

Mn2+3 Publications

Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi250Manganese1
Binding sitei310UDP-alpha-D-galactose1 Publication1
Metal bindingi343Manganese; via tele nitrogen1
Binding sitei355N-acetyl-D-glucosamine2 Publications1

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB
  • galactosyltransferase activity Source: UniProtKB
  • lactose synthase activity Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • N-acetyllactosamine synthase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • UDP-galactosyltransferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS01519-MONOMER.
ZFISH:HS01519-MONOMER.
BRENDAi2.4.1.133. 2681.
2.4.1.38. 2681.
ReactomeiR-HSA-1300644. Interaction With The Zona Pellucida.
R-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-2022854. Keratan sulfate biosynthesis.
R-HSA-5653890. Lactose synthesis.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-975577. N-Glycan antennae elongation.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,4-galactosyltransferase 1 (EC:2.4.1.-)
Short name:
Beta-1,4-GalTase 1
Short name:
Beta4Gal-T1
Short name:
b4Gal-T1
Alternative name(s):
UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1
Cleaved into the following chain:
Including the following 4 domains:
Lactose synthase A protein (EC:2.4.1.22)
N-acetyllactosamine synthase (EC:2.4.1.90)
Alternative name(s):
Nal synthase
Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase (EC:2.4.1.38)
Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase (EC:2.4.1.-)
Gene namesi
Name:B4GALT1
Synonyms:GGTB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:924. B4GALT1.

Subcellular locationi

Isoform Long :
  • Golgi apparatusGolgi stack membrane 1 Publication; Single-pass type II membrane protein
  • Cell membrane 1 Publication; Single-pass type II membrane protein
  • Cell surface 1 Publication
  • Cell projectionfilopodium By similarity

  • 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).By similarity1 Publication
Isoform Short :
  • Golgi apparatusGolgi stack membrane 1 Publication; Single-pass type II membrane protein

  • Note: Found in trans cisternae of Golgi.1 Publication
Processed beta-1,4-galactosyltransferase 1 :
  • Secreted 1 Publication

  • Note: Soluble form found in body fluids.1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 24CytoplasmicSequence analysisAdd BLAST24
Transmembranei25 – 44Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini45 – 398LumenalSequence analysisAdd BLAST354

GO - Cellular componenti

  • basolateral plasma membrane Source: UniProtKB
  • brush border membrane Source: UniProtKB
  • desmosome Source: UniProtKB
  • external side of plasma membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • filopodium Source: UniProtKB-SubCell
  • glycocalyx Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: Reactome
  • Golgi trans cisterna Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 2D (CDG2D)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:607091

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi282Y → G: Reduction in N-acetylglucosamine binding. 1 Publication1
Mutagenesisi285Y → F: No change in enzymatic activity. 1 Publication1
Mutagenesisi307Y → G: Reduction in N-acetylglucosamine and UDP-galactose binding. 1 Publication1
Mutagenesisi308W → G: Reduction in N-acetylglucosamine binding. 1 Publication1
Mutagenesisi310W → G: Reduction in N-acetylglucosamine binding. 1 Publication1
Mutagenesisi340M → H: Favors the closed conformation of the enzyme. 1 Publication1

Keywords - Diseasei

Congenital disorder of glycosylation

Organism-specific databases

DisGeNETi2683.
MalaCardsiB4GALT1.
MIMi607091. phenotype.
OpenTargetsiENSG00000086062.
Orphaneti79332. B4GALT1-CDG.
PharmGKBiPA25223.

Chemistry databases

ChEMBLiCHEMBL4384.
DrugBankiDB00141. N-Acetyl-D-glucosamine.

Polymorphism and mutation databases

BioMutaiB4GALT1.
DMDMi116241264.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000296229? – 398Processed beta-1,4-galactosyltransferase 1
ChainiPRO_00000122781 – 398Beta-1,4-galactosyltransferase 1Add BLAST398

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi113N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi130 ↔ 172
Disulfide bondi243 ↔ 262

Post-translational modificationi

The soluble form derives from the membrane forms by proteolytic processing.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei77 – 78Cleavage; to produce soluble form2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP15291.
MaxQBiP15291.
PaxDbiP15291.
PeptideAtlasiP15291.
PRIDEiP15291.

PTM databases

iPTMnetiP15291.
PhosphoSitePlusiP15291.
SwissPalmiP15291.

Expressioni

Tissue specificityi

Ubiquitously expressed, but at very low levels in fetal and adult brain.

