ABO

Functionⁱ

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 activityⁱ

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.2 Publications

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.2 Publications

Cofactorⁱ

Mn²⁺1 PublicationNote: Binds 1 Mn²⁺ ion per subunit.1 Publication

Pathwayⁱ: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	126	UDP-N-acetyl-galactosamineCombined sources5 Publications	1
Metal bindingⁱ	211	ManganeseCombined sources4 Publications	1
Metal bindingⁱ	213	ManganeseCombined sources4 Publications	1
Binding siteⁱ	233	Glycoprotein fucosyl-galactosyl groupCombined sources1 Publication	1
Binding siteⁱ	245	Glycoprotein fucosyl-galactosyl groupCombined sources3 Publications	1
Active siteⁱ	303	NucleophileBy similarity	1
Binding siteⁱ	303	Glycoprotein fucosyl-galactosyl groupCombined sources3 Publications	1
Binding siteⁱ	326	Glycoprotein fucosyl-galactosyl groupCombined sources2 Publications	1

GO - Molecular functionⁱ

antigen binding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 12198488
fucosylgalactoside 3-alpha-galactosyltransferase activity Source: UniProtKB-EC
glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC
manganese ion binding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 12198488
nucleotide binding
Source: CAFA
Inferred from mutant phenotypeⁱ
- 12198488
transferase activity, transferring glycosyl groups Source: GO_Central

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

carbohydrate metabolic process Source: InterPro
glycolipid biosynthetic process Source: GO_Central
lipid glycosylation Source: GO_Central
protein glycosylation Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Blood group antigen, Glycosyltransferase, Transferase
Ligand	Manganese, Metal-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS10887-MONOMER
BRENDAⁱ	2.4.1.37 2681 2.4.1.40 2681
UniPathwayⁱ	UPA00378

Protein family/group databases

Carbohydrate-Active enZymes More...CAZyⁱ	GT6 Glycosyltransferase Family 6

CAZyⁱ

GT6 Glycosyltransferase Family 6

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Histo-blood group ABO system transferase Alternative name(s): Fucosylglycoprotein 3-alpha-galactosyltransferase Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase (EC:2.4.1.402 Publications) Glycoprotein-fucosylgalactoside alpha-galactosyltransferase (EC:2.4.1.372 Publications) Histo-blood group A transferase Short name: A transferase Histo-blood group B transferase Short name: B transferase NAGAT Cleaved into the following chain: Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
Gene namesⁱ	Name:ABO
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Unplaced

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:79 ABO
MIMⁱ	110300 gene
neXtProtⁱ	NX_P16442

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 32	CytoplasmicSequence analysisAdd BLAST	32
Transmembraneⁱ	33 – 53	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST	21
Topological domainⁱ	54 – 354	LumenalSequence analysisAdd BLAST	301

Keywords - Cellular componentⁱ

Golgi apparatus, Membrane, Secreted

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	214	M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. 1 Publication	1
Mutagenesisⁱ	234	P → S: Alters substrate specificity of group B transferase.	1
Mutagenesisⁱ	303	E → A: Decreases specific activity of group B transferase almost to zero. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	28
MIMⁱ	616093 phenotype
PharmGKBⁱ	PA24415

Chemistry databases

ChEMBLⁱ	CHEMBL2321639
Drug and drug target database More...DrugBankⁱ	DB04681 BETA-METHYLLACTOSIDE DB04680 GALACTOSE GREASE DB03501 Galactose-uridine-5'-diphosphate DB04679 H TYPE I TRISACCHARIDE DB04678 H TYPE II TRISACCHARIDE DB07633 octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranoside DB03435 Uridine-5'-Diphosphate DB02196 Uridine-Diphosphate-N-Acetylgalactosamine

Polymorphism and mutation databases

BioMutaⁱ	ABO
DMDMⁱ	114949

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000012268	1 – 354	Histo-blood group ABO system transferaseAdd BLAST		354
ChainⁱPRO_0000012269	54 – 354	Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble formAdd BLAST		301

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Glycosylationⁱ	113	N-linked (GlcNAc...) asparagineSequence analysis		1

Post-translational modificationⁱ

The soluble form derives from the membrane form by proteolytic processing.

