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Histo-blood group ABO system transferase (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) (A transferase) (Histo-blood group B transferase) (B transferase) (NAGAT) [Cleaved into: Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form]

 BGAT_HUMAN              Reviewed;         354 AA.
P16442; B0JDB9; O14758; Q14490; Q53I57; Q6ISD4; Q6KFZ2; Q70V27;
Q99484; Q99485; Q9NY01; Q9UQ68; Q9UQ69;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-DEC-1992, sequence version 2.
20-JUN-2018, entry version 198.
RecName: Full=Histo-blood group ABO system transferase;
AltName: Full=Fucosylglycoprotein 3-alpha-galactosyltransferase;
AltName: Full=Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase;
AltName: Full=Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase;
EC=2.4.1.40 {ECO:0000269|PubMed:12198488, ECO:0000269|PubMed:17259183};
AltName: Full=Glycoprotein-fucosylgalactoside alpha-galactosyltransferase;
EC=2.4.1.37 {ECO:0000269|PubMed:12198488, ECO:0000269|PubMed:17259183};
AltName: Full=Histo-blood group A transferase;
Short=A transferase;
AltName: Full=Histo-blood group B transferase;
Short=B transferase;
AltName: Full=NAGAT;
Contains:
RecName: Full=Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form;
Name=ABO;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2104828;
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 [GENOMIC DNA].
PubMed=2333095; DOI=10.1038/345229a0;
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], POLYMORPHISM, AND VARIANT LEU-156.
PubMed=7598760; DOI=10.1006/bbrc.1995.1044;
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.
PubMed=7779106; DOI=10.1006/bbrc.1995.1817;
Bennett E.P., Steffensen R., Clausen H., Weghuis D.O.,
Geurts van Kessel A.;
Biochem. Biophys. Res. Commun. 211:347-347(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], POLYMORPHISM, 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].
TISSUE=Peripheral blood;
PubMed=16533287; DOI=10.1111/j.1537-2995.2006.00740.x;
Seltsam A., Das Gupta C., Bade-Doeding C., Blasczyk R.;
"A weak blood group A phenotype caused by a translation-initiator
mutation in the ABO gene.";
Transfusion 46:434-440(2006).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Peripheral blood;
PubMed=17764507; DOI=10.1111/j.1537-2995.2007.01475.x;
Seltsam A., Wagner F.F., Gruger D., Gupta C.D., Bade-Doeding C.,
Blasczyk R.;
"Weak blood group B phenotypes may be caused by variations in the
CCAAT-binding factor/NF-Y enhancer region of the ABO gene.";
Transfusion 47:2330-2335(2007).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, AND VARIANTS ARG-230;
SER-235; MET-266 AND ALA-268.
TISSUE=Peripheral blood;
PubMed=18513251; DOI=10.1111/j.1537-2995.2008.01782.x;
Seltsam A., Gruger D., Just B., Figueiredo C., Gupta C.D.,
Deluca D.S., Blasczyk R.;
"Aberrant intracellular trafficking of a variant B
glycosyltransferase.";
Transfusion 48:1898-1905(2008).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, 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 variation discovery resource;
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], POLYMORPHISM, AND VARIANTS
GLY-176; SER-235; MET-266 AND ALA-268.
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, POLYMORPHISM, AND
VARIANTS SER-74; LEU-156; MET-163; GLY-176; TRP-198; SER-235; MET-266;
ALA-268; ARG-268; ARG-288 AND MET-346.
PubMed=12829588; DOI=10.1182/blood-2003-03-0955;
Seltsam A., Hallensleben M., Kollmann A., Blasczyk R.;
"The nature of diversity and diversification at the ABO locus.";
Blood 102:3035-3042(2003).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354, POLYMORPHISM, 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;
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).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354.
PubMed=9800297; DOI=10.1046/j.1365-3148.1998.00161.x;
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).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, POLYMORPHISM, AND
VARIANTS GLY-176; SER-235; MET-266 AND ALA-268.
PubMed=15104652; DOI=10.1111/j.1537-2995.2004.03346.x;
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).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-354, POLYMORPHISM, 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.
[16]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-334, POLYMORPHISM, AND
VARIANTS MET-266 AND ALA-268.
PubMed=1449469; DOI=10.1016/0006-291X(92)91538-2;
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).
[17]
CHARACTERIZATION, AND POLYMORPHISM.
PubMed=2121736;
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).
[18]
POLYMORPHISM, AND VARIANT ALA-234.
PubMed=10462501; DOI=10.1006/bbrc.1999.1246;
Yu L.C., Lee H.L., Chan Y.S., Lin M.;
"The molecular basis for the B(A) allele: an amino acid alteration in
the human histoblood group B alpha-(1,3)-galactosyltransferase
increases its intrinsic alpha-(1,3)-N-acetylgalactosaminyltransferase
activity.";
Biochem. Biophys. Res. Commun. 262:487-493(1999).
[19]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 64-354 IN COMPLEX WITH
MANGANESE AND UDP-N-ACETYL-D-GALACTOSAMINE, METAL-BINDING, MUTAGENESIS
OF GLU-303, AND CATALYTIC ACTIVITY.
PubMed=12198488; DOI=10.1038/nsb832;
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).
[20]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 OF MUTANT SER-234 IN
COMPLEX WITH GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOG.
PubMed=12529355; DOI=10.1074/jbc.M212002200;
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).
[21]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 64-345 IN COMPLEXES WITH
MANGANESE; UDP; UDP-N-ACETYL-GALACTOSAMINE; UDP-GALACTOSE AND
GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOGS.
PubMed=12972418; DOI=10.1074/jbc.M308770200;
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).
[22]
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.
PubMed=15475562; DOI=10.1074/jbc.M500897200;
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).
[23]
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 MANGANESE AND GLYCOPROTEIN FUCOSYL-GALACTOSE ANALOGS.
PubMed=16326711; DOI=10.1074/jbc.M507620200;
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).
[24]
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, AND CATALYTIC ACTIVITY.
PubMed=17259183; DOI=10.1074/jbc.M610998200;
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).
-!- 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. {ECO:0000269|PubMed:12198488,
ECO:0000269|PubMed:17259183}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000269|PubMed:12198488,
ECO:0000269|PubMed:17259183}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17259183};
Note=Binds 1 Mn(2+) ion per subunit.
{ECO:0000269|PubMed:17259183};
-!- PATHWAY: Protein modification; protein glycosylation.
{ECO:0000305}.
-!- 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: Genetic variations in ABO define the ABO blood group
system [MIM:616093]. The ABO blood group system is the most
important blood group system in blood transfusion. The sequence
shown here is that of the A transferase. The B form differs by a
few residues substitution. Residues 266 and 268 are important for
specificity. The reference genome assembly (GRCh38/hg38) describes
a non-functional O-type ABO allele. The O-type ABO allele results
in a guanine deletion (NM_020469.2: c.286delG). This deletion
induces a frameshift and creates a premature stop codon resulting
in a truncated (117 amino acids) protein deprived of any
glycosyltransferase activity (PubMed:2333095).
