Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P16442

- BGAT_HUMAN

UniProt

P16442 - BGAT_HUMAN

Protein

Histo-blood group ABO system transferase

Gene

ABO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (01 Dec 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.

    Catalytic activityi

    UDP-N-acetyl-alpha-beta-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1->2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1->3)-(alpha-L-fucosyl-(1->2))-beta-D-galactose.
    UDP-alpha-D-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R.

    Cofactori

    Binds 1 manganese ion per subunit.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei126 – 1261UDP-N-acetyl-galactosamine
    Metal bindingi211 – 2111Manganese
    Metal bindingi213 – 2131Manganese
    Binding sitei233 – 2331Glycoprotein fucosyl-galactosyl group
    Binding sitei245 – 2451Glycoprotein fucosyl-galactosyl group
    Binding sitei303 – 3031Glycoprotein fucosyl-galactosyl group
    Binding sitei326 – 3261Glycoprotein fucosyl-galactosyl group

    GO - Molecular functioni

    1. fucosylgalactoside 3-alpha-galactosyltransferase activity Source: UniProtKB-EC
    2. glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. protein glycosylation Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Blood group antigen, Glycosyltransferase, Transferase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT6. Glycosyltransferase Family 6.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histo-blood group ABO system transferase
    Alternative name(s):
    Fucosylglycoprotein 3-alpha-galactosyltransferase
    Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
    Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase (EC:2.4.1.40)
    Glycoprotein-fucosylgalactoside alpha-galactosyltransferase (EC:2.4.1.37)
    Histo-blood group A transferase
    Short name:
    A transferase
    Histo-blood group B transferase
    Short name:
    B transferase
    NAGAT
    Cleaved into the following chain:
    Gene namesi
    Name:ABO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:79. ABO.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted
    Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi214 – 2141M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. 1 Publication
    Mutagenesisi234 – 2341P → S: Alters substrate specificity of group B transferase.
    Mutagenesisi303 – 3031E → A: Decreases specific activity of group B transferase almost to zero. 1 Publication

    Organism-specific databases

    MIMi110300. gene+phenotype.
    PharmGKBiPA24415.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 354354Histo-blood group ABO system transferasePRO_0000012268Add
    BLAST
    Chaini54 – 354301Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble formPRO_0000012269Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP16442.
    PRIDEiP16442.

    PTM databases

    PhosphoSiteiP16442.

    Expressioni

    Gene expression databases

    GenevestigatoriP16442.

    Interactioni

    Protein-protein interaction databases

    BioGridi106546. 1 interaction.

