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UniProtKB/Swiss-Prot entry P16442


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BGAT_HUMAN
Primary accession number P16442
Secondary accession numbers O14758 Q14490 Q6ISD4 Q6KFZ2 Q70V27 Q99484 Q99485 Q9NY01 Q9UQ68 Q9UQ69
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on December 1, 1992 (Sequence version 2)
Annotations were last modified on    July 1, 2008 (Entry version 101)
Name and origin of the protein
Protein name Histo-blood group ABO system transferase
Synonym NAGAT
Includes Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase
     (EC 2.4.1.40)
     (Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase)
     (Histo-blood group A transferase)
     (A transferase)
Glycoprotein-fucosylgalactoside alpha-galactosyltransferase
     (EC 2.4.1.37)
     (Fucosylglycoprotein 3-alpha-galactosyltransferase)
     (Histo-blood group B transferase)
     (B transferase)
Contains Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
Gene name
Name: ABO
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2104828 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto F., Marken J., Tsuji T., White T., Clausen H., Hakomori S.;
"Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc alpha 1-->2Gal alpha 1-->3GalNAc transferase (histo-blood group A transferase) mRNA.";
J. Biol. Chem. 265:1146-1151(1990).
[2]
NUCLEOTIDE SEQUENCE.
DOI=10.1038/345229a0; PubMed=2333095 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto F., Clausen H., White T., Marken J., Hakomori S.;
"Molecular genetic basis of the histo-blood group ABO system.";
Nature 345:229-233(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-156.
DOI=10.1006/bbrc.1995.1044; PubMed=7598760 [NCBI, ExPASy, EBI, Israel, Japan]
Bennett E.P., Steffensen R., Clausen H., Weghuis D.O., Geurts van Kessel A.;
"Genomic cloning of the human histo-blood group ABO locus.";
Biochem. Biophys. Res. Commun. 206:318-325(1995).
[4]
ERRATUM.
DOI=10.1006/bbrc.1995.1817; PubMed=7779106 [NCBI, ExPASy, EBI, Israel, Japan]
Bennett E.P., Steffensen R., Clausen H., Weghuis D.O., Geurts van Kessel A.;
"Genomic cloning of the human histo-blood group ABO locus.";
Biochem. Biophys. Res. Commun. 211:347-347(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS LEU-156; GLY-176; SER-235 AND MET-266.
Yamamoto F.;
"Human histo-blood group ABO gene locus alleles.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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.
SeattleSNPs program for genomic applications;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-176; SER-235; MET-266 AND ALA-268.
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, AND VARIANTS SER-74; LEU-156; MET-163; GLY-176; SER-235; MET-266; ALA-268; ARG-268; ARG-288 AND MET-346.
DOI=10.1182/blood-2003-03-0955; PubMed=12829588 [NCBI, ExPASy, EBI, Israel, Japan]
Seltsam A., Hallensleben M., Kollmann A., Blasczyk R.;
"The nature of diversity and diversification at the ABO locus.";
Blood 102:3035-3042(2003).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354, AND 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.
PubMed=8839869 [NCBI, ExPASy, EBI, Israel, Japan]
Ogasawara K., Yabe R., Uchikawa M., Saitou N., Bannai M., Nakata K., Takenaka M., Fujisawa K., Ishikawa Y., Juji T., Tokunaga K.;
"Molecular genetic analysis of variant phenotypes of the ABO blood group system.";
Blood 88:2732-2737(1996).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354.
DOI=10.1046/j.1365-3148.1998.00161.x; PubMed=9800297 [NCBI, ExPASy, EBI, Israel, Japan]
Olsson M.L., Chester M.A.;
"Heterogeneity of the blood group Ax allele: genetic recombination of common alleles can result in the Ax phenotype.";
Transfus. Med. 8:231-238(1998).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, AND VARIANTS GLY-176; SER-235; MET-266 AND ALA-268.
DOI=10.1111/j.1537-2995.2004.03346.x; PubMed=15104652 [NCBI, ExPASy, EBI, Israel, Japan]
Roubinet F., Despiau S., Calafell F., Jin F., Bertanpetit J., Saitou N., Blancher A.;
"Evolution of the O alleles of the human ABO blood group gene.";
Transfusion 44:707-715(2004).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-354, AND VARIANTS GLY-176; SER-235 AND MET-346.
