Protein Annotations for NAGAT, BGAT

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Name	Gene Symbol	Rec Full Name	Protein Information	Quick Quote	Price, Turnaround
BGAT_HUMAN, Homo sapiens (human)	ABO	NAGAT	Functions		Quote
BGAT_HUMAN, Homo sapiens (human)	ABO	NAGAT	Protein Domains		Quote

Protein Names

Recommended name:	Histo-blood group ABO system transferase;
Alternative name(s):	Fucosylglycoprotein 3-alpha-galactosyltransferase Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-galactosyltransferase Histo-blood group A transferase Histo-blood group B transferase NAGAT Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form

Protein IDs
(Accession numbers)

UniProtKB	P16442
NCBI RefSeq	NP_065202.2, NM_020469.2.

Organism

Latin Name/ (Common Name)	Homo sapiens (Human).
Taxonomic Identifier (NCBI)	9606

Gene Names

ABO [GenPool]

GeneID

Genome
Annotation (Ensembl)

Protein Sequence

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

General annotation

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.
Cofactor	Binds 1 manganese ion per subunit.
Subunit structure
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.
Tissue specificity
Induction
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 byproteolytic processing.
Involvement in disease

References

"Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc alpha 1-->2Gal alpha 1-->3GalNAc transferase (histo-bloodgroup A transferase) mRNA.";,Yamamoto F., Marken J., Tsuji T., White T., Clausen H., Hakomori S.;,J. Biol. Chem. 265:1146-1151(1990)., PubMeb:2104828
"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)., PubMeb:2333095 DOI:10.1038/345229a0
"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)., PubMeb:7598760 DOI:10.1006/bbrc.1995.1044
Bennett E.P., Steffensen R., Clausen H., Weghuis D.O.,Geurts van Kessel A.;,Biochem. Biophys. Res. Commun. 211:347-347(1995)., PubMeb:7779106 DOI:10.1006/bbrc.1995.1817
"Human histo-blood group ABO gene locus alleles.";,Yamamoto F.;,Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
"A weak blood group A phenotype caused by a translation-initiatormutation in the ABO gene.";,Seltsam A., Das Gupta C., Bade-Doeding C., Blasczyk R.;,Transfusion 46:434-440(2006).,PubMeb:16533287 DOI:10.1111/j.1537-2995.2006.00740.x
"Weak blood group B phenotypes may be caused by variations in theCCAAT-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).,PubMeb:17764507 DOI:10.1111/j.1537-2995.2007.01475.x
"Aberrant intracellular trafficking of a variant Bglycosyltransferase.";,Seltsam A., Gruger D., Just B., Figueiredo C., Gupta C.D.,Deluca D.S., Blasczyk R.;,Transfusion 48:1898-1905(2008).,PubMeb:18513251 DOI:10.1111/j.1537-2995.2008.01782.x
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
"The status, quality, and expansion of the NIH full-length cDNAproject: the Mammalian Gene Collection (MGC).";,Genome Res. 14:2121-2127(2004).,PubMeb:15489334 DOI:10.1101/gr.2596504
"The nature of diversity and diversification at the ABO locus.";,Seltsam A., Hallensleben M., Kollmann A., Blasczyk R.;,Blood 102:3035-3042(2003).,PubMeb:12829588 DOI:10.1182/blood-2003-03-0955
"Molecular genetic analysis of variant phenotypes of the ABO bloodgroup 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)., PubMeb:8839869
"Heterogeneity of the blood group Ax allele: genetic recombination ofcommon alleles can result in the Ax phenotype.";,Olsson M.L., Chester M.A.;,Transfus. Med. 8:231-238(1998)., PubMeb:9800297 DOI:10.1046/j.1365-3148.1998.00161.x
"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).,PubMeb:15104652 DOI:10.1111/j.1537-2995.2004.03346.x
"A novel B Transferase.";,Seltsam A., Hallensleben M., Salama A., Blasczyk R.;,Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
"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)., PubMeb:1449469 DOI:10.1016/0006-291X(92)91538-2
"Sugar-nucleotide donor specificity of histo-blood group A and Btransferases is based on amino acid substitutions.";,Yamamoto F., Hakomori S.;,J. Biol. Chem. 265:19257-19262(1990)., PubMeb:2121736
"The structural basis for specificity in human ABO(H) blood groupbiosynthesis.";,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)., PubMeb:12198488 DOI:10.1038/nsb832
"A single point mutation reverses the donor specificity of human bloodgroup 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).,PubMeb:12529355 DOI:10.1074/jbc.M212002200
"The influence of an intramolecular hydrogen bond in differentialrecognition of inhibitory acceptor analogs by human ABO(H) blood groupA 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).,PubMeb:12972418 DOI:10.1074/jbc.M308770200
"Structural basis for the inactivity of human blood group O2glycosyltransferase.";,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).,PubMeb:15475562 DOI:10.1074/jbc.M500897200
"Differential recognition of the type I and II H antigen acceptors bythe 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).,PubMeb:16326711 DOI:10.1074/jbc.M507620200
"Structural effects of naturally occurring human blood group Bgalactosyltransferase 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).,PubMeb:17259183 DOI:10.1074/jbc.M610998200

