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Protein

Exostosin-1

Gene

EXT1

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

Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor. Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).2 Publications

<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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Mn2+By similarity

<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.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘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 sitei518SubstrateBy similarity1
<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 bindingi567Manganese; catalyticBy similarity1
Binding sitei595SubstrateBy similarity1
<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 sitei654By similarity1

<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
LigandManganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS00012-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.4.1.224 2681
2.4.1.225 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-2022928 HS-GAG biosynthesis
R-HSA-3656237 Defective EXT2 causes exostoses 2
R-HSA-3656253 Defective EXT1 causes exostoses 1, TRPS2 and CHDS

SIGNOR Signaling Network Open Resource

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SIGNORi
Q16394

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

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UniPathwayi
UPA00378

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GT47 Glycosyltransferase Family 47
GT64 Glycosyltransferase Family 64

<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:
Exostosin-1 (EC:2.4.1.224, EC:2.4.1.225)
Alternative name(s):
Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
Multiple exostoses protein 1
Putative tumor suppressor protein EXT1
<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:EXT1
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000182197.10

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3512 EXT1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608177 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q16394

<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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 domaini1 – 7CytoplasmicSequence analysis7
<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>Transmembranei8 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini29 – 746LumenalSequence analysisAdd BLAST718

Keywords - Cellular componenti

Endoplasmic reticulum, 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

<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

Hereditary multiple exostoses 1 (EXT1)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionEXT is a genetically heterogeneous bone disorder caused by genes segregating on human chromosomes 8, 11, and 19 and designated EXT1, EXT2 and EXT3 respectively. EXT is a dominantly inherited skeletal disorder primarily affecting endochondral bone during growth. The disease is characterized by formation of numerous cartilage-capped, benign bone tumors (osteocartilaginous exostoses or osteochondromas) that are often accompanied by skeletal deformities and short stature. In a small percentage of cases exostoses have exhibited malignant transformation resulting in an osteosarcoma or chondrosarcoma. Osteochondromas development can also occur as a sporadic event.
See also OMIM:133700
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_01281527Q → K in EXT1; no loss of activity. 1
Natural variantiVAR_012816164D → H in EXT1; loss of activity. 1 Publication1
Natural variantiVAR_012817215 – 221Missing in EXT1. 7
Natural variantiVAR_002370280R → G in EXT1; loss of activity. 3 Publications1
Natural variantiVAR_002371280R → S in EXT1; loss of activity. 1 Publication1
Natural variantiVAR_002372339G → D in EXT1; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs119103288EnsemblClinVar.1
Natural variantiVAR_002373340R → C in EXT1; loss of activity; still able to form an oligomeric complex. 1 PublicationCorresponds to variant dbSNP:rs119103290EnsemblClinVar.1
Natural variantiVAR_002374340R → H in EXT1; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs119103287EnsemblClinVar.1
Natural variantiVAR_002375340R → L in EXT1; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs119103287EnsemblClinVar.1
Natural variantiVAR_002376340R → S in EXT1; loss of activity. 1 Publication1
Natural variantiVAR_012821486A → V in EXT1; no loss of activity. 1 PublicationCorresponds to variant dbSNP:rs188859975EnsemblClinVar.1
Natural variantiVAR_012822496P → L in EXT1; no loss of activity. 1 Publication1
Natural variantiVAR_002377627Missing in EXT1; loss of activity. 1 Publication1
Tricho-rhino-phalangeal syndrome 2 (TRPS2)
The gene represented in this entry is involved in disease pathogenesis. A chromosomal aberration resulting in the loss of functional copies of TRPS1 and EXT1 has been found in TRPS2 patients.
Disease descriptionA syndrome that combines the clinical features of tricho-rhino-phalangeal syndrome type 1 and multiple exostoses type 1. Affected individuals manifest multiple dysmorphic facial features including large, laterally protruding ears, a bulbous nose, an elongated upper lip, as well as sparse scalp hair, winged scapulae, multiple cartilaginous exostoses, redundant skin, and mental retardation.
See also OMIM:150230
Chondrosarcoma (CHDSA)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA malignant neoplasm derived from cartilage cells. Chondrosarcomas range from slow-growing non-metastasizing lesions to highly aggressive metastasizing sarcomas.
See also OMIM:215300