Seltsam A., Hallensleben M., Salama A., Blasczyk R.;
"A novel B Transferase.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-334, AND VARIANTS MET-266 AND ALA-268.
DOI=10.1016/0006-291X(92)91538-2; PubMed=1449469 [NCBI, ExPASy, EBI, Israel, Japan]
Kominato Y., McNeill P.D., Yamamoto M., Russell M., Hakomori S., Yamamoto F.;
"Animal histo-blood group ABO genes.";
Biochem. Biophys. Res. Commun. 189:154-164(1992).
[14]
CHARACTERIZATION.
PubMed=2121736 [NCBI, ExPASy, EBI, Israel, Japan]
Yamamoto F., Hakomori S.;
"Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions.";
J. Biol. Chem. 265:19257-19262(1990).
[15]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 64-354, METAL-BINDING, AND MUTAGENESIS OF GLU-303.
DOI=10.1038/nsb832; PubMed=12198488 [NCBI, ExPASy, EBI, Israel, Japan]
Patenaude S.I., Seto N.O.L., Borisova S.N., Szpacenko A., Marcus S.L., Palcic M.M., Evans S.V.;
"The structural basis for specificity in human ABO(H) blood group biosynthesis.";
Nat. Struct. Biol. 9:685-690(2002).
[16]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 OF MUTANT SER-234 IN COMPLEX WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOG.
DOI=10.1074/jbc.M212002200; PubMed=12529355 [NCBI, ExPASy, EBI, Israel, Japan]
Marcus S.L., Polakowski R., Seto N.O.L., Leinala E., Borisova S., Blancher A., Roubinet F., Evans S.V., Palcic M.M.;
"A single point mutation reverses the donor specificity of human blood group B-synthesizing galactosyltransferase.";
J. Biol. Chem. 278:12403-12405(2003).
[17]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 IN COMPLEXES WITH UDP; UDP-N-ACETYL-GALACTOSAMINE; UDP-GALACTOSE AND GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOGS.
DOI=10.1074/jbc.M308770200; PubMed=12972418 [NCBI, ExPASy, EBI, Israel, Japan]
Nguyen H.P., Seto N.O.L., Cai Y., Leinala E.K., Borisova S.N., Palcic M.M., Evans S.V.;
"The influence of an intramolecular hydrogen bond in differential recognition of inhibitory acceptor analogs by human ABO(H) blood group A and B glycosyltransferases.";
J. Biol. Chem. 278:49191-49195(2003).
[18]
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.
DOI=10.1074/jbc.M500897200; PubMed=15475562 [NCBI, ExPASy, EBI, Israel, Japan]
Lee H.J., Barry C.H., Borisova S.N., Seto N.O.L., Zheng R.B., Blancher A., Evans S.V., Palcic M.M.;
"Structural basis for the inactivity of human blood group O2 glycosyltransferase.";
J. Biol. Chem. 280:525-529(2005).
[19]
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.
DOI=10.1074/jbc.M507620200; PubMed=16326711 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases.";
J. Biol. Chem. 281:3625-3632(2006).
[20]
X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND THR-214, COFACTOR, CHARACTERIZATION OF VARIANT ARG-214, AND MUTAGENESIS OF MET-214.
DOI=10.1074/jbc.M610998200; PubMed=17259183 [NCBI, ExPASy, EBI, Israel, Japan]
Persson M., Letts J.A., Hosseini-Maaf B., Borisova S.N., Palcic M.M., Evans S.V., Olsson M.L.;
"Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif.";
J. Biol. Chem. 282:9564-9570(2007).
Comments
  • FUNCTION: 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 ACTIVITY: UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-(alpha-L-fucosyl-(1,2))-D-galactose.
  • CATALYTIC ACTIVITY: UDP-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D-galactosyl-(1->3)-(alpha-L-fucosyl-(1->2))-D-galactosyl-R.
  • COFACTOR: Binds 1 manganese ion per subunit.
  • PATHWAY: Protein modification; protein glycosylation.
  • SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
  • DOMAIN: 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.
  • PTM: The soluble form derives from the membrane form by proteolytic processing.
  • POLYMORPHISM: 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.
