Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 134 (12 Aug 2020)
Sequence version 1 (01 Jun 2003)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Xylosyltransferase 1

Gene

XYLT1

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 the first step in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans, such as DCN. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein (PubMed:15461586, PubMed:17189265, PubMed:24581741, PubMed:23982343). Required for normal embryonic and postnatal skeleton development, especially of the long bones (PubMed:24581741, PubMed:23982343). Required for normal maturation of chondrocytes during bone development, and normal onset of ossification (By similarity).By similarity4 Publications

Miscellaneous

Activity is strongly reduced in seminal plasma of infertile men.1 Publication

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

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

a divalent metal cation2 Publications

<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

  1. KM=0.9 µM for recombinant bikunin2 Publications
  1. Vmax=764 pmol/h/mg enzyme with recombinant bikunin as substrate2 Publications

<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: chondroitin sulfate biosynthesis

This protein is involved in the pathway chondroitin sulfate biosynthesis, which is part of Glycan metabolism.2 Publications
View all proteins of this organism that are known to be involved in the pathway chondroitin sulfate biosynthesis and in Glycan metabolism.

Pathwayi: heparan sulfate biosynthesis

This protein is involved in the pathway heparan sulfate biosynthesis, which is part of Glycan metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway heparan sulfate biosynthesis and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei333UDP-xylose; via carbonyl oxygenCombined sources1 Publication1
Binding sitei361UDP-xyloseCombined sources1 Publication1
Binding sitei575UDP-xyloseCombined sources1 Publication1

<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
LigandMetal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS02509-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.2.26, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q86Y38

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1971475, A tetrasaccharide linker sequence is required for GAG synthesis

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q86Y38

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

More...
UniPathwayi
UPA00755
UPA00756

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT14, Glycosyltransferase Family 14

<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:
Xylosyltransferase 1 (EC:2.4.2.267 Publications)
Alternative name(s):
Peptide O-xylosyltransferase 1
Xylosyltransferase I
Short name:
XT-I
Short name:
XylT-I
<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:XYLT1
Synonyms:XT1
<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 16

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000103489.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:15516, XYLT1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
608124, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q86Y38

<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 Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 – 17CytoplasmicSequence analysisAdd BLAST17
<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>Transmembranei18 – 38Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini39 – 959LumenalSequence analysisAdd BLAST921

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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Desbuquois dysplasia 2 (DBQD2)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA chondrodysplasia characterized by severe prenatal and postnatal growth retardation (less than -5 SD), joint laxity, short extremities, progressive scoliosis, round face, midface hypoplasia, prominent bulging eyes. The main radiologic features are short long bones with metaphyseal splay, a 'Swedish key' appearance of the proximal femur (exaggerated trochanter), and advance carpal and tarsal bone age. Two forms of Desbuquois dysplasia are distinguished on the basis of the presence or absence of characteristic hand anomalies: an extra ossification center distal to the second metacarpal, delta phalanx, bifid distal thumb phalanx, and phalangeal dislocations.
Related information in OMIM
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_071273481R → W in DBQD2; causes retention in the endoplasmic reticulum; impairs dermatan sulfate proteoglycan synthesis. 2 PublicationsCorresponds to variant dbSNP:rs587777366EnsemblClinVar.1
Natural variantiVAR_071274598R → C in DBQD2; causes retention in the endoplasmic reticulum. 2 PublicationsCorresponds to variant dbSNP:rs587777367EnsemblClinVar.1
Pseudoxanthoma elasticum (PXE)1 Publication
The gene represented in this entry acts as a disease modifier.
Disease descriptionA multisystem disorder characterized by accumulation of mineralized and fragmented elastic fibers in the skin, vascular walls, and Burch membrane in the eye. Clinically, patients exhibit characteristic lesions of the posterior segment of the eye including peau d'orange, angioid streaks, and choroidal neovascularizations, of the skin including soft, ivory colored papules in a reticular pattern that predominantly affect the neck and large flexor surfaces, and of the cardiovascular system with peripheral and coronary arterial occlusive disease as well as gastrointestinal bleedings.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071271115A → S in PXE; acts as a modifier of disease severity; results in higher serum xylosyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs61758388EnsemblClinVar.1

