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P08037

- B4GT1_BOVIN

UniProt

P08037 - B4GT1_BOVIN

Protein

Beta-1,4-galactosyltransferase 1

Gene

B4GALT1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 3 (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.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi254 – 2541Manganese
    Binding sitei314 – 3141UDP-alpha-D-galactose
    Metal bindingi347 – 3471Manganese; via tele nitrogen
    Binding sitei359 – 3591N-acetyl-D-glucosamine

    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. lactose synthase activity Source: UniProtKB
    5. manganese ion binding Source: UniProtKB
    6. N-acetyllactosamine synthase activity Source: UniProtKB
    7. protein binding Source: IntAct
    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: Ensembl
    4. branching morphogenesis of an epithelial tube Source: Ensembl
    5. cell adhesion Source: Ensembl
    6. development of secondary sexual characteristics Source: Ensembl
    7. epithelial cell development Source: Ensembl
    8. extracellular matrix organization Source: Ensembl
    9. galactose metabolic process Source: Ensembl
    10. lactose biosynthetic process Source: Ensembl
    11. leukocyte migration Source: Ensembl
    12. mammary gland development Source: Ensembl
    13. negative regulation of cell proliferation Source: Ensembl
    14. oligosaccharide biosynthetic process Source: UniProtKB
    15. penetration of zona pellucida Source: Ensembl
    16. positive regulation of apoptotic process involved in mammary gland involution Source: Ensembl
    17. positive regulation of epithelial cell proliferation involved in wound healing Source: Ensembl
    18. protein N-linked glycosylation Source: UniProtKB
    19. regulation of acrosome reaction Source: Ensembl
    20. regulation of cellular component movement Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_205470. Pre-NOTCH Processing in Golgi.
    REACT_210187. Interaction With The Zona Pellucida.
    REACT_211440. Keratan sulfate biosynthesis.
    REACT_225710. N-Glycan antennae elongation.
    SABIO-RKP08037.
    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:GALT, GGTB2
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 8

    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 region Source: UniProtKB-SubCell
    6. glycocalyx Source: UniProtKB
    7. Golgi apparatus Source: UniProtKB
    8. Golgi cisterna membrane Source: UniProtKB-SubCell
    9. Golgi trans cisterna Source: UniProtKB
    10. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi314 – 3141W → A: Reduces galactosyltransferase activity, lactose synthase activity and substrate binding by 99%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 402Processed beta-1,4-galactosyltransferase 1PRO_0000296228
    Chaini1 – 402402Beta-1,4-galactosyltransferase 1PRO_0000012276Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi90 – 901N-linked (GlcNAc...)1 Publication
    Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi134 ↔ 176
    Disulfide bondi247 ↔ 266

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP08037.
    PRIDEiP08037.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LalbaP2975210EBI-1031436,EBI-1031454From a different organism.

    Protein-protein interaction databases

    IntActiP08037. 1 interaction.

    Structurei

    Secondary structure

    1
    402
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi149 – 1513
    Helixi155 – 1617
    Turni167 – 1693
    Beta strandi174 – 1774
    Beta strandi181 – 19010
    Helixi192 – 20817
    Beta strandi212 – 2209
    Beta strandi222 – 2243
    Helixi228 – 24215
    Beta strandi247 – 2515
    Beta strandi255 – 2595
    Helixi278 – 2803
    Beta strandi292 – 2976
    Helixi298 – 3036
    Beta strandi313 – 3164
    Helixi317 – 32711
    Turni337 – 3404
    Beta strandi341 – 3444
    Turni347 – 3493
    Helixi351 – 3533
    Helixi359 – 3646
    Helixi366 – 3694
    Turni370 – 3723
    Helixi375 – 3773
    Beta strandi381 – 3877
    Beta strandi392 – 3976

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FGXX-ray2.40A/B115-402[»]
    1FR8X-ray2.40A/B115-402[»]
    1NF5X-ray2.00B/D130-402[»]
    1NHEX-ray2.50B/D130-402[»]
    1NKHX-ray2.00B/D130-402[»]
    1NMMX-ray2.00B/D130-402[»]
    1NQIX-ray2.00B/D130-402[»]
    1NWGX-ray2.32B/D130-402[»]
    1O0RX-ray2.30A/B130-402[»]
    1O23X-ray2.32B/D130-402[»]
    1OQMX-ray2.10B/D130-402[»]
    1PZTX-ray1.92A130-402[»]
    1PZYX-ray2.30B/D130-402[»]
    1TVYX-ray2.30A/B130-402[»]
    1TW1X-ray2.30A/B130-402[»]
    1TW5X-ray2.30A/B130-402[»]
    1YROX-ray1.90B/D130-402[»]
    2FYCX-ray2.00B/D130-402[»]
    2FYDX-ray2.00B/D130-400[»]
    4KRVX-ray2.40A/B130-402[»]
    ProteinModelPortaliP08037.
    SMRiP08037. Positions 131-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08037.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2424CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini45 – 402358LumenalSequence 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
    Regioni187 – 1915UDP-alpha-D-galactose binding
    Regioni226 – 2283UDP-alpha-D-galactose binding
    Regioni253 – 2542UDP-alpha-D-galactose binding
    Regioni316 – 3194N-acetyl-D-glucosamine binding
    Regioni347 – 3493UDP-alpha-D-galactose binding