  • SIMILARITY: Belongs to the glycosyltransferase 6 family.
  • WEB RESOURCE: Name=GGDB; Note=GlycoGene database; URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/";.
  • WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/abo/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J05175; AAA36792.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84746; CAA59233.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84747; CAA59233.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84748; CAA59233.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84749; CAA59233.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84750; CAA59233.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84751; CAA59233.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X84752; CAA59233.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134412; AAD26572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134413; AAD26573.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134414; AAD26574.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134418; AAD26575.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134417; AAD26575.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134420; AAD26576.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134419; AAD26576.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134430; AAD26581.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF134429; AAD26581.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY268591; AAP03430.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC069595; AAH69595.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ536135; CAD60222.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ536136; CAD60223.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D82842; BAA11591.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D82843; BAA11592.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF016622; AAB86462.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF448199; AAQ04662.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF448200; AAQ04663.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ276689; CAB81779.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR PC1165; PC1165.
RefSeq NP_065202.2; -.
UniGene Hs.654423
3D structure databases
PDB
1LZ0; X-ray; 1.80 A; A=64-354.[ExPASy / RCSB / EBI]
1LZ7; X-ray; 1.65 A; A=64-354.[ExPASy / RCSB / EBI]
1LZI; X-ray; 1.35 A; A=64-354.[ExPASy / RCSB / EBI]
1LZJ; X-ray; 1.32 A; A=64-354.[ExPASy / RCSB / EBI]
1R7T; X-ray; 2.09 A; A=64-345.[ExPASy / RCSB / EBI]
1R7U; X-ray; 1.61 A; A=64-345.[ExPASy / RCSB / EBI]
1R7V; X-ray; 2.09 A; A=64-345.[ExPASy / RCSB / EBI]
1R7X; X-ray; 1.97 A; A=64-345.[ExPASy / RCSB / EBI]
1R7Y; X-ray; 1.75 A; A=64-345.[ExPASy / RCSB / EBI]
1R80; X-ray; 1.65 A; A=64-345.[ExPASy / RCSB / EBI]
1R81; X-ray; 1.75 A; A=64-345.[ExPASy / RCSB / EBI]
1R82; X-ray; 1.55 A; A=64-345.[ExPASy / RCSB / EBI]
1WSZ; X-ray; 1.59 A; A=64-354.[ExPASy / RCSB / EBI]
1WT0; X-ray; 1.80 A; A=64-354.[ExPASy / RCSB / EBI]
1WT1; X-ray; 1.55 A; A=64-354.[ExPASy / RCSB / EBI]
1WT2; X-ray; 1.90 A; A=64-354.[ExPASy / RCSB / EBI]
1WT3; X-ray; 1.80 A; A=64-354.[ExPASy / RCSB / EBI]
1XZ6; X-ray; 1.55 A; A=64-354.[ExPASy / RCSB / EBI]
1ZHJ; X-ray; 1.59 A; A=64-354.[ExPASy / RCSB / EBI]
1ZI1; X-ray; 1.57 A; A=64-354.[ExPASy / RCSB / EBI]
1ZI3; X-ray; 1.69 A; A=64-354.[ExPASy / RCSB / EBI]
1ZI4; X-ray; 1.85 A; A=64-354.[ExPASy / RCSB / EBI]
1ZI5; X-ray; 1.55 A; A=64-354.[ExPASy / RCSB / EBI]
