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P15291

- B4GT1_HUMAN

UniProt

P15291 - B4GT1_HUMAN

Protein

Beta-1,4-galactosyltransferase 1

Gene

B4GALT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 5 (17 Oct 2006)
      Previous versions | rss
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    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

    Manganese.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. penetration of zona pellucida Source: Ensembl
    23. positive regulation of apoptotic process involved in mammary gland involution Source: Ensembl
    24. positive regulation of epithelial cell proliferation involved in wound healing Source: Ensembl
    25. post-translational protein modification Source: Reactome
    26. protein N-linked glycosylation Source: UniProtKB
    27. protein N-linked glycosylation via asparagine Source: Reactome
    28. regulation of acrosome reaction Source: Ensembl
    29. regulation of cellular component movement Source: Ensembl
    30. single fertilization Source: Reactome
    31. small molecule metabolic process Source: Reactome

    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

    Chain Processed beta-1,4-galactosyltransferase 1 : Secreted
    Note: Soluble form found in body fluids.

    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: UniProt
    6. extracellular vesicular exosome Source: UniProt
    7. glycocalyx Source: UniProtKB
    8. Golgi apparatus Source: UniProtKB
    9. Golgi cisterna membrane Source: UniProtKB-SubCell
    10. Golgi membrane Source: Reactome
    11. Golgi trans cisterna Source: UniProtKB
    12. integral component of membrane Source: UniProtKB-KW
    13. membrane Source: UniProtKB
    14. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Congenital 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.

    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

    ArrayExpressiP15291.
    BgeeiP15291.
    CleanExiHS_B4GALT1.
    GenevestigatoriP15291.

    Organism-specific databases

    HPAiHPA010806.
    HPA010807.

    Interactioni

    Subunit structurei

    Homodimer; and heterodimer with alpha-lactalbumin to form lactose synthase.4 Publications

    Protein-protein interaction databases

    BioGridi108950. 11 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 – 1577
    Turni163 – 1653
    Beta strandi170 – 1734
    Beta strandi177 – 18610
    Helixi188 – 20417
    Beta strandi208 – 2169
    Beta strandi218 – 2203
    Helixi224 – 23815
    Beta strandi243 – 2475
    Beta strandi251 – 2555
    Helixi274 – 2763
    Beta strandi288 – 2936
    Helixi294 – 2996
    Beta strandi309 – 3124
    Helixi313 – 32311
    Turni333 – 3353
    Beta strandi337 – 3404
    Helixi347 – 3493
    Helixi359 – 3657
    Turni366 – 3683
    Helixi371 – 3733
    Beta strandi377 – 3848
    Beta strandi387 – 3937

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2424CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini45 – 398354LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei25 – 4420Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    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.
    HOVERGENiHBG058334.
    InParanoidiP15291.
    KOiK07966.
    OMAiVGGRYTP.
    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. Align

