UniProtKB - P16442 (BGAT_HUMAN)
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- BLAST>sp|P16442|BGAT_HUMAN Histo-blood group ABO system transferase OS=Homo sapiens OX=9606 GN=ABO PE=1 SV=2 MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDH LQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTV FAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKR WQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSS REAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVW HDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
- Align
Histo-blood group ABO system transferase
ABO
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>Select a section on the left to see content.
<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 catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"The structural basis for specificity in human ABO(H) blood group biosynthesis."
Patenaude S.I., Seto N.O.L., Borisova S.N., Szpacenko A., Marcus S.L., Palcic M.M., Evans S.V.
Nat. Struct. Biol. 9:685-690(2002) [PubMed] [Europe PMC] [Abstract]Cited for: 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, CATALYTIC ACTIVITY. - Ref.23"Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif."
Persson M., Letts J.A., Hosseini-Maaf B., Borisova S.N., Palcic M.M., Evans S.V., Olsson M.L.
J. Biol. Chem. 282:9564-9570(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND THR-214, COFACTOR, CHARACTERIZATION OF VARIANT ARG-214, MUTAGENESIS OF MET-214, CATALYTIC ACTIVITY.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.18"The structural basis for specificity in human ABO(H) blood group biosynthesis."
Patenaude S.I., Seto N.O.L., Borisova S.N., Szpacenko A., Marcus S.L., Palcic M.M., Evans S.V.
Nat. Struct. Biol. 9:685-690(2002) [PubMed] [Europe PMC] [Abstract]Cited for: 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, CATALYTIC ACTIVITY. - Ref.23"Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif."
Persson M., Letts J.A., Hosseini-Maaf B., Borisova S.N., Palcic M.M., Evans S.V., Olsson M.L.
J. Biol. Chem. 282:9564-9570(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND THR-214, COFACTOR, CHARACTERIZATION OF VARIANT ARG-214, MUTAGENESIS OF MET-214, CATALYTIC ACTIVITY.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.23"Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif."
Persson M., Letts J.A., Hosseini-Maaf B., Borisova S.N., Palcic M.M., Evans S.V., Olsson M.L.
J. Biol. Chem. 282:9564-9570(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND THR-214, COFACTOR, CHARACTERIZATION OF VARIANT ARG-214, MUTAGENESIS OF MET-214, CATALYTIC ACTIVITY.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.23"Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif."
Persson M., Letts J.A., Hosseini-Maaf B., Borisova S.N., Palcic M.M., Evans S.V., Olsson M.L.
J. Biol. Chem. 282:9564-9570(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 64-354 OF MUTANTS ARG-214 AND THR-214, COFACTOR, CHARACTERIZATION OF VARIANT ARG-214, MUTAGENESIS OF MET-214, CATALYTIC ACTIVITY.
<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
This protein is involved in the pathway protein glycosylation, which is part of Protein modification.CuratedView 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 | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ 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 sitei | 126 | UDP-N-acetyl-galactosamineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ 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 bindingi | 211 | ManganeseCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ 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 bindingi | 213 | ManganeseCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 233 | Glycoprotein fucosyl-galactosyl groupCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 245 | Glycoprotein fucosyl-galactosyl groupCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 303 | NucleophileBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 303 | Glycoprotein fucosyl-galactosyl groupCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ 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 sitei | 326 | Glycoprotein fucosyl-galactosyl groupCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<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
- antigen binding Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- fucosylgalactoside 3-alpha-galactosyltransferase activity Source: UniProtKB-EC
- glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC
- manganese ion binding Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- nucleotide binding Source: CAFA <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- transferase activity, transferring glycosyl groups Source: GO_Central
<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 - Biological processi
- carbohydrate metabolic process Source: InterPro
- glycolipid biosynthetic process Source: GO_Central
- lipid glycosylation Source: GO_Central
- protein glycosylation Source: UniProtKB-UniPathway
<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 function | Blood group antigen, Glycosyltransferase, Transferase |
| Ligand | Manganese, 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 |
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_and_taxonomy_section">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 transferaseAlternative name(s): Fucosylglycoprotein 3-alpha-galactosyltransferase Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase (EC:2.4.1.402 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Glycoprotein-fucosylgalactoside alpha-galactosyltransferase (EC:2.4.1.372 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Histo-blood group A transferase Short name: A transferase Histo-blood group B transferase Short name: B transferase NAGAT Cleaved into the following chain: |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 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 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 |
|
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
Extracellular region or secreted
Golgi apparatus
Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Golgi apparatus
- Golgi apparatus Source: GO_Central
- Golgi cisterna membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB-KW
- vesicle Source: GO_Central
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 domaini | 1 – 32 | CytoplasmicSequence analysisAdd BLAST | 32 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei | 33 – 53 | Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST | 21 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 domaini | 54 – 354 | LumenalSequence analysisAdd BLAST | 301 |
