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Q9NPZ5

- B3GA2_HUMAN

UniProt

Q9NPZ5 - B3GA2_HUMAN

Protein

Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2

Gene

B3GAT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins.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 sitei118 – 1181UDP-glucuronateBy similarity
    Binding sitei155 – 1551UDP-glucuronateBy similarity
    Binding sitei160 – 1601UDP-glucuronateBy similarity
    Metal bindingi187 – 1871ManganeseBy similarity
    Sitei218 – 2181Interaction with galactose moiety of substrate glycoproteinBy similarity
    Active sitei273 – 2731Proton donor/acceptorBy similarity
    Sitei310 – 3101Interaction with galactose moiety of substrate glycoproteinBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi87 – 893UDP-glucuronate bindingBy similarity
    Nucleotide bindingi185 – 1873UDP-glucuronate bindingBy similarity
    Nucleotide bindingi300 – 3023UDP-glucuronate bindingBy similarity

    GO - Molecular functioni

    1. galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW

    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:HS03557-MONOMER.
    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 2 (EC:2.4.1.135)
    Alternative name(s):
    Beta-1,3-glucuronyltransferase 2
    GlcAT-D
    UDP-glucuronosyltransferase S
    Short name:
    GlcAT-S
    Short name:
    Glucuronosyltransferase S
    Gene namesi
    Name:B3GAT2
    Synonyms:GLCATS, KIAA1963
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:922. B3GAT2.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25216.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2PRO_0000195172Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9NPZ5.
    PRIDEiQ9NPZ5.

    Expressioni

    Tissue specificityi

    Expressed in the trachea, retina, spinal cord, hippocampus and other brain regions, and, at lower levels, in testis and ovary.

    Gene expression databases

    BgeeiQ9NPZ5.
    CleanExiHS_B3GAT2.
    GenevestigatoriQ9NPZ5.

    Organism-specific databases

    HPAiHPA012059.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    STRINGi9606.ENSP00000230053.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi82 – 887
    Helixi94 – 10512
    Beta strandi111 – 12111
    Helixi124 – 1329
    Beta strandi137 – 1415
    Helixi157 – 17014
    Beta strandi173 – 1753
    Beta strandi180 – 1834
    Helixi193 – 1986
    Beta strandi202 – 2065
    Beta strandi209 – 2124
    Beta strandi215 – 2239
    Beta strandi226 – 2316
    Helixi244 – 2463
    Beta strandi247 – 2504
    Helixi251 – 2566
    Beta strandi266 – 2683
    Helixi269 – 2713
    Helixi272 – 2787
    Helixi283 – 2853
    Helixi290 – 2934
    Beta strandi313 – 3153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D0JX-ray2.00A/B/C/D78-323[»]
    ProteinModelPortaliQ9NPZ5.
    SMRiQ9NPZ5. Positions 78-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NPZ5.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 22CytoplasmicSequence Analysis
    Topological domaini24 – 323300LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei3 – 2321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni234 – 24310Interaction with galactose moiety of substrate glycoproteinBy similarity

    Sequence similaritiesi

    Belongs to the glycosyltransferase 43 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG292627.
    HOGENOMiHOG000261693.
    HOVERGENiHBG050650.
    InParanoidiQ9NPZ5.
    KOiK10157.
    OMAiFILLPWV.
    OrthoDBiEOG7QG44X.
    PhylomeDBiQ9NPZ5.
    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.

    Q9NPZ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKSALFTRFF ILLPWILIVI IMLDVDTRRP VPPLTPRPYF SPYAVGRGGA    50
    RLPLRRGGPA HGTQKRNQSR PQPQPEPQLP TIYAITPTYS RPVQKAELTR 100
    LANTFRQVAQ LHWILVEDAA ARSELVSRFL ARAGLPSTHL HVPTPRRYKR 150
    PGLPRATEQR NAGLAWLRQR HQHQRAQPGV LFFADDDNTY SLELFQEMRT 200
    TRKVSVWPVG LVGGRRYERP LVENGKVVGW YTGWRADRPF AIDMAGFAVS 250
    LQVILSNPKA VFKRRGSQPG MQESDFLKQI TTVEELEPKA NNCTKVLVWH 300
    TRTEKVNLAN EPKYHLDTVK IEV 323
    Length:323
    Mass (Da):36,919
    Last modified:June 1, 2001 - v2
    Checksum:i85058D52D2D28463
    GO