Keywords - PTMⁱ

Glycoprotein

Proteomic databases

PeptideAtlas More...PeptideAtlasⁱ	P16442
PRIDEⁱ	P16442
ProteomicsDBⁱ	53361

PTM databases

iPTMnetⁱ	P16442
PhosphoSitePlusⁱ	P16442

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	106546, 3 interactors

BioGridⁱ

106546, 3 interactors

Chemistry databases

BindingDBⁱ

P16442

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	82 – 84	Combined sources	3
Beta strandⁱ	93 – 95	Combined sources	3
Helixⁱ	102 – 111	Combined sources	10
Beta strandⁱ	115 – 122	Combined sources	8
Helixⁱ	124 – 129	Combined sources	6
Helixⁱ	130 – 140	Combined sources	11
Beta strandⁱ	145 – 154	Combined sources	10
Helixⁱ	156 – 158	Combined sources	3
Beta strandⁱ	168 – 174	Combined sources	7
Helixⁱ	181 – 198	Combined sources	18
Helixⁱ	200 – 203	Combined sources	4
Beta strandⁱ	205 – 210	Combined sources	6
Beta strandⁱ	212 – 216	Combined sources	5
Helixⁱ	222 – 224	Combined sources	3
Beta strandⁱ	226 – 232	Combined sources	7
Turnⁱ	234 – 238	Combined sources	5
Helixⁱ	241 – 243	Combined sources	3
Beta strandⁱ	269 – 273	Combined sources	5
Helixⁱ	274 – 293	Combined sources	20
Helixⁱ	301 – 312	Combined sources	12
Beta strandⁱ	316 – 319	Combined sources	4
Helixⁱ	321 – 323	Combined sources	3
Helixⁱ	327 – 330	Combined sources	4
Beta strandⁱ	341 – 343	Combined sources	3
Helixⁱ	348 – 351	Combined sources	4

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00339
ProteinModelPortalⁱ	P16442
SMRⁱ	P16442
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P16442

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	121 – 123	UDP-N-acetyl-galactosamine bindingCombined sources5 Publications		3
Regionⁱ	211 – 213	UDP-N-acetyl-galactosamine bindingCombined sources5 Publications		3

Domainⁱ

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.

Sequence similaritiesⁱ

Belongs to the glycosyltransferase 6 family.Curated

Keywords - Domainⁱ

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENⁱ	HBG003563
InParanoidⁱ	P16442
KEGG Orthology (KO) More...KOⁱ	K00709
PhylomeDBⁱ	P16442

Family and domain databases

Gene3Dⁱ	3.90.550.10, 1 hit
InterProⁱ	View protein in InterPro IPR005076 Glyco_trans_6 IPR029044 Nucleotide-diphossugar_trans
PANTHERⁱ	PTHR10462 PTHR10462, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03414 Glyco_transf_6, 1 hit
SUPFAMⁱ	SSF53448 SSF53448, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show all Align All

P16442-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG 
        60         70         80         90        100
FCMAVREPDH LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF 
       110        120        130        140        150
NIDILNEQFR LQNTTIGLTV FAIKKYVAFL KLFLETAEKH FMVGHRVHYY 
       160        170        180        190        200
VFTDQPAAVP RVTLGTGRQL SVLEVRAYKR WQDVSMRRME MISDFCERRF 
       210        220        230        240        250
LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPGFYGSS REAFTYERRP 
       260        270        280        290        300
QSQAYIPKDE GDFYYLGGFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW 
       310        320        330        340        350
HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA 

VRNP

Length:354

Mass (Da):40,934

Last modified:December 1, 1992 - v2

Checksum:ⁱA03DA16E630C1608

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A087X009	A0A087X009_HUMAN	Histo-blood group ABO system transf... Histo-blood group ABO system transferase	ABO	373	Annotation score:
A0A087X0C2	A0A087X0C2_HUMAN	Histo-blood group ABO system transf... Histo-blood group ABO system transferase	ABO	353	Annotation score:

Polymorphismⁱ

Genetic variations in ABO define the ABO blood group system [MIMⁱ: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).13 Publications