{ECO:0000269|PubMed:10462501, ECO:0000269|PubMed:12829588,
ECO:0000269|PubMed:1449469, ECO:0000269|PubMed:15104652,
ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:18513251,
ECO:0000269|PubMed:2121736, ECO:0000269|PubMed:2333095,
ECO:0000269|PubMed:7598760, ECO:0000269|PubMed:8839869,
ECO:0000269|Ref.15, ECO:0000269|Ref.5, ECO:0000269|Ref.9}.
-!- SIMILARITY: Belongs to the glycosyltransferase 6 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/abo/";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Histo-blood group ABO system transferase;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_450";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Histo-blood group ABO system transferase;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_502";
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EMBL; J05175; AAA36792.1; -; mRNA.
EMBL; X84746; CAA59233.1; -; Genomic_DNA.
EMBL; X84747; CAA59233.1; JOINED; Genomic_DNA.
EMBL; X84748; CAA59233.1; JOINED; Genomic_DNA.
EMBL; X84749; CAA59233.1; JOINED; Genomic_DNA.
EMBL; X84750; CAA59233.1; JOINED; Genomic_DNA.
EMBL; X84751; CAA59233.1; JOINED; Genomic_DNA.
EMBL; X84752; CAA59233.1; JOINED; Genomic_DNA.
EMBL; AF134412; AAD26572.1; -; mRNA.
EMBL; AF134413; AAD26573.1; -; mRNA.
EMBL; AF134414; AAD26574.1; -; mRNA.
EMBL; AH007586; AAD26575.1; -; Genomic_DNA.
EMBL; AH007587; AAD26576.1; -; Genomic_DNA.
EMBL; AH007592; AAD26581.1; -; Genomic_DNA.
EMBL; AJ920329; CAI79116.1; -; Genomic_DNA.
EMBL; AM423110; CAM28424.1; -; Genomic_DNA.
EMBL; AM492698; CAM34526.1; -; Genomic_DNA.
EMBL; AM492699; CAM34527.1; -; Genomic_DNA.
EMBL; AY268591; AAP03430.1; -; Genomic_DNA.
EMBL; BC069595; AAH69595.1; -; mRNA.
EMBL; BC111575; AAI11576.1; -; mRNA.
EMBL; AJ536135; CAD60222.1; -; Genomic_DNA.
EMBL; AJ536136; CAD60223.1; -; Genomic_DNA.
EMBL; D82842; BAA11591.2; -; Genomic_DNA.
EMBL; D82843; BAA11592.2; -; Genomic_DNA.
EMBL; AF016622; AAB86462.1; -; Genomic_DNA.
EMBL; AF448199; AAQ04662.1; -; Genomic_DNA.
EMBL; AF448200; AAQ04663.1; -; Genomic_DNA.
EMBL; AJ276689; CAB81779.1; -; Genomic_DNA.
PIR; PC1165; PC1165.
RefSeq; NP_065202.2; NM_020469.2.
UniGene; Hs.654423; -.
PDB; 1LZ0; X-ray; 1.80 A; A=64-354.
PDB; 1LZ7; X-ray; 1.65 A; A=64-354.
PDB; 1LZI; X-ray; 1.35 A; A=64-354.
PDB; 1LZJ; X-ray; 1.32 A; A=64-354.
PDB; 1R7T; X-ray; 2.09 A; A=64-345.
PDB; 1R7U; X-ray; 1.61 A; A=64-345.
PDB; 1R7V; X-ray; 2.09 A; A=64-345.
PDB; 1R7X; X-ray; 1.97 A; A=64-345.
PDB; 1R7Y; X-ray; 1.75 A; A=64-345.
PDB; 1R80; X-ray; 1.65 A; A=64-345.
PDB; 1R81; X-ray; 1.75 A; A=64-345.
PDB; 1R82; X-ray; 1.55 A; A=64-345.
PDB; 1WSZ; X-ray; 1.59 A; A=64-354.
PDB; 1WT0; X-ray; 1.80 A; A=64-354.
PDB; 1WT1; X-ray; 1.55 A; A=64-354.
PDB; 1WT2; X-ray; 1.90 A; A=64-354.
PDB; 1WT3; X-ray; 1.80 A; A=64-354.
PDB; 1XZ6; X-ray; 1.55 A; A=64-354.
PDB; 1ZHJ; X-ray; 1.59 A; A=64-354.
PDB; 1ZI1; X-ray; 1.57 A; A=64-354.
PDB; 1ZI3; X-ray; 1.69 A; A=64-354.
PDB; 1ZI4; X-ray; 1.85 A; A=64-354.
PDB; 1ZI5; X-ray; 1.55 A; A=64-354.
PDB; 1ZIZ; X-ray; 1.49 A; A=64-354.
PDB; 1ZJ0; X-ray; 1.67 A; A=64-354.
PDB; 1ZJ1; X-ray; 1.65 A; A=64-354.
PDB; 1ZJ2; X-ray; 1.69 A; A=64-354.
PDB; 1ZJ3; X-ray; 1.69 A; A=64-354.
PDB; 1ZJO; X-ray; 1.64 A; A=64-354.
PDB; 1ZJP; X-ray; 1.59 A; A=64-354.
PDB; 2A8U; X-ray; 1.69 A; A=64-354.
PDB; 2A8W; X-ray; 1.59 A; A=64-354.
PDB; 2I7B; X-ray; 1.99 A; A=64-354.
PDB; 2O1F; X-ray; 1.99 A; A=64-354.
PDB; 2O1G; X-ray; 1.71 A; A=64-354.
PDB; 2O1H; X-ray; 1.67 A; A=64-354.
PDB; 2PGV; X-ray; 1.79 A; A=64-354.
PDB; 2PGY; X-ray; 2.39 A; A=64-354.
PDB; 2RIT; X-ray; 1.43 A; A=64-354.
PDB; 2RIX; X-ray; 1.75 A; A=64-354.
PDB; 2RIY; X-ray; 1.55 A; A=64-354.
PDB; 2RIZ; X-ray; 1.45 A; A=64-354.
PDB; 2RJ0; X-ray; 1.52 A; A=64-354.
PDB; 2RJ1; X-ray; 1.55 A; A=64-354.
PDB; 2RJ4; X-ray; 1.47 A; A=64-354.
PDB; 2RJ5; X-ray; 1.45 A; A=64-354.
PDB; 2RJ6; X-ray; 1.41 A; A=64-354.
PDB; 2RJ7; X-ray; 1.70 A; A=64-354.
PDB; 2RJ8; X-ray; 1.69 A; A=64-354.
PDB; 2RJ9; X-ray; 1.69 A; A=64-354.
PDB; 2Y7A; X-ray; 2.06 A; A/B/C/D=64-354.