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Gene & Protein

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Protein Domain Databases

InterPro	IPR005076, Glyco_trans_6.
Gene3D
PANTHER	PTHR10462, Glyco_trans_6; 1.
Pfam	PF03414, Glyco_transf_6; 1.
PRINTS
SUPFAM
PROSITE

3D Structure
Database (PDB)

Entry	Method	Resolution (A)	Chain	Positions	PDBsum
1LZ0	X-ray	1.80 A	A	64-354	[>>]
1LZ7	X-ray	1.65 A	A	64-354	[>>]
1LZI	X-ray	1.35 A	A	64-354	[>>]
1LZJ	X-ray	1.32 A	A	64-354	[>>]
1R7T	X-ray	2.09 A	A	64-345	[>>]
1R7U	X-ray	1.61 A	A	64-345	[>>]
1R7V	X-ray	2.09 A	A	64-345	[>>]
1R7X	X-ray	1.97 A	A	64-345	[>>]
1R7Y	X-ray	1.75 A	A	64-345	[>>]
1R80	X-ray	1.65 A	A	64-345	[>>]
1R81	X-ray	1.75 A	A	64-345	[>>]
1R82	X-ray	1.55 A	A	64-345	[>>]
1WSZ	X-ray	1.59 A	A	64-354	[>>]
1WT0	X-ray	1.80 A	A	64-354	[>>]
1WT1	X-ray	1.55 A	A	64-354	[>>]
1WT2	X-ray	1.90 A	A	64-354	[>>]
1WT3	X-ray	1.80 A	A	64-354	[>>]
1XZ6	X-ray	1.55 A	A	64-354	[>>]
1ZHJ	X-ray	1.59 A	A	64-354	[>>]
1ZI1	X-ray	1.57 A	A	64-354	[>>]
1ZI3	X-ray	1.69 A	A	64-354	[>>]
1ZI4	X-ray	1.85 A	A	64-354	[>>]
1ZI5	X-ray	1.55 A	A	64-354	[>>]
1ZIZ	X-ray	1.49 A	A	64-354	[>>]
1ZJ0	X-ray	1.67 A	A	64-354	[>>]
1ZJ1	X-ray	1.65 A	A	64-354	[>>]
1ZJ2	X-ray	1.69 A	A	64-354	[>>]
1ZJ3	X-ray	1.69 A	A	64-354	[>>]
1ZJO	X-ray	1.64 A	A	64-354	[>>]
1ZJP	X-ray	1.59 A	A	64-354	[>>]
2A8U	X-ray	1.69 A	A	64-354	[>>]
2A8W	X-ray	1.59 A	A	64-354	[>>]
2I7B	X-ray	1.99 A	A	64-354	[>>]
2O1F	X-ray	1.99 A	A	64-354	[>>]
2O1G	X-ray	1.71 A	A	64-354	[>>]
2O1H	X-ray	1.67 A	A	64-354	[>>]
2PGV	X-ray	1.79 A	A	64-354	[>>]
2PGY	X-ray	2.39 A	A	64-354	[>>]
2RIT	X-ray	1.43 A	A	64-354	[>>]
2RIX	X-ray	1.75 A	A	64-354	[>>]
2RIY	X-ray	1.55 A	A	64-354	[>>]
2RIZ	X-ray	1.45 A	A	64-354	[>>]
2RJ0	X-ray	1.52 A	A	64-354	[>>]
2RJ1	X-ray	1.55 A	A	64-354	[>>]
2RJ4	X-ray	1.47 A	A	64-354	[>>]
2RJ5	X-ray	1.45 A	A	64-354	[>>]
2RJ6	X-ray	1.41 A	A	64-354	[>>]
2RJ7	X-ray	1.70 A	A	64-354	[>>]
2RJ8	X-ray	1.69 A	A	64-354	[>>]
2RJ9	X-ray	1.69 A	A	64-354	[>>]
3I0C	X-ray	1.55 A	A	69-354	[>>]
3I0D	X-ray	1.90 A	A	69-354	[>>]
3I0E	X-ray	1.81 A	A	69-354	[>>]
3I0F	X-ray	1.56 A	A	69-354	[>>]
3I0G	X-ray	1.40 A	A	69-354	[>>]
3I0H	X-ray	2.00 A	A	69-354	[>>]
3I0I	X-ray	1.90 A	X	69-354	[>>]
3I0J	X-ray	1.48 A	A	69-354	[>>]
3I0K	X-ray	2.20 A	A	69-354	[>>]
3I0L	X-ray	1.60 A	A	69-354	[>>]
3IOH	X-ray	1.25 A	A	64-354	[>>]
3IOI	X-ray	1.45 A	A	64-354	[>>]
3IOJ	X-ray	1.65 A	A/B	64-354	[>>]

