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Entry version 159 (16 Oct 2019)
Sequence version 2 (02 Nov 2010)
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Protein

Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1

Gene

POMGNT1

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

Participates in O-mannosyl glycosylation by catalyzing the addition of N-acetylglucosamine to O-linked mannose on glycoproteins (PubMed:11709191, PubMed:27493216, PubMed:28512129). Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins, providing the necessary basis for the addition of further carbohydrate moieties (PubMed:11709191, PubMed:27493216). Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity.6 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+1 Publication1 PublicationNote: The manganese ion interacts primarily with the substrate UDP-N-acetylglucosamine.1 Publication

<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=1.85 mM for mannosylpeptide2 Publications
  2. KM=0.73 mM for UDP-GlcNAc2 Publications
  3. KM=30 mM for Man(alpha1-)O-benzyl2 Publications
  4. KM=12 mM for CYA[Man(alpha1-)O-T]AV2 Publications

    pH dependencei

    Optimum pH is 6.0.2 Publications

    <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.5 Publications
    View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei129Carbohydrate1 Publication1
    Binding sitei179Carbohydrate1 Publication1
    Binding sitei207Carbohydrate1 Publication1
    Binding sitei338UDP-GlcNAcCombined sources1 Publication1
    Binding sitei371UDP-GlcNAcCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi395ManganeseCombined sources1 Publication1
    Metal bindingi500ManganeseCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi307 – 311UDP-GlcNAcCombined sources1 Publication5
    Nucleotide bindingi394 – 395UDP-GlcNAcCombined sources1 Publication2
    Nucleotide bindingi506 – 507UDP-GlcNAcCombined sources1 Publication2

    <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:ENSG00000085998-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-5083628 Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3
    R-HSA-5173105 O-linked glycosylation

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q8WZA1

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

    More...
    UniPathwayi
    UPA00378

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GT13 Glycosyltransferase Family 13

    <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:
    Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (EC:2.4.1.-6 Publications)
    Short name:
    POMGnT1
    Alternative name(s):
    UDP-GlcNAc:alpha-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.2
    Short name:
    GnT I.2
    <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:POMGNT1
    Synonyms:MGAT1.2
    ORF Names:UNQ746/PRO1475
    <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 1

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:19139 POMGNT1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    606822 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q8WZA1

    <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_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 – 37CytoplasmicSequence analysisAdd BLAST37
    <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>Transmembranei38 – 58Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini59 – 660Lumenal1 PublicationAdd BLAST602

    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

    <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

    Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A3 (MDDGA3)8 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal recessive disorder characterized by congenital muscular dystrophy, ocular abnormalities, cobblestone lissencephaly, and cerebellar and pontine hypoplasia. Patients present severe congenital myopia, congenital glaucoma, pallor of the optic disks, retinal hypoplasia, mental retardation, hydrocephalus, abnormal electroencephalograms, generalized muscle weakness and myoclonic jerks. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease.
    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_065021176T → P in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs386834030EnsemblClinVar.1
    Natural variantiVAR_065022198S → R in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs386834032EnsemblClinVar.1
    Natural variantiVAR_023101223E → K in MDDGA3; specific activity abolished in the membrane bound form but not the soluble form. 3 PublicationsCorresponds to variant dbSNP:rs386834036EnsemblClinVar.1
    Natural variantiVAR_023102265R → H in MDDGA3; found on the same allele as Q-311; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs386834010EnsemblClinVar.1
    Natural variantiVAR_023103269C → Y in MDDGA3; specific activity abolished of the membrane bound form but not the soluble form. 3 PublicationsCorresponds to variant dbSNP:rs386834037EnsemblClinVar.1
    Natural variantiVAR_023104311R → Q in MDDGA3 and MDDGB3. 2 PublicationsCorresponds to variant dbSNP:rs193919336EnsemblClinVar.1
    Natural variantiVAR_065023367R → H in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs762972459Ensembl.1
    Natural variantiVAR_023105425W → S in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs386834011EnsemblClinVar.1
    Natural variantiVAR_065024427D → H in MDDGA3. 1 Publication1
    Natural variantiVAR_023106442R → C in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs28940869EnsemblClinVar.1
    Natural variantiVAR_023107490C → Y in MDDGA3 and MDDGB3. 3 PublicationsCorresponds to variant dbSNP:rs267606960EnsemblClinVar.1
    Natural variantiVAR_023108493P → R in MDDGA3; specific activity abolished. 2 PublicationsCorresponds to variant dbSNP:rs28942068EnsemblClinVar.1
    Natural variantiVAR_023109550S → N in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs193919335EnsemblClinVar.1
    Muscular dystrophy-dystroglycanopathy congenital with mental retardation B3 (MDDGB3)3 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal recessive disorder characterized by congenital muscular dystrophy associated with mental retardation and mild structural brain abnormalities. Clinical features include mental retardation, white matter changes, cerebellar cysts, pontine hypoplasia, myopia, optic atrophy, decreased alpha-dystroglycan on muscle biopsy and increased serum creatine kinase.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_023104311R → Q in MDDGA3 and MDDGB3. 2 PublicationsCorresponds to variant dbSNP:rs193919336EnsemblClinVar.1
    Natural variantiVAR_023107490C → Y in MDDGA3 and MDDGB3. 3 PublicationsCorresponds to variant dbSNP:rs267606960EnsemblClinVar.1
    Natural variantiVAR_065026605R → P in MDDGB3. 1 PublicationCorresponds to variant dbSNP:rs267606962EnsemblClinVar.1
    Muscular dystrophy-dystroglycanopathy limb-girdle C3 (MDDGC3)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA rare form of limb-girdle muscular dystrophy with normal cognition. Muscle biopsy shows dystrophic changes with variable staining for glycosylated alpha-dystroglycan.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_065025556D → N in MDDGC3; normal enzyme activity but altered kinetic properties. 1 PublicationCorresponds to variant dbSNP:rs74374973EnsemblClinVar.1
    Retinitis pigmentosa 76 (RP76)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of retinitis pigmentosa, a retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. RP76 inheritance is autosomal recessive.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_077054120L → R in RP76; no effect on protein abundance; reduced acetylglucosaminyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs886037949EnsemblClinVar.1
    Natural variantiVAR_076524156E → K in RP76; reduced acetylglucosaminyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs886037947EnsemblClinVar.1
    Natural variantiVAR_076525287I → S in RP76; reduced acetylglucosaminyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs200863680EnsemblClinVar.1
    Natural variantiVAR_076526502G → A in RP76. 1 PublicationCorresponds to variant dbSNP:rs886037948EnsemblClinVar.1