Gene expression databases

BgeeiENSG00000086062.
CleanExiHS_B4GALT1.
ExpressionAtlasiP15291. baseline and differential.
GenevisibleiP15291. HS.

Organism-specific databases

HPAiHPA010806.
HPA010807.

Interactioni

Subunit structurei

Homodimer; 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).By similarity4 Publications

GO - Molecular functioni

  • alpha-tubulin binding Source: UniProtKB
  • beta-tubulin binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi108950. 28 interactors.
IntActiP15291. 4 interactors.
MINTiMINT-5004065.
STRINGi9606.ENSP00000369055.

Chemistry databases

BindingDBiP15291.

Structurei

Secondary structure

1398
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi151 – 157Combined sources7
Turni163 – 165Combined sources3
Beta strandi170 – 173Combined sources4
Beta strandi177 – 186Combined sources10
Helixi188 – 204Combined sources17
Beta strandi208 – 216Combined sources9
Beta strandi218 – 220Combined sources3
Helixi224 – 238Combined sources15
Beta strandi243 – 247Combined sources5
Beta strandi251 – 255Combined sources5
Helixi274 – 276Combined sources3
Beta strandi288 – 293Combined sources6
Helixi294 – 299Combined sources6
Beta strandi309 – 312Combined sources4
Helixi313 – 323Combined sources11
Turni333 – 335Combined sources3
Beta strandi337 – 340Combined sources4
Helixi347 – 349Combined sources3
Helixi359 – 365Combined sources7
Turni366 – 368Combined sources3
Helixi371 – 373Combined sources3
Beta strandi377 – 384Combined sources8
Beta strandi387 – 393Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AE7X-ray2.00A/B/C126-398[»]
2AECX-ray2.00A/B/C126-398[»]
2AESX-ray2.00A/B/C126-398[»]
2AGDX-ray1.90A/B/C126-398[»]
2AH9X-ray2.00A/B/C126-398[»]
2FY7X-ray1.70A126-398[»]
2FYAX-ray1.90A126-398[»]
2FYBX-ray1.90A126-398[»]
3EE5X-ray2.20A/B/C126-398[»]
4EE3X-ray2.30A/B/C126-398[»]
4EE4X-ray1.95A/B/C126-398[»]
4EE5X-ray2.20A/B/C126-398[»]
4EEAX-ray2.00A/B/C126-398[»]
4EEGX-ray2.20A/B/C126-398[»]
4EEMX-ray2.20A/B/C126-398[»]
4EEOX-ray2.30A/B/C126-398[»]
4L41X-ray2.70C126-398[»]
ProteinModelPortaliP15291.
SMRiP15291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15291.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni183 – 187UDP-alpha-D-galactose binding5
Regioni222 – 224UDP-alpha-D-galactose bindingBy similarity3
Regioni249 – 250UDP-alpha-D-galactose binding2
Regioni312 – 315N-acetyl-D-glucosamine binding4
Regioni343 – 346UDP-alpha-D-galactose binding4

Sequence similaritiesi

Belongs to the glycosyltransferase 7 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3916. Eukaryota.
ENOG410ZYYA. LUCA.
GeneTreeiENSGT00760000119140.
HOVERGENiHBG058334.
InParanoidiP15291.
KOiK07966.
OMAiAHTRETM.
OrthoDBiEOG091G0P66.
PhylomeDBiP15291.
TreeFamiTF312834.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 2 hits.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform Long (identifier: P15291-1) [UniParc]FASTAAdd to basket
Also known as: Cell surface

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.

« Hide

        10         20         30         40         50
MRLREPLLSG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLSRL
60 70 80 90 100
PQLVGVSTPL QGGSNSAAAI GQSSGELRTG GARPPPPLGA SSQPRPGGDS
110 120 130 140 150
SPVVDSGPGP ASNLTSVPVP HTTALSLPAC PEESPLLVGP MLIEFNMPVD
160 170 180 190 200
LELVAKQNPN VKMGGRYAPR DCVSPHKVAI IIPFRNRQEH LKYWLYYLHP
210 220 230 240 250
VLQRQQLDYG IYVINQAGDT IFNRAKLLNV GFQEALKDYD YTCFVFSDVD
260 270 280 290 300
LIPMNDHNAY RCFSQPRHIS VAMDKFGFSL PYVQYFGGVS ALSKQQFLTI
310 320 330 340 350
NGFPNNYWGW GGEDDDIFNR LVFRGMSISR PNAVVGRCRM IRHSRDKKNE
360 370 380 390
PNPQRFDRIA HTKETMLSDG LNSLTYQVLD VQRYPLYTQI TVDIGTPS
Length:398
Mass (Da):43,920
Last modified:October 17, 2006 - v5
Checksum:i29B224C83C61E165
GO
Isoform Short (identifier: P15291-2) [UniParc]FASTAAdd to basket
Also known as: Golgi complex

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.