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>Mutagenesisi257C → A: No effect. 1 Publication1
Mutagenesisi276C → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi285C → A: No effect. 1 Publication1
Mutagenesisi301C → A: No effect. 1 Publication1
Mutagenesisi314D → G: No effect. 1 Publication1
Mutagenesisi316D → G: No effect. 1 Publication1
Mutagenesisi462Q → A or W: No effect on enzyme activity. 1 Publication1
Mutagenesisi462Q → R: Decreased enzyme activity. 1 Publication1
Mutagenesisi471C → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi494D → A: Decreased enzyme activity. 1 Publication1
Mutagenesisi494D → N: Loss of enzyme activity. 1 Publication1
Mutagenesisi529E → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi542C → A: No effect. 1 Publication1
Mutagenesisi557R → N: No effect on enzyme activity. 1 Publication1
Mutagenesisi561C → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi562 – 572Missing : Loss of enzyme activity. 1 PublicationAdd BLAST11
Mutagenesisi563C → A: No effect. 1 Publication1
Mutagenesisi572C → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi574C → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi598R → A: Strongly decreased enzyme activity; when associated with A-599. 1 Publication1
Mutagenesisi599K → A: Decreased enzyme activity. Strongly decreased enzyme activity; when associated with A-598. 1 Publication1
Mutagenesisi675C → A: No effect. 1 Publication1
Mutagenesisi745D → E: No effect. 1 Publication1
Mutagenesisi745D → G: Abolishes enzyme activity but does not affect UDP-binding. 1 Publication1
Mutagenesisi746W → D, N or G: Strongly reduced enzyme activity but does not affect UDP-binding. 1 Publication1
Mutagenesisi747D → G or E: Reduced enzyme activity but does not affect UDP-binding. 1 Publication1
Mutagenesisi749K → A: No effect on enzyme activity. 1 Publication1
Mutagenesisi750E → K: No effect on enzyme activity. 1 Publication1
Mutagenesisi754R → E: No effect on enzyme activity. 1 Publication1
Mutagenesisi920C → A: No effect. 1 Publication1
Mutagenesisi927C → A: No effect. 1 Publication1
Mutagenesisi933C → A: No effect. 1 Publication1

Keywords - Diseasei

Disease mutation, Dwarfism

Organism-specific databases

DisGeNET

More...
DisGeNETi
64131

MalaCards human disease database

More...
MalaCardsi
XYLT1
MIMi264800, phenotype
615777, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000103489

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
1425, Desbuquois syndrome
370930, XYLT1-CDG

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA37973

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q86Y38, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
XYLT1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
71164803

<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_00001914001 – 959Xylosyltransferase 1Add BLAST959

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>Glycosylationi226N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi257 ↔ 285Combined sources1 Publication
Disulfide bondi301 ↔ 542Combined sources1 Publication
Glycosylationi421N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi561 ↔ 574Combined sources1 Publication
Disulfide bondi563 ↔ 572Combined sources1 Publication
Disulfide bondi675 ↔ 927Combined sources1 Publication
Glycosylationi777N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi920 ↔ 933Combined sources1 Publication

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

Contains 7 disulfide bonds.1 Publication
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q86Y38

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q86Y38

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q86Y38

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q86Y38

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

More...
PaxDbi
Q86Y38

PeptideAtlas

More...
PeptideAtlasi
Q86Y38

PRoteomics IDEntifications database

More...
PRIDEi
Q86Y38

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
70370

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q86Y38, 4 sites, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q86Y38

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

More...
PhosphoSitePlusi
Q86Y38

<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

Widely expressed. Expressed at higher level in placenta, kidney and pancreas. Weakly expressed in skeletal muscle.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000103489, Expressed in tibia and 234 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q86Y38, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000103489, Tissue enhanced (lymphoid)

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
122080, 4 interactors

Protein interaction database and analysis system

More...
IntActi
Q86Y38, 3 interactors

Molecular INTeraction database

More...
MINTi
Q86Y38

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000261381

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q86Y38, protein

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

Secondary structure

1959
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q86Y38

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni390 – 392UDP-xylose bindingCombined sources1 Publication3
Regioni494 – 495UDP-xylose bindingCombined sources1 Publication2
Regioni598 – 599UDP-xylose bindingCombined sources1 Publication2

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0799, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157381

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012840_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q86Y38

KEGG Orthology (KO)

More...
KOi
K00771

Identification of Orthologs from Complete Genome Data

More...
OMAi
AKEICGG

Database of Orthologous Groups

More...
OrthoDBi
564384at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q86Y38

TreeFam database of animal gene trees

More...
TreeFami
TF315534

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003406, Glyco_trans_14
IPR039864, Xylosyltrans
IPR043538, XYLT
IPR024448, XylT_C

The PANTHER Classification System

More...
PANTHERi
PTHR46025, PTHR46025, 1 hit
PTHR46025:SF2, PTHR46025:SF2, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02485, Branch, 1 hit
PF12529, Xylo_C, 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>Sequencei

<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.