PDB; 3I0C; X-ray; 1.55 A; A=69-354.
PDB; 3I0D; X-ray; 1.90 A; A=69-354.
PDB; 3I0E; X-ray; 1.81 A; A=69-354.
PDB; 3I0F; X-ray; 1.56 A; A=69-354.
PDB; 3I0G; X-ray; 1.40 A; A=69-354.
PDB; 3I0H; X-ray; 2.00 A; A=69-354.
PDB; 3I0I; X-ray; 1.90 A; X=69-354.
PDB; 3I0J; X-ray; 1.48 A; A=69-354.
PDB; 3I0K; X-ray; 2.20 A; A=69-354.
PDB; 3I0L; X-ray; 1.60 A; A=69-354.
PDB; 3IOH; X-ray; 1.25 A; A=64-354.
PDB; 3IOI; X-ray; 1.45 A; A=64-354.
PDB; 3IOJ; X-ray; 1.65 A; A/B=64-354.
PDB; 3SX3; X-ray; 1.45 A; A=64-354.
PDB; 3SX5; X-ray; 1.43 A; A=64-354.
PDB; 3SX7; X-ray; 1.42 A; A=64-354.
PDB; 3SX8; X-ray; 1.47 A; A=64-354.
PDB; 3SXA; X-ray; 1.50 A; A=64-354.
PDB; 3SXB; X-ray; 1.49 A; A=64-354.
PDB; 3SXC; X-ray; 1.90 A; A=64-354.
PDB; 3SXD; X-ray; 1.55 A; A=64-354.
PDB; 3SXE; X-ray; 1.49 A; A=64-354.
PDB; 3SXG; X-ray; 1.86 A; A=64-354.
PDB; 3U0X; X-ray; 1.85 A; A/B=64-354.
PDB; 3U0Y; X-ray; 1.60 A; A/B=64-354.
PDB; 3V0L; X-ray; 1.75 A; A=64-354.
PDB; 3V0M; X-ray; 1.68 A; A/B=64-354.
PDB; 3V0N; X-ray; 1.75 A; A/B=64-354.
PDB; 3V0O; X-ray; 1.65 A; A/B=64-354.
PDB; 3V0P; X-ray; 1.90 A; A/B=64-354.
PDB; 3V0Q; X-ray; 1.80 A; A/B=64-354.
PDB; 3ZGF; X-ray; 1.70 A; A/B=64-354.
PDB; 3ZGG; X-ray; 1.90 A; A=64-354.
PDB; 4C2S; X-ray; 2.48 A; A/B=64-354.
PDB; 4FQW; X-ray; 2.02 A; A=64-354.
PDB; 4FRA; X-ray; 1.43 A; A=64-354.
PDB; 4FRB; X-ray; 1.54 A; A=64-354.
PDB; 4FRD; X-ray; 1.55 A; A=64-354.
PDB; 4FRE; X-ray; 1.85 A; A=64-354.
PDB; 4FRH; X-ray; 1.80 A; A=64-354.
PDB; 4FRL; X-ray; 1.90 A; A=64-354.
PDB; 4FRM; X-ray; 1.90 A; A=64-354.
PDB; 4FRO; X-ray; 1.75 A; A=64-354.
PDB; 4FRP; X-ray; 2.00 A; A=64-354.
PDB; 4FRQ; X-ray; 2.35 A; A=64-354.
PDB; 4GBP; X-ray; 2.15 A; A=64-354.
PDB; 4KC1; X-ray; 1.50 A; A=64-346.
PDB; 4KC2; X-ray; 1.70 A; A=64-346.
PDB; 4KC4; X-ray; 1.60 A; A=64-346.
PDB; 4KXO; X-ray; 2.00 A; A=64-354.
PDB; 4Y62; X-ray; 1.60 A; A=1-354.
PDB; 4Y63; X-ray; 1.30 A; A=1-354.
PDB; 4Y64; X-ray; 1.60 A; A=1-354.
PDB; 5BXC; X-ray; 1.40 A; A=64-354.
PDB; 5C1G; X-ray; 1.46 A; A=64-354.
PDB; 5C1H; X-ray; 1.55 A; A=64-354.
PDB; 5C1L; X-ray; 1.40 A; A=64-354.
PDB; 5C36; X-ray; 1.55 A; A=64-354.
PDB; 5C38; X-ray; 1.45 A; A=64-354.
PDB; 5C3A; X-ray; 1.33 A; A=64-354.
PDB; 5C3B; X-ray; 1.40 A; A=64-354.
PDB; 5C3D; X-ray; 1.39 A; A=64-354.
PDB; 5C47; X-ray; 1.39 A; A=64-354.
PDB; 5C48; X-ray; 1.46 A; A=64-354.
PDB; 5C49; X-ray; 1.49 A; A=64-354.
PDB; 5C4B; X-ray; 1.54 A; A=64-354.
PDB; 5C4C; X-ray; 1.43 A; A=64-354.
PDB; 5C4D; X-ray; 1.40 A; A=64-354.
PDB; 5C4E; X-ray; 1.55 A; A=64-354.
PDB; 5C4F; X-ray; 1.41 A; A=64-354.
PDB; 5C8R; X-ray; 1.45 A; A=64-354.
PDB; 5CMF; X-ray; 1.95 A; X=64-345.
PDB; 5CMG; X-ray; 1.83 A; X=64-354.
PDB; 5CMH; X-ray; 1.61 A; A=64-354.
PDB; 5CMI; X-ray; 1.85 A; A=64-354.
PDB; 5CMJ; X-ray; 1.73 A; A=64-354.
PDB; 5CQL; X-ray; 1.69 A; X=64-354.
PDB; 5CQM; X-ray; 1.65 A; X=64-354.
PDB; 5CQN; X-ray; 1.61 A; X=64-354.
PDB; 5CQO; X-ray; 1.69 A; A=64-354.
PDB; 5CQP; X-ray; 1.83 A; A=64-354.
PDB; 5M79; X-ray; 1.30 A; A=64-354.
PDB; 5M7A; X-ray; 1.30 A; A=64-354.
PDB; 5M7B; X-ray; 1.50 A; A=64-354.
PDB; 5M7C; X-ray; 1.60 A; A/B=64-354.
PDB; 5M7D; X-ray; 1.20 A; A=64-354.
PDB; 5TJK; X-ray; 1.45 A; A=64-354.
PDB; 5TJL; X-ray; 1.89 A; A=64-354.
PDB; 5TJN; X-ray; 1.47 A; A=64-354.
PDB; 5TJO; X-ray; 1.57 A; A=64-354.
PDBsum; 1LZ0; -.
PDBsum; 1LZ7; -.
PDBsum; 1LZI; -.
PDBsum; 1LZJ; -.
PDBsum; 1R7T; -.
PDBsum; 1R7U; -.
PDBsum; 1R7V; -.
PDBsum; 1R7X; -.
