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P16442 (BGAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:ABO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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-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.

Cofactor

Binds 1 manganese ion per subunit. Ref.23

Pathway

Protein modification; protein glycosylation.

Subcellular location

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.

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.

Post-translational modification

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.

Sequence similarities

Belongs to the glycosyltransferase 6 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Histo-blood group ABO system transferase
PRO_0000012268
Chain54 – 354301Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
PRO_0000012269

Regions

Topological domain1 – 3232Cytoplasmic Potential
Transmembrane33 – 5321Helical; Signal-anchor for type II membrane protein; Potential
Topological domain54 – 354301Lumenal Potential
Region121 – 1233UDP-N-acetyl-galactosamine binding
Region211 – 2133UDP-N-acetyl-galactosamine binding

Sites

Metal binding2111Manganese
Metal binding2131Manganese
Binding site1261UDP-N-acetyl-galactosamine
Binding site2331Glycoprotein fucosyl-galactosyl group
Binding site2451Glycoprotein fucosyl-galactosyl group
Binding site3031Glycoprotein fucosyl-galactosyl group
Binding site3261Glycoprotein fucosyl-galactosyl group

Amino acid modifications

Glycosylation1131N-linked (GlcNAc...) Potential

Natural variations

Natural variant351G → R. Ref.9
Corresponds to variant rs8176696 [ dbSNP | Ensembl ].
VAR_019147
Natural variant361V → F. Ref.9
Corresponds to variant rs688976 [ dbSNP | Ensembl ].
VAR_019148
Natural variant631R → H. Ref.9
Corresponds to variant rs549446 [ dbSNP | Ensembl ].
VAR_019149
Natural variant741P → S. Ref.9 Ref.11 Ref.21
Corresponds to variant rs512770 [ dbSNP | Ensembl ].
VAR_019150
Natural variant80 – 812CR → W.
VAR_003408
Natural variant1561P → L in allele A2. Ref.3 Ref.5 Ref.9 Ref.11 Ref.12
Corresponds to variant rs1053878 [ dbSNP | Ensembl ].
VAR_003409
Natural variant1611R → H. Ref.9
Corresponds to variant rs8176738 [ dbSNP | Ensembl ].
VAR_019151
Natural variant1631T → M in allele Aw08. Ref.11
Corresponds to variant rs55756402 [ dbSNP | Ensembl ].
VAR_036738
Natural variant1761R → G in group B transferase. Ref.5 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15
Corresponds to variant rs7853989 [ dbSNP | Ensembl ].
VAR_003410
Natural variant1981R → W in allele Aw07.
Corresponds to variant rs56223957 [ dbSNP | Ensembl ].
VAR_036739
Natural variant1991R → C. Ref.9
Corresponds to variant rs8176739 [ dbSNP | Ensembl ].
VAR_019152
Natural variant2141M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. Ref.12 Ref.23
Corresponds to variant rs55827808 [ dbSNP | Ensembl ].
VAR_036740
Natural variant2161F → I. Ref.9 Ref.12
Corresponds to variant rs8176740 [ dbSNP | Ensembl ].
VAR_019153
Natural variant2231E → D in allele B106. Ref.12
VAR_036741
Natural variant2301G → R in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation. Ref.8
VAR_055227
Natural variant2351G → S in group B transferase. Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15
Corresponds to variant rs8176743 [ dbSNP | Ensembl ].
VAR_003411
Natural variant2571P → L.
Corresponds to variant rs8176745 [ dbSNP | Ensembl ].
VAR_033540
Natural variant2661L → M in group B transferase; important for the specificity. Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
Corresponds to variant rs8176746 [ dbSNP | Ensembl ].
VAR_003412
Natural variant2681G → A in group B transferase; important for the specificity. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16
Corresponds to variant rs8176747 [ dbSNP | Ensembl ].
VAR_003413
Natural variant2681G → R. Ref.11 Ref.21
Corresponds to variant rs8176747 [ dbSNP | Ensembl ].
VAR_033541
Natural variant2771V → M. Ref.9 Ref.12
Corresponds to variant rs8176748 [ dbSNP | Ensembl ].
VAR_019154
Natural variant2881M → R. Ref.11
VAR_036742
Natural variant2911D → N in allele B104. Ref.12
VAR_036743
Natural variant3461K → M in allele Bw08. Ref.11 Ref.15
VAR_036744
Natural variant3521R → G in allele A107. Ref.12
VAR_036745
Natural variant3521R → W in allele A106 and allele B3. Ref.12
VAR_003414

