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Entry version 170 (02 Jun 2021)
Sequence version 1 (01 Oct 1996)
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Protein

4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5

Gene

FUT5

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

Catalyzes preferentially the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl-beta-D-glucosamine (GlcNAc) of an N-acetyllactosamine unit (type 2 chain) of an oligosacccharide, or a glycoprotein- and a glycolipid-linked N-acetyllactosamine unit via an alpha (1,3) linkage and participates to the surface espression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens (PubMed:14718375, PubMed:1740457, PubMed:7721776, PubMed:9737988, PubMed:17604274, PubMed:9737989).

Preferentially transfers fucose to the GlcNAc of an internal N-acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor substrate (PubMed:7721776, PubMed:17604274).

Also catalyzes to a lesser extend the transfer of L-fucose to the GlcNAc of a type 1 (beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl) or H-type 1 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc) chain oligosacccharide via an alpha (1,4) linkage (PubMed:14718375, PubMed:1740457, PubMed:7721776, PubMed:9737988, PubMed:17604274).

Preferentially catalyzes sialylated type 2 oligosacccharide acceptors over neutral type 2 or H type 2 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc) oligosacccharide acceptors (PubMed:1740457, PubMed:9737989).

Lactose-based structures are also acceptor substrates (PubMed:1740457, PubMed:7721776).

6 Publications

<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 describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 1.70 min(-1) for the alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc (PubMed:9737989). kcat is 9.3 min(-1) for the beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine (PubMed:9737988).2 Publications
  1. KM=38 µM for GDP-fucose1 Publication
  2. KM=1.1 µM for alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc-sp-biotin1 Publication
  3. KM=18.8 µM for GDP-fucose1 Publication
  4. KM=60 mM for beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine1 Publication
  5. KM=3.4 mM for beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine1 Publication
  1. Vmax=1 nmol/h/mg enzyme toward GDP-fucose1 Publication
  2. Vmax=38 nmol/h/mg enzyme toward alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc-sp-biotin1 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.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

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

GO - Biological processi

<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 functionGlycosyltransferase, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS05379-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.4.1.152, 2681
2.4.1.65, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
Q11128

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-9037629, Lewis blood group biosynthesis

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

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UniPathwayi
UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

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CAZyi
GT10, Glycosyltransferase Family 10

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001430

<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:
4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5 (EC:2.4.1.1521 Publication)
Alternative name(s):
3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT5 (EC:2.4.1.651 Publication)
Fucosyltransferase 5
Fucosyltransferase V
Short name:
Fuc-TV1 Publication
Short name:
FucT-V
Galactoside 3-L-fucosyltransferase
<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:FUT5Imported
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:4016, FUT5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
136835, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q11128

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000130383.7

<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 – 15CytoplasmicSequence analysisAdd BLAST15
<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>Transmembranei16 – 34Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST19
Topological domaini35 – 374LumenalSequence analysisAdd BLAST340