<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>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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi | 214 | M → T or V: Alters substrate specificity so that both UDP-N-acetyl-D-galactosamine and UDP-galactose are utilized. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi | 234 | P → S: Alters substrate specificity of group B transferase. | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi | 303 | E → A: Decreases specific activity of group B transferase almost to zero. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 28 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 616093 phenotype |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA24415 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...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
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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000012268 | 1 – 354 | Histo-blood group ABO system transferaseAdd BLAST | 354 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000012269 | 54 – 354 | Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble formAdd BLAST | 301 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi | 113 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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
<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>Keywords - PTMi
GlycoproteinProteomic databases
PeptideAtlas More...PeptideAtlasi | P16442 |
PRoteomics IDEntifications database More...PRIDEi | P16442 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 53361 |
PTM databases
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 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P16442 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 82 – 84 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 93 – 95 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 102 – 111 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 115 – 122 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 124 – 129 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 130 – 140 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 145 – 154 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 156 – 158 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 168 – 174 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 181 – 198 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 18 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 200 – 203 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 205 – 210 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 212 – 216 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 222 – 224 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 226 – 232 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 234 – 238 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 241 – 243 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 269 – 273 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 274 – 293 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 301 – 312 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 316 – 319 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 321 – 323 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 327 – 330 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 341 – 343 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 348 – 351 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
Database of protein disorder More...DisProti | DP00339 |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P16442 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P16442 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | 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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 121 – 123 | UDP-N-acetyl-galactosamine bindingCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <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>Regioni | 211 – 213 | UDP-N-acetyl-galactosamine bindingCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 |
<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
<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
<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>Keywords - Domaini
Signal-anchor, Transmembrane, Transmembrane helixPhylogenomic databases
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG003563 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P16442 |
KEGG Orthology (KO) More...KOi | K00709 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P16442 |
Family and domain databases
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.
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
<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_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi
Online Mendelian Inheritance in Man (OMIM)
More...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<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Molecular genetic basis of the histo-blood group ABO system."
Yamamoto F., Clausen H., White T., Marken J., Hakomori S.
Nature 345:229-233(1990) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. - Ref.3"Genomic cloning of the human histo-blood group ABO locus."
Bennett E.P., Steffensen R., Clausen H., Weghuis D.O., Geurts van Kessel A.
Biochem. Biophys. Res. Commun. 206:318-325(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, VARIANT LEU-156. - Ref.4"Human histo-blood group ABO gene locus alleles."
Yamamoto F.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], POLYMORPHISM, VARIANTS LEU-156; GLY-176; SER-235 AND MET-266. - Ref.7"Aberrant intracellular trafficking of a variant B glycosyltransferase."
Seltsam A., Gruger D., Just B., Figueiredo C., Gupta C.D., Deluca D.S., Blasczyk R.
Transfusion 48:1898-1905(2008) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, VARIANTS ARG-230; SER-235; MET-266 AND ALA-268. - Ref.8SeattleSNPs variation discovery resource
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], POLYMORPHISM, 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. - Ref.9"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], POLYMORPHISM, VARIANTS GLY-176; SER-235; MET-266 AND ALA-268. - Ref.10"The nature of diversity and diversification at the ABO locus."
Seltsam A., Hallensleben M., Kollmann A., Blasczyk R.
Blood 102:3035-3042(2003) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, POLYMORPHISM, VARIANTS SER-74; LEU-156; MET-163; GLY-176; TRP-198; SER-235; MET-266; ALA-268; ARG-268; ARG-288 AND MET-346. - Ref.11"Molecular genetic analysis of variant phenotypes of the ABO blood group system."
Ogasawara K., Yabe R., Uchikawa M., Saitou N., Bannai M., Nakata K., Takenaka M., Fujisawa K., Ishikawa Y., Juji T., Tokunaga K.
Blood 88:2732-2737(1996) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-354, POLYMORPHISM, 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. - Ref.13"Evolution of the O alleles of the human ABO blood group gene."
Roubinet F., Despiau S., Calafell F., Jin F., Bertanpetit J., Saitou N., Blancher A.
Transfusion 44:707-715(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-354, POLYMORPHISM, VARIANTS GLY-176; SER-235; MET-266 AND ALA-268. - Ref.14"A novel B Transferase."
Seltsam A., Hallensleben M., Salama A., Blasczyk R.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 126-354, POLYMORPHISM, VARIANTS GLY-176; SER-235 AND MET-346. - Ref.15"Animal histo-blood group ABO genes."
Kominato Y., McNeill P.D., Yamamoto M., Russell M., Hakomori S., Yamamoto F.