    Sequence cautioni

    The sequence BAB70889.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB85549.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY070019 mRNA. Translation: AAL57718.1.
    AY070110, AY070108, AY070109 Genomic DNA. Translation: AAL58977.1.
    AB075843 mRNA. Translation: BAB85549.1. Different initiation.
    AL121961, AL450320 Genomic DNA. Translation: CAI42145.1.
    AL450320, AL121961 Genomic DNA. Translation: CAI39582.1.
    AK055248 mRNA. Translation: BAB70889.1. Different initiation.
    CCDSiCCDS4974.1.
    RefSeqiNP_542780.1. NM_080742.2.
    UniGeneiHs.713609.

    Genome annotation databases

    EnsembliENST00000230053; ENSP00000230053; ENSG00000112309.
    GeneIDi135152.
    KEGGihsa:135152.
    UCSCiuc003pfv.3. human.

    Polymorphism databases

    DMDMi14285363.

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY070019 mRNA. Translation: AAL57718.1 .
    AY070110 , AY070108 , AY070109 Genomic DNA. Translation: AAL58977.1 .
    AB075843 mRNA. Translation: BAB85549.1 . Different initiation.
    AL121961 , AL450320 Genomic DNA. Translation: CAI42145.1 .
    AL450320 , AL121961 Genomic DNA. Translation: CAI39582.1 .
    AK055248 mRNA. Translation: BAB70889.1 . Different initiation.
    CCDSi CCDS4974.1.
    RefSeqi NP_542780.1. NM_080742.2.
    UniGenei Hs.713609.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D0J X-ray 2.00 A/B/C/D 78-323 [» ]
    ProteinModelPortali Q9NPZ5.
    SMRi Q9NPZ5. Positions 78-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000230053.

    Protein family/group databases

    CAZyi GT43. Glycosyltransferase Family 43.

    Polymorphism databases

    DMDMi 14285363.

    Proteomic databases

    PaxDbi Q9NPZ5.
    PRIDEi Q9NPZ5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230053 ; ENSP00000230053 ; ENSG00000112309 .
    GeneIDi 135152.
    KEGGi hsa:135152.
    UCSCi uc003pfv.3. human.

    Organism-specific databases

    CTDi 135152.
    GeneCardsi GC06M071566.
    HGNCi HGNC:922. B3GAT2.
    HPAi HPA012059.
    MIMi 607497. gene.
    neXtProti NX_Q9NPZ5.
    PharmGKBi PA25216.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292627.
    HOGENOMi HOG000261693.
    HOVERGENi HBG050650.
    InParanoidi Q9NPZ5.
    KOi K10157.
    OMAi FILLPWV.
    OrthoDBi EOG7QG44X.
    PhylomeDBi Q9NPZ5.
    TreeFami TF313522.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci MetaCyc:HS03557-MONOMER.
    Reactomei REACT_121408. A tetrasaccharide linker sequence is required for GAG synthesis.

    Miscellaneous databases

    EvolutionaryTracei Q9NPZ5.
    GeneWikii B3GAT2.
    GenomeRNAii 135152.
    NextBioi 83461.
    PROi Q9NPZ5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NPZ5.
    CleanExi HS_B3GAT2.
    Genevestigatori Q9NPZ5.

    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, characterization, and chromosome mapping of the human GlcAT-S gene."
      Marcos I., Galan J.J., Borrego S., Antinolo G.
      J. Hum. Genet. 47:677-680(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
      Nagase T., Kikuno R., Ohara O.
      DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] OF 157-323.
      Tissue: Fetal brain.
    5. "Crystal structure of GlcAT-S, a human glucuronyltransferase, involved in the biosynthesis of the HNK-1 carbohydrate epitope."
      Shiba T., Kakuda S., Ishiguro M., Morita I., Oka S., Kawasaki T., Wakatsuki S., Kato R.
      Proteins 65:499-508(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 78-323.

    Entry informationi

    Entry nameiB3GA2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPZ5
    Secondary accession number(s): Q5JS09, Q8TF38, Q96NK4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 130 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 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3