1ZIZ; X-ray; 1.49 A; A=64-354.[ExPASy / RCSB / EBI]
1ZJ0; X-ray; 1.67 A; A=64-354.[ExPASy / RCSB / EBI]
1ZJ1; X-ray; 1.65 A; A=64-354.[ExPASy / RCSB / EBI]
1ZJ2; X-ray; 1.69 A; A=64-354.[ExPASy / RCSB / EBI]
1ZJ3; X-ray; 1.69 A; A=64-354.[ExPASy / RCSB / EBI]
1ZJO; X-ray; 1.64 A; A=64-354.[ExPASy / RCSB / EBI]
2A8U; X-ray; 1.69 A; A=64-354.[ExPASy / RCSB / EBI]
2A8W; X-ray; 1.59 A; A=64-354.[ExPASy / RCSB / EBI]
2O1G; X-ray; 1.71 A; A=64-354.[ExPASy / RCSB / EBI]
2O1H; X-ray; 1.67 A; A=64-354.[ExPASy / RCSB / EBI]
2PGY; X-ray; 2.39 A; A=64-354.[ExPASy / RCSB / EBI]
2RIT; X-ray; 1.43 A; A=64-354.[ExPASy / RCSB / EBI]
2RIX; X-ray; 1.75 A; A=64-354.[ExPASy / RCSB / EBI]
2RIY; X-ray; 1.55 A; A=64-354.[ExPASy / RCSB / EBI]
2RIZ; X-ray; 1.45 A; A=64-354.[ExPASy / RCSB / EBI]
2RJ0; X-ray; 1.52 A; A=64-354.[ExPASy / RCSB / EBI]
2RJ1; X-ray; 1.55 A; A=64-354.[ExPASy / RCSB / EBI]
2RJ4; X-ray; 1.47 A; A=64-354.[ExPASy / RCSB / EBI]
2RJ5; X-ray; 1.45 A; A=64-354.[ExPASy / RCSB / EBI]
2RJ6; X-ray; 1.41 A; A=64-354.[ExPASy / RCSB / EBI]
2RJ7; X-ray; 1.70 A; A=64-354.[ExPASy / RCSB / EBI]
2RJ8; X-ray; 1.69 A; A=64-354.[ExPASy / RCSB / EBI]
2RJ9; X-ray; 1.69 A; A=64-354.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1LZ0; -.
1LZ7; -.
1LZI; -.
1LZJ; -.
1R7T; -.
1R7U; -.
1R7V; -.
1R7X; -.
1R7Y; -.
1R80; -.
1R81; -.
1R82; -.
1WSZ; -.
1WT0; -.
1WT1; -.
1WT2; -.
1WT3; -.
1XZ6; -.
1ZHJ; -.
1ZI1; -.
1ZI3; -.
1ZI4; -.
1ZI5; -.
1ZIZ; -.
1ZJ0; -.
1ZJ1; -.
1ZJ2; -.
1ZJ3; -.
1ZJO; -.
2A8U; -.
2A8W; -.
2O1G; -.
2O1H; -.
2PGY; -.
2RIT; -.
2RIX; -.
2RIY; -.
2RIZ; -.
2RJ0; -.
2RJ1; -.
2RJ4; -.
2RJ5; -.
2RJ6; -.
2RJ7; -.
2RJ8; -.
2RJ9; -.
DisProt DP00338; -.
DP00339; -.
ModBase P16442.
Organism-specific databases
H-InvDB HIX0034767; -.
HGNC HGNC:79; ABO.
GeneLynx ABO; Homo sapiens.
GenAtlas ABO.
MIM 110300; gene+phenotype. [NCBI / EBI]
PharmGKB PA24415; -.
GeneCards P16442.
Gene expression databases
ArrayExpress P16442; -.
GermOnline ENSG00000175164; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0030173; Cellular component: integral to Golgi membrane (non-traceable author statement from UniProtKB).
GO:0004381; Molecular function: fucosylgalactoside 3-alpha-galactosyltransferase activity (non-traceable author statement from UniProtKB).
GO:0004380; Molecular function: glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity (non-traceable author statement from UniProtKB).
GO:0006486; Biological process: protein amino acid glycosylation (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR005076; Glyco_trans_6.
Graphical view of domain structure.
PANTHER PTHR10462; Glyco_trans_6; 1.
Pfam PF03414; Glyco_transf_6; 1.
Pfam graphical view of domain structure.
BLOCKS P16442.
Genome annotation databases
Ensembl ENSG00000175164; Homo sapiens. [Contig view]
GeneID 28; -.
KEGG hsa:28; -.
Phylogenomic databases
HOVERGEN P16442; -.
Other
LinkHub P16442; -.
SOURCE ABO; Homo sapiens.
ProtoNet P16442.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Blood group antigen; Direct protein sequencing; Glycoprotein; Glycosyltransferase; Golgi apparatus; Manganese; Membrane; Metal-binding; Polymorphism; Secreted; Signal-anchor; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   354  354     Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase. PRO_0000012268
CHAIN   54   354  301     Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form. PRO_0000012269
TOPO_DOM   1    32  32     Cytoplasmic (Potential). 