PDBsum; 1R7Y; -.
PDBsum; 1R80; -.
PDBsum; 1R81; -.
PDBsum; 1R82; -.
PDBsum; 1WSZ; -.
PDBsum; 1WT0; -.
PDBsum; 1WT1; -.
PDBsum; 1WT2; -.
PDBsum; 1WT3; -.
PDBsum; 1XZ6; -.
PDBsum; 1ZHJ; -.
PDBsum; 1ZI1; -.
PDBsum; 1ZI3; -.
PDBsum; 1ZI4; -.
PDBsum; 1ZI5; -.
PDBsum; 1ZIZ; -.
PDBsum; 1ZJ0; -.
PDBsum; 1ZJ1; -.
PDBsum; 1ZJ2; -.
PDBsum; 1ZJ3; -.
PDBsum; 1ZJO; -.
PDBsum; 1ZJP; -.
PDBsum; 2A8U; -.
PDBsum; 2A8W; -.
PDBsum; 2I7B; -.
PDBsum; 2O1F; -.
PDBsum; 2O1G; -.
PDBsum; 2O1H; -.
PDBsum; 2PGV; -.
PDBsum; 2PGY; -.
PDBsum; 2RIT; -.
PDBsum; 2RIX; -.
PDBsum; 2RIY; -.
PDBsum; 2RIZ; -.
PDBsum; 2RJ0; -.
PDBsum; 2RJ1; -.
PDBsum; 2RJ4; -.
PDBsum; 2RJ5; -.
PDBsum; 2RJ6; -.
PDBsum; 2RJ7; -.
PDBsum; 2RJ8; -.
PDBsum; 2RJ9; -.
PDBsum; 2Y7A; -.
PDBsum; 3I0C; -.
PDBsum; 3I0D; -.
PDBsum; 3I0E; -.
PDBsum; 3I0F; -.
PDBsum; 3I0G; -.
PDBsum; 3I0H; -.
PDBsum; 3I0I; -.
PDBsum; 3I0J; -.
PDBsum; 3I0K; -.
PDBsum; 3I0L; -.
PDBsum; 3IOH; -.
PDBsum; 3IOI; -.
PDBsum; 3IOJ; -.
PDBsum; 3SX3; -.
PDBsum; 3SX5; -.
PDBsum; 3SX7; -.
PDBsum; 3SX8; -.
PDBsum; 3SXA; -.
PDBsum; 3SXB; -.
PDBsum; 3SXC; -.
PDBsum; 3SXD; -.
PDBsum; 3SXE; -.
PDBsum; 3SXG; -.
PDBsum; 3U0X; -.
PDBsum; 3U0Y; -.
PDBsum; 3V0L; -.
PDBsum; 3V0M; -.
PDBsum; 3V0N; -.
PDBsum; 3V0O; -.
PDBsum; 3V0P; -.
PDBsum; 3V0Q; -.
PDBsum; 3ZGF; -.
PDBsum; 3ZGG; -.
PDBsum; 4C2S; -.
PDBsum; 4FQW; -.
PDBsum; 4FRA; -.
PDBsum; 4FRB; -.
PDBsum; 4FRD; -.
PDBsum; 4FRE; -.
PDBsum; 4FRH; -.
PDBsum; 4FRL; -.
PDBsum; 4FRM; -.
PDBsum; 4FRO; -.
PDBsum; 4FRP; -.
PDBsum; 4FRQ; -.
PDBsum; 4GBP; -.
PDBsum; 4KC1; -.
PDBsum; 4KC2; -.
PDBsum; 4KC4; -.
PDBsum; 4KXO; -.
PDBsum; 4Y62; -.
PDBsum; 4Y63; -.
PDBsum; 4Y64; -.
PDBsum; 5BXC; -.
PDBsum; 5C1G; -.
PDBsum; 5C1H; -.
PDBsum; 5C1L; -.
PDBsum; 5C36; -.
PDBsum; 5C38; -.
PDBsum; 5C3A; -.
PDBsum; 5C3B; -.
PDBsum; 5C3D; -.
PDBsum; 5C47; -.
PDBsum; 5C48; -.
PDBsum; 5C49; -.
PDBsum; 5C4B; -.
PDBsum; 5C4C; -.
PDBsum; 5C4D; -.
PDBsum; 5C4E; -.
PDBsum; 5C4F; -.
PDBsum; 5C8R; -.
PDBsum; 5CMF; -.
PDBsum; 5CMG; -.
PDBsum; 5CMH; -.
PDBsum; 5CMI; -.
PDBsum; 5CMJ; -.
PDBsum; 5CQL; -.
PDBsum; 5CQM; -.
PDBsum; 5CQN; -.
PDBsum; 5CQO; -.
PDBsum; 5CQP; -.
PDBsum; 5M79; -.
PDBsum; 5M7A; -.
PDBsum; 5M7B; -.
PDBsum; 5M7C; -.
PDBsum; 5M7D; -.
PDBsum; 5TJK; -.
PDBsum; 5TJL; -.
PDBsum; 5TJN; -.
PDBsum; 5TJO; -.
DisProt; DP00339; -.
ProteinModelPortal; P16442; -.
SMR; P16442; -.
BioGrid; 106546; 3.
BindingDB; P16442; -.
ChEMBL; CHEMBL2321639; -.
DrugBank; DB04681; BETA-METHYLLACTOSIDE.
DrugBank; DB04680; GALACTOSE GREASE.
DrugBank; DB03501; Galactose-uridine-5'-diphosphate.
DrugBank; DB04679; H TYPE I TRISACCHARIDE.
DrugBank; DB04678; H TYPE II TRISACCHARIDE.
DrugBank; DB07633; octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranoside.
DrugBank; DB03435; Uridine-5'-Diphosphate.
DrugBank; DB02196; Uridine-Diphosphate-N-Acetylgalactosamine.
CAZy; GT6; Glycosyltransferase Family 6.
iPTMnet; P16442; -.
PhosphoSitePlus; P16442; -.
BioMuta; ABO; -.
DMDM; 114949; -.
PeptideAtlas; P16442; -.
PRIDE; P16442; -.
ProteomicsDB; 53361; -.
DNASU; 28; -.
GeneID; 28; -.
KEGG; hsa:28; -.
CTD; 28; -.
DisGeNET; 28; -.
GeneCards; ABO; -.
HGNC; HGNC:79; ABO.
MIM; 110300; gene.
MIM; 616093; phenotype.
neXtProt; NX_P16442; -.
PharmGKB; PA24415; -.
HOVERGEN; HBG003563; -.
InParanoid; P16442; -.
KO; K00709; -.
PhylomeDB; P16442; -.
BioCyc; MetaCyc:HS10887-MONOMER; -.
BRENDA; 2.4.1.37; 2681.
BRENDA; 2.4.1.40; 2681.
UniPathway; UPA00378; -.
EvolutionaryTrace; P16442; -.