    Structurei

    Secondary structure

    1
    354
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi82 – 843
    Beta strandi93 – 953
    Helixi102 – 11110
    Beta strandi115 – 1228
    Helixi124 – 1296
    Helixi130 – 14011
    Beta strandi145 – 15410
    Helixi156 – 1583
    Beta strandi168 – 1747
    Helixi181 – 19818
    Helixi200 – 2034
    Beta strandi205 – 2106
    Beta strandi212 – 2165
    Helixi222 – 2243
    Beta strandi226 – 2327
    Turni234 – 2385
    Helixi241 – 2433
    Beta strandi269 – 2735
    Helixi274 – 29320
    Turni299 – 3013
    Helixi302 – 31211
    Beta strandi316 – 3194
    Helixi321 – 3233
    Helixi327 – 3304
    Beta strandi341 – 3433
    Helixi348 – 3514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LZ0X-ray1.80A64-354[»]
    1LZ7X-ray1.65A64-354[»]
    1LZIX-ray1.35A64-354[»]
    1LZJX-ray1.32A64-354[»]
    1R7TX-ray2.09A64-345[»]
    1R7UX-ray1.61A64-345[»]
    1R7VX-ray2.09A64-345[»]
    1R7XX-ray1.97A64-345[»]
    1R7YX-ray1.75A64-345[»]
    1R80X-ray1.65A64-345[»]
    1R81X-ray1.75A64-345[»]
    1R82X-ray1.55A64-345[»]
    1WSZX-ray1.59A64-354[»]
    1WT0X-ray1.80A64-354[»]
    1WT1X-ray1.55A64-354[»]
    1WT2X-ray1.90A64-354[»]
    1WT3X-ray1.80A64-354[»]
    1XZ6X-ray1.55A64-354[»]
    1ZHJX-ray1.59A64-354[»]
    1ZI1X-ray1.57A64-354[»]
    1ZI3X-ray1.69A64-354[»]
    1ZI4X-ray1.85A64-354[»]
    1ZI5X-ray1.55A64-354[»]
    1ZIZX-ray1.49A64-354[»]
    1ZJ0X-ray1.67A64-354[»]
    1ZJ1X-ray1.65A64-354[»]
    1ZJ2X-ray1.69A64-354[»]
    1ZJ3X-ray1.69A64-354[»]
    1ZJOX-ray1.64A64-354[»]
    1ZJPX-ray1.59A64-354[»]
    2A8UX-ray1.69A64-354[»]
    2A8WX-ray1.59A64-354[»]
    2I7BX-ray1.99A64-354[»]
    2O1FX-ray1.99A64-354[»]
    2O1GX-ray1.71A64-354[»]
    2O1HX-ray1.67A64-354[»]
    2PGVX-ray1.79A64-354[»]
    2PGYX-ray2.39A64-354[»]
    2RITX-ray1.43A64-354[»]
    2RIXX-ray1.75A64-354[»]
    2RIYX-ray1.55A64-354[»]
    2RIZX-ray1.45A64-354[»]
    2RJ0X-ray1.52A64-354[»]
    2RJ1X-ray1.55A64-354[»]
    2RJ4X-ray1.47A64-354[»]
    2RJ5X-ray1.45A64-354[»]
    2RJ6X-ray1.41A64-354[»]
    2RJ7X-ray1.70A64-354[»]
    2RJ8X-ray1.69A64-354[»]
    2RJ9X-ray1.69A64-354[»]
    2Y7AX-ray2.06A/B/C/D64-354[»]
    3I0CX-ray1.55A69-354[»]
    3I0DX-ray1.90A69-354[»]
    3I0EX-ray1.81A69-354[»]
    3I0FX-ray1.56A69-354[»]
    3I0GX-ray1.40A69-354[»]
    3I0HX-ray2.00A69-354[»]
    3I0IX-ray1.90X69-354[»]
    3I0JX-ray1.48A69-354[»]
    3I0KX-ray2.20A69-354[»]
    3I0LX-ray1.60A69-354[»]
    3IOHX-ray1.25A64-354[»]
    3IOIX-ray1.45A64-354[»]
    3IOJX-ray1.65A/B64-354[»]
    3SX3X-ray1.45A64-354[»]
    3SX5X-ray1.43A64-354[»]
    3SX7X-ray1.42A64-354[»]
    3SX8X-ray1.47A64-354[»]
    3SXAX-ray1.50A64-354[»]
    3SXBX-ray1.49A64-354[»]
    3SXCX-ray1.90A64-354[»]
    3SXDX-ray1.55A64-354[»]
    3SXEX-ray1.49A64-354[»]
    3SXGX-ray1.86A64-354[»]
    3U0XX-ray1.85A/B64-354[»]
    3U0YX-ray1.60A/B64-354[»]
    3V0LX-ray1.75A64-354[»]
    3V0MX-ray1.68A/B64-354[»]
    3V0NX-ray1.75A/B64-354[»]
    3V0OX-ray1.65A/B64-354[»]
    3V0PX-ray1.90A/B64-354[»]
    3V0QX-ray1.80A/B64-354[»]
    3ZGFX-ray1.70A/B64-354[»]
    3ZGGX-ray1.90A64-354[»]
    4C2SX-ray2.48A/B64-354[»]
    4FQWX-ray2.02A64-354[»]
    4FRAX-ray1.43A64-354[»]
    4FRBX-ray1.54A64-354[»]
    4FRDX-ray1.55A64-354[»]
    4FREX-ray1.85A64-354[»]
    4FRHX-ray1.80A64-354[»]
    4FRLX-ray1.90A64-354[»]
    4FRMX-ray1.90A64-354[»]
    4FROX-ray1.75A64-354[»]
    4FRPX-ray2.00A64-354[»]
    4FRQX-ray2.35A64-354[»]
    4GBPX-ray2.15A64-354[»]
    4KC1X-ray1.50A64-346[»]
    4KC2X-ray1.70A64-346[»]
    4KC4X-ray1.60A64-346[»]
    4KXOX-ray2.00A64-354[»]
    DisProtiDP00339.
    ProteinModelPortaliP16442.
    SMRiP16442. Positions 64-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16442.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3232CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini54 – 354301LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei33 – 5321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni121 – 1233UDP-N-acetyl-galactosamine binding
    Regioni211 – 2133UDP-N-acetyl-galactosamine binding

