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Q9P2W7

- B3GA1_HUMAN

UniProt

Q9P2W7 - B3GA1_HUMAN

Protein

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1

Gene

B3GAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group By similarity.By similarity

    Catalytic activityi

    UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein.

    Cofactori

    Manganese.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei122 – 1221UDP-glucuronate
    Binding sitei165 – 1651UDP-glucuronate
    Binding sitei170 – 1701UDP-glucuronateBy similarity
    Metal bindingi197 – 1971ManganeseBy similarity
    Sitei228 – 2281Interaction with galactose moiety of substrate glycoprotein
    Active sitei284 – 2841Proton donor/acceptor
    Sitei321 – 3211Interaction with galactose moiety of substrate glycoproteinBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi91 – 933UDP-glucuronate binding
    Nucleotide bindingi195 – 1973UDP-glucuronate binding
    Nucleotide bindingi311 – 3133UDP-glucuronate binding

    GO - Molecular functioni

    1. galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity Source: Ensembl

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. chondroitin sulfate metabolic process Source: Reactome
    3. glycosaminoglycan metabolic process Source: Reactome
    4. protein glycosylation Source: UniProtKB-UniPathway
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03272-MONOMER.
    BRENDAi2.4.1.135. 2681.
    ReactomeiREACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT43. Glycosyltransferase Family 43.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 (EC:2.4.1.135)
    Alternative name(s):
    Beta-1,3-glucuronyltransferase 1
    Glucuronosyltransferase P
    Short name:
    GlcAT-P
    UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase
    Short name:
    GlcUAT-P
    Gene namesi
    Name:B3GAT1
    Synonyms:GLCATP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:921. B3GAT1.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: Reactome
    2. integral component of membrane Source: ProtInc

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25215.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 334334Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1PRO_0000195167Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei103 – 1031PhosphothreonineBy similarity
    Modified residuei108 – 1081PhosphothreonineBy similarity
    Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9P2W7.
    PRIDEiQ9P2W7.

    PTM databases

    PhosphoSiteiQ9P2W7.

    Expressioni

    Tissue specificityi

    Mainly expressed in the brain.

    Gene expression databases

    ArrayExpressiQ9P2W7.
    BgeeiQ9P2W7.
    CleanExiHS_B3GAT1.
    GenevestigatoriQ9P2W7.

    Organism-specific databases

    HPAiCAB002500.
    CAB010893.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    BioGridi117990. 2 interactions.
    IntActiQ9P2W7. 2 interactions.
    STRINGi9606.ENSP00000307875.

    Structurei

    Secondary structure

    1
    334
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi85 – 928
    Helixi98 – 10912
    Beta strandi112 – 12514
    Helixi128 – 13710
    Beta strandi140 – 1456
    Helixi150 – 1534
    Helixi167 – 18014
    Beta strandi183 – 1853
    Beta strandi189 – 1935
    Beta strandi198 – 2003
    Helixi202 – 2098
    Beta strandi212 – 2165
    Beta strandi219 – 2213
    Beta strandi225 – 2328
    Beta strandi238 – 2425
    Beta strandi244 – 2463
    Helixi255 – 2573
    Beta strandi258 – 2614
    Helixi262 – 2676
    Beta strandi275 – 2784
    Helixi283 – 2919
    Helixi294 – 2963
    Beta strandi297 – 2993
    Helixi301 – 3044
    Helixi320 – 3223
    Turni323 – 3253

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V82X-ray1.85A/B83-334[»]
    1V83X-ray1.90A/B83-334[»]
    1V84X-ray1.82A/B83-334[»]
    ProteinModelPortaliQ9P2W7.
    SMRiQ9P2W7. Positions 83-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P2W7.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini28 – 334307LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni245 – 25410Interaction with galactose moiety of substrate glycoprotein

    Sequence similaritiesi

    Belongs to the glycosyltransferase 43 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG310844.
    HOVERGENiHBG050650.
    InParanoidiQ9P2W7.
    KOiK00735.
    OrthoDBiEOG7QG44X.
    PhylomeDBiQ9P2W7.
    TreeFamiTF313522.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR005027. Glyco_trans_43.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR10896. PTHR10896. 1 hit.
    PfamiPF03360. Glyco_transf_43. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9P2W7-1 [UniParc]FASTAAdd to Basket