GeneWiki; ABO_(gene); -.
GenomeRNAi; 28; -.
PRO; PR:P16442; -.
Proteomes; UP000005640; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031982; C:vesicle; IBA:GO_Central.
GO; GO:0003823; F:antigen binding; IMP:CAFA.
GO; GO:0004381; F:fucosylgalactoside 3-alpha-galactosyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0004380; F:glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0030145; F:manganese ion binding; IMP:CAFA.
GO; GO:0000166; F:nucleotide binding; IMP:CAFA.
GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0009247; P:glycolipid biosynthetic process; IBA:GO_Central.
GO; GO:0030259; P:lipid glycosylation; IBA:GO_Central.
GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR005076; Glyco_trans_6.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
PANTHER; PTHR10462; PTHR10462; 1.
Pfam; PF03414; Glyco_transf_6; 1.
SUPFAM; SSF53448; SSF53448; 1.
1: Evidence at protein level;
3D-structure; Blood group antigen; Complete proteome;
Direct protein sequencing; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Manganese; Membrane; Metal-binding; Polymorphism;
Reference proteome; Secreted; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 354 Histo-blood group ABO system transferase.
/FTId=PRO_0000012268.
CHAIN 54 354 Fucosylglycoprotein alpha-N-
acetylgalactosaminyltransferase soluble
form.
/FTId=PRO_0000012269.
TOPO_DOM 1 32 Cytoplasmic. {ECO:0000255}.
TRANSMEM 33 53 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 54 354 Lumenal. {ECO:0000255}.
REGION 121 123 UDP-N-acetyl-galactosamine binding.
{ECO:0000244|PDB:1LZI,
ECO:0000244|PDB:1LZJ,
ECO:0000244|PDB:1R7Y,
ECO:0000244|PDB:1R80,
ECO:0000244|PDB:1R81,
ECO:0000244|PDB:1R82,
ECO:0000244|PDB:1WT3,
ECO:0000244|PDB:1ZI5,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJO,
ECO:0000244|PDB:1ZJP,
ECO:0000244|PDB:2A8U,
ECO:0000244|PDB:2A8W,
ECO:0000244|PDB:2O1H,
ECO:0000244|PDB:2RIX,
ECO:0000244|PDB:2RJ0,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ5,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:2Y7A,
ECO:0000244|PDB:3I0D,
ECO:0000244|PDB:3I0F,
ECO:0000244|PDB:3I0G,
ECO:0000244|PDB:3I0I,
ECO:0000244|PDB:3I0K,
ECO:0000244|PDB:3I0L,
ECO:0000244|PDB:3IOI,
ECO:0000244|PDB:3IOJ,
ECO:0000244|PDB:3SX3,
ECO:0000244|PDB:3SX5,
ECO:0000244|PDB:3SX7,
ECO:0000244|PDB:3SX8,
ECO:0000244|PDB:3SXA,
ECO:0000244|PDB:3SXB,
ECO:0000244|PDB:3SXC,
ECO:0000244|PDB:3SXD,
ECO:0000244|PDB:3SXE,
ECO:0000244|PDB:3SXG,
ECO:0000244|PDB:3U0Y,
ECO:0000244|PDB:3V0L,
ECO:0000244|PDB:3V0N,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:3ZGF,
ECO:0000244|PDB:3ZGG,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4FQW,
ECO:0000244|PDB:4FRA,
ECO:0000244|PDB:4FRB,
ECO:0000244|PDB:4FRD,
ECO:0000244|PDB:4FRE,
ECO:0000244|PDB:4FRH,
ECO:0000244|PDB:4FRL,
ECO:0000244|PDB:4FRM,
ECO:0000244|PDB:4FRO,
ECO:0000244|PDB:4FRP,
ECO:0000244|PDB:4FRQ,
ECO:0000244|PDB:4GBP,
ECO:0000244|PDB:4KC1,
ECO:0000244|PDB:4KC2,
ECO:0000244|PDB:4KC4,
ECO:0000269|PubMed:12198488,
ECO:0000269|PubMed:12972418,
ECO:0000269|PubMed:15475562,
ECO:0000269|PubMed:16326711,
ECO:0000269|PubMed:17259183}.
REGION 211 213 UDP-N-acetyl-galactosamine binding.
{ECO:0000244|PDB:1LZI,
ECO:0000244|PDB:1LZJ,
ECO:0000244|PDB:1R7Y,
ECO:0000244|PDB:1R80,
ECO:0000244|PDB:1R81,
ECO:0000244|PDB:1R82,
ECO:0000244|PDB:1WT1,
ECO:0000244|PDB:1WT2,
ECO:0000244|PDB:1WT3,
ECO:0000244|PDB:1ZI5,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJO,
ECO:0000244|PDB:1ZJP,
ECO:0000244|PDB:2A8U,
ECO:0000244|PDB:2A8W,
ECO:0000244|PDB:2O1H,
ECO:0000244|PDB:2RIX,
ECO:0000244|PDB:2RJ0,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ5,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:2Y7A,
ECO:0000244|PDB:3I0D,
ECO:0000244|PDB:3I0F,
ECO:0000244|PDB:3I0G,
ECO:0000244|PDB:3I0I,
ECO:0000244|PDB:3I0K,
ECO:0000244|PDB:3I0L,
ECO:0000244|PDB:3IOI,
ECO:0000244|PDB:3IOJ,
ECO:0000244|PDB:3SX3,
ECO:0000244|PDB:3SX5,
ECO:0000244|PDB:3SX7,
ECO:0000244|PDB:3SX8,
ECO:0000244|PDB:3SXA,
ECO:0000244|PDB:3SXB,
ECO:0000244|PDB:3SXC,
ECO:0000244|PDB:3SXD,
ECO:0000244|PDB:3SXE,
ECO:0000244|PDB:3SXG,
ECO:0000244|PDB:3U0Y,
ECO:0000244|PDB:3V0L,
ECO:0000244|PDB:3V0N,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:3ZGF,
ECO:0000244|PDB:3ZGG,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4FQW,
ECO:0000244|PDB:4FRA,
ECO:0000244|PDB:4FRB,
ECO:0000244|PDB:4FRD,
ECO:0000244|PDB:4FRE,
ECO:0000244|PDB:4FRH,
ECO:0000244|PDB:4FRL,
ECO:0000244|PDB:4FRM,
ECO:0000244|PDB:4FRO,
ECO:0000244|PDB:4FRP,
ECO:0000244|PDB:4FRQ,
ECO:0000244|PDB:4GBP,
ECO:0000244|PDB:4KC1,
ECO:0000244|PDB:4KC2,
ECO:0000244|PDB:4KC4,
ECO:0000269|PubMed:12198488,
ECO:0000269|PubMed:12972418,
ECO:0000269|PubMed:15475562,
ECO:0000269|PubMed:16326711,
ECO:0000269|PubMed:17259183}.