    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>Mutagenesisi1 – 65Missing : Gives rise to a soluble form. 1 PublicationAdd BLAST65
    Mutagenesisi129R → A: Decreased protein stability. Decreased enzyme activity. 1 Publication1
    Mutagenesisi179D → A: Moderately increased enzyme activity. Decreased affinity for N-acetylglucosamine. 1 Publication1
    Mutagenesisi207R → A: Decreased enzyme activity. Impairs protein stability. 1 Publication1
    Mutagenesisi473W → A: Abolishes in vitro enzyme activity; when associated with A-477. 1 Publication1
    Mutagenesisi474D → A: Nearly abolishes enzyme activity. 1 Publication1
    Mutagenesisi477M → A: Abolishes in vitro enzyme activity; when associated with A-473. 1 Publication1
    Mutagenesisi481M → A: Decreased enzyme activity. 1 Publication1
    Mutagenesisi507N → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi600W → A: Abolishes enzyme activity. 1 Publication1

    Keywords - Diseasei

    Congenital muscular dystrophy, Disease mutation, Dystroglycanopathy, Limb-girdle muscular dystrophy, Lissencephaly, Retinitis pigmentosa

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    55624

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

    More...
    GeneReviewsi
    POMGNT1

    MalaCards human disease database

    More...
    MalaCardsi
    POMGNT1
    MIMi253280 phenotype
    613151 phenotype
    613157 phenotype
    617123 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000085998

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

    More...
    Orphaneti
    206564 Autosomal recessive limb-girdle muscular dystrophy type 2O
    370959 Congenital muscular dystrophy with cerebellar involvement
    588 Muscle-eye-brain disease
    791 Retinitis pigmentosa
    899 Walker-Warburg syndrome

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA142671161

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    Q8WZA1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2321629

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    POMGNT1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    311033411

    <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_00001913901 – 660Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1Add BLAST660

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei7PhosphoserineCombined sources1
    <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 bondi254 ↔ 281Combined sources1 Publication
    Disulfide bondi269 ↔ 279Combined sources1 Publication
    Disulfide bondi421 ↔ 490Combined sources1 Publication
    Disulfide bondi562 ↔ 596Combined sources1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q8WZA1

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q8WZA1

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q8WZA1

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q8WZA1

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

    More...
    PaxDbi
    Q8WZA1

    PeptideAtlas

    More...
    PeptideAtlasi
    Q8WZA1

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q8WZA1

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    65277
    75242 [Q8WZA1-1]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q8WZA1

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

    More...
    PhosphoSitePlusi
    Q8WZA1

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q8WZA1

    <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

    Constitutively expressed. An additional weaker band is also detected in spinal cord, lymph node, and trachea. Expressed especially in astrocytes. Also expressed in immature and mature neurons.2 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000085998 Expressed in 214 organ(s), highest expression level in C1 segment of cervical spinal cord

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q8WZA1 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q8WZA1 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA044518

    <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

    Interacts with DAG1 (via O-linked mannose moiety) (PubMed:27493216).