Keywords - Cellular componenti

Golgi apparatus, Membrane

<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>Mutagenesisi86N → H: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 oligosaccharide acceptor; when associated with I-87 and S-92. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 oligosaccharide acceptors; when associated with I-87 and S-92. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with I-87 and S-92. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with I-87 and S-92. 1 Publication1
Mutagenesisi87T → I: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with H-86 and S-92. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-86 and S-92. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with H-86 and S-92. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with H-86 and S-92. 1 Publication1
Mutagenesisi87T → K: Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with R-124; E-125 and V-126. Significantly decreases cell-surface expression of VIM2 antigen; when associated with R-124; E-125 and V-126. 1 Publication1
Mutagenesisi92P → S: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity; when associated with H-86 and I-87. Increases significantly 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with H-86 and I-87. Decreases of 50% the 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity with type 2 glycolipid nLc4Cer; when associated with H-86 and I-87. Increases significantly the 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity with type 1 glycolipid Lc4Cer; when associated with H-86 and I-87. 1 Publication1
Mutagenesisi101A → T: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated withH-105; R-110; K-111 and T-118. 1 Publication1
Mutagenesisi105N → H: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; R-110; K-111 and T-118. 1 Publication1
Mutagenesisi110S → R: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; K-111 and T-118. 1 Publication1
Mutagenesisi111S → K: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; R-110 and T-118. 1 Publication1
Mutagenesisi118A → T: Does not affect 4-galactosyl-N-acetylglucosaminide 3-alpha-L- and 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity; when associated with T-101; H-105; R-110 and K-111. 1 Publication1
Mutagenesisi124W → A: Decreases both alpha-(1,3)-fucosyltransferase and alpha-(1,4)-fucosyltransferase activity of 50%. 1 Publication1
Mutagenesisi124W → R: Increases alpha-(1,3)-fucosyltransferase activity. Loss of alpha-(1,4)-fucosyltransferase activity. Loss of site-specific fucosylation; when associated with E-125 and V-126. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; E-125 and V-126. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; E-125 and V-126. 2 Publications1
Mutagenesisi124W → V: Does not affect alpha-(1,3)-fucosyltransferase activity. Loss of alpha-(1,4)-fucosyltransferase activity. 1 Publication1
Mutagenesisi125D → E: Loss of site-specific fucosylation; when associated with R-124 and V-126. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; R-124 and V-126. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; R-124 and V-126. 1 Publication1
Mutagenesisi126I → V: Loss of site-specific fucosylation; when associated with R-124 and E-125. Reverses the preferential fucosylation properties leading to production of 72% of sialyl-lewis x; when associated with K-87; R-124 and E-125. Significantly decreases to cell-surface expression of VIM2 antigen; when associated with K-87; R-124 and E-125. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
2527

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28432

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q11128, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3146

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
FUT5

Domain mapping of disease mutations (DMDM)

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DMDMi
1730135

<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_00002211051 – 3744-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5Add BLAST374

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>Glycosylationi60N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi105N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi167N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi198N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q11128

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q11128

MaxQB - The MaxQuant DataBase

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MaxQBi
Q11128

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q11128

PeptideAtlas

More...
PeptideAtlasi
Q11128

PRoteomics IDEntifications database

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PRIDEi
Q11128

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
58871

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
Q11128, 4 sites

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q11128

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

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PhosphoSitePlusi
Q11128

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Liver, colon and testis and trace amounts in T-cells and brain.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000130383, Expressed in bone marrow and 13 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q11128, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q11128, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000130383, Tissue enhanced (bone)

<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

STRING: functional protein association networks

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STRINGi
9606.ENSP00000466880

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q11128

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q11128, 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

<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

<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 10 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2619, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q11128

Database of Orthologous Groups

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OrthoDBi
551308at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q11128

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.11660, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR031481, Glyco_tran_10_N
IPR001503, Glyco_trans_10
IPR038577, GT10-like_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11929, PTHR11929, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17039, Glyco_tran_10_N, 1 hit
PF00852, Glyco_transf_10, 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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q11128-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDPLGPAKPQ WLWRRCLAGL LFQLLVAVCF FSYLRVSRDD ATGSPRPGLM
60 70 80 90 100
AVEPVTGAPN GSRCQDSMAT PAHPTLLILL WTWPFNTPVA LPRCSEMVPG
110 120 130 140 150
AADCNITADS SVYPQADAVI VHHWDIMYNP SANLPPPTRP QGQRWIWFSM
160 170 180 190 200
ESPSNCRHLE ALDGYFNLTM SYRSDSDIFT PYGWLEPWSG QPAHPPLNLS
210 220 230 240 250
AKTELVAWAV SNWKPDSARV RYYQSLQAHL KVDVYGRSHK PLPKGTMMET
260 270 280 290 300
LSRYKFYLAF ENSLHPDYIT EKLWRNALEA WAVPVVLGPS RSNYERFLPP
310 320 330 340 350
DAFIHVDDFQ SPKDLARYLQ ELDKDHARYL SYFRWRETLR PRSFSWALAF
360 370
CKACWKLQQE SRYQTVRSIA AWFT
Length:374
Mass (Da):43,008
Last modified:October 1, 1996 - v1
<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:iB825281521B57939
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7ENC0K7ENC0_HUMAN
4-galactosyl-N-acetylglucosaminide ...
FUT5
374Annotation score:

Annotation score:2 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>

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_022122187P → L. Corresponds to variant dbSNP:rs778970Ensembl.1
Natural variantiVAR_055845338T → M. Corresponds to variant dbSNP:rs4807054EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M81485 Genomic DNA Translation: AAA98117.1
U27329 mRNA Translation: AAC50188.1
U27330 mRNA Translation: AAC50189.1
AK291087 mRNA Translation: BAF83776.1
AC024592 Genomic DNA No translation available.
CH471139 Genomic DNA Translation: EAW69134.1
BC140905 mRNA Translation: AAI40906.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS12154.1

Protein sequence database of the Protein Information Resource

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PIRi
A42270

NCBI Reference Sequences

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RefSeqi
NP_002025.2, NM_002034.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000252675; ENSP00000252675; ENSG00000130383

Database of genes from NCBI RefSeq genomes

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GeneIDi
2527

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2527

UCSC genome browser

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UCSCi
uc060sei.1, human

<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

Functional Glycomics Gateway - GTase

Fucosyltransferase 5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81485 Genomic DNA Translation: AAA98117.1
U27329 mRNA Translation: AAC50188.1
U27330 mRNA Translation: AAC50189.1
AK291087 mRNA Translation: BAF83776.1
AC024592 Genomic DNA No translation available.
CH471139 Genomic DNA Translation: EAW69134.1
BC140905 mRNA Translation: AAI40906.1
CCDSiCCDS12154.1
PIRiA42270
RefSeqiNP_002025.2, NM_002034.2

3D structure databases

Database of comparative protein structure models

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ModBasei
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SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi9606.ENSP00000466880

Chemistry databases

BindingDBiQ11128
ChEMBLiCHEMBL3146
SwissLipidsiSLP:000001430

Protein family/group databases

CAZyiGT10, Glycosyltransferase Family 10

PTM databases

GlyGeniQ11128, 4 sites
iPTMnetiQ11128
PhosphoSitePlusiQ11128

Genetic variation databases

BioMutaiFUT5
DMDMi1730135

Proteomic databases

jPOSTiQ11128
MassIVEiQ11128
MaxQBiQ11128
PaxDbiQ11128
PeptideAtlasiQ11128
PRIDEiQ11128
ProteomicsDBi58871

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
24015, 36 antibodies

The DNASU plasmid repository

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DNASUi
2527

Genome annotation databases

EnsembliENST00000252675; ENSP00000252675; ENSG00000130383
GeneIDi2527
KEGGihsa:2527
UCSCiuc060sei.1, human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2527
DisGeNETi2527

GeneCards: human genes, protein and diseases

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GeneCardsi
FUT5
HGNCiHGNC:4016, FUT5
HPAiENSG00000130383, Tissue enhanced (bone)
MIMi136835, gene
neXtProtiNX_Q11128
PharmGKBiPA28432
VEuPathDBiHostDB:ENSG00000130383.7

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG2619, Eukaryota
InParanoidiQ11128
OrthoDBi551308at2759
PhylomeDBiQ11128

Enzyme and pathway databases

UniPathwayiUPA00378
BioCyciMetaCyc:HS05379-MONOMER
BRENDAi2.4.1.152, 2681
2.4.1.65, 2681
PathwayCommonsiQ11128
ReactomeiR-HSA-9037629, Lewis blood group biosynthesis

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
2527, 8 hits in 972 CRISPR screens

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
FUT5

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

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GenomeRNAii
2527
PharosiQ11128, Tbio

Protein Ontology

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PROi
PR:Q11128
RNActiQ11128, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000130383, Expressed in bone marrow and 13 other tissues
ExpressionAtlasiQ11128, baseline and differential
GenevisibleiQ11128, HS

Family and domain databases

Gene3Di3.40.50.11660, 1 hit
InterProiView protein in InterPro
IPR031481, Glyco_tran_10_N
IPR001503, Glyco_trans_10
IPR038577, GT10-like_sf
PANTHERiPTHR11929, PTHR11929, 1 hit
PfamiView protein in Pfam
PF17039, Glyco_tran_10_N, 1 hit
PF00852, Glyco_transf_10, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiFUT5_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: Q11128
Secondary accession number(s): A8K4X2
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 2, 2021
This is version 170 of the entry and version 1 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

Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families
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