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    MPKRRDILAI VLIVLPWTLL ITVWHQSTLA PLLAVHKDEG SDPRRETPPG    50
    ADPREYCTSD RDIVEVVRTE YVYTRPPPWS DTLPTIHVVT PTYSRPVQKA 100
    ELTRMANTLL HVPNLHWLVV EDAPRRTPLT ARLLRDTGLN YTHLHVETPR 150
    NYKLRGDARD PRIPRGTMQR NLALRWLRET FPRNSSQPGV VYFADDDNTY 200
    SLELFEEMRS TRRVSVWPVA FVGGLRYEAP RVNGAGKVVG WKTVFDPHRP 250
    FAIDMAGFAV NLRLILQRSQ AYFKLRGVKG GYQESSLLRE LVTLNDLEPK 300
    AANCTKILVW HTRTEKPVLV NEGKKGFTDP SVEI 334
    Length:334
    Mass (Da):38,256
    Last modified:July 22, 2008 - v2
    Checksum:i0DF42399D19701B3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti240 – 2401G → R in BAA96077. (PubMed:10783264)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti131 – 1311A → T.
    Corresponds to variant rs35434644 [ dbSNP | Ensembl ].
    VAR_044538

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029396 mRNA. Translation: BAA96077.1.
    CR457098 mRNA. Translation: CAG33379.1.
    BC010466 mRNA. Translation: AAH10466.1.
    CCDSiCCDS8500.1.
    RefSeqiNP_061114.2. NM_018644.3.
    NP_473366.1. NM_054025.2.
    UniGeneiHs.381050.

    Genome annotation databases

    EnsembliENST00000312527; ENSP00000307875; ENSG00000109956.
    ENST00000392580; ENSP00000376359; ENSG00000109956.
    ENST00000524765; ENSP00000433847; ENSG00000109956.
    GeneIDi27087.
    KEGGihsa:27087.
    UCSCiuc001qhq.3. human.

    Polymorphism databases

    DMDMi205830910.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029396 mRNA. Translation: BAA96077.1 .
    CR457098 mRNA. Translation: CAG33379.1 .
    BC010466 mRNA. Translation: AAH10466.1 .
    CCDSi CCDS8500.1.
    RefSeqi NP_061114.2. NM_018644.3.
    NP_473366.1. NM_054025.2.
    UniGenei Hs.381050.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V82 X-ray 1.85 A/B 83-334 [» ]
    1V83 X-ray 1.90 A/B 83-334 [» ]
    1V84 X-ray 1.82 A/B 83-334 [» ]
    ProteinModelPortali Q9P2W7.
    SMRi Q9P2W7. Positions 83-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117990. 2 interactions.
    IntActi Q9P2W7. 2 interactions.
    STRINGi 9606.ENSP00000307875.

    Protein family/group databases

    CAZyi GT43. Glycosyltransferase Family 43.

    PTM databases

    PhosphoSitei Q9P2W7.

    Polymorphism databases

    DMDMi 205830910.

    Proteomic databases

    PaxDbi Q9P2W7.
    PRIDEi Q9P2W7.

    Protocols and materials databases

    DNASUi 27087.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312527 ; ENSP00000307875 ; ENSG00000109956 .
    ENST00000392580 ; ENSP00000376359 ; ENSG00000109956 .
    ENST00000524765 ; ENSP00000433847 ; ENSG00000109956 .
    GeneIDi 27087.
    KEGGi hsa:27087.
    UCSCi uc001qhq.3. human.

    Organism-specific databases

    CTDi 27087.
    GeneCardsi GC11M134281.
    H-InvDB HIX0010301.
    HGNCi HGNC:921. B3GAT1.
    HPAi CAB002500.
    CAB010893.
    MIMi 151290. gene.
    neXtProti NX_Q9P2W7.
    PharmGKBi PA25215.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310844.
    HOVERGENi HBG050650.
    InParanoidi Q9P2W7.
    KOi K00735.
    OrthoDBi EOG7QG44X.
    PhylomeDBi Q9P2W7.
    TreeFami TF313522.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci MetaCyc:HS03272-MONOMER.
    BRENDAi 2.4.1.135. 2681.
    Reactomei REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.

    Miscellaneous databases

    EvolutionaryTracei Q9P2W7.
    GeneWikii B3GAT1.
    GenomeRNAii 27087.
    NextBioi 49699.
    PROi Q9P2W7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P2W7.
    Bgeei Q9P2W7.
    CleanExi HS_B3GAT1.
    Genevestigatori Q9P2W7.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR005027. Glyco_trans_43.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    PANTHERi PTHR10896. PTHR10896. 1 hit.
    Pfami PF03360. Glyco_transf_43. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and chromosomal mapping of human glucuronyltransferase involved in biosynthesis of the HNK-1 carbohydrate epitope."
      Mitsumoto Y., Oka S., Sakuma H., Inazawa J., Kawasaki T.
      Genomics 65:166-173(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1."
      Kakuda S., Shiba T., Ishiguro M., Tagawa H., Oka S., Kajihara Y., Kawasaki T., Wakatsuki S., Kato R.
      J. Biol. Chem. 279:22693-22703(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 83-334 IN COMPLEX WITH UDP-GLUCURONIC ACID AND GALACTOSE MOIETY OF SUBSTRATE GLYCOPROTEIN.

    Entry informationi

    Entry nameiB3GA1_HUMAN
    AccessioniPrimary (citable) accession number: Q9P2W7
    Secondary accession number(s): Q96FS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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