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_019147	35	G → R1 PublicationCorresponds to variant dbSNP:rs8176696Ensembl.	1
Natural variantⁱVAR_019148	36	V → F1 PublicationCorresponds to variant dbSNP:rs688976Ensembl.	1
Natural variantⁱVAR_019149	63	R → H1 PublicationCorresponds to variant dbSNP:rs549446Ensembl.	1
Natural variantⁱVAR_019150	74	P → S2 PublicationsCorresponds to variant dbSNP:rs512770Ensembl.	1
Natural variantⁱVAR_003408	80 – 81	CR → W.	2
Natural variantⁱVAR_003409	156	P → L in allele A2. 5 PublicationsCorresponds to variant dbSNP:rs1053878EnsemblClinVar.	1
Natural variantⁱVAR_019151	161	R → H1 PublicationCorresponds to variant dbSNP:rs8176738Ensembl.	1
Natural variantⁱVAR_036738	163	T → M in allele Aw08. 1 PublicationCorresponds to variant dbSNP:rs55756402Ensembl.	1
Natural variantⁱVAR_003410	176	R → G in allele Aw08 and allele Bw08. 7 PublicationsCorresponds to variant dbSNP:rs7853989Ensembl.	1
Natural variantⁱVAR_036739	198	R → W in allele Aw07. 1 Publication	1
Natural variantⁱVAR_019152	199	R → C1 PublicationCorresponds to variant dbSNP:rs8176739Ensembl.	1
Natural variantⁱVAR_036740	214	M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. 2 Publications	1
Natural variantⁱVAR_019153	216	F → I2 PublicationsCorresponds to variant dbSNP:rs8176740Ensembl.	1
Natural variantⁱVAR_036741	223	E → D in allele B106. 1 Publication	1
Natural variantⁱVAR_055227	230	G → R in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation. 1 Publication	1
Natural variantⁱVAR_072628	234	P → A in allele B(A). 1 Publication	1
Natural variantⁱVAR_003411	235	G → S in allele Bw08. 8 PublicationsCorresponds to variant dbSNP:rs8176743Ensembl.	1
Natural variantⁱVAR_033540	257	P → L. Corresponds to variant dbSNP:rs8176745Ensembl.	1
Natural variantⁱVAR_003412	266	L → M in allele Bw08. 8 PublicationsCorresponds to variant dbSNP:rs8176746Ensembl.	1
Natural variantⁱVAR_003413	268	G → A in allele Bw08. 7 PublicationsCorresponds to variant dbSNP:rs8176747EnsemblClinVar.	1
Natural variantⁱVAR_033541	268	G → R in allele Aw08. 1 PublicationCorresponds to variant dbSNP:rs41302905Ensembl.	1
Natural variantⁱVAR_019154	277	V → M2 PublicationsCorresponds to variant dbSNP:rs8176748Ensembl.	1
Natural variantⁱVAR_036742	288	M → R1 Publication	1
Natural variantⁱVAR_036743	291	D → N in allele B104. 1 Publication	1
Natural variantⁱVAR_036744	346	K → M in allele Bw08. 2 Publications	1
Natural variantⁱVAR_036745	352	R → G in allele A107. 1 Publication	1
Natural variantⁱVAR_003414	352	R → W in allele A106 and allele B3. 1 Publication	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J05175 mRNA Translation: AAA36792.1 X84746 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
PIRⁱ	PC1165
NCBI Reference Sequences More...RefSeqⁱ	NP_065202.2, NM_020469.2
UniGeneⁱ	Hs.654423

Genome annotation databases

GeneIDⁱ	28
KEGGⁱ	hsa:28

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P16442	Histo-blood group ABO system transferase		HUMAN		354	UniRef100_P16442
ABO blood group (transferase A, alpha 1-3-N-acetylgalactosaminyltransferase transferase B, alpha 1-3-galactosyltransferase) (Fragment)		HUMAN		344
ABO glycosyltransferase (Fragment)		HUMAN		229
Transferase		HUMAN		237
N-terminal truncated ABO glycosyltransferase		HUMAN		213

Protein	Similar proteins		Species	Score	Length	Source
P16442	Histo-blood group ABO system transferase		HUMAN		354	UniRef90_P16442
ABO isoform 1		PANTR		354
Uncharacterized protein		MANLE		344
Uncharacterized protein		PANPA		344
ABO blood group (transferase A, alpha 1-3-N-acetylgalactosaminyltransferase transferase B, alpha 1-3-galactosyltransferase) (Fragment)		HUMAN		344
+83

Protein	Similar proteins		Species	Score	Length	Source
P16442	Histo-blood group ABO system transferase		HUMAN		354	UniRef50_P16442
ABO isoform 1		PANTR		354
Uncharacterized protein		MANLE		344
Uncharacterized protein		PANPA		344
Uncharacterized protein		FELCA		483
+128

Cross-referencesⁱ

Web resourcesⁱ

SeattleSNPs

Functional Glycomics Gateway - GTase

Histo-blood group ABO system transferase

Functional Glycomics Gateway - GTase

Histo-blood group ABO system transferase

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	J05175 mRNA Translation: AAA36792.1 X84746 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
PIRⁱ	PC1165
RefSeqⁱ	NP_065202.2, NM_020469.2
UniGeneⁱ	Hs.654423