ACT_SITE 303 303 Nucleophile.
{ECO:0000250|UniProtKB:P14769}.
METAL 211 211 Manganese. {ECO:0000244|PDB:1LZJ,
ECO:0000244|PDB:1R80,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJP,
ECO:0000244|PDB:2A8U,
ECO:0000244|PDB:2O1H,
ECO:0000244|PDB:2RIX,
ECO:0000244|PDB:2RJ0,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ5,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:3I0F,
ECO:0000244|PDB:3IOI,
ECO:0000244|PDB:3IOJ,
ECO:0000244|PDB:3SX3,
ECO:0000244|PDB:3SX5,
ECO:0000244|PDB:3SX7,
ECO:0000244|PDB:3SXA,
ECO:0000244|PDB:3SXB,
ECO:0000244|PDB:3SXD,
ECO:0000244|PDB:3SXE,
ECO:0000244|PDB:3SXG,
ECO:0000244|PDB:3U0Y,
ECO:0000244|PDB:3V0L,
ECO:0000244|PDB:3V0M,
ECO:0000244|PDB:3V0N,
ECO:0000244|PDB:3V0O,
ECO:0000244|PDB:3V0P,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:3ZGF,
ECO:0000244|PDB:3ZGG,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4FRB,
ECO:0000244|PDB:4FRD,
ECO:0000244|PDB:4FRH,
ECO:0000244|PDB:4FRL,
ECO:0000244|PDB:4FRO,
ECO:0000244|PDB:4FRP,
ECO:0000244|PDB:4FRQ,
ECO:0000244|PDB:4GBP,
ECO:0000269|PubMed:12198488,
ECO:0000269|PubMed:12972418,
ECO:0000269|PubMed:16326711,
ECO:0000269|PubMed:17259183}.
METAL 213 213 Manganese. {ECO:0000244|PDB:1LZJ,
ECO:0000244|PDB:1R80,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJP,
ECO:0000244|PDB:2A8U,
ECO:0000244|PDB:2O1H,
ECO:0000244|PDB:2RIX,
ECO:0000244|PDB:2RJ0,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ5,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:3I0F,
ECO:0000244|PDB:3IOI,
ECO:0000244|PDB:3IOJ,
ECO:0000244|PDB:3SX3,
ECO:0000244|PDB:3SX5,
ECO:0000244|PDB:3SX7,
ECO:0000244|PDB:3SXA,
ECO:0000244|PDB:3SXB,
ECO:0000244|PDB:3SXD,
ECO:0000244|PDB:3SXE,
ECO:0000244|PDB:3SXG,
ECO:0000244|PDB:3U0Y,
ECO:0000244|PDB:3V0L,
ECO:0000244|PDB:3V0M,
ECO:0000244|PDB:3V0N,
ECO:0000244|PDB:3V0O,
ECO:0000244|PDB:3V0P,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:3ZGF,
ECO:0000244|PDB:3ZGG,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4FRB,
ECO:0000244|PDB:4FRD,
ECO:0000244|PDB:4FRH,
ECO:0000244|PDB:4FRL,
ECO:0000244|PDB:4FRO,
ECO:0000244|PDB:4FRP,
ECO:0000244|PDB:4FRQ,
ECO:0000244|PDB:4GBP,
ECO:0000269|PubMed:12198488,
ECO:0000269|PubMed:12972418,
ECO:0000269|PubMed:16326711,
ECO:0000269|PubMed:17259183}.
BINDING 126 126 UDP-N-acetyl-galactosamine.
{ECO:0000244|PDB:1LZI,
ECO:0000244|PDB:1LZJ,
ECO:0000244|PDB:1R7Y,
ECO:0000244|PDB:1R80,
ECO:0000244|PDB:1R81,
ECO:0000244|PDB:1R82,
ECO:0000244|PDB:1WT1,
ECO:0000244|PDB:1WT2,
ECO:0000244|PDB:1WT3,
ECO:0000244|PDB:1ZI5,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJO,
ECO:0000244|PDB:1ZJP,
ECO:0000244|PDB:2A8U,
ECO:0000244|PDB:2A8W,
ECO:0000244|PDB:2O1H,
ECO:0000244|PDB:2RIX,
ECO:0000244|PDB:2RJ0,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ5,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:2Y7A,
ECO:0000244|PDB:3I0D,
ECO:0000244|PDB:3I0F,
ECO:0000244|PDB:3I0G,
ECO:0000244|PDB:3I0I,
ECO:0000244|PDB:3I0K,
ECO:0000244|PDB:3I0L,
ECO:0000244|PDB:3IOI,
ECO:0000244|PDB:3IOJ,
ECO:0000244|PDB:3SX3,
ECO:0000244|PDB:3SX5,
ECO:0000244|PDB:3SX7,
ECO:0000244|PDB:3SX8,
ECO:0000244|PDB:3SXA,
ECO:0000244|PDB:3SXB,
ECO:0000244|PDB:3SXC,
ECO:0000244|PDB:3SXD,
ECO:0000244|PDB:3SXE,
ECO:0000244|PDB:3SXG,
ECO:0000244|PDB:3U0Y,
ECO:0000244|PDB:3V0L,
ECO:0000244|PDB:3V0N,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:3ZGF,
ECO:0000244|PDB:3ZGG,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4FQW,
ECO:0000244|PDB:4FRA,
ECO:0000244|PDB:4FRB,
ECO:0000244|PDB:4FRD,
ECO:0000244|PDB:4FRE,
ECO:0000244|PDB:4FRH,
ECO:0000244|PDB:4FRL,
ECO:0000244|PDB:4FRM,
ECO:0000244|PDB:4FRO,
ECO:0000244|PDB:4FRP,
ECO:0000244|PDB:4FRQ,
ECO:0000244|PDB:4GBP,
ECO:0000244|PDB:4KC1,
ECO:0000244|PDB:4KC2,
ECO:0000244|PDB:4KC4,
ECO:0000269|PubMed:12198488,
ECO:0000269|PubMed:12972418,
ECO:0000269|PubMed:15475562,
ECO:0000269|PubMed:16326711,
ECO:0000269|PubMed:17259183}.
BINDING 233 233 Glycoprotein fucosyl-galactosyl group.
{ECO:0000244|PDB:1ZHJ,
ECO:0000244|PDB:1ZI3,
ECO:0000244|PDB:1ZI4,
ECO:0000244|PDB:1ZI5,
ECO:0000244|PDB:1ZJ1,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJ3,
ECO:0000244|PDB:2A8U,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:3SX3,
ECO:0000244|PDB:3SX7,
ECO:0000244|PDB:3SX8,
ECO:0000244|PDB:3SXA,
ECO:0000244|PDB:3SXG,
ECO:0000244|PDB:3V0M,
ECO:0000244|PDB:3V0N,
ECO:0000244|PDB:3V0O,
ECO:0000244|PDB:3V0P,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:3ZGF,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4FQW,
ECO:0000244|PDB:4FRA,
ECO:0000244|PDB:4FRB,
ECO:0000244|PDB:4FRD,
ECO:0000244|PDB:4FRE,
ECO:0000244|PDB:4FRH,
ECO:0000244|PDB:4FRL,
ECO:0000244|PDB:4FRM,
ECO:0000244|PDB:4FRO,
ECO:0000244|PDB:4FRP,
ECO:0000244|PDB:4FRQ,
ECO:0000244|PDB:4GBP,
ECO:0000244|PDB:4KC1,
ECO:0000244|PDB:4KC2,
ECO:0000244|PDB:4KC4,
ECO:0000269|PubMed:16326711}.