    Sequence similaritiesi

    Belongs to the glycosyltransferase 7 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG327897.
    GeneTreeiENSGT00740000115031.
    HOGENOMiHOG000231027.
    HOVERGENiHBG058334.
    InParanoidiP08037.
    KOiK07966.
    OMAiVGGRYTP.
    OrthoDBiEOG7060R0.
    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: P08037-1) [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

    MKFREPLLGG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLRRL    50
    PQLVGVHPPL QGSSHGAAAI GQPSGELRLR GVAPPPPLQN SSKPRSRAPS 100
    NLDAYSHPGP GPGPGSNLTS APVPSTTTRS LTACPEESPL LVGPMLIEFN 150
    IPVDLKLVEQ QNPKVKLGGR YTPMDCISPH KVAIIIPFRN RQEHLKYWLY 200
    YLHPILQRQQ LDYGIYVINQ AGESMFNRAK LLNVGFKEAL KDYDYNCFVF 250
    SDVDLIPMND HNTYRCFSQP RHISVAMDKF GFSLPYVQYF GGVSALSKQQ 300
    FLSINGFPNN YWGWGGEDDD IYNRLAFRGM SVSRPNAVIG KCRMIRHSRD 350
    KKNEPNPQRF DRIAHTKETM LSDGLNSLTY MVLEVQRYPL YTKITVDIGT 400
    PS 402
    Length:402
    Mass (Da):44,843
    Last modified:October 17, 2006 - v3
    Checksum:iFABF94E74E0C6F81
    GO
    Isoform Short (identifier: P08037-2) [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:389
    Mass (Da):43,484
    Checksum:i6C016BFC25872CCA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 662HG → QA(PubMed:2105947)Curated
    Sequence conflicti158 – 1581V → I in CAA32695. (PubMed:2502398)Curated
    Sequence conflicti187 – 1871P → L in CAA32695. (PubMed:2502398)Curated
    Sequence conflicti205 – 2062IL → MV in CAA32695. (PubMed:2502398)Curated
    Sequence conflicti282 – 2821F → L in AAA30534. (PubMed:2419911)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313Missing in isoform Short. CuratedVSP_018801Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14558 mRNA. Translation: CAA32695.1.
    BC120415 mRNA. Translation: AAI20416.1.
    M13214 mRNA. Translation: AAA30534.1.
    AF515786 mRNA. Translation: AAM54035.2.
    M25398 Genomic DNA. Translation: AAA30533.1.
    J05217 mRNA. Translation: AAA30559.1.
    PIRiI45897.
    S05018.
    RefSeqiNP_803478.1. NM_177512.2.
    UniGeneiBt.5141.

    Genome annotation databases

    EnsembliENSBTAT00000020286; ENSBTAP00000020286; ENSBTAG00000015249. [P08037-2]
    GeneIDi281781.
    KEGGibta:281781.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14558 mRNA. Translation: CAA32695.1 .
    BC120415 mRNA. Translation: AAI20416.1 .
    M13214 mRNA. Translation: AAA30534.1 .
    AF515786 mRNA. Translation: AAM54035.2 .
    M25398 Genomic DNA. Translation: AAA30533.1 .
    J05217 mRNA. Translation: AAA30559.1 .
    PIRi I45897.
    S05018.
    RefSeqi NP_803478.1. NM_177512.2.
    UniGenei Bt.5141.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FGX X-ray 2.40 A/B 115-402 [» ]
    1FR8 X-ray 2.40 A/B 115-402 [» ]
    1NF5 X-ray 2.00 B/D 130-402 [» ]
    1NHE X-ray 2.50 B/D 130-402 [» ]
    1NKH X-ray 2.00 B/D 130-402 [» ]
    1NMM X-ray 2.00 B/D 130-402 [» ]
    1NQI X-ray 2.00 B/D 130-402 [» ]
    1NWG X-ray 2.32 B/D 130-402 [» ]
    1O0R X-ray 2.30 A/B 130-402 [» ]
    1O23 X-ray 2.32 B/D 130-402 [» ]
    1OQM X-ray 2.10 B/D 130-402 [» ]
    1PZT X-ray 1.92 A 130-402 [» ]
    1PZY X-ray 2.30 B/D 130-402 [» ]
    1TVY X-ray 2.30 A/B 130-402 [» ]
    1TW1 X-ray 2.30 A/B 130-402 [» ]
    1TW5 X-ray 2.30 A/B 130-402 [» ]
    1YRO X-ray 1.90 B/D 130-402 [» ]
    2FYC X-ray 2.00 B/D 130-402 [» ]
    2FYD X-ray 2.00 B/D 130-400 [» ]
    4KRV X-ray 2.40 A/B 130-402 [» ]
    ProteinModelPortali P08037.
    SMRi P08037. Positions 131-402.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08037. 1 interaction.

