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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei77 – 782Cleavage; to produce soluble form
Metal bindingi250 – 2501Manganese
Binding sitei310 – 3101UDP-alpha-D-galactose1 Publication
Metal bindingi343 – 3431Manganese; via tele nitrogen
Binding sitei355 – 3551N-acetyl-D-glucosamine2 Publications

GO - Molecular functioni

  1. alpha-tubulin binding Source: UniProtKB
  2. beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity Source: UniProtKB
  3. beta-tubulin binding Source: UniProtKB
  4. galactosyltransferase activity Source: UniProtKB
  5. lactose synthase activity Source: UniProtKB
  6. manganese ion binding Source: UniProtKB
  7. N-acetyllactosamine synthase activity Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB
  9. UDP-galactosyltransferase activity Source: UniProtKB

GO - Biological processi

  1. acute inflammatory response Source: Ensembl
  2. angiogenesis involved in wound healing Source: Ensembl
  3. binding of sperm to zona pellucida Source: Reactome
  4. branching morphogenesis of an epithelial tube Source: Ensembl
  5. carbohydrate metabolic process Source: Reactome
  6. cell adhesion Source: Ensembl
  7. cellular protein metabolic process Source: Reactome
  8. development of secondary sexual characteristics Source: Ensembl
  9. epithelial cell development Source: Ensembl
  10. extracellular matrix organization Source: Ensembl
  11. galactose metabolic process Source: Ensembl
  12. glycosaminoglycan metabolic process Source: Reactome
  13. keratan sulfate biosynthetic process Source: Reactome
  14. keratan sulfate metabolic process Source: Reactome
  15. lactose biosynthetic process Source: Ensembl
  16. leukocyte migration Source: Ensembl
  17. mammary gland development Source: Ensembl
  18. multicellular organism reproduction Source: Reactome
  19. negative regulation of cell proliferation Source: Ensembl
  20. Notch signaling pathway Source: Reactome
  21. oligosaccharide biosynthetic process Source: UniProtKB
  22. pathogenesis Source: Reactome
  23. penetration of zona pellucida Source: Ensembl
  24. positive regulation of apoptotic process involved in mammary gland involution Source: Ensembl
  25. positive regulation of epithelial cell proliferation involved in wound healing Source: Ensembl
  26. post-translational protein modification Source: Reactome
  27. protein N-linked glycosylation Source: UniProtKB
  28. protein N-linked glycosylation via asparagine Source: Reactome
  29. regulation of acrosome reaction Source: Ensembl
  30. regulation of cellular component movement Source: Ensembl
  31. single fertilization Source: Reactome
  32. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS01519-MONOMER.
BRENDAi2.4.1.38. 2681.
ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
REACT_121120. Keratan sulfate biosynthesis.
REACT_163933. Interaction With The Zona Pellucida.
REACT_25085. 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
ProteomesiUP000005640: 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
Chain Processed beta-1,4-galactosyltransferase 1 : Secreted
Note: Soluble form found in body fluids.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2424CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei25 – 4420Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini45 – 398354LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basolateral plasma membrane Source: UniProtKB
  2. brush border membrane Source: UniProtKB
  3. desmosome Source: UniProtKB
  4. external side of plasma membrane Source: UniProtKB
  5. extracellular space Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProtKB
  7. filopodium Source: UniProtKB-SubCell
  8. glycocalyx Source: UniProtKB
  9. Golgi apparatus Source: UniProtKB
  10. Golgi cisterna membrane Source: UniProtKB-SubCell
  11. Golgi membrane Source: Reactome
  12. Golgi trans cisterna Source: UniProtKB
  13. integral component of membrane Source: UniProtKB-KW
  14. membrane Source: UniProtKB
  15. 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

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi282 – 2821Y → G: Reduction in N-acetylglucosamine binding. 1 Publication
Mutagenesisi285 – 2851Y → F: No change in enzymatic activity. 1 Publication
Mutagenesisi307 – 3071Y → G: Reduction in N-acetylglucosamine and UDP-galactose binding. 1 Publication
Mutagenesisi308 – 3081W → G: Reduction in N-acetylglucosamine binding. 1 Publication
Mutagenesisi310 – 3101W → G: Reduction in N-acetylglucosamine binding. 1 Publication
Mutagenesisi340 – 3401M → H: Favors the closed conformation of the enzyme. 1 Publication

Keywords - Diseasei

Congenital disorder of glycosylation

Organism-specific databases

MIMi607091. phenotype.
Orphaneti79332. B4GALT1-CDG.
PharmGKBiPA25223.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 398Processed beta-1,4-galactosyltransferase 1PRO_0000296229
Chaini1 – 398398Beta-1,4-galactosyltransferase 1PRO_0000012278Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi130 ↔ 172
Disulfide bondi243 ↔ 262

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP15291.
PaxDbiP15291.
PRIDEiP15291.