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi27Q → A or P: No effect on heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi27Missing : No effect on heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi164D → E: Abolishes heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi164Missing : Abolishes heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi316N → A: No effect on heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi316Missing : No effect on heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi486A → H: No effect on heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi486Missing : No effect on heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi496P → H: No effect on heparan-sulfate biosynthesis. 1 Publication1
Mutagenesisi496Missing : No effect on heparan-sulfate biosynthesis. 1 Publication1

Keywords - Diseasei

Disease mutation, Hereditary multiple exostoses, Tumor suppressor

Organism-specific databases

DisGeNET

More...
DisGeNETi
2131

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
EXT1

MalaCards human disease database

More...
MalaCardsi
EXT1
MIMi133700 phenotype
150230 phenotype
215300 phenotype

Open Targets

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OpenTargetsi
ENSG00000182197

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

More...
Orphaneti
55880 Chondrosarcoma
321 Multiple osteochondromas
502 Trichorhinophalangeal syndrome type 2

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA27924

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
EXT1

Domain mapping of disease mutations (DMDM)

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DMDMi
20141422

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001496481 – 746Exostosin-1Add BLAST746

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Glycosylationi89N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi330N-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 bondi652 ↔ 704By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q16394

MaxQB - The MaxQuant DataBase

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MaxQBi
Q16394

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

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PaxDbi
Q16394

PeptideAtlas

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PeptideAtlasi
Q16394

PRoteomics IDEntifications database

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PRIDEi
Q16394

ProteomicsDB human proteome resource

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ProteomicsDBi
60869

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q16394

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

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PhosphoSitePlusi
Q16394

<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

Ubiquitous.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000182197 Expressed in 234 organ(s), highest expression level in thoracic aorta

CleanEx database of gene expression profiles

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CleanExi
HS_EXT1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q16394 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q16394 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA044394

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms a homo/hetero-oligomeric complex with EXT2.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108432, 30 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q16394

Protein interaction database and analysis system

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IntActi
Q16394, 2 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000367446

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q16394

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

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SMRi
Q16394

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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>Regioni544 – 549Substrate bindingBy similarity6
Regioni565 – 567Substrate bindingBy similarity3
Regioni650 – 654Substrate bindingBy similarity5
Regioni688 – 701Substrate bindingBy similarityAdd BLAST14

<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 47 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1021 Eukaryota
ENOG410XTFH LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155321

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000266990

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG003459

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q16394

KEGG Orthology (KO)

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KOi
K02366

Identification of Orthologs from Complete Genome Data

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OMAi
SHYWDDS

Database of Orthologous Groups

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OrthoDBi
EOG091G0BDR

Database for complete collections of gene phylogenies

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PhylomeDBi
Q16394

TreeFam database of animal gene trees

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TreeFami
TF314231

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.90.550.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004263 Exostosin
IPR027670 Exostosin-1
IPR015338 EXT_C
IPR029044 Nucleotide-diphossugar_trans

The PANTHER Classification System

More...
PANTHERi
PTHR11062 PTHR11062, 1 hit
PTHR11062:SF97 PTHR11062:SF97, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03016 Exostosin, 1 hit
PF09258 Glyco_transf_64, 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>Sequence (1+)i

<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.