    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

    MRLREPLLSG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLSRL    50
    PQLVGVSTPL QGGSNSAAAI GQSSGELRTG GARPPPPLGA SSQPRPGGDS 100
    SPVVDSGPGP ASNLTSVPVP HTTALSLPAC PEESPLLVGP MLIEFNMPVD 150
    LELVAKQNPN VKMGGRYAPR DCVSPHKVAI IIPFRNRQEH LKYWLYYLHP 200
    VLQRQQLDYG IYVINQAGDT IFNRAKLLNV GFQEALKDYD YTCFVFSDVD 250
    LIPMNDHNAY RCFSQPRHIS VAMDKFGFSL PYVQYFGGVS ALSKQQFLTI 300
    NGFPNNYWGW GGEDDDIFNR LVFRGMSISR PNAVVGRCRM IRHSRDKKNE 350
    PNPQRFDRIA HTKETMLSDG LNSLTYQVLD VQRYPLYTQI TVDIGTPS 398
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6535.1. [P15291-1 ]
    PIRi JQ1030.
    RefSeqi NP_001488.2. NM_001497.3. [P15291-1 ]
    UniGenei Hs.272011.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AE7 X-ray 2.00 A/B/C 126-398 [» ]
    2AEC X-ray 2.00 A/B/C 126-398 [» ]
    2AES X-ray 2.00 A/B/C 126-398 [» ]
    2AGD X-ray 1.90 A/B/C 126-398 [» ]
    2AH9 X-ray 2.00 A/B/C 126-398 [» ]
    2FY7 X-ray 1.70 A 126-398 [» ]
    2FYA X-ray 1.90 A 126-398 [» ]
    2FYB X-ray 1.90 A 126-398 [» ]
    3EE5 X-ray 2.20 A/B/C 126-398 [» ]
    4EE3 X-ray 2.30 A/B/C 126-398 [» ]
    4EE4 X-ray 1.95 A/B/C 126-398 [» ]
    4EE5 X-ray 2.20 A/B/C 126-398 [» ]
    4EEA X-ray 2.00 A/B/C 126-398 [» ]
    4EEG X-ray 2.20 A/B/C 126-398 [» ]
    4EEM X-ray 2.20 A/B/C 126-398 [» ]
    4EEO X-ray 2.30 A/B/C 126-398 [» ]
    4L41 X-ray 2.70 C 126-398 [» ]
    ProteinModelPortali P15291.
    SMRi P15291. Positions 126-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108950. 11 interactions.
    IntActi P15291. 2 interactions.
    MINTi MINT-5004065.
    STRINGi 9606.ENSP00000369055.

    Chemistry

    BindingDBi P15291.
    ChEMBLi CHEMBL4384.
    DrugBanki DB00141. N-Acetyl-D-glucosamine.

    Protein family/group databases

    CAZyi GT7. Glycosyltransferase Family 7.

    PTM databases

    PhosphoSitei P15291.

    Polymorphism databases

    DMDMi 116241264.

    Proteomic databases

    MaxQBi P15291.
    PaxDbi P15291.
    PRIDEi P15291.

    Protocols and materials databases

    DNASUi 2683.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379731 ; ENSP00000369055 ; ENSG00000086062 . [P15291-1 ]
    GeneIDi 2683.
    KEGGi hsa:2683.
    UCSCi uc003zsg.2. human. [P15291-1 ]

    Organism-specific databases

    CTDi 2683.
    GeneCardsi GC09M033100.
    GeneReviewsi B4GALT1.
    HGNCi HGNC:924. B4GALT1.
    HPAi HPA010806.
    HPA010807.
    MIMi 137060. gene.
    607091. phenotype.
    neXtProti NX_P15291.
    Orphaneti 79332. B4GALT1-CDG.
    PharmGKBi PA25223.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327897.
    HOVERGENi HBG058334.
    InParanoidi P15291.
    KOi K07966.
    OMAi VGGRYTP.
    OrthoDBi EOG7060R0.
    PhylomeDBi P15291.
    TreeFami TF312834.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci MetaCyc:HS01519-MONOMER.
    BRENDAi 2.4.1.38. 2681.
    Reactomei REACT_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

    ChiTaRSi B4GALT1. human.
    EvolutionaryTracei P15291.
    GeneWikii B4GALT1.
    GenomeRNAii 2683.
    NextBioi 10594.
    PROi P15291.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15291.
    Bgeei P15291.
    CleanExi HS_B4GALT1.
    Genevestigatori P15291.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR003859. Galactosyl_T.
    IPR027791. Galactosyl_T_C.
    IPR027995. Galactosyl_T_N.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    PANTHERi PTHR19300. PTHR19300. 1 hit.
    Pfami PF02709. Glyco_transf_7C. 1 hit.
    PF13733. Glyco_transf_7N. 1 hit.
    [Graphical view ]
    PRINTSi PR02050. B14GALTRFASE.
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. "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.
    18. "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.
    19. "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: October 1, 2014
    This is version 167 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