BINDING 245 245 Glycoprotein fucosyl-galactosyl group.
{ECO:0000244|PDB:1R7T,
ECO:0000244|PDB:1R7U,
ECO:0000244|PDB:1WT2,
ECO:0000244|PDB:1ZHJ,
ECO:0000244|PDB:1ZI3,
ECO:0000244|PDB:1ZI4,
ECO:0000244|PDB:1ZI5,
ECO:0000244|PDB:1ZIZ,
ECO:0000244|PDB:1ZJ0,
ECO:0000244|PDB:1ZJ1,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJ3,
ECO:0000244|PDB:2A8U,
ECO:0000244|PDB:2RIY,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ6,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:3SX3,
ECO:0000244|PDB:3SX5,
ECO:0000244|PDB:3SX7,
ECO:0000244|PDB:3SX8,
ECO:0000244|PDB:3SXA,
ECO:0000244|PDB:3SXB,
ECO:0000244|PDB:3SXC,
ECO:0000244|PDB:3SXD,
ECO:0000244|PDB:3SXE,
ECO:0000244|PDB:3SXG,
ECO:0000244|PDB:3V0M,
ECO:0000244|PDB:3V0O,
ECO:0000244|PDB:3V0P,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4FQW,
ECO:0000244|PDB:4FRA,
ECO:0000244|PDB:4FRB,
ECO:0000244|PDB:4FRD,
ECO:0000244|PDB:4FRE,
ECO:0000244|PDB:4FRH,
ECO:0000244|PDB:4FRL,
ECO:0000244|PDB:4FRM,
ECO:0000244|PDB:4FRO,
ECO:0000244|PDB:4FRP,
ECO:0000244|PDB:4FRQ,
ECO:0000244|PDB:4GBP,
ECO:0000244|PDB:4KC1,
ECO:0000244|PDB:4KC2,
ECO:0000244|PDB:4KC4,
ECO:0000269|PubMed:12972418,
ECO:0000269|PubMed:15475562,
ECO:0000269|PubMed:16326711}.
BINDING 303 303 Glycoprotein fucosyl-galactosyl group.
{ECO:0000244|PDB:1R7T,
ECO:0000244|PDB:1R7U,
ECO:0000244|PDB:1WT2,
ECO:0000244|PDB:1ZHJ,
ECO:0000244|PDB:1ZI3,
ECO:0000244|PDB:1ZI4,
ECO:0000244|PDB:1ZI5,
ECO:0000244|PDB:1ZIZ,
ECO:0000244|PDB:1ZJ0,
ECO:0000244|PDB:1ZJ1,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJ3,
ECO:0000244|PDB:2A8U,
ECO:0000244|PDB:2RIY,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ6,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:3I0G,
ECO:0000244|PDB:3I0L,
ECO:0000244|PDB:3IOI,
ECO:0000244|PDB:3SX3,
ECO:0000244|PDB:3SX5,
ECO:0000244|PDB:3SX7,
ECO:0000244|PDB:3SX8,
ECO:0000244|PDB:3SXA,
ECO:0000244|PDB:3SXB,
ECO:0000244|PDB:3SXC,
ECO:0000244|PDB:3SXD,
ECO:0000244|PDB:3SXE,
ECO:0000244|PDB:3SXG,
ECO:0000244|PDB:3V0L,
ECO:0000244|PDB:3V0M,
ECO:0000244|PDB:3V0O,
ECO:0000244|PDB:3V0P,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:3ZGG,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4FQW,
ECO:0000244|PDB:4FRA,
ECO:0000244|PDB:4FRB,
ECO:0000244|PDB:4FRD,
ECO:0000244|PDB:4FRE,
ECO:0000244|PDB:4FRH,
ECO:0000244|PDB:4FRL,
ECO:0000244|PDB:4FRM,
ECO:0000244|PDB:4FRO,
ECO:0000244|PDB:4FRP,
ECO:0000244|PDB:4FRQ,
ECO:0000244|PDB:4GBP,
ECO:0000244|PDB:4KC1,
ECO:0000244|PDB:4KC2,
ECO:0000244|PDB:4KC4,
ECO:0000269|PubMed:12972418,
ECO:0000269|PubMed:15475562,
ECO:0000269|PubMed:16326711}.
BINDING 326 326 Glycoprotein fucosyl-galactosyl group.
{ECO:0000244|PDB:1R7T,
ECO:0000244|PDB:1ZI4,
ECO:0000244|PDB:1ZI5,
ECO:0000244|PDB:1ZJ2,
ECO:0000244|PDB:1ZJ3,
ECO:0000244|PDB:2RIY,
ECO:0000244|PDB:2RJ1,
ECO:0000244|PDB:2RJ4,
ECO:0000244|PDB:2RJ6,
ECO:0000244|PDB:2RJ7,
ECO:0000244|PDB:2RJ8,
ECO:0000244|PDB:2RJ9,
ECO:0000244|PDB:3V0M,
ECO:0000244|PDB:3V0O,
ECO:0000244|PDB:3V0P,
ECO:0000244|PDB:3V0Q,
ECO:0000244|PDB:4C2S,
ECO:0000244|PDB:4KC1,
ECO:0000244|PDB:4KC2,
ECO:0000244|PDB:4KC4,
ECO:0000269|PubMed:12972418,
ECO:0000269|PubMed:16326711}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 35 35 G -> R (in dbSNP:rs8176696).
{ECO:0000269|Ref.9}.
/FTId=VAR_019147.
VARIANT 36 36 V -> F (in dbSNP:rs688976).
{ECO:0000269|Ref.9}.
/FTId=VAR_019148.
VARIANT 63 63 R -> H (in dbSNP:rs549446).
{ECO:0000269|Ref.9}.
/FTId=VAR_019149.
VARIANT 74 74 P -> S (in dbSNP:rs512770).
{ECO:0000269|PubMed:12829588,
ECO:0000269|Ref.9}.
/FTId=VAR_019150.
VARIANT 80 81 CR -> W.
/FTId=VAR_003408.
VARIANT 156 156 P -> L (in allele A2; dbSNP:rs1053878).
{ECO:0000269|PubMed:12829588,
ECO:0000269|PubMed:7598760,
ECO:0000269|PubMed:8839869,
ECO:0000269|Ref.5, ECO:0000269|Ref.9}.