PTM databases

PhosphoSiteiP15291.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP15291.
CleanExiHS_B4GALT1.
ExpressionAtlasiP15291. baseline and differential.
GenevestigatoriP15291.

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

Protein-protein interaction databases

BioGridi108950. 18 interactions.
IntActiP15291. 2 interactions.
MINTiMINT-5004065.
STRINGi9606.ENSP00000369055.

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi151 – 1577Combined sources
Turni163 – 1653Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi177 – 18610Combined sources
Helixi188 – 20417Combined sources
Beta strandi208 – 2169Combined sources
Beta strandi218 – 2203Combined sources
Helixi224 – 23815Combined sources
Beta strandi243 – 2475Combined sources
Beta strandi251 – 2555Combined sources
Helixi274 – 2763Combined sources
Beta strandi288 – 2936Combined sources
Helixi294 – 2996Combined sources
Beta strandi309 – 3124Combined sources
Helixi313 – 32311Combined sources
Turni333 – 3353Combined sources
Beta strandi337 – 3404Combined sources
Helixi347 – 3493Combined sources
Helixi359 – 3657Combined sources
Turni366 – 3683Combined sources
Helixi371 – 3733Combined sources
Beta strandi377 – 3848Combined sources
Beta strandi387 – 3937Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 126-398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15291.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 1875UDP-alpha-D-galactose binding
Regioni222 – 2243UDP-alpha-D-galactose bindingBy similarity
Regioni249 – 2502UDP-alpha-D-galactose binding
Regioni312 – 3154N-acetyl-D-glucosamine binding
Regioni343 – 3464UDP-alpha-D-galactose binding

Sequence similaritiesi

Belongs to the glycosyltransferase 7 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG327897.
GeneTreeiENSGT00760000119140.
HOVERGENiHBG058334.
InParanoidiP15291.
KOiK07966.
OMAiAHTRETM.
OrthoDBiEOG7060R0.
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. 1 hit.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101G → R in CAA31611 (PubMed:1384956).Curated
Sequence conflicti10 – 101G → R in BAA06188 (PubMed:7579794).Curated
Sequence conflicti11 – 111Missing in AAA35936 (PubMed:3144273).Curated
Sequence conflicti11 – 111Missing in AAB00776 (PubMed:1903938).Curated
Sequence conflicti11 – 111Missing in AAA68220 (PubMed:7540104).Curated
Sequence conflicti31 – 322AL → VW in AAA35936 (PubMed:3144273).Curated
Sequence conflicti31 – 322AL → VW in AAA35937 (PubMed:3144273).Curated
Sequence conflicti31 – 322AL → VW in AAA68220 (PubMed:7540104).Curated
Sequence conflicti35 – 351G → R in CAA31611 (PubMed:1384956).Curated
Sequence conflicti76 – 761E → D in BAA06188 (PubMed:7579794).Curated
Sequence conflicti91 – 11525SSQPR…ASNLT → GKHAKSSFKQFLLQIKELSN PIDLD in AAA68219 (PubMed:7540104).CuratedAdd
BLAST
Sequence conflicti212 – 2121Y → YGIY in CAA32247 (PubMed:3144273).Curated
Sequence conflicti212 – 2121Y → YGIY in AAB00776 (PubMed:1903938).Curated
Sequence conflicti260 – 2601Y → D in AAA68218 (PubMed:7540104).Curated
Sequence conflicti292 – 2921L → S in BAA06188 (PubMed:7579794).Curated
Sequence conflicti337 – 3371R → T in BAA06188 (PubMed:7579794).Curated
Sequence conflicti340 – 3412MI → PA in AAA68220 (PubMed:7540104).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211R → W.
Corresponds to variant rs1065764 [ dbSNP | Ensembl ].
VAR_054019
Natural varianti257 – 2571H → R.
Corresponds to variant rs9169 [ dbSNP | Ensembl ].
VAR_054020

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313Missing in isoform Short. CuratedVSP_018802Add
BLAST

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.2. human. [P15291-1]

Polymorphism databases

DMDMi116241264.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

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
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. Positions 126-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108950. 18 interactions.
IntActiP15291. 2 interactions.
MINTiMINT-5004065.
STRINGi9606.ENSP00000369055.

Chemistry

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

Protein family/group databases

CAZyiGT7. Glycosyltransferase Family 7.

PTM databases

PhosphoSiteiP15291.

Polymorphism databases

DMDMi116241264.

Proteomic databases

MaxQBiP15291.
PaxDbiP15291.
PRIDEiP15291.

