Reviewed, UniProtKB/Swiss-Prot P16442 (BGAT_HUMAN)

Names and origin

Protein names

Recommended name:
    Histo-blood group ABO system transferase
Alternative name(s):
    NAGAT
    Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase
    EC=2.4.1.40
    Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
    Histo-blood group A transferase
      Short name=A transferase
    Glycoprotein-fucosylgalactoside alpha-galactosyltransferase
    EC=2.4.1.37
    Fucosylglycoprotein 3-alpha-galactosyltransferase
    Histo-blood group B transferase
      Short name=B transferase
Cleaved into the following chain:
    1- Recommended name:
            Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form

Gene names

Name:

ABO

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-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. 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. Ref.23
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.
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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Signal-anchor Transmembrane
Ligand	Manganese Metal-binding
Molecular function	Blood group antigen Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	protein amino acid glycosylation Non-traceable author statement. Source: UniProtKB
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Non-traceable author statement. Source: UniProtKB integral to Golgi membrane Non-traceable author statement. Source: UniProtKB
Molecular function	fucosylgalactoside 3-alpha-galactosyltransferase activity Non-traceable author statement. Source: UniProtKB glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Non-traceable author statement. Source: UniProtKB manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 354

354

Histo-blood group ABO system transferase

PRO_0000012268

Chain

54 – 354

301

Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form

PRO_0000012269

Regions

Topological domain

1 – 32

32

Cytoplasmic Potential

Transmembrane

33 – 53

21

Signal-anchor for type II membrane protein Potential

Topological domain

54 – 354

301

Lumenal Potential

Region

121 – 123

3

UDP-N-acetyl-galactosamine binding

Region

211 – 213

3

UDP-N-acetyl-galactosamine binding

Sites

Metal binding

211

1

Manganese

Metal binding

213

1

Manganese

Binding site

126

1

UDP-N-acetyl-galactosamine

Binding site

233

1

Glycoprotein fucosyl-galactosyl group

Binding site

245

1

Glycoprotein fucosyl-galactosyl group

Binding site

303

1

Glycoprotein fucosyl-galactosyl group

Binding site

326

1

Glycoprotein fucosyl-galactosyl group

Amino acid modifications

Glycosylation

113

1

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

35

1

G → R: dbSNP rs8176696. Ref.6

VAR_019147

Natural variant

36

1

V → F: dbSNP rs688976. Ref.6

VAR_019148

Natural variant

63

1

R → H: dbSNP rs549446. Ref.6

VAR_019149

Natural variant

74

1

P → S: dbSNP rs512770. Ref.6 Ref.11

VAR_019150

Natural variant

80 – 81

2

CR → W

VAR_003408

Natural variant

156

1

P → L in allele A2. dbSNP rs1053878. Ref.6 Ref.11 Ref.3 Ref.5 Ref.12

VAR_003409

Natural variant

161

1

R → H: dbSNP rs8176738. Ref.6

VAR_019151

Natural variant

163

1

T → M in allele Aw08. Ref.11

VAR_036738

Natural variant

176

1

R → G in group B transferase. dbSNP rs7853989. Ref.6 Ref.11 Ref.5 Ref.12 Ref.10 Ref.14

VAR_003410

Natural variant

198

1

R → W in allele Aw07.

VAR_036739

Natural variant

199

1

R → C: dbSNP rs8176739. Ref.6

VAR_019152

Natural variant

214

1

M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. Ref.23 Ref.12

VAR_036740

Natural variant

216

1

F → I: dbSNP rs8176740. Ref.6 Ref.12

VAR_019153

Natural variant

223

1

E → D in allele B106. Ref.12

VAR_036741

Natural variant

230

1

G → R in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation.

VAR_055227

Natural variant

235

1

G → S in group B transferase. dbSNP rs8176743. Ref.6 Ref.11 Ref.5 Ref.12 Ref.10 Ref.14

VAR_003411

Natural variant

257

1

P → L: dbSNP rs8176745.