    Domaini

    The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis.

    Sequence similaritiesi

    Belongs to the glycosyltransferase 6 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG43612.
    HOVERGENiHBG003563.
    InParanoidiP16442.
    KOiK00709.
    OrthoDBiEOG7BZVSQ.
    PhylomeDBiP16442.

    Family and domain databases

    Gene3Di3.90.550.10. 1 hit.
    InterProiIPR005076. Glyco_trans_6.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR10462. PTHR10462. 1 hit.
    PfamiPF03414. Glyco_transf_6. 1 hit.
    [Graphical view]
    SUPFAMiSSF53448. SSF53448. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16442-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG    50
    FCMAVREPDH LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF 100
    NIDILNEQFR LQNTTIGLTV FAIKKYVAFL KLFLETAEKH FMVGHRVHYY 150
    VFTDQPAAVP RVTLGTGRQL SVLEVRAYKR WQDVSMRRME MISDFCERRF 200
    LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPGFYGSS REAFTYERRP 250
    QSQAYIPKDE GDFYYLGGFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW 300
    HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA 350
    VRNP 354
    Length:354
    Mass (Da):40,934
    Last modified:December 1, 1992 - v2
    Checksum:iA03DA16E630C1608
    GO

    Polymorphismi

    The sequence shown is that of the A transferase. The B form differs by a few residues substitutions. The O phenotype results from a single base frameshift in the N-terminal extremity of the gene, resulting in a severly truncated protein without catalytic activity.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti35 – 351G → R.1 Publication
    Corresponds to variant rs8176696 [ dbSNP | Ensembl ].
    VAR_019147
    Natural varianti36 – 361V → F.1 Publication
    Corresponds to variant rs688976 [ dbSNP | Ensembl ].
    VAR_019148
    Natural varianti63 – 631R → H.1 Publication
    Corresponds to variant rs549446 [ dbSNP | Ensembl ].
    VAR_019149
    Natural varianti74 – 741P → S.2 Publications
    Corresponds to variant rs512770 [ dbSNP | Ensembl ].
    VAR_019150
    Natural varianti80 – 812CR → W.
    VAR_003408
    Natural varianti156 – 1561P → L in allele A2. 5 Publications
    Corresponds to variant rs1053878 [ dbSNP | Ensembl ].
    VAR_003409
    Natural varianti161 – 1611R → H.1 Publication
    Corresponds to variant rs8176738 [ dbSNP | Ensembl ].
    VAR_019151
    Natural varianti163 – 1631T → M in allele Aw08. 1 Publication
    Corresponds to variant rs55756402 [ dbSNP | Ensembl ].
    VAR_036738
    Natural varianti176 – 1761R → G in group B transferase. 7 Publications
    Corresponds to variant rs7853989 [ dbSNP | Ensembl ].
    VAR_003410
    Natural varianti198 – 1981R → W in allele Aw07.
    Corresponds to variant rs56223957 [ dbSNP | Ensembl ].
    VAR_036739
    Natural varianti199 – 1991R → C.1 Publication
    Corresponds to variant rs8176739 [ dbSNP | Ensembl ].
    VAR_019152
    Natural varianti214 – 2141M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. 1 Publication
    Corresponds to variant rs55827808 [ dbSNP | Ensembl ].
    VAR_036740
    Natural varianti216 – 2161F → I.2 Publications
    Corresponds to variant rs8176740 [ dbSNP | Ensembl ].
    VAR_019153
    Natural varianti223 – 2231E → D in allele B106. 1 Publication
    VAR_036741
    Natural varianti230 – 2301G → R in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation. 1 Publication
    VAR_055227
    Natural varianti235 – 2351G → S in group B transferase. 8 Publications
    Corresponds to variant rs8176743 [ dbSNP | Ensembl ].
    VAR_003411
    Natural varianti257 – 2571P → L.
    Corresponds to variant rs8176745 [ dbSNP | Ensembl ].
    VAR_033540
    Natural varianti266 – 2661L → M in group B transferase; important for the specificity. 8 Publications
    Corresponds to variant rs8176746 [ dbSNP | Ensembl ].
    VAR_003412
    Natural varianti268 – 2681G → A in group B transferase; important for the specificity. 7 Publications
    Corresponds to variant rs8176747 [ dbSNP | Ensembl ].
    VAR_003413
    Natural varianti268 – 2681G → R.1 Publication
    Corresponds to variant rs8176747 [ dbSNP | Ensembl ].
    VAR_033541
    Natural varianti277 – 2771V → M.2 Publications
    Corresponds to variant rs8176748 [ dbSNP | Ensembl ].
    VAR_019154
    Natural varianti288 – 2881M → R.1 Publication
    VAR_036742
    Natural varianti291 – 2911D → N in allele B104. 1 Publication
    VAR_036743
    Natural varianti346 – 3461K → M in allele Bw08. 2 Publications
    VAR_036744
    Natural varianti352 – 3521R → G in allele A107. 1 Publication
    VAR_036745
    Natural varianti352 – 3521R → W in allele A106 and allele B3. 1 Publication
    VAR_003414