Sequence
Annotation

Feature key	Position(s)	Length	Description
Polypeptide chain	1 - 354	354	Histo-blood group ABO system transferase. /FTId=PRO_0000012268.
Polypeptide chain	54 - 354	301	Fucosylglycoprotein alpha-N- /FTId=PRO_0000012269.
Topological domain	1 - 32	32	Cytoplasmic (Potential).
Topological domain	54 - 354	301	Lumenal (Potential).
Transmembrane region	33 - 53	21	Helical; Signal-anchor for type II
Region	121 - 123	3	UDP-N-acetyl-galactosamine binding.
Region	211 - 213	3	UDP-N-acetyl-galactosamine binding.
Metal ion	211	1	Manganese.
Metal ion	213	1	Manganese.
Binding	126	1	UDP-N-acetyl-galactosamine.
Binding	233	1	Glycoprotein fucosyl-galactosyl group.
Binding	245	1	Glycoprotein fucosyl-galactosyl group.
Binding	303	1	Glycoprotein fucosyl-galactosyl group.
Binding	326	1	Glycoprotein fucosyl-galactosyl group.
Glycosylation site	113	1	N-linked (GlcNAc...) (Potential).
Natural variance	35	1	G -> R (in dbSNP:rs8176696). /FTId=VAR_019147.
Natural variance	36	1	V -> F (in dbSNP:rs688976). /FTId=VAR_019148.
Natural variance	63	1	R -> H (in dbSNP:rs549446). /FTId=VAR_019149.
Natural variance	74	1	P -> S (in dbSNP:rs512770). /FTId=VAR_019150.
Natural variance	80 - 81	2	CR -> W. /FTId=VAR_003408.
Natural variance	156	1	P -> L (in allele A2; dbSNP:rs1053878). /FTId=VAR_003409.
Natural variance	161	1	R -> H (in dbSNP:rs8176738). /FTId=VAR_019151.
Natural variance	163	1	T -> M (in allele Aw08; /FTId=VAR_036738.
Natural variance	176	1	R -> G (in group B transferase; /FTId=VAR_003410.
Natural variance	198	1	R -> W (in allele Aw07; /FTId=VAR_036739.
Natural variance	199	1	R -> C (in dbSNP:rs8176739). /FTId=VAR_019152.
Natural variance	214	1	M -> R (in allele Bel01; loss of /FTId=VAR_036740.
Natural variance	216	1	F -> I (in dbSNP:rs8176740). /FTId=VAR_019153.
Natural variance	223	1	E -> D (in allele B106). /FTId=VAR_036741.
Natural variance	230	1	G -> R (in group B transferase; lower- /FTId=VAR_055227.
Natural variance	235	1	G -> S (in group B transferase; /FTId=VAR_003411.
Natural variance	257	1	P -> L (in dbSNP:rs8176745). /FTId=VAR_033540.
Natural variance	266	1	L -> M (in group B transferase; important /FTId=VAR_003412.
Natural variance	268	1	G -> A (in group B transferase; important /FTId=VAR_003413.
Natural variance	268	1	G -> R (in dbSNP:rs8176747). /FTId=VAR_033541.
Natural variance	277	1	V -> M (in dbSNP:rs8176748). /FTId=VAR_019154.
Natural variance	288	1	M -> R. /FTId=VAR_036742.
Natural variance	291	1	D -> N (in allele B104). /FTId=VAR_036743.
Natural variance	346	1	K -> M (in allele Bw08). /FTId=VAR_036744.
Natural variance	352	1	R -> G (in allele A107). /FTId=VAR_036745.
Natural variance	352	1	R -> W (in allele A106 and allele B3). /FTId=VAR_003414.
Mutagenesis	214	1	M->T,V: Alters substrate specificity so
Mutagenesis	234	1	P->S: Alters substrate specificity of
Mutagenesis	303	1	E->A: Decreases specific activity of
Strand	82 - 84	3
Strand	93 - 95	3
Strand	115 - 122	8
Strand	145 - 154	10
Strand	168 - 174	7
Strand	205 - 210	6
Strand	212 - 216	5
Strand	226 - 232	7
Strand	269 - 273	5
Strand	316 - 319	4
Strand	341 - 343	3
Helix	102 - 110	9
Helix	124 - 129	6
Helix	130 - 140	11
Helix	156 - 158	3
Helix	197 - 203	7
Helix	222 - 224	3
Helix	241 - 243	3
Helix	274 - 293	20
Helix	301 - 312	12
Helix	321 - 323	3
Helix	327 - 330	4
Helix	348 - 351	4
Turn	111 - 113	3
Turn	234 - 238	5

Protein-protein
Interaction
Databases

DIP
IntAct
MINT
STRING	P16442

Binary Interactions

With

Entry

#Exp.

IntAct

Enzyme and Pathway Databases

Pathway Interaction DB
Reactome

Phylogenomic Database

HOVERGEN	HBG003563
InParanoid	P16442
OMA
OrthoDB

Proteomics
Database (PRIDE)

P16442

Comparative
Toxicogenomics
Database (CTD)

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