    Chemistry

    BindingDBi P08037.
    ChEMBLi CHEMBL3214.

    Protein family/group databases

    CAZyi GT7. Glycosyltransferase Family 7.

    Proteomic databases

    PaxDbi P08037.
    PRIDEi P08037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000020286 ; ENSBTAP00000020286 ; ENSBTAG00000015249 . [P08037-2 ]
    GeneIDi 281781.
    KEGGi bta:281781.

    Organism-specific databases

    CTDi 2683.

    Phylogenomic databases

    eggNOGi NOG327897.
    GeneTreei ENSGT00740000115031.
    HOGENOMi HOG000231027.
    HOVERGENi HBG058334.
    InParanoidi P08037.
    KOi K07966.
    OMAi VGGRYTP.
    OrthoDBi EOG7060R0.
    TreeFami TF312834.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    Reactomei REACT_205470. Pre-NOTCH Processing in Golgi.
    REACT_210187. Interaction With The Zona Pellucida.
    REACT_211440. Keratan sulfate biosynthesis.
    REACT_225710. N-Glycan antennae elongation.
    SABIO-RK P08037.

    Miscellaneous databases

    EvolutionaryTracei P08037.
    NextBioi 20805694.

    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. "Cloning of cDNA encoding the membrane-bound form of bovine beta 1,4-galactosyltransferase."
      D'Agostaro G., Bendiak B., Tropak M.
      Eur. J. Biochem. 183:211-217(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Fetal skin.
    3. "Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library."
      Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R., Hollis G.F.
      Proc. Natl. Acad. Sci. U.S.A. 83:1573-1577(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 69-402.
    4. "Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1-4)galactosyltransferase."
      Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K.
      Proc. Natl. Acad. Sci. U.S.A. 83:4720-4724(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 74-402.
    5. Qasba P.K., Narimatsu H., Masibay A.S.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 164; 256 AND 265.
    6. "Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7 cells."
      Masibay A.S., Qasba P.K.
      Proc. Natl. Acad. Sci. U.S.A. 86:5733-5737(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-77.
    7. "Bovine beta 1-->4-galactosyltransferase: two sets of mRNA transcripts encode two forms of the protein with different amino-terminal domains. In vitro translation experiments demonstrate that both the short and the long forms of the enzyme are type II membrane-bound glycoproteins."
      Russo R.N., Shaper N.L., Shaper J.H.
      J. Biol. Chem. 265:3324-3331(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-165.
    8. "Identification of a region of UDP-galactose:N-acetylglucosamine beta 4-galactosyltransferase involved in UDP-galactose binding by differential labeling."
      Yadav S.P., Brew K.
      J. Biol. Chem. 265:14163-14169(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-90.
    9. "Structure and function in galactosyltransferase. Sequence locations of alpha-lactalbumin binding site, thiol groups, and disulfide bond."
      Yadav S.P., Brew K.
      J. Biol. Chem. 266:698-703(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISULFIDE BOND.
    10. "Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose."
      Gastinel L.N., Cambillau C., Bourne Y.
      EMBO J. 18:3546-3557(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 115-402 IN COMPLEX WITH SUBSTRATE, DISULFIDE BONDS.
    11. "Crystal structure of lactose synthase reveals a large conformational change in its catalytic component, the beta1,4-galactosyltransferase-I."
      Ramakrishnan B., Qasba P.K.
      J. Mol. Biol. 310:205-218(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS.
    12. "Crystal structure of beta1,4-galactosyltransferase complex with UDP-Gal reveals an oligosaccharide acceptor binding site."
      Ramakrishnan B., Balaji P.V., Qasba P.K.
      J. Mol. Biol. 318:491-502(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 117-402 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS.
    13. "The role of tryptophan 314 in the conformational changes of beta1,4-galactosyltransferase-I."
      Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K.
      J. Mol. Biol. 331:1065-1076(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-402 OF MUTANT THR-342 IN COMPLEX WITH SUBSTRATE AND MANGANESE IONS, MUTAGENESIS OF TRP-314.

    Entry informationi

    Entry nameiB4GT1_BOVIN
    AccessioniPrimary (citable) accession number: P08037
    Secondary accession number(s): Q0VC05, Q8MIG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 160 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3