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05175 mRNA. Translation: AAA36792.1.
    X84746
    , X84747, X84748, X84749, X84750, X84751, X84752 Genomic DNA. Translation: CAA59233.1.
    AF134412 mRNA. Translation: AAD26572.1.
    AF134413 mRNA. Translation: AAD26573.1.
    AF134414 mRNA. Translation: AAD26574.1.
    AH007586 Genomic DNA. Translation: AAD26575.1.
    AH007587 Genomic DNA. Translation: AAD26576.1.
    AH007592 Genomic DNA. Translation: AAD26581.1.
    AJ920329 Genomic DNA. Translation: CAI79116.1.
    AM423110 Genomic DNA. Translation: CAM28424.1.
    AM492698 Genomic DNA. Translation: CAM34526.1.
    AM492699 Genomic DNA. Translation: CAM34527.1.
    AY268591 Genomic DNA. Translation: AAP03430.1.
    BC069595 mRNA. Translation: AAH69595.1.
    BC111575 mRNA. Translation: AAI11576.1.
    AJ536135 Genomic DNA. Translation: CAD60222.1.
    AJ536136 Genomic DNA. Translation: CAD60223.1.
    D82842 Genomic DNA. Translation: BAA11591.2.
    D82843 Genomic DNA. Translation: BAA11592.2.
    AF016622 Genomic DNA. Translation: AAB86462.1.
    AF448199 Genomic DNA. Translation: AAQ04662.1.
    AF448200 Genomic DNA. Translation: AAQ04663.1.
    AJ276689 Genomic DNA. Translation: CAB81779.1.
    PIRiPC1165.
    RefSeqiNP_065202.2. NM_020469.2.
    UniGeneiHs.654423.

    Genome annotation databases

    GeneIDi28.
    KEGGihsa:28.
    UCSCiuc004cda.1. human.

    Polymorphism databases

    DMDMi114949.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    GGDB

    GlycoGene database

    SeattleSNPs
    Functional Glycomics Gateway - GTase

    Histo-blood group ABO system transferase

    Functional Glycomics Gateway - GTase

    Histo-blood group ABO system transferase

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05175 mRNA. Translation: AAA36792.1 .
    X84746
    , X84747 , X84748 , X84749 , X84750 , X84751 , X84752 Genomic DNA. Translation: CAA59233.1 .
    AF134412 mRNA. Translation: AAD26572.1 .
    AF134413 mRNA. Translation: AAD26573.1 .
    AF134414 mRNA. Translation: AAD26574.1 .
    AH007586 Genomic DNA. Translation: AAD26575.1 .
    AH007587 Genomic DNA. Translation: AAD26576.1 .
    AH007592 Genomic DNA. Translation: AAD26581.1 .
    AJ920329 Genomic DNA. Translation: CAI79116.1 .
    AM423110 Genomic DNA. Translation: CAM28424.1 .
    AM492698 Genomic DNA. Translation: CAM34526.1 .
    AM492699 Genomic DNA. Translation: CAM34527.1 .
    AY268591 Genomic DNA. Translation: AAP03430.1 .
    BC069595 mRNA. Translation: AAH69595.1 .
    BC111575 mRNA. Translation: AAI11576.1 .
    AJ536135 Genomic DNA. Translation: CAD60222.1 .
    AJ536136 Genomic DNA. Translation: CAD60223.1 .
    D82842 Genomic DNA. Translation: BAA11591.2 .
    D82843 Genomic DNA. Translation: BAA11592.2 .
    AF016622 Genomic DNA. Translation: AAB86462.1 .
    AF448199 Genomic DNA. Translation: AAQ04662.1 .
    AF448200 Genomic DNA. Translation: AAQ04663.1 .
    AJ276689 Genomic DNA. Translation: CAB81779.1 .
    PIRi PC1165.
    RefSeqi NP_065202.2. NM_020469.2.
    UniGenei Hs.654423.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LZ0 X-ray 1.80 A 64-354 [» ]
    1LZ7 X-ray 1.65 A 64-354 [» ]
    1LZI X-ray 1.35 A 64-354 [» ]
    1LZJ X-ray 1.32 A 64-354 [» ]
    1R7T X-ray 2.09 A 64-345 [» ]
    1R7U X-ray 1.61 A 64-345 [» ]
    1R7V X-ray 2.09 A 64-345 [» ]
    1R7X X-ray 1.97 A 64-345 [» ]
    1R7Y X-ray 1.75 A 64-345 [» ]
    1R80 X-ray 1.65 A 64-345 [» ]
    1R81 X-ray 1.75 A 64-345 [» ]
    1R82 X-ray 1.55 A 64-345 [» ]
    1WSZ X-ray 1.59 A 64-354 [» ]
    1WT0 X-ray 1.80 A 64-354 [» ]
    1WT1 X-ray 1.55 A 64-354 [» ]
    1WT2 X-ray 1.90 A 64-354 [» ]
    1WT3 X-ray 1.80 A 64-354 [» ]
    1XZ6 X-ray 1.55 A 64-354 [» ]
    1ZHJ X-ray 1.59 A 64-354 [» ]
    1ZI1 X-ray 1.57 A 64-354 [» ]
    1ZI3 X-ray 1.69 A 64-354 [» ]
    1ZI4 X-ray 1.85 A 64-354 [» ]
    1ZI5 X-ray 1.55 A 64-354 [» ]
    1ZIZ X-ray 1.49 A 64-354 [» ]
    1ZJ0 X-ray 1.67 A 64-354 [» ]
    1ZJ1 X-ray 1.65 A 64-354 [» ]
    1ZJ2 X-ray 1.69 A 64-354 [» ]
    1ZJ3 X-ray 1.69 A 64-354 [» ]