Protocols and materials databases

DNASUi2683.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379731; ENSP00000369055; ENSG00000086062. [P15291-1]
GeneIDi2683.
KEGGihsa:2683.
UCSCiuc003zsg.2. human. [P15291-1]

Organism-specific databases

CTDi2683.
GeneCardsiGC09M033100.
GeneReviewsiB4GALT1.
HGNCiHGNC:924. B4GALT1.
HPAiHPA010806.
HPA010807.
MIMi137060. gene.
607091. phenotype.
neXtProtiNX_P15291.
Orphaneti79332. B4GALT1-CDG.
PharmGKBiPA25223.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327897.
GeneTreeiENSGT00760000119140.
HOVERGENiHBG058334.
InParanoidiP15291.
KOiK07966.
OMAiAHTRETM.
OrthoDBiEOG7060R0.
PhylomeDBiP15291.
TreeFamiTF312834.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciMetaCyc:HS01519-MONOMER.
BRENDAi2.4.1.38. 2681.
ReactomeiREACT_118798. Pre-NOTCH Processing in Golgi.
REACT_121120. Keratan sulfate biosynthesis.
REACT_163933. Interaction With The Zona Pellucida.
REACT_25085. N-Glycan antennae elongation.

Miscellaneous databases

ChiTaRSiB4GALT1. human.
EvolutionaryTraceiP15291.
GeneWikiiB4GALT1.
GenomeRNAii2683.
NextBioi10594.
PROiP15291.
SOURCEiSearch...

Gene expression databases

BgeeiP15291.
CleanExiHS_B4GALT1.
ExpressionAtlasiP15291. baseline and differential.
GenevestigatoriP15291.

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. 1 hit.
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF13733. Glyco_transf_7N. 1 hit.
[Graphical view]
PRINTSiPR02050. B14GALTRFASE.
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase)."
    Masri K.A., Appert H.E., Fukuda M.N.
    Biochem. Biophys. Res. Commun. 157:657-663(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Near identity of HeLa cell galactosyltransferase with the human placental enzyme."
    Watzele G., Berger E.G.
    Nucleic Acids Res. 18:7174-7174(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Genomic structure and expression of human beta-1,4-galactosyltransferase."
    Mengle-Gaw L., McCoy-Haman M.F., Tiemeier D.C.
    Biochem. Biophys. Res. Commun. 176:1269-1276(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies."
    Uejima T., Uemura M., Nozawa S., Narimatsu H.
    Cancer Res. 52:6158-6163(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  5. "The beta 1, 4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells."
    Kudo T., Narimatsu H.
    Glycobiology 5:397-403(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  6. "Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones."
    Chatterjee S.K., Mukerjee S., Tripathi P.K.
    Int. J. Biochem. Cell Biol. 27:329-336(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Fetal liver.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
    Tissue: Testis.
  8. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 138-398, PARTIAL PROTEIN SEQUENCE.
  11. "Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence."
    Appert H.E., Rutherford T.J., Tarr G.E., Thomford N.R., McCorquodale D.J.
    Biochem. Biophys. Res. Commun. 138:224-229(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 78-94.
  12. "Analysis of the substrate binding sites of human galactosyltransferase by protein engineering."
    Aoki D., Appert H.E., Johnson D., Wong S.S., Fukuda M.N.
    EMBO J. 9:3171-3178(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 274-326, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TYR-282; TYR-285; TYR-307; TRP-308 AND TRP-310.
  13. "Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase."
    Lopez L.C., Youakim A., Evans S.C., Shur B.D.
    J. Biol. Chem. 266:15984-15991(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION, SUBCELLULAR LOCATION.
  14. "Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins."
    Yamaguchi N., Fukuda M.N.
    J. Biol. Chem. 270:12170-12176(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  15. "Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions."
    Amado M., Almeida R., Schwientek T., Clausen H.
    Biochim. Biophys. Acta 1473:35-53(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal structures of Met340His mutant of human beta1,4-galactosyltransferase-I with a pentasaccharide and trisaccharides of the N-glycan moiety."
    Ramasamy V., Ramakrishnan B., Boeggeman E., Ratner D.M., Seeberger P.H., Qasba P.K.
    J. Mol. Biol. 353:53-67(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 126-397 OF MUTANT HIS-340 IN COMPLEX WITH MANGANESE IONS AND N-ACETYL-D-GLUCOSAMINE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, MUTAGENESIS OF MET-340, DISULFIDE BONDS.
  19. "Structural snapshots of beta-1,4-galactosyltransferase-I along the kinetic pathway."
    Ramakrishnan B., Ramasamy V., Qasba P.K.
    J. Mol. Biol. 357:1619-1633(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 126-397 OF MUTANT HIS-340 IN COMPLEX WITH MANGANESE IONS AND UDP, COFACTOR, DISULFIDE BONDS.
  20. "Deoxygenated disaccharide analogs as specific inhibitors of beta1-4-galactosyltransferase 1 and selectin-mediated tumor metastasis."
    Brown J.R., Yang F., Sinha A., Ramakrishnan B., Tor Y., Qasba P.K., Esko J.D.
    J. Biol. Chem. 284:4952-4959(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 126-398 IN COMPLEX WITH MANGANESE IONS AND N-ACETYL-D-GLUCOSAMINE, COFACTOR.

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: March 4, 2015
This is version 171 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

External Data

Dasty 3

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 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.