TRANSMEM   33    53  21     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   54   354  301     Lumenal (Potential). 
REGION   121   123  3     UDP-N-acetyl-galactosamine binding. 
REGION   211   213  3     UDP-N-acetyl-galactosamine binding. 
METAL   211   211        Manganese. 
METAL   213   213        Manganese. 
BINDING   126   126        UDP-N-acetyl-galactosamine. 
BINDING   233   233        Glycoprotein fucosyl-galactosyl group. 
BINDING   245   245        Glycoprotein fucosyl-galactosyl group. 
BINDING   303   303        Glycoprotein fucosyl-galactosyl group. 
BINDING   326   326        Glycoprotein fucosyl-galactosyl group. 
CARBOHYD   113   113        N-linked (GlcNAc...) (Potential). 
VARIANT   35    35  1     G -> R (in dbSNP:rs8176696 [NCBI]). VAR_019147 
VARIANT   36    36  1     V -> F (in dbSNP:rs688976 [NCBI]). VAR_019148 
VARIANT   63    63  1     R -> H (in dbSNP:rs549446 [NCBI]). VAR_019149 
VARIANT   74    74  1     P -> S (in dbSNP:rs512770 [NCBI]). VAR_019150 [3D]
VARIANT   80    81  2     CR -> W. VAR_003408
VARIANT   156   156  1     P -> L (in allele A2; dbSNP:rs1053878 [NCBI]). VAR_003409 [3D]
VARIANT   161   161  1     R -> H (in dbSNP:rs8176738 [NCBI]). VAR_019151 [3D]
VARIANT   163   163  1     T -> M (in allele Aw08). VAR_036738 [3D]
VARIANT   176   176  1     R -> G (in group B transferase; dbSNP:rs7853989 [NCBI]). VAR_003410 [3D]
VARIANT   198   198  1     R -> W (in allele Aw07). VAR_036739 [3D]
VARIANT   199   199  1     R -> C (in dbSNP:rs8176739 [NCBI]). VAR_019152 [3D]
VARIANT   214   214  1     M -> R (in allele Bel01; loss of manganese binding and reduced catalytic activity). VAR_036740 [3D]
VARIANT   216   216  1     F -> I (in dbSNP:rs8176740 [NCBI]). VAR_019153 [3D]
VARIANT   223   223  1     E -> D (in allele B106). VAR_036741 [3D]
VARIANT   235   235  1     G -> S (in group B transferase; dbSNP:rs8176743 [NCBI]). VAR_003411 [3D]
VARIANT   257   257  1     P -> L (in dbSNP:rs8176745 [NCBI]). VAR_033540 [3D]
VARIANT   266   266  1     L -> M (in group B transferase; important for the specificity; dbSNP:rs8176746 [NCBI]). VAR_003412 [3D]
VARIANT   268   268  1     G -> A (in group B transferase; important for the specificity; dbSNP:rs8176747 [NCBI]). VAR_003413 [3D]
VARIANT   268   268  1     G -> R (in dbSNP:rs8176747 [NCBI]). VAR_033541 [3D]
VARIANT   277   277  1     V -> M (in dbSNP:rs8176748 [NCBI]). VAR_019154 [3D]
VARIANT   288   288  1     M -> R. VAR_036742 [3D]
VARIANT   291   291  1     D -> N (in allele B104). VAR_036743 [3D]
VARIANT   346   346  1     K -> M (in allele Bw08). VAR_036744 
VARIANT   352   352  1     R -> G (in allele A107). VAR_036745 
VARIANT   352   352  1     R -> W (in allele A106 and allele B3). VAR_003414 
MUTAGEN   214   214        M->T,V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. 
MUTAGEN   234   234        P->S: Alters substrate specificity of group B transferase. 
MUTAGEN   303   303        E->A: Decreases specific activity of group B transferase almost to zero. 
STRAND   82    84  3      
STRAND   93    95  3      
HELIX   102   110  9      
TURN   111   113  3      
STRAND   115   122  8      
HELIX   124   129  6      
HELIX   130   140  11      
STRAND   145   154  10      
HELIX   156   158  3      
STRAND   168   174  7