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

Q16394-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQAKKRYFIL LSAGSCLALL FYFGGLQFRA SRSHSRREEH SGRNGLHHPS
60 70 80 90 100
PDHFWPRFPD ALRPFVPWDQ LENEDSSVHI SPRQKRDANS SIYKGKKCRM
110 120 130 140 150
ESCFDFTLCK KNGFKVYVYP QQKGEKIAES YQNILAAIEG SRFYTSDPSQ
160 170 180 190 200
ACLFVLSLDT LDRDQLSPQY VHNLRSKVQS LHLWNNGRNH LIFNLYSGTW
210 220 230 240 250
PDYTEDVGFD IGQAMLAKAS ISTENFRPNF DVSIPLFSKD HPRTGGERGF
260 270 280 290 300
LKFNTIPPLR KYMLVFKGKR YLTGIGSDTR NALYHVHNGE DVVLLTTCKH
310 320 330 340 350
GKDWQKHKDS RCDRDNTEYE KYDYREMLHN ATFCLVPRGR RLGSFRFLEA
360 370 380 390 400
LQAACVPVML SNGWELPFSE VINWNQAAVI GDERLLLQIP STIRSIHQDK
410 420 430 440 450
ILALRQQTQF LWEAYFSSVE KIVLTTLEII QDRIFKHISR NSLIWNKHPG
460 470 480 490 500
GLFVLPQYSS YLGDFPYYYA NLGLKPPSKF TAVIHAVTPL VSQSQPVLKL
510 520 530 540 550
LVAAAKSQYC AQIIVLWNCD KPLPAKHRWP ATAVPVVVIE GESKVMSSRF
560 570 580 590 600
LPYDNIITDA VLSLDEDTVL STTEVDFAFT VWQSFPERIV GYPARSHFWD
610 620 630 640 650
NSKERWGYTS KWTNDYSMVL TGAAIYHKYY HYLYSHYLPA SLKNMVDQLA
660 670 680 690 700
NCEDILMNFL VSAVTKLPPI KVTQKKQYKE TMMGQTSRAS RWADPDHFAQ
710 720 730 740
RQSCMNTFAS WFGYMPLIHS QMRLDPVLFK DQVSILRKKY RDIERL
Length:746
Mass (Da):86,255
Last modified:March 27, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i842CD7E6C1312C1A
GO

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

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H7C1H6H7C1H6_HUMAN
Exostosin-1
EXT1
207Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8WF54F8WF54_HUMAN
Exostosin-1
EXT1
41Annotation score:

Annotation score:1 out of 5

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti60 – 61DA → EP (PubMed:7550340).Curated2
Sequence conflicti60 – 61DA → EP (Ref. 3) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01281527Q → K in EXT1; no loss of activity. 1
Natural variantiVAR_012816164D → H in EXT1; loss of activity. 1 Publication1
Natural variantiVAR_012818215 – 222MLAKASIS → I in isolated osteochondroma; somatic mutation. 1 Publication8
Natural variantiVAR_012817215 – 221Missing in EXT1. 7
Natural variantiVAR_012819235 – 239Missing in multiple osteochondromas. 1 Publication5
Natural variantiVAR_002370280R → G in EXT1; loss of activity. 3 Publications1
Natural variantiVAR_002371280R → S in EXT1; loss of activity. 1 Publication1
Natural variantiVAR_012820316N → S in chondrosarcoma; no loss of activity. 1 Publication1
Natural variantiVAR_002372339G → D in EXT1; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs119103288EnsemblClinVar.1
Natural variantiVAR_002373340R → C in EXT1; loss of activity; still able to form an oligomeric complex. 1 PublicationCorresponds to variant dbSNP:rs119103290EnsemblClinVar.1
Natural variantiVAR_002374340R → H in EXT1; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs119103287EnsemblClinVar.1
Natural variantiVAR_002375340R → L in EXT1; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs119103287EnsemblClinVar.1
Natural variantiVAR_002376340R → S in EXT1; loss of activity. 1 Publication1
Natural variantiVAR_012821486A → V in EXT1; no loss of activity. 1 PublicationCorresponds to variant dbSNP:rs188859975EnsemblClinVar.1
Natural variantiVAR_012822496P → L in EXT1; no loss of activity. 1 Publication1
Natural variantiVAR_002377627Missing in EXT1; loss of activity. 1 Publication1

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
S79639 mRNA Translation: AAB62283.1
AK313129 mRNA Translation: BAG35949.1
CH471060 Genomic DNA Translation: EAW91972.1
BC001174 mRNA Translation: AAH01174.1
U70539 Genomic DNA Translation: AAC51154.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS6324.1