Q86Y38-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVAAPCARRL ARRSHSALLA ALTVLLLQTL VVWNFSSLDS GAGERRGGAA
60 70 80 90 100
VGGGEQPPPA PAPRRERRDL PAEPAAARGG GGGGGGGGGG RGPQARARGG
110 120 130 140 150
GPGEPRGQQP ASRGALPARA LDPHPSPLIT LETQDGYFSH RPKEKVRTDS
160 170 180 190 200
NNENSVPKDF ENVDNSNFAP RTQKQKHQPE LAKKPPSRQK ELLKRKLEQQ
210 220 230 240 250
EKGKGHTFPG KGPGEVLPPG DRAAANSSHG KDVSRPPHAR KTGGSSPETK
260 270 280 290 300
YDQPPKCDIS GKEAISALSR AKSKHCRQEI GETYCRHKLG LLMPEKVTRF
310 320 330 340 350
CPLEGKANKN VQWDEDSVEY MPANPVRIAF VLVVHGRASR QLQRMFKAIY
360 370 380 390 400
HKDHFYYIHV DKRSNYLHRQ VLQVSRQYSN VRVTPWRMAT IWGGASLLST
410 420 430 440 450
YLQSMRDLLE MTDWPWDFFI NLSAADYPIR TNDQLVAFLS RYRDMNFLKS
460 470 480 490 500
HGRDNARFIR KQGLDRLFLE CDAHMWRLGD RRIPEGIAVD GGSDWFLLNR
510 520 530 540 550
RFVEYVTFST DDLVTKMKQF YSYTLLPAES FFHTVLENSP HCDTMVDNNL
560 570 580 590 600
RITNWNRKLG CKCQYKHIVD WCGCSPNDFK PQDFHRFQQT ARPTFFARKF
610 620 630 640 650
EAVVNQEIIG QLDYYLYGNY PAGTPGLRSY WENVYDEPDG IHSLSDVTLT
660 670 680 690 700
LYHSFARLGL RRAETSLHTD GENSCRYYPM GHPASVHLYF LADRFQGFLI
710 720 730 740 750
KHHATNLAVS KLETLETWVM PKKVFKIASP PSDFGRLQFS EVGTDWDAKE
760 770 780 790 800
RLFRNFGGLL GPMDEPVGMQ KWGKGPNVTV TVIWVDPVNV IAATYDILIE
810 820 830 840 850
STAEFTHYKP PLNLPLRPGV WTVKILHHWV PVAETKFLVA PLTFSNRQPI
860 870 880 890 900
KPEEALKLHN GPLRNAYMEQ SFQSLNPVLS LPINPAQVEQ ARRNAASTGT
910 920 930 940 950
ALEGWLDSLV GGMWTAMDIC ATGPTACPVM QTCSQTAWSS FSPDPKSELG

AVKPDGRLR
Length:959
Mass (Da):107,569
Last modified:June 1, 2003 - 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:i056FC3F66EFD4D81
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071271115A → S in PXE; acts as a modifier of disease severity; results in higher serum xylosyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs61758388EnsemblClinVar.1
Natural variantiVAR_049324325P → R. Corresponds to variant dbSNP:rs28709752Ensembl.1
Natural variantiVAR_071272406R → W1 PublicationCorresponds to variant dbSNP:rs201009902Ensembl.1
Natural variantiVAR_071273481R → W in DBQD2; causes retention in the endoplasmic reticulum; impairs dermatan sulfate proteoglycan synthesis. 2 PublicationsCorresponds to variant dbSNP:rs587777366EnsemblClinVar.1
Natural variantiVAR_071274598R → C in DBQD2; causes retention in the endoplasmic reticulum. 2 PublicationsCorresponds to variant dbSNP:rs587777367EnsemblClinVar.1
Natural variantiVAR_071275665T → M1 PublicationCorresponds to variant dbSNP:rs79030430Ensembl.1
Natural variantiVAR_049325766P → A. Corresponds to variant dbSNP:rs12325439Ensembl.1
Natural variantiVAR_049326839V → I. Corresponds to variant dbSNP:rs7200466Ensembl.1
Natural variantiVAR_049327892R → Q. Corresponds to variant dbSNP:rs35309694Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ539163 mRNA Translation: CAD62248.1
AJ277441 mRNA Translation: CAC16787.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10569.1