    1ZJO X-ray 1.64 A 64-354 [» ]
    1ZJP X-ray 1.59 A 64-354 [» ]
    2A8U X-ray 1.69 A 64-354 [» ]
    2A8W X-ray 1.59 A 64-354 [» ]
    2I7B X-ray 1.99 A 64-354 [» ]
    2O1F X-ray 1.99 A 64-354 [» ]
    2O1G X-ray 1.71 A 64-354 [» ]
    2O1H X-ray 1.67 A 64-354 [» ]
    2PGV X-ray 1.79 A 64-354 [» ]
    2PGY X-ray 2.39 A 64-354 [» ]
    2RIT X-ray 1.43 A 64-354 [» ]
    2RIX X-ray 1.75 A 64-354 [» ]
    2RIY X-ray 1.55 A 64-354 [» ]
    2RIZ X-ray 1.45 A 64-354 [» ]
    2RJ0 X-ray 1.52 A 64-354 [» ]
    2RJ1 X-ray 1.55 A 64-354 [» ]
    2RJ4 X-ray 1.47 A 64-354 [» ]
    2RJ5 X-ray 1.45 A 64-354 [» ]
    2RJ6 X-ray 1.41 A 64-354 [» ]
    2RJ7 X-ray 1.70 A 64-354 [» ]
    2RJ8 X-ray 1.69 A 64-354 [» ]
    2RJ9 X-ray 1.69 A 64-354 [» ]
    2Y7A X-ray 2.06 A/B/C/D 64-354 [» ]
    3I0C X-ray 1.55 A 69-354 [» ]
    3I0D X-ray 1.90 A 69-354 [» ]
    3I0E X-ray 1.81 A 69-354 [» ]
    3I0F X-ray 1.56 A 69-354 [» ]
    3I0G X-ray 1.40 A 69-354 [» ]
    3I0H X-ray 2.00 A 69-354 [» ]
    3I0I X-ray 1.90 X 69-354 [» ]
    3I0J X-ray 1.48 A 69-354 [» ]
    3I0K X-ray 2.20 A 69-354 [» ]
    3I0L X-ray 1.60 A 69-354 [» ]
    3IOH X-ray 1.25 A 64-354 [» ]
    3IOI X-ray 1.45 A 64-354 [» ]
    3IOJ X-ray 1.65 A/B 64-354 [» ]
    3SX3 X-ray 1.45 A 64-354 [» ]
    3SX5 X-ray 1.43 A 64-354 [» ]
    3SX7 X-ray 1.42 A 64-354 [» ]
    3SX8 X-ray 1.47 A 64-354 [» ]
    3SXA X-ray 1.50 A 64-354 [» ]
    3SXB X-ray 1.49 A 64-354 [» ]
    3SXC X-ray 1.90 A 64-354 [» ]
    3SXD X-ray 1.55 A 64-354 [» ]
    3SXE X-ray 1.49 A 64-354 [» ]
    3SXG X-ray 1.86 A 64-354 [» ]
    3U0X X-ray 1.85 A/B 64-354 [» ]
    3U0Y X-ray 1.60 A/B 64-354 [» ]
    3V0L X-ray 1.75 A 64-354 [» ]
    3V0M X-ray 1.68 A/B 64-354 [» ]
    3V0N X-ray 1.75 A/B 64-354 [» ]
    3V0O X-ray 1.65 A/B 64-354 [» ]
    3V0P X-ray 1.90 A/B 64-354 [» ]
    3V0Q X-ray 1.80 A/B 64-354 [» ]
    3ZGF X-ray 1.70 A/B 64-354 [» ]
    3ZGG X-ray 1.90 A 64-354 [» ]
    4C2S X-ray 2.48 A/B 64-354 [» ]
    4FQW X-ray 2.02 A 64-354 [» ]
    4FRA X-ray 1.43 A 64-354 [» ]
    4FRB X-ray 1.54 A 64-354 [» ]
    4FRD X-ray 1.55 A 64-354 [» ]
    4FRE X-ray 1.85 A 64-354 [» ]
    4FRH X-ray 1.80 A 64-354 [» ]
    4FRL X-ray 1.90 A 64-354 [» ]
    4FRM X-ray 1.90 A 64-354 [» ]
    4FRO X-ray 1.75 A 64-354 [» ]
    4FRP X-ray 2.00 A 64-354 [» ]
    4FRQ X-ray 2.35 A 64-354 [» ]
    4GBP X-ray 2.15 A 64-354 [» ]
    4KC1 X-ray 1.50 A 64-346 [» ]
    4KC2 X-ray 1.70 A 64-346 [» ]
    4KC4 X-ray 1.60 A 64-346 [» ]
    4KXO X-ray 2.00 A 64-354 [» ]
    DisProti DP00339.
    ProteinModelPortali P16442.
    SMRi P16442. Positions 64-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106546. 1 interaction.

    Chemistry

    ChEMBLi CHEMBL2321639.

    Protein family/group databases

    CAZyi GT6. Glycosyltransferase Family 6.

    PTM databases

    PhosphoSitei P16442.

    Polymorphism databases

    DMDMi 114949.

    Proteomic databases

    PaxDbi P16442.
    PRIDEi P16442.

    Protocols and materials databases

    DNASUi 28.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 28.
    KEGGi hsa:28.
    UCSCi uc004cda.1. human.

    Organism-specific databases

    CTDi 28.
    GeneCardsi GC09M136130.
    HGNCi HGNC:79. ABO.
    MIMi 110300. gene+phenotype.
    neXtProti NX_P16442.
    PharmGKBi PA24415.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG43612.
    HOVERGENi HBG003563.
    InParanoidi P16442.
    KOi K00709.
    OrthoDBi EOG7BZVSQ.
    PhylomeDBi P16442.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    EvolutionaryTracei P16442.
    GeneWikii ABO_(gene).
    GenomeRNAii 28.
    NextBioi 97.
    PROi P16442.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P16442.

    Family and domain databases

    Gene3Di 3.90.550.10. 1 hit.
    InterProi IPR005076. Glyco_trans_6.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    PANTHERi PTHR10462. PTHR10462. 1 hit.
    Pfami PF03414. Glyco_transf_6. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53448. SSF53448. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc alpha 1-->2Gal alpha 1-->3GalNAc transferase (histo-blood group A transferase) mRNA."
      Yamamoto F., Marken J., Tsuji T., White T., Clausen H., Hakomori S.
      J. Biol. Chem. 265:1146-1151(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Molecular genetic basis of the histo-blood group ABO system."
      Yamamoto F., Clausen H., White T., Marken J., Hakomori S.
      Nature 345:229-233(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-156.
    4. "Human histo-blood group ABO gene locus alleles."
      Yamamoto F.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS LEU-156; GLY-176; SER-235 AND MET-266.
    5. "A weak blood group A phenotype caused by a translation-initiator mutation in the ABO gene."
      Seltsam A., Das Gupta C., Bade-Doeding C., Blasczyk R.
      Transfusion 46:434-440(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Peripheral blood.
    6. "Weak blood group B phenotypes may be caused by variations in the CCAAT-binding factor/NF-Y enhancer region of the ABO gene."
      Seltsam A., Wagner F.F., Gruger D., Gupta C.D., Bade-Doeding C., Blasczyk R.
      Transfusion 47:2330-2335(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Peripheral blood.
    7. "Aberrant intracellular trafficking of a variant B glycosyltransferase."
      Seltsam A., Gruger D., Just B., Figueiredo C., Gupta C.D., Deluca D.S., Blasczyk R.
      Transfusion 48:1898-1905(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-230; SER-235; MET-266 AND ALA-268.
      Tissue: Peripheral blood.
    8. SeattleSNPs variation discovery resource
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-35; PHE-36; HIS-63; SER-74; LEU-156; HIS-161; GLY-176; CYS-199; ILE-216; SER-235; MET-266; ALA-268 AND MET-277.
    9. "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], VARIANTS GLY-176; SER-235; MET-266 AND ALA-268.
    10. "The nature of diversity and diversification at the ABO locus."
      Seltsam A., Hallensleben M., Kollmann A., Blasczyk R.
      Blood 102:3035-3042(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, VARIANTS SER-74; LEU-156; MET-163; GLY-176; SER-235; MET-266; ALA-268; ARG-268; ARG-288 AND MET-346.
    11. "Molecular genetic analysis of variant phenotypes of the ABO blood group system."
      Ogasawara K., Yabe R., Uchikawa M., Saitou N., Bannai M., Nakata K., Takenaka M., Fujisawa K., Ishikawa Y., Juji T., Tokunaga K.
      Blood 88:2732-2737(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354, VARIANTS LEU-156; GLY-176; ARG-214; ILE-216; ASP-223; SER-235; MET-266; ALA-268; MET-277; ASN-291; GLY-352 AND TRP-352.