VAR_033540

Natural variant

266

1

L → M in group B transferase; important for the specificity. dbSNP rs8176746. Ref.6 Ref.11 Ref.5 Ref.12 Ref.10 Ref.14 Ref.16

VAR_003412

Natural variant

268

1

G → A in group B transferase; important for the specificity. dbSNP rs8176747. Ref.6 Ref.11 Ref.12 Ref.10 Ref.14 Ref.16

VAR_003413

Natural variant

268

1

G → R: dbSNP rs8176747. Ref.6 Ref.11 Ref.12 Ref.10 Ref.14 Ref.16

VAR_033541

Natural variant

277

1

V → M: dbSNP rs8176748. Ref.6 Ref.12

VAR_019154

Natural variant

288

1

M → R Ref.11

VAR_036742

Natural variant

291

1

D → N in allele B104. Ref.12

VAR_036743

Natural variant

346

1

K → M in allele Bw08. Ref.11 Ref.12

VAR_036744

Natural variant

352

1

R → G in allele A107. Ref.12

VAR_036745

Natural variant

352

1

R → W in allele A106 and allele B3. Ref.12

VAR_003414

Experimental info

Mutagenesis

214

1

M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. Ref.23

Mutagenesis

234

1

P → S: Alters substrate specificity of group B transferase.

Mutagenesis

303

1

E → A: Decreases specific activity of group B transferase almost to zero. Ref.18

Secondary structure

1

.

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354

Helix Strand Turn

Details...

Beta strand

82 – 84

3

Beta strand

93 – 95

3

Helix

102 – 110

9

Turn

111 – 113

3

Beta strand

115 – 122

8

Helix

124 – 129

6

Helix

130 – 140

11

Beta strand

145 – 154

10

Helix

156 – 158

3

Beta strand

168 – 174

7

Helix

197 – 203

7

Beta strand

205 – 210

6

Beta strand

212 – 216

5

Helix

222 – 224

3

Beta strand

226 – 232

7

Turn

234 – 238

5

Helix

241 – 243

3

Beta strand

269 – 273

5

Helix

274 – 293

20

Helix

301 – 312

12

Beta strand

316 – 319

4

Helix

321 – 323

3

Helix

327 – 330

4

Beta strand

341 – 343

3

Helix

348 – 351

4

Sequences

	Sequence		Length	Mass (Da)
	P16442-1 [UniParc]. Last modified December 1, 1992. Version 2. Checksum: A03DA16E630C1608	FASTA	354	40,934
	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

References

	« Hide 'large scale' referencesShow '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: 2104828] [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: 2333095] [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: 7598760] [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: 7779106] [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: 16533287] [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: 17764507] [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: 18513251] [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: 15489334] [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: 12829588] [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: 8839869] [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: 9800297] [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: 15104652] [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: 1449469] [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: 2121736] [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: 12198488] [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: 12529355] [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: 12972418] [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: 15475562] [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: 16326711] [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: 17259183] [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

EMBLGenBankDDBJ

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.
AF134418, AF134417 Genomic DNA. Translation: AAD26575.1.
AF134420, AF134419 Genomic DNA. Translation: AAD26576.1.
AF134430, AF134429 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.

IPI

IPI00420082.

PIR

PC1165.

RefSeq

NP_065202.2.

UniGene

Hs.654423

3D structure databases

PDBPDBe

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	[»]

DisProt

DP00338.
DP00339.

ModBase

Search...

Protein family/group databases

CAZy

GT6. Glycosyltransferase Family 6.

Genome annotation databases

Ensembl

ENSG00000175164. Homo sapiens. [Contig view]

GeneID

28.

KEGG

hsa:28.

Organism-specific databases

GeneCards

GC09M135120.

H-InvDB

HIX0034767.

HGNC

HGNC:79. ABO.

MIM

110300. gene+phenotype.

PharmGKB

PA24415.

GenAtlas

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Phylogenomic databases

HOVERGEN

P16442.

Enzyme and pathway databases

BRENDA

2.4.1.37. 247.
2.4.1.40. 247.

Gene expression databases

ArrayExpress

P16442.

Bgee

P16442.

GermOnline

ENSG00000175164. Homo sapiens.

Family and domain databases

InterPro

IPR005076. Glyco_trans_6.
[Graphical view]

PANTHER

PTHR10462. Glyco_trans_6. 1 hit.

Pfam

PF03414. Glyco_transf_6. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

97.

SOURCE

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Entry information

Entry name

BGAT_HUMAN

Accession

Primary (citable) accession number: P16442
Secondary accession number(s): B0JDB9 , 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:	July 7, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)