Experimental info

Mutagenesis2141M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. Ref.23
Mutagenesis2341P → S: Alters substrate specificity of group B transferase.
Mutagenesis3031E → A: Decreases specific activity of group B transferase almost to zero. Ref.18

Secondary structure

.................................................. 354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16442 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: A03DA16E630C1608

FASTA35440,934
        10         20         30         40         50         60 
MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG FCMAVREPDH 

        70         80         90        100        110        120 
LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF NIDILNEQFR LQNTTIGLTV 

       130        140        150        160        170        180 
FAIKKYVAFL KLFLETAEKH FMVGHRVHYY VFTDQPAAVP RVTLGTGRQL SVLEVRAYKR 

       190        200        210        220        230        240 
WQDVSMRRME MISDFCERRF LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPGFYGSS 

       250        260        270        280        290        300 
REAFTYERRP QSQAYIPKDE GDFYYLGGFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW 

       310        320        330        340        350 
HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA VRNP 

« Hide

References

« Hide 'large scale' references
[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]"Genomic cloning of the human histo-blood group ABO locus."
Bennett E.P., Steffensen R., Clausen H., Weghuis D.O., Geurts van Kessel A.
Biochem. Biophys. Res. Commun. 206:318-325(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-156.
[4]Erratum
Bennett E.P., Steffensen R., Clausen H., Weghuis D.O., Geurts van Kessel A.
Biochem. Biophys. Res. Commun. 211:347-347(1995) [PubMed] [Europe PMC] [Abstract]
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"Animal histo-blood group ABO genes."
Kominato Y., McNeill P.D., Yamamoto M., Russell M., Hakomori S., Yamamoto F.
Biochem. Biophys. Res. Commun. 189:154-164(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-334, VARIANTS MET-266 AND ALA-268.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

SeattleSNPs
Functional Glycomics Gateway - GTase

Histo-blood group ABO system transferase

Functional Glycomics Gateway - GTase

Histo-blood group ABO system transferase

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05175 mRNA. Translation: AAA36792.1.
X84746 expand/collapse EMBL AC list , 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.
PIRPC1165.
RefSeqNP_065202.2. NM_020469.2.
UniGeneHs.654423.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00339.
ProteinModelPortalP16442.
SMRP16442. Positions 64-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106546. 1 interaction.

Chemistry

ChEMBLCHEMBL2321639.

Protein family/group databases

CAZyGT6. Glycosyltransferase Family 6.

PTM databases

PhosphoSiteP16442.

Polymorphism databases

DMDM114949.

Proteomic databases

PaxDbP16442.
PRIDEP16442.

Protocols and materials databases

DNASU28.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000319878; ENSP00000439154; ENSG00000256062.
GeneID28.
KEGGhsa:28.
UCSCuc004cda.1. human.

Organism-specific databases

CTD28.
GeneCardsGC09M136130.
HGNCHGNC:79. ABO.
MIM110300. gene+phenotype.
neXtProtNX_P16442.
PharmGKBPA24415.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43612.
HOVERGENHBG003563.
InParanoidP16442.
KOK00709.
OrthoDBEOG7BZVSQ.
PhylomeDBP16442.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

GenevestigatorP16442.

Family and domain databases

InterProIPR005076. Glyco_trans_6.
[Graphical view]
PANTHERPTHR10462. PTHR10462. 1 hit.
PfamPF03414. Glyco_transf_6. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16442.
GeneWikiABO_(gene).
GenomeRNAi28.
NextBio97.
PROP16442.
SOURCESearch...

Entry information

Entry nameBGAT_HUMAN
AccessionPrimary (citable) accession number: P16442
Secondary accession number(s): B0JDB9 expand/collapse secondary AC list , O14758, Q14490, Q53I57, Q6ISD4, Q6KFZ2, Q70V27, Q99484, Q99485, Q9NY01, Q9UQ68, Q9UQ69
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries