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UniProtKB - P16442 (BGAT_HUMAN)

Entry version 218 (02 Jun 2021)
Sequence version 2 (01 Dec 1992)
Previous versions | rss
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Protein

Histo-blood group ABO system transferase

Gene

ABO

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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

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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei126UDP-N-acetyl-galactosamineCombined sources5 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi211ManganeseCombined sources4 Publications1
Metal bindingi213ManganeseCombined sources4 Publications1
Binding sitei233Glycoprotein fucosyl-galactosyl groupCombined sources1 Publication1
Binding sitei245Glycoprotein fucosyl-galactosyl groupCombined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei303NucleophileBy similarity1
Binding sitei303Glycoprotein fucosyl-galactosyl groupCombined sources3 Publications1
Binding sitei326Glycoprotein fucosyl-galactosyl groupCombined sources2 Publications1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionBlood group antigen, Glycosyltransferase, Transferase
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS10887-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.1.37, 2681
2.4.1.40, 2681
2.4.1.88, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P16442

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-9033807, ABO blood group biosynthesis

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GT6, Glycosyltransferase Family 6

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ABO
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:79, ABO

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		110300, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P16442

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 32CytoplasmicSequence analysisAdd BLAST32
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei33 – 53Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini54 – 354LumenalSequence analysisAdd BLAST301

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi214M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. 1 Publication1
Mutagenesisi234P → S: Alters substrate specificity of group B transferase. 1
Mutagenesisi303E → A: Decreases specific activity of group B transferase almost to zero. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		28
MIMi616093, phenotype

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA24415

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P16442, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2321639

Drug and drug target database

More...DrugBanki		DB04141, 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol
DB03772, 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,5-Diol
DB07357, 4-AMINO-2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,5-DIOL
DB07378, 4-AMINO-2-OCTYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,5-DIOL
DB04681, BETA-METHYLLACTOSIDE
DB04680, GALACTOSE GREASE
DB03501, Galactose-uridine-5'-diphosphate
DB04678, H TYPE II TRISACCHARIDE
DB04679, Human blood group H type 1 trisaccharide
DB07341, octyl 3-amino-3-deoxy-2-O-(2,6-dideoxy-alpha-L-lyxo-hexopyranosyl)-beta-D-galactopyranoside
DB07633, octyl 3-deoxy-2-O-(6-deoxy-alpha-L-galactopyranosyl)-beta-D-xylo-hexopyranoside
DB03435, Uridine-5'-Diphosphate
DB02196, Uridine-Diphosphate-N-Acetylgalactosamine

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ABO

Domain mapping of disease mutations (DMDM)

More...DMDMi		114949

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000122681 – 354Histo-blood group ABO system transferaseAdd BLAST354
ChainiPRO_000001226954 – 354Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble formAdd BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi113N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

Keywords - PTMi

Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P16442

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P16442

PeptideAtlas

More...PeptideAtlasi		P16442

PRoteomics IDEntifications database

More...PRIDEi		P16442

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53361

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P16442, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P16442

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P16442

<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

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		106546, 3 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000483018

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P16442

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P16442, protein

<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

1354
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P16442

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P16442

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni121 – 123UDP-N-acetyl-galactosamine bindingCombined sources5 Publications3
Regioni211 – 213UDP-N-acetyl-galactosamine bindingCombined sources5 Publications3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<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

Belongs to the glycosyltransferase 6 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QQAJ, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P16442

Database of Orthologous Groups

More...OrthoDBi		1204439at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P16442

Family and domain databases

Database of protein disorder

More...DisProti		DP00339

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.550.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005076, Glyco_trans_6
IPR029044, Nucleotide-diphossugar_trans

The PANTHER Classification System

More...PANTHERi		PTHR10462, PTHR10462, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03414, Glyco_transf_6, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53448, SSF53448, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P16442-1 [UniParc]FASTAAdd 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA03DA16E630C1608
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087X0C2A0A087X0C2_HUMAN
Histo-blood group ABO system transf...
ABO
353Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087X009A0A087X009_HUMAN
Histo-blood group ABO system transf...
ABO
373Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A7P0TA91A0A7P0TA91_HUMAN
Histo-blood group ABO system transf...
ABO
23Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01914735G → R1 PublicationCorresponds to variant dbSNP:rs8176696Ensembl.1
Natural variantiVAR_01914836V → F1 PublicationCorresponds to variant dbSNP:rs688976EnsemblClinVar.1
Natural variantiVAR_01914963R → H1 PublicationCorresponds to variant dbSNP:rs549446Ensembl.1
Natural variantiVAR_01915074P → S2 PublicationsCorresponds to variant dbSNP:rs512770EnsemblClinVar.1
Natural variantiVAR_00340880 – 81CR → W. 2
Natural variantiVAR_003409156P → L in allele A2. 5 PublicationsCorresponds to variant dbSNP:rs1053878EnsemblClinVar.1
Natural variantiVAR_019151161R → H1 PublicationCorresponds to variant dbSNP:rs8176738Ensembl.1
Natural variantiVAR_036738163T → M in allele Aw08. 1 PublicationCorresponds to variant dbSNP:rs55756402Ensembl.1
Natural variantiVAR_003410176R → G in allele Aw08 and allele Bw08. 7 PublicationsCorresponds to variant dbSNP:rs7853989Ensembl.1
Natural variantiVAR_036739198R → W in allele Aw07. 1 Publication1
Natural variantiVAR_019152199R → C1 PublicationCorresponds to variant dbSNP:rs8176739Ensembl.1
Natural variantiVAR_036740214M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. 2 Publications1
Natural variantiVAR_019153216F → I2 PublicationsCorresponds to variant dbSNP:rs8176740EnsemblClinVar.1
Natural variantiVAR_036741223E → D in allele B106. 1 Publication1
Natural variantiVAR_055227230G → R in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation. 1 Publication1
Natural variantiVAR_072628234P → A in allele B(A). 1 Publication1
Natural variantiVAR_003411235G → S in allele Bw08. 8 PublicationsCorresponds to variant dbSNP:rs8176743Ensembl.1
Natural variantiVAR_033540257P → L. Corresponds to variant dbSNP:rs8176745Ensembl.1
Natural variantiVAR_003412266L → M in allele Bw08. 8 PublicationsCorresponds to variant dbSNP:rs8176746Ensembl.1
Natural variantiVAR_003413268G → A in allele Bw08. 7 PublicationsCorresponds to variant dbSNP:rs8176747EnsemblClinVar.1
Natural variantiVAR_033541268G → R in allele Aw08. 1 PublicationCorresponds to variant dbSNP:rs41302905Ensembl.1
Natural variantiVAR_019154277V → M2 PublicationsCorresponds to variant dbSNP:rs8176748Ensembl.1
Natural variantiVAR_036742288M → R1 Publication1
Natural variantiVAR_036743291D → N in allele B104. 1 Publication1
Natural variantiVAR_036744346K → M in allele Bw08. 2 Publications1
Natural variantiVAR_036745352R → G in allele A107. 1 Publication1
Natural variantiVAR_003414352R → W in allele A106 and allele B3. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

Protein sequence database of the Protein Information Resource

More...PIRi		PC1165

NCBI Reference Sequences

More...RefSeqi		NP_065202.2, NM_020469.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		28

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:28

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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%5Freferences%5Fsection">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

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
PIRiPC1165
RefSeqiNP_065202.2, NM_020469.2

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 entryMethodResolution (Å)ChainPositionsPDBsum
1LZ0X-ray1.80A64-354[»]
1LZ7X-ray1.65A64-354[»]
1LZIX-ray1.35A64-354[»]
1LZJX-ray1.32A64-354[»]
1R7TX-ray2.09A64-345[»]
1R7UX-ray1.61A64-345[»]
1R7VX-ray2.09A64-345[»]
1R7XX-ray1.97A64-345[»]
1R7YX-ray1.75A64-345[»]
1R80X-ray1.65A64-345[»]
1R81X-ray1.75A64-345[»]
1R82X-ray1.55A64-345[»]
1WSZX-ray1.59A64-354[»]
1WT0X-ray1.80A64-354[»]
1WT1X-ray1.55A64-354[»]
1WT2X-ray1.90A64-354[»]
1WT3X-ray1.80A64-354[»]
1XZ6X-ray1.55A64-354[»]
1ZHJX-ray1.59A64-354[»]
1ZI1X-ray1.57A64-354[»]
1ZI3X-ray1.69A64-354[»]
1ZI4X-ray1.85A64-354[»]
1ZI5X-ray1.55A64-354[»]
1ZIZX-ray1.49A64-354[»]
1ZJ0X-ray1.67A64-354[»]
1ZJ1X-ray1.65A64-354[»]
1ZJ2X-ray1.69A64-354[»]
1ZJ3X-ray1.69A64-354[»]
1ZJOX-ray1.64A64-354[»]
1ZJPX-ray1.59A64-354[»]
2A8UX-ray1.69A64-354[»]
2A8WX-ray1.59A64-354[»]
2I7BX-ray1.99A64-354[»]
2O1FX-ray1.99A64-354[»]
2O1GX-ray1.71A64-354[»]
2O1HX-ray1.67A64-354[»]
2PGVX-ray1.79A64-354[»]
2PGYX-ray2.39A64-354[»]
2RITX-ray1.43A64-354[»]
2RIXX-ray1.75A64-354[»]
2RIYX-ray1.55A64-354[»]
2RIZX-ray1.45A64-354[»]
2RJ0X-ray1.52A64-354[»]
2RJ1X-ray1.55A64-354[»]
2RJ4X-ray1.47A64-354[»]
2RJ5X-ray1.45A64-354[»]
2RJ6X-ray1.41A64-354[»]
2RJ7X-ray1.70A64-354[»]
2RJ8X-ray1.69A64-354[»]
2RJ9X-ray1.69A64-354[»]
2Y7AX-ray2.06A/B/C/D64-354[»]
3I0CX-ray1.55A69-354[»]
3I0DX-ray1.90A69-354[»]
3I0EX-ray1.81A69-354[»]
3I0FX-ray1.56A69-354[»]
3I0GX-ray1.40A69-354[»]
3I0HX-ray2.00A69-354[»]
3I0IX-ray1.90X69-354[»]
3I0JX-ray1.48A69-354[»]
3I0KX-ray2.20A69-354[»]
3I0LX-ray1.60A69-354[»]
3IOHX-ray1.25A64-354[»]
3IOIX-ray1.45A64-354[»]
3IOJX-ray1.65A/B64-354[»]
3SX3X-ray1.45A64-354[»]
3SX5X-ray1.43A64-354[»]
3SX7X-ray1.42A64-354[»]
3SX8X-ray1.47A64-354[»]
3SXAX-ray1.50A64-354[»]
3SXBX-ray1.49A64-354[»]
3SXCX-ray1.90A64-354[»]
3SXDX-ray1.55A64-354[»]
3SXEX-ray1.49A64-354[»]
3SXGX-ray1.86A64-354[»]
3U0XX-ray1.85A/B64-354[»]
3U0YX-ray1.60A/B64-354[»]
3V0LX-ray1.75A64-354[»]
3V0MX-ray1.68A/B64-354[»]
3V0NX-ray1.75A/B64-354[»]
3V0OX-ray1.65A/B64-354[»]
3V0PX-ray1.90A/B64-354[»]
3V0QX-ray1.80A/B64-354[»]
3ZGFX-ray1.70A/B64-354[»]
3ZGGX-ray1.90A64-354[»]
4C2SX-ray2.48A/B64-354[»]
4FQWX-ray2.02A64-354[»]
4FRAX-ray1.43A64-354[»]
4FRBX-ray1.54A64-354[»]
4FRDX-ray1.55A64-354[»]
4FREX-ray1.85A64-354[»]
4FRHX-ray1.80A64-354[»]
4FRLX-ray1.90A64-354[»]
4FRMX-ray1.90A64-354[»]
4FROX-ray1.75A64-354[»]
4FRPX-ray2.00A64-354[»]
4FRQX-ray2.35A64-354[»]
4GBPX-ray2.15A64-354[»]
4KC1X-ray1.50A64-346[»]
4KC2X-ray1.70A64-346[»]
4KC4X-ray1.60A64-346[»]
4KXOX-ray2.00A64-354[»]
4Y62X-ray1.60A1-354[»]
4Y63X-ray1.30A1-354[»]
4Y64X-ray1.60A1-354[»]
5BXCX-ray1.40A64-354[»]
5C1GX-ray1.46A64-354[»]
5C1HX-ray1.55A64-354[»]
5C1LX-ray1.40A64-354[»]
5C36X-ray1.55A64-354[»]
5C38X-ray1.45A64-354[»]
5C3AX-ray1.33A64-354[»]
5C3BX-ray1.40A64-354[»]
5C3DX-ray1.39A64-354[»]
5C47X-ray1.39A64-354[»]
5C48X-ray1.46A64-354[»]
5C49X-ray1.49A64-354[»]
5C4BX-ray1.54A64-354[»]
5C4CX-ray1.43A64-354[»]
5C4DX-ray1.40A64-354[»]
5C4EX-ray1.55A64-354[»]
5C4FX-ray1.41A64-354[»]
5C8RX-ray1.45A64-354[»]
5CMFX-ray1.95X64-345[»]
5CMGX-ray1.83X64-354[»]
5CMHX-ray1.61A64-354[»]
5CMIX-ray1.85A64-354[»]
5CMJX-ray1.73A64-354[»]
5CQLX-ray1.69X64-354[»]
5CQMX-ray1.65X64-354[»]
5CQNX-ray1.61X64-354[»]
5CQOX-ray1.69A64-354[»]
5CQPX-ray1.83A64-354[»]
5M79X-ray1.30A64-354[»]
5M7AX-ray1.30A64-354[»]
5M7BX-ray1.50A64-354[»]
5M7CX-ray1.60A/B64-354[»]
5M7DX-ray1.20A64-354[»]
5TJKX-ray1.45A64-354[»]
5TJLX-ray1.89A64-354[»]
5TJNX-ray1.47A64-354[»]
5TJOX-ray1.57A64-354[»]
6BJIX-ray1.54A64-354[»]
6BJJX-ray1.45A64-354[»]
6BJKX-ray2.12A64-354[»]
6BJLX-ray1.69A64-345[»]
6BJMX-ray1.45A64-345[»]
6GWYX-ray1.40A64-354[»]
6GWZX-ray1.65A64-354[»]
6GX0X-ray1.25A64-354[»]
6GX1X-ray1.60A64-354[»]
6GX2X-ray1.07A64-354[»]
SMRiP16442
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi106546, 3 interactors
STRINGi9606.ENSP00000483018

Chemistry databases

BindingDBiP16442
ChEMBLiCHEMBL2321639
DrugBankiDB04141, 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,4,5-Triol
DB03772, 2-Hexyloxy-6-Hydroxymethyl-Tetrahydro-Pyran-3,5-Diol
DB07357, 4-AMINO-2-HEXYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,5-DIOL
DB07378, 4-AMINO-2-OCTYLOXY-6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,5-DIOL
DB04681, BETA-METHYLLACTOSIDE
DB04680, GALACTOSE GREASE
DB03501, Galactose-uridine-5'-diphosphate
DB04678, H TYPE II TRISACCHARIDE
DB04679, Human blood group H type 1 trisaccharide
DB07341, octyl 3-amino-3-deoxy-2-O-(2,6-dideoxy-alpha-L-lyxo-hexopyranosyl)-beta-D-galactopyranoside
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

CAZyiGT6, Glycosyltransferase Family 6

PTM databases

GlyGeniP16442, 1 site
iPTMnetiP16442
PhosphoSitePlusiP16442

Genetic variation databases

BioMutaiABO
DMDMi114949

Proteomic databases

jPOSTiP16442
MassIVEiP16442
PeptideAtlasiP16442
PRIDEiP16442
ProteomicsDBi53361

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		28

Genome annotation databases

GeneIDi28
KEGGihsa:28

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		28
DisGeNETi28

GeneCards: human genes, protein and diseases

More...GeneCardsi		ABO
HGNCiHGNC:79, ABO
MIMi110300, gene
616093, phenotype
neXtProtiNX_P16442
PharmGKBiPA24415

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502QQAJ, Eukaryota
InParanoidiP16442
OrthoDBi1204439at2759
PhylomeDBiP16442

Enzyme and pathway databases

UniPathwayiUPA00378
BioCyciMetaCyc:HS10887-MONOMER
BRENDAi2.4.1.37, 2681
2.4.1.40, 2681
2.4.1.88, 2681
PathwayCommonsiP16442
ReactomeiR-HSA-9033807, ABO blood group biosynthesis

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		28, 4 hits in 128 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		ABO, human
EvolutionaryTraceiP16442

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		ABO_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		28
PharosiP16442, Tbio

Protein Ontology

More...PROi		PR:P16442
RNActiP16442, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Family and domain databases

DisProtiDP00339
Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR005076, Glyco_trans_6
IPR029044, Nucleotide-diphossugar_trans
PANTHERiPTHR10462, PTHR10462, 1 hit
PfamiView protein in Pfam
PF03414, Glyco_transf_6, 1 hit
SUPFAMiSSF53448, SSF53448, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBGAT_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P16442
Secondary accession number(s): B0JDB9
, O14758, Q14490, Q53I57, Q6ISD4, Q6KFZ2, Q70V27, Q99484, Q99485, Q9NY01, Q9UQ68, Q9UQ69
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 1, 1992
Last modified: June 2, 2021
This is version 218 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Blood group antigen proteins
    Nomenclature of blood group antigens and list of entries
  2. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  3. Human entries with genetic variants
    List of human entries with genetic variants
  4. Human variants curated from literature reports
    Index of human variants curated from literature reports
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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