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	2Y7A	X-ray	2.06	A/B/C/D	64-354	[»]
	3I0C	X-ray	1.55	A	69-354	[»]
	3I0D	X-ray	1.90	A	69-354	[»]
	3I0E	X-ray	1.81	A	69-354	[»]
	3I0F	X-ray	1.56	A	69-354	[»]
	3I0G	X-ray	1.40	A	69-354	[»]
	3I0H	X-ray	2.00	A	69-354	[»]
	3I0I	X-ray	1.90	X	69-354	[»]
	3I0J	X-ray	1.48	A	69-354	[»]
	3I0K	X-ray	2.20	A	69-354	[»]
	3I0L	X-ray	1.60	A	69-354	[»]
	3IOH	X-ray	1.25	A	64-354	[»]
	3IOI	X-ray	1.45	A	64-354	[»]
3IOJ	X-ray	1.65	A/B	64-354	[»]
3SX3	X-ray	1.45	A	64-354	[»]
3SX5	X-ray	1.43	A	64-354	[»]
3SX7	X-ray	1.42	A	64-354	[»]
3SX8	X-ray	1.47	A	64-354	[»]
3SXA	X-ray	1.50	A	64-354	[»]
3SXB	X-ray	1.49	A	64-354	[»]
3SXC	X-ray	1.90	A	64-354	[»]
3SXD	X-ray	1.55	A	64-354	[»]
3SXE	X-ray	1.49	A	64-354	[»]
3SXG	X-ray	1.86	A	64-354	[»]
3U0X	X-ray	1.85	A/B	64-354	[»]
3U0Y	X-ray	1.60	A/B	64-354	[»]
3V0L	X-ray	1.75	A	64-354	[»]
3V0M	X-ray	1.68	A/B	64-354	[»]
3V0N	X-ray	1.75	A/B	64-354	[»]
3V0O	X-ray	1.65	A/B	64-354	[»]
3V0P	X-ray	1.90	A/B	64-354	[»]
3V0Q	X-ray	1.80	A/B	64-354	[»]
3ZGF	X-ray	1.70	A/B	64-354	[»]
3ZGG	X-ray	1.90	A	64-354	[»]
4C2S	X-ray	2.48	A/B	64-354	[»]
4FQW	X-ray	2.02	A	64-354	[»]
4FRA	X-ray	1.43	A	64-354	[»]
4FRB	X-ray	1.54	A	64-354	[»]
4FRD	X-ray	1.55	A	64-354	[»]
4FRE	X-ray	1.85	A	64-354	[»]
4FRH	X-ray	1.80	A	64-354	[»]
4FRL	X-ray	1.90	A	64-354	[»]
4FRM	X-ray	1.90	A	64-354	[»]
4FRO	X-ray	1.75	A	64-354	[»]
4FRP	X-ray	2.00	A	64-354	[»]
4FRQ	X-ray	2.35	A	64-354	[»]
4GBP	X-ray	2.15	A	64-354	[»]
4KC1	X-ray	1.50	A	64-346	[»]
4KC2	X-ray	1.70	A	64-346	[»]
4KC4	X-ray	1.60	A	64-346	[»]
4KXO	X-ray	2.00	A	64-354	[»]
4Y62	X-ray	1.60	A	1-354	[»]
4Y63	X-ray	1.30	A	1-354	[»]
4Y64	X-ray	1.60	A	1-354	[»]
5BXC	X-ray	1.40	A	64-354	[»]
5C1G	X-ray	1.46	A	64-354	[»]
5C1H	X-ray	1.55	A	64-354	[»]
5C1L	X-ray	1.40	A	64-354	[»]
5C36	X-ray	1.55	A	64-354	[»]
5C38	X-ray	1.45	A	64-354	[»]
5C3A	X-ray	1.33	A	64-354	[»]
5C3B	X-ray	1.40	A	64-354	[»]
5C3D	X-ray	1.39	A	64-354	[»]
5C47	X-ray	1.39	A	64-354	[»]
5C48	X-ray	1.46	A	64-354	[»]
5C49	X-ray	1.49	A	64-354	[»]
5C4B	X-ray	1.54	A	64-354	[»]
5C4C	X-ray	1.43	A	64-354	[»]
5C4D	X-ray	1.40	A	64-354	[»]
5C4E	X-ray	1.55	A	64-354	[»]
5C4F	X-ray	1.41	A	64-354	[»]
5C8R	X-ray	1.45	A	64-354	[»]
5CMF	X-ray	1.95	X	64-345	[»]
5CMG	X-ray	1.83	X	64-354	[»]
5CMH	X-ray	1.61	A	64-354	[»]
5CMI	X-ray	1.85	A	64-354	[»]
5CMJ	X-ray	1.73	A	64-354	[»]
5CQL	X-ray	1.69	X	64-354	[»]
5CQM	X-ray	1.65	X	64-354	[»]
5CQN	X-ray	1.61	X	64-354	[»]
5CQO	X-ray	1.69	A	64-354	[»]
5CQP	X-ray	1.83	A	64-354	[»]
5M79	X-ray	1.30	A	64-354	[»]
5M7A	X-ray	1.30	A	64-354	[»]
5M7B	X-ray	1.50	A	64-354	[»]
5M7C	X-ray	1.60	A/B	64-354	[»]
5M7D	X-ray	1.20	A	64-354	[»]
5TJK	X-ray	1.45	A	64-354	[»]
5TJL	X-ray	1.89	A	64-354	[»]
5TJN	X-ray	1.47	A	64-354	[»]
5TJO	X-ray	1.57	A	64-354	[»]
DisProtⁱ	DP00339
ProteinModelPortalⁱ	P16442
SMRⁱ	P16442
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	106546, 3 interactors