/FTId=VAR_003409.
VARIANT 161 161 R -> H (in dbSNP:rs8176738).
{ECO:0000269|Ref.9}.
/FTId=VAR_019151.
VARIANT 163 163 T -> M (in allele Aw08;
dbSNP:rs55756402).
{ECO:0000269|PubMed:12829588}.
/FTId=VAR_036738.
VARIANT 176 176 R -> G (in allele Aw08 and allele Bw08;
dbSNP:rs7853989).
{ECO:0000269|PubMed:12829588,
ECO:0000269|PubMed:15104652,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8839869,
ECO:0000269|Ref.15, ECO:0000269|Ref.5,
ECO:0000269|Ref.9}.
/FTId=VAR_003410.
VARIANT 198 198 R -> W (in allele Aw07).
{ECO:0000269|PubMed:12829588}.
/FTId=VAR_036739.
VARIANT 199 199 R -> C (in dbSNP:rs8176739).
{ECO:0000269|Ref.9}.
/FTId=VAR_019152.
VARIANT 214 214 M -> R (in allele Bel01; loss of
manganese binding and reduced catalytic
activity). {ECO:0000269|PubMed:17259183,
ECO:0000269|PubMed:8839869}.
/FTId=VAR_036740.
VARIANT 216 216 F -> I (in dbSNP:rs8176740).
{ECO:0000269|PubMed:8839869,
ECO:0000269|Ref.9}.
/FTId=VAR_019153.
VARIANT 223 223 E -> D (in allele B106).
{ECO:0000269|PubMed:8839869}.
/FTId=VAR_036741.
VARIANT 230 230 G -> R (in group B transferase; lower-
level protein expression and
intracellular cytoplasmic mislocation).
{ECO:0000269|PubMed:18513251}.
/FTId=VAR_055227.
VARIANT 234 234 P -> A (in allele B(A)).
{ECO:0000269|PubMed:10462501}.
/FTId=VAR_072628.
VARIANT 235 235 G -> S (in allele Bw08; dbSNP:rs8176743).
{ECO:0000269|PubMed:12829588,
ECO:0000269|PubMed:15104652,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18513251,
ECO:0000269|PubMed:8839869,
ECO:0000269|Ref.15, ECO:0000269|Ref.5,
ECO:0000269|Ref.9}.
/FTId=VAR_003411.
VARIANT 257 257 P -> L (in dbSNP:rs8176745).
/FTId=VAR_033540.
VARIANT 266 266 L -> M (in allele Bw08; dbSNP:rs8176746).
{ECO:0000269|PubMed:12829588,
ECO:0000269|PubMed:1449469,
ECO:0000269|PubMed:15104652,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18513251,
ECO:0000269|PubMed:8839869,
ECO:0000269|Ref.5, ECO:0000269|Ref.9}.
/FTId=VAR_003412.
VARIANT 268 268 G -> A (in allele Bw08; dbSNP:rs8176747).
{ECO:0000269|PubMed:12829588,
ECO:0000269|PubMed:1449469,
ECO:0000269|PubMed:15104652,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18513251,
ECO:0000269|PubMed:8839869,
ECO:0000269|Ref.9}.
/FTId=VAR_003413.
VARIANT 268 268 G -> R (in allele Aw08;
dbSNP:rs41302905).
{ECO:0000269|PubMed:12829588}.
/FTId=VAR_033541.
VARIANT 277 277 V -> M (in dbSNP:rs8176748).
{ECO:0000269|PubMed:8839869,
ECO:0000269|Ref.9}.
/FTId=VAR_019154.
VARIANT 288 288 M -> R. {ECO:0000269|PubMed:12829588}.
/FTId=VAR_036742.
VARIANT 291 291 D -> N (in allele B104).
{ECO:0000269|PubMed:8839869}.
/FTId=VAR_036743.
VARIANT 346 346 K -> M (in allele Bw08).
{ECO:0000269|PubMed:12829588,
ECO:0000269|Ref.15}.
/FTId=VAR_036744.
VARIANT 352 352 R -> G (in allele A107).
{ECO:0000269|PubMed:8839869}.
/FTId=VAR_036745.
VARIANT 352 352 R -> W (in allele A106 and allele B3).
{ECO:0000269|PubMed:8839869}.
/FTId=VAR_003414.
MUTAGEN 214 214 M->T,V: Alters substrate specificity so
that both UDP-N-acetyl-D-galactosamine
and UDP-galactose are utilized.
{ECO:0000269|PubMed:17259183}.
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.
{ECO:0000269|PubMed:12198488}.
STRAND 82 84 {ECO:0000244|PDB:5M7D}.
STRAND 93 95 {ECO:0000244|PDB:5M7D}.
HELIX 102 111 {ECO:0000244|PDB:5M7D}.
STRAND 115 122 {ECO:0000244|PDB:5M7D}.
HELIX 124 129 {ECO:0000244|PDB:5M7D}.
HELIX 130 140 {ECO:0000244|PDB:5M7D}.
STRAND 145 154 {ECO:0000244|PDB:5M7D}.
HELIX 156 158 {ECO:0000244|PDB:5M7D}.
STRAND 168 174 {ECO:0000244|PDB:5M7D}.
HELIX 181 198 {ECO:0000244|PDB:5M7D}.
HELIX 200 203 {ECO:0000244|PDB:5M7D}.
STRAND 205 210 {ECO:0000244|PDB:5M7D}.
STRAND 212 216 {ECO:0000244|PDB:5M7D}.
HELIX 222 224 {ECO:0000244|PDB:5M7D}.
STRAND 226 232 {ECO:0000244|PDB:5M7D}.
TURN 234 238 {ECO:0000244|PDB:5M7D}.
HELIX 241 243 {ECO:0000244|PDB:5M7D}.
STRAND 269 273 {ECO:0000244|PDB:5M7D}.
HELIX 274 293 {ECO:0000244|PDB:5M7D}.
HELIX 301 312 {ECO:0000244|PDB:5M7D}.
STRAND 316 319 {ECO:0000244|PDB:5M7D}.
HELIX 321 323 {ECO:0000244|PDB:5M7D}.
HELIX 327 330 {ECO:0000244|PDB:5M7D}.
STRAND 341 343 {ECO:0000244|PDB:5M7D}.
HELIX 348 351 {ECO:0000244|PDB:5M7D}.
SEQUENCE 354 AA; 40934 MW; A03DA16E630C1608 CRC64;
MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG FCMAVREPDH
LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF NIDILNEQFR LQNTTIGLTV
FAIKKYVAFL KLFLETAEKH FMVGHRVHYY VFTDQPAAVP RVTLGTGRQL SVLEVRAYKR
WQDVSMRRME MISDFCERRF LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPGFYGSS
REAFTYERRP QSQAYIPKDE GDFYYLGGFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW
HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA VRNP


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