NCBI Reference Sequences

More...
RefSeqi
NP_071449.1, NM_022166.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000261381; ENSP00000261381; ENSG00000103489

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
64131

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:64131

UCSC genome browser

More...
UCSCi
uc002dfa.4, human

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

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ539163 mRNA Translation: CAD62248.1
AJ277441 mRNA Translation: CAC16787.1
CCDSiCCDS10569.1
RefSeqiNP_071449.1, NM_022166.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6EJ7X-ray2.00A232-959[»]
6EJ8X-ray2.09A232-959[»]
6EJ9X-ray2.02A232-959[»]
6EJAX-ray1.94A232-959[»]
6EJBX-ray2.56A232-959[»]
6EJCX-ray2.06A232-959[»]
6EJDX-ray2.68A232-959[»]
6EJEX-ray2.43A232-959[»]
6FOAX-ray1.87A232-959[»]
SMRiQ86Y38
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi122080, 4 interactors
IntActiQ86Y38, 3 interactors
MINTiQ86Y38
STRINGi9606.ENSP00000261381

Protein family/group databases

CAZyiGT14, Glycosyltransferase Family 14

PTM databases

GlyGeniQ86Y38, 4 sites, 1 O-linked glycan (1 site)
iPTMnetiQ86Y38
PhosphoSitePlusiQ86Y38

Polymorphism and mutation databases

BioMutaiXYLT1
DMDMi71164803

Proteomic databases

EPDiQ86Y38
jPOSTiQ86Y38
MassIVEiQ86Y38
MaxQBiQ86Y38
PaxDbiQ86Y38
PeptideAtlasiQ86Y38
PRIDEiQ86Y38
ProteomicsDBi70370

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
2316, 104 antibodies

Genome annotation databases

EnsembliENST00000261381; ENSP00000261381; ENSG00000103489
GeneIDi64131
KEGGihsa:64131
UCSCiuc002dfa.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
64131
DisGeNETi64131
EuPathDBiHostDB:ENSG00000103489.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
XYLT1
HGNCiHGNC:15516, XYLT1
HPAiENSG00000103489, Tissue enhanced (lymphoid)
MalaCardsiXYLT1
MIMi264800, phenotype
608124, gene
615777, phenotype
neXtProtiNX_Q86Y38
OpenTargetsiENSG00000103489
Orphaneti1425, Desbuquois syndrome
370930, XYLT1-CDG
PharmGKBiPA37973

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0799, Eukaryota
GeneTreeiENSGT00940000157381
HOGENOMiCLU_012840_0_0_1
InParanoidiQ86Y38
KOiK00771
OMAiAKEICGG
OrthoDBi564384at2759
PhylomeDBiQ86Y38
TreeFamiTF315534

Enzyme and pathway databases

UniPathwayiUPA00755
UPA00756
BioCyciMetaCyc:HS02509-MONOMER
BRENDAi2.4.2.26, 2681
PathwayCommonsiQ86Y38
ReactomeiR-HSA-1971475, A tetrasaccharide linker sequence is required for GAG synthesis
SignaLinkiQ86Y38

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
64131, 5 hits in 870 CRISPR screens

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

More...
ChiTaRSi
XYLT1, human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
XYLT1

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

More...
GenomeRNAii
64131
PharosiQ86Y38, Tbio

Protein Ontology

More...
PROi
PR:Q86Y38
RNActiQ86Y38, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000103489, Expressed in tibia and 234 other tissues
GenevisibleiQ86Y38, HS

Family and domain databases

InterProiView protein in InterPro
IPR003406, Glyco_trans_14
IPR039864, Xylosyltrans
IPR043538, XYLT
IPR024448, XylT_C
PANTHERiPTHR46025, PTHR46025, 1 hit
PTHR46025:SF2, PTHR46025:SF2, 1 hit
PfamiView protein in Pfam
PF02485, Branch, 1 hit
PF12529, Xylo_C, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiXYLT1_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: Q86Y38
Secondary accession number(s): Q9H1B6
<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: May 10, 2005
Last sequence update: June 1, 2003
Last modified: August 12, 2020
This is version 134 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again