Show »
Length:385
Mass (Da):42,538
Checksum:iA28CB67033107C83
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti10G → R in CAA31611 (PubMed:1384956).Curated1
Sequence conflicti10G → R in BAA06188 (PubMed:7579794).Curated1
Sequence conflicti11Missing in AAA35936 (PubMed:3144273).Curated1
Sequence conflicti11Missing in AAB00776 (PubMed:1903938).Curated1
Sequence conflicti11Missing in AAA68220 (PubMed:7540104).Curated1
Sequence conflicti31 – 32AL → VW in AAA35936 (PubMed:3144273).Curated2
Sequence conflicti31 – 32AL → VW in AAA35937 (PubMed:3144273).Curated2
Sequence conflicti31 – 32AL → VW in AAA68220 (PubMed:7540104).Curated2
Sequence conflicti35G → R in CAA31611 (PubMed:1384956).Curated1
Sequence conflicti76E → D in BAA06188 (PubMed:7579794).Curated1
Sequence conflicti91 – 115SSQPR…ASNLT → GKHAKSSFKQFLLQIKELSN PIDLD in AAA68219 (PubMed:7540104).CuratedAdd BLAST25
Sequence conflicti212Y → YGIY in CAA32247 (PubMed:3144273).Curated1
Sequence conflicti212Y → YGIY in AAB00776 (PubMed:1903938).Curated1
Sequence conflicti260Y → D in AAA68218 (PubMed:7540104).Curated1
Sequence conflicti292L → S in BAA06188 (PubMed:7579794).Curated1
Sequence conflicti337R → T in BAA06188 (PubMed:7579794).Curated1
Sequence conflicti340 – 341MI → PA in AAA68220 (PubMed:7540104).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05401921R → W.Corresponds to variant rs1065764dbSNPEnsembl.1
Natural variantiVAR_054020257H → R.Corresponds to variant rs9169dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0188021 – 13Missing in isoform Short. CuratedAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14085 mRNA. Translation: CAA32247.1.
M22921 mRNA. Translation: AAA35936.1.
M22921 mRNA. Translation: AAA35937.1.
X55415 mRNA. Translation: CAA39073.1.
X55415 mRNA. Translation: CAA39074.1.
M70432
, M70427, M70428, M70429, M70430, M70431 Genomic DNA. Translation: AAB00776.1.
X13223 mRNA. Translation: CAA31611.1.
D29805 mRNA. Translation: BAA06188.1.
U10472 mRNA. Translation: AAA68218.1.
U10473 mRNA. Translation: AAA68219.1.
U10474 mRNA. Translation: AAA68220.1.
CH471071 Genomic DNA. Translation: EAW58520.1.
CH471071 Genomic DNA. Translation: EAW58521.1.
AK312797 mRNA. Translation: BAG35657.1.
AL161445 Genomic DNA. Translation: CAD13306.1.
M13701 mRNA. Translation: AAA35935.1.
CCDSiCCDS6535.1. [P15291-1]
PIRiJQ1030.
RefSeqiNP_001488.2. NM_001497.3. [P15291-1]
UniGeneiHs.272011.

Genome annotation databases

EnsembliENST00000379731; ENSP00000369055; ENSG00000086062. [P15291-1]
GeneIDi2683.
KEGGihsa:2683.
UCSCiuc003zsg.3. human. [P15291-1]