    12. "Heterogeneity of the blood group Ax allele: genetic recombination of common alleles can result in the Ax phenotype."
      Olsson M.L., Chester M.A.
      Transfus. Med. 8:231-238(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354.
    13. "Evolution of the O alleles of the human ABO blood group gene."
      Roubinet F., Despiau S., Calafell F., Jin F., Bertanpetit J., Saitou N., Blancher A.
      Transfusion 44:707-715(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, VARIANTS GLY-176; SER-235; MET-266 AND ALA-268.
    14. "A novel B Transferase."
      Seltsam A., Hallensleben M., Salama A., Blasczyk R.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-354, VARIANTS GLY-176; SER-235 AND MET-346.
    15. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-334, VARIANTS MET-266 AND ALA-268.
    16. "Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions."
      Yamamoto F., Hakomori S.
      J. Biol. Chem. 265:19257-19262(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    17. "The structural basis for specificity in human ABO(H) blood group biosynthesis."
      Patenaude S.I., Seto N.O.L., Borisova S.N., Szpacenko A., Marcus S.L., Palcic M.M., Evans S.V.
      Nat. Struct. Biol. 9:685-690(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 64-354, METAL-BINDING, MUTAGENESIS OF GLU-303.
    18. "A single point mutation reverses the donor specificity of human blood group B-synthesizing galactosyltransferase."
      Marcus S.L., Polakowski R., Seto N.O.L., Leinala E., Borisova S., Blancher A., Roubinet F., Evans S.V., Palcic M.M.
      J. Biol. Chem. 278:12403-12405(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 OF MUTANT SER-234 IN COMPLEX WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOG.
    19. "The influence of an intramolecular hydrogen bond in differential recognition of inhibitory acceptor analogs by human ABO(H) blood group A and B glycosyltransferases."
      Nguyen H.P., Seto N.O.L., Cai Y., Leinala E.K., Borisova S.N., Palcic M.M., Evans S.V.
      J. Biol. Chem. 278:49191-49195(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 IN COMPLEXES WITH UDP; UDP-N-ACETYL-GALACTOSAMINE; UDP-GALACTOSE AND GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOGS.
    20. "Structural basis for the inactivity of human blood group O2 glycosyltransferase."
      Lee H.J., Barry C.H., Borisova S.N., Seto N.O.L., Zheng R.B., Blancher A., Evans S.V., Palcic M.M.
      J. Biol. Chem. 280:525-529(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 64-354 OF MUTANTS SER-74 AND ARG-268 IN COMPLEXES WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOG AND UDP-N-ACETYL-GALACTOSAMINE.
    21. "Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases."
      Letts J.A., Rose N.L., Fang Y.R., Barry C.H., Borisova S.N., Seto N.O.L., Palcic M.M., Evans S.V.
      J. Biol. Chem. 281:3625-3632(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 64-354 OF HISTO-BLOOD GROUP GROUP A TRANSFERASE AND HISTO-BLOOD GROUP GROUP B TRANSFERASE IN COMPLEXES WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOGS.
    22. "Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif."
      Persson M., Letts J.A., Hosseini-Maaf B., Borisova S.N., Palcic M.M., Evans S.V., Olsson M.L.
      J. Biol. Chem. 282:9564-9570(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND THR-214, COFACTOR, CHARACTERIZATION OF VARIANT ARG-214, MUTAGENESIS OF MET-214.

    Entry informationi

    Entry nameiBGAT_HUMAN
    AccessioniPrimary (citable) accession number: P16442
    Secondary accession number(s): B0JDB9
    , O14758, Q14490, Q53I57, Q6ISD4, Q6KFZ2, Q70V27, Q99484, Q99485, Q9NY01, Q9UQ68, Q9UQ69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 164 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, Direct protein sequencing, Reference proteome

    Documents

    1. Blood group antigen proteins
      Nomenclature of blood group antigens and list of entries
    2. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3