NCBI Reference Sequences

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RefSeqi
NP_000118.2, NM_000127.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.492618

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000378204; ENSP00000367446; ENSG00000182197

Database of genes from NCBI RefSeq genomes

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GeneIDi
2131

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2131

UCSC genome browser

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UCSCi
uc003yok.3 human

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_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

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S79639 mRNA Translation: AAB62283.1
AK313129 mRNA Translation: BAG35949.1
CH471060 Genomic DNA Translation: EAW91972.1
BC001174 mRNA Translation: AAH01174.1
U70539 Genomic DNA Translation: AAC51154.1
CCDSiCCDS6324.1
RefSeqiNP_000118.2, NM_000127.2
UniGeneiHs.492618

3D structure databases

ProteinModelPortaliQ16394
SMRiQ16394
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108432, 30 interactors
CORUMiQ16394
IntActiQ16394, 2 interactors
STRINGi9606.ENSP00000367446

Protein family/group databases

CAZyiGT47 Glycosyltransferase Family 47
GT64 Glycosyltransferase Family 64

PTM databases

iPTMnetiQ16394
PhosphoSitePlusiQ16394

Polymorphism and mutation databases

BioMutaiEXT1
DMDMi20141422

Proteomic databases

EPDiQ16394
MaxQBiQ16394
PaxDbiQ16394
PeptideAtlasiQ16394
PRIDEiQ16394
ProteomicsDBi60869

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2131
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378204; ENSP00000367446; ENSG00000182197
GeneIDi2131
KEGGihsa:2131
UCSCiuc003yok.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2131
DisGeNETi2131
EuPathDBiHostDB:ENSG00000182197.10

GeneCards: human genes, protein and diseases

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GeneCardsi
EXT1
GeneReviewsiEXT1
HGNCiHGNC:3512 EXT1
HPAiHPA044394
MalaCardsiEXT1
MIMi133700 phenotype
150230 phenotype
215300 phenotype
608177 gene
neXtProtiNX_Q16394
OpenTargetsiENSG00000182197
Orphaneti55880 Chondrosarcoma
321 Multiple osteochondromas
502 Trichorhinophalangeal syndrome type 2
PharmGKBiPA27924

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1021 Eukaryota
ENOG410XTFH LUCA
GeneTreeiENSGT00940000155321
HOGENOMiHOG000266990
HOVERGENiHBG003459
InParanoidiQ16394
KOiK02366
OMAiSHYWDDS
OrthoDBiEOG091G0BDR
PhylomeDBiQ16394
TreeFamiTF314231

Enzyme and pathway databases

UniPathwayi
UPA00378

BioCyciMetaCyc:HS00012-MONOMER
BRENDAi2.4.1.224 2681
2.4.1.225 2681
ReactomeiR-HSA-2022928 HS-GAG biosynthesis
R-HSA-3656237 Defective EXT2 causes exostoses 2
R-HSA-3656253 Defective EXT1 causes exostoses 1, TRPS2 and CHDS
SIGNORiQ16394

Miscellaneous databases

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

More...
ChiTaRSi
EXT1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
EXT1

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

More...
GenomeRNAii
2131

Protein Ontology

More...
PROi
PR:Q16394

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000182197 Expressed in 234 organ(s), highest expression level in thoracic aorta
CleanExiHS_EXT1
ExpressionAtlasiQ16394 baseline and differential
GenevisibleiQ16394 HS

Family and domain databases

Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR004263 Exostosin
IPR027670 Exostosin-1
IPR015338 EXT_C
IPR029044 Nucleotide-diphossugar_trans
PANTHERiPTHR11062 PTHR11062, 1 hit
PTHR11062:SF97 PTHR11062:SF97, 1 hit
PfamiView protein in Pfam
PF03016 Exostosin, 1 hit
PF09258 Glyco_transf_64, 1 hit
SUPFAMiSSF53448 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 nameiEXT1_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: Q16394
Secondary accession number(s): B2R7V2, Q9BVI9
<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 historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 27, 2002
Last modified: December 5, 2018
This is version 191 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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