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Beta-1,4-galactosyltransferase 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14085 mRNA. Translation: CAA32247.1.
M22921 mRNA. Translation: AAA35936.1.
M22921 mRNA. Translation: AAA35937.1.
X55415 mRNA. Translation: CAA39073.1.
X55415 mRNA. Translation: CAA39074.1.
M70432
, M70427, M70428, M70429, M70430, M70431 Genomic DNA. Translation: AAB00776.1.
X13223 mRNA. Translation: CAA31611.1.
D29805 mRNA. Translation: BAA06188.1.
U10472 mRNA. Translation: AAA68218.1.
U10473 mRNA. Translation: AAA68219.1.
U10474 mRNA. Translation: AAA68220.1.
CH471071 Genomic DNA. Translation: EAW58520.1.
CH471071 Genomic DNA. Translation: EAW58521.1.
AK312797 mRNA. Translation: BAG35657.1.
AL161445 Genomic DNA. Translation: CAD13306.1.
M13701 mRNA. Translation: AAA35935.1.
CCDSiCCDS6535.1. [P15291-1]
PIRiJQ1030.
RefSeqiNP_001488.2. NM_001497.3. [P15291-1]
UniGeneiHs.272011.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AE7X-ray2.00A/B/C126-398[»]
2AECX-ray2.00A/B/C126-398[»]
2AESX-ray2.00A/B/C126-398[»]
2AGDX-ray1.90A/B/C126-398[»]
2AH9X-ray2.00A/B/C126-398[»]
2FY7X-ray1.70A126-398[»]
2FYAX-ray1.90A126-398[»]
2FYBX-ray1.90A126-398[»]
3EE5X-ray2.20A/B/C126-398[»]
4EE3X-ray2.30A/B/C126-398[»]
4EE4X-ray1.95A/B/C126-398[»]
4EE5X-ray2.20A/B/C126-398[»]
4EEAX-ray2.00A/B/C126-398[»]
4EEGX-ray2.20A/B/C126-398[»]
4EEMX-ray2.20A/B/C126-398[»]
4EEOX-ray2.30A/B/C126-398[»]
4L41X-ray2.70C126-398[»]
ProteinModelPortaliP15291.
SMRiP15291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108950. 28 interactors.
IntActiP15291. 4 interactors.
MINTiMINT-5004065.
STRINGi9606.ENSP00000369055.

Chemistry databases

BindingDBiP15291.
ChEMBLiCHEMBL4384.
DrugBankiDB00141. N-Acetyl-D-glucosamine.

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

PTM databases

iPTMnetiP15291.
PhosphoSitePlusiP15291.
SwissPalmiP15291.

Polymorphism and mutation databases

BioMutaiB4GALT1.
DMDMi116241264.

Proteomic databases

EPDiP15291.
MaxQBiP15291.
PaxDbiP15291.
PeptideAtlasiP15291.
PRIDEiP15291.

Protocols and materials databases

DNASUi2683.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379731; ENSP00000369055; ENSG00000086062. [P15291-1]
GeneIDi2683.
KEGGihsa:2683.
UCSCiuc003zsg.3. human. [P15291-1]

Organism-specific databases

CTDi2683.
DisGeNETi2683.
GeneCardsiB4GALT1.
GeneReviewsiB4GALT1.
HGNCiHGNC:924. B4GALT1.
HPAiHPA010806.
HPA010807.
MalaCardsiB4GALT1.
MIMi137060. gene.
607091. phenotype.
neXtProtiNX_P15291.
OpenTargetsiENSG00000086062.
Orphaneti79332. B4GALT1-CDG.
PharmGKBiPA25223.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3916. Eukaryota.
ENOG410ZYYA. LUCA.
GeneTreeiENSGT00760000119140.
HOVERGENiHBG058334.
InParanoidiP15291.
KOiK07966.
OMAiAHTRETM.
OrthoDBiEOG091G0P66.
PhylomeDBiP15291.
TreeFamiTF312834.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:HS01519-MONOMER.
ZFISH:HS01519-MONOMER.
BRENDAi2.4.1.133. 2681.
2.4.1.38. 2681.
ReactomeiR-HSA-1300644. Interaction With The Zona Pellucida.
R-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-2022854. Keratan sulfate biosynthesis.
R-HSA-5653890. Lactose synthesis.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-975577. N-Glycan antennae elongation.

Miscellaneous databases

ChiTaRSiB4GALT1. human.
EvolutionaryTraceiP15291.
GeneWikiiB4GALT1.
GenomeRNAii2683.
PROiP15291.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000086062.
CleanExiHS_B4GALT1.
ExpressionAtlasiP15291. baseline and differential.
GenevisibleiP15291. HS.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR003859. Galactosyl_T.
IPR027791. Galactosyl_T_C.
IPR027995. Galactosyl_T_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR19300. PTHR19300. 2 hits.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiB4GT1_HUMAN
AccessioniPrimary (citable) accession number: P15291
Secondary accession number(s): B2R710
, D3DRL2, Q12909, Q12910, Q12911, Q14456, Q14509, Q14523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 189 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.