BioGridⁱ

106546, 3 interactors

Chemistry databases

BindingDBⁱ	P16442
ChEMBLⁱ	CHEMBL2321639
DrugBankⁱ	DB04681 BETA-METHYLLACTOSIDE DB04680 GALACTOSE GREASE DB03501 Galactose-uridine-5'-diphosphate DB04679 H TYPE I TRISACCHARIDE DB04678 H TYPE II TRISACCHARIDE DB07633 octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranoside DB03435 Uridine-5'-Diphosphate DB02196 Uridine-Diphosphate-N-Acetylgalactosamine

Protein family/group databases

CAZyⁱ	GT6 Glycosyltransferase Family 6

CAZyⁱ

GT6 Glycosyltransferase Family 6

PTM databases

iPTMnetⁱ	P16442
PhosphoSitePlusⁱ	P16442

Polymorphism and mutation databases

BioMutaⁱ	ABO
DMDMⁱ	114949

Proteomic databases

PeptideAtlasⁱ	P16442
PRIDEⁱ	P16442
ProteomicsDBⁱ	53361

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	28
Structural Biology Knowledgebase	Search...

Genome annotation databases

GeneIDⁱ	28
KEGGⁱ	hsa:28

Organism-specific databases

CTDⁱ	28
DisGeNETⁱ	28
GeneCardsⁱ	ABO
HGNCⁱ	HGNC:79 ABO
MIMⁱ	110300 gene 616093 phenotype
neXtProtⁱ	NX_P16442
PharmGKBⁱ	PA24415
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

HOVERGENⁱ	HBG003563
InParanoidⁱ	P16442
KOⁱ	K00709
PhylomeDBⁱ	P16442

Enzyme and pathway databases

UniPathwayⁱ	UPA00378
BioCycⁱ	MetaCyc:HS10887-MONOMER
BRENDAⁱ	2.4.1.37 2681 2.4.1.40 2681

Miscellaneous databases

EvolutionaryTraceⁱ	P16442
GeneWikiⁱ	ABO_(gene)
GenomeRNAiⁱ	28
Protein Ontology More...PROⁱ	PR:P16442
SOURCEⁱ	Search...

Family and domain databases

Gene3Dⁱ	3.90.550.10, 1 hit
InterProⁱ	View protein in InterPro IPR005076 Glyco_trans_6 IPR029044 Nucleotide-diphossugar_trans
PANTHERⁱ	PTHR10462 PTHR10462, 1 hit
Pfamⁱ	View protein in Pfam PF03414 Glyco_transf_6, 1 hit
SUPFAMⁱ	SSF53448 SSF53448, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BGAT_HUMAN
Accessionⁱ	P16442Primary (citable) accession number: P16442 Secondary accession number(s): B0JDB9 Q9UQ69
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
	Last sequence update:	December 1, 1992
	Last modified:	June 20, 2018
	This is version 198 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Blood group antigen proteins
Nomenclature of blood group antigens and list of entries
SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
PATHWAY comments
Index of metabolic and biosynthesis pathways
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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UniProtKB - P16442 (BGAT_HUMAN)

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Histo-blood group ABO system transferase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Golgi apparatus

Extracellular region or secreted

Golgi apparatus

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Pathwayⁱ: protein glycosylation

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