Biochem. Biophys. Res. Commun. 189:154-164(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-334, POLYMORPHISM, VARIANTS MET-266 AND ALA-268. - Ref.16"Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions."
Yamamoto F., Hakomori S.
J. Biol. Chem. 265:19257-19262(1990) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION, POLYMORPHISM. - Ref.17"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."
Yu L.C., Lee H.L., Chan Y.S., Lin M.
Biochem. Biophys. Res. Commun. 262:487-493(1999) [PubMed] [Europe PMC] [Abstract]Cited for: POLYMORPHISM, VARIANT ALA-234.
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_019147 | 35 | G → R1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_019148 | 36 | V → F1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_019149 | 63 | R → H1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_019150 | 74 | P → S2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_003408 | 80 – 81 | CR → W. | 2 | |
| <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_003409 | 156 | P → L in allele A2. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_019151 | 161 | R → H1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_036738 | 163 | T → M in allele Aw08. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_003410 | 176 | R → G in allele Aw08 and allele Bw08. 7 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_036739 | 198 | R → W in allele Aw07. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_019152 | 199 | R → C1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_036740 | 214 | M → R in allele Bel01; loss of manganese binding and reduced catalytic activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_019153 | 216 | F → I2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_036741 | 223 | E → D in allele B106. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_055227 | 230 | G → R in group B transferase; lower-level protein expression and intracellular cytoplasmic mislocation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_072628 | 234 | P → A in allele B(A). 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_003411 | 235 | G → S in allele Bw08. 8 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_033540 | 257 | P → L. Corresponds to variant dbSNP:rs8176745Ensembl. | 1 | |
| <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_003412 | 266 | L → M in allele Bw08. 8 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_003413 | 268 | G → A in allele Bw08. 7 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_033541 | 268 | G → R in allele Aw08. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_019154 | 277 | V → M2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_036742 | 288 | M → R1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_036743 | 291 | D → N in allele B104. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_036744 | 346 | K → M in allele Bw08. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_036745 | 352 | R → G in allele A107. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_003414 | 352 | R → W in allele A106 and allele B3. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | J05175 mRNA Translation: AAA36792.1 X84746 , X84747, X84748, X84749, X84750, X84751, X84752 Genomic DNA Translation: CAA59233.1 AF134412 mRNA Translation: AAD26572.1 AF134413 mRNA Translation: AAD26573.1 AF134414 mRNA Translation: AAD26574.1 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 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.654423 |
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>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>Keywords - Coding sequence diversityi
Polymorphism<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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P16442 | Histo-blood group ABO system transferase | 354 | |||
| UPI00051265C9 | 401 | ||||
| UPI0004F085B9 | 347 | ||||
| ABO, alpha 1-3-N-acetylgalactosaminyltransferase and alpha 1-3-galactosyltransferase | 344 | ||||
| UPI0005FB9467 | 366 | ||||
| +126 | |||||
<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
| 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: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | J05175 mRNA Translation: AAA36792.1 X84746 , X84747, X84748, X84749, X84750, X84751, X84752 Genomic DNA Translation: CAA59233.1 AF134412 mRNA Translation: AAD26572.1 AF134413 mRNA Translation: AAD26573.1 AF134414 mRNA Translation: AAD26574.1 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 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.654423 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks 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 | [»] | |
Database of protein disorder More...DisProti | DP00339 | |||||
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P16442 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P16442 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 106546, 3 interactors |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P16442 |
ChEMBL database of bioactive drug-like small molecules More...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 |
Protein family/group databases
Carbohydrate-Active enZymes More...CAZyi | GT6 Glycosyltransferase Family 6 |
PTM databases
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 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ABO |
Domain mapping of disease mutations (DMDM) More...DMDMi | 114949 |
Proteomic databases
PeptideAtlas More...PeptideAtlasi | P16442 |
PRoteomics IDEntifications database More...PRIDEi | P16442 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 53361 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 28 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Database of genes from NCBI RefSeq genomes More...GeneIDi | 28 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:28 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 28 |
DisGeNET More...DisGeNETi | 28 |
GeneCards: human genes, protein and diseases More...GeneCardsi | ABO |
Human Gene Nomenclature Database More...HGNCi | HGNC:79 ABO |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 110300 gene 616093 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P16442 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA24415 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG003563 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P16442 |
KEGG Orthology (KO) More...KOi | K00709 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P16442 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00378 |
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 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P16442 |
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 |
Protein Ontology More...PROi | PR:P16442 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Family and domain databases
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 |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | 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 namei | BGAT_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>Accessioni | P16442Primary (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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>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. | ||
| <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 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. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Blood group antigen proteins
Nomenclature of blood group antigens and list of entries - Human chromosome 9
Human chromosome 9: entries, gene names and cross-references to MIM - 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 - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