    Interacts (via transmembrane domain) with FKTN; the interaction is direct and is required for normal location in Golgi membranes (PubMed:17034757).

    2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    120763, 29 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q8WZA1, 21 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000361060

    <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

    1660
    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
    Q8WZA1

    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>Regioni92 – 288Carbohydrate-binding stem domain1 PublicationAdd BLAST197
    Regioni300 – 646Catalytic2 PublicationsAdd BLAST347
    Regioni473 – 481Interaction with O-glycosylated substrate glycoprotein1 Publication9
    Regioni506 – 512Interaction with O-glycosylated substrate glycoprotein1 Publication7
    Regioni600 – 605Interaction with O-glycosylated substrate glycoprotein1 Publication6

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi263 – 267Poly-Arg5

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

    Amino acid residues between 299-311 are important for both protein expression and enzymatic activity. The minimal catalytic domain is located between positions 299-651. Single amino acid substitutions in the stem domain from MEB patients abolished the activity of the membrane-bound form but not the soluble form. This suggests that the stem domain of the soluble form is unnecessary for activity, but that some amino acids play a crucial role in the membrane-bound form.1 Publication
    The stem domain mediates specific interaction with beta-linked N-acetylglucosamine moieties of O-glycosylated proteins. It also interacts with its product, N-acetyl-beta-D-glucosaminyl-(1->2)-O-alpha-D-mannosylprotein.1 Publication

    <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 13 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG410IFXX Eukaryota
    ENOG410YMAS LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00530000063632

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000231121

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q8WZA1

    KEGG Orthology (KO)

    More...
    KOi
    K09666

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    KKGGEVY

    Database of Orthologous Groups

    More...
    OrthoDBi
    607108at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q8WZA1

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF320555

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd13937 PANDER_GnT-1_2_like, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.90.550.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR004139 Glyco_trans_13
    IPR039477 ILEI/PANDER_dom
    IPR029044 Nucleotide-diphossugar_trans
    IPR039474 POMGNT1_PANDER-like

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03071 GNT-I, 1 hit
    PF15711 ILEI, 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>. 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>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

    Isoform 1 (identifier: Q8WZA1-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MDDWKPSPLI KPFGARKKRS WYLTWKYKLT NQRALRRFCQ TGAVLFLLVT
    60 70 80 90 100
    VIVNIKLILD TRRAISEANE DPEPEQDYDE ALGRLEPPRR RGSGPRRVLD
    110 120 130 140 150
    VEVYSSRSKV YVAVDGTTVL EDEAREQGRG IHVIVLNQAT GHVMAKRVFD
    160 170 180 190 200
    TYSPHEDEAM VLFLNMVAPG RVLICTVKDE GSFHLKDTAK ALLRSLGSQA
    210 220 230 240 250
    GPALGWRDTW AFVGRKGGPV FGEKHSKSPA LSSWGDPVLL KTDVPLSSAE
    260 270 280 290 300
    EAECHWADTE LNRRRRRFCS KVEGYGSVCS CKDPTPIEFS PDPLPDNKVL
    310 320 330 340 350
    NVPVAVIAGN RPNYLYRMLR SLLSAQGVSP QMITVFIDGY YEEPMDVVAL
    360 370 380 390 400
    FGLRGIQHTP ISIKNARVSQ HYKASLTATF NLFPEAKFAV VLEEDLDIAV
    410 420 430 440 450
    DFFSFLSQSI HLLEEDDSLY CISAWNDQGY EHTAEDPALL YRVETMPGLG
    460 470 480 490 500
    WVLRRSLYKE ELEPKWPTPE KLWDWDMWMR MPEQRRGREC IIPDVSRSYH
    510 520 530 540 550
    FGIVGLNMNG YFHEAYFKKH KFNTVPGVQL RNVDSLKKEA YEVEVHRLLS
    560 570 580 590 600
    EAEVLDHSKN PCEDSFLPDT EGHTYVAFIR MEKDDDFTTW TQLAKCLHIW
    610 620 630 640 650
    DLDVRGNHRG LWRLFRKKNH FLMVGVPASP YSVKKPPSVT PIFLEPPPKE
    660
    EGAPGAPEQT
    Length:660
    Mass (Da):75,252
    Last modified:November 2, 2010 - 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:iC58D0E543E033F17
    GO
    Isoform 2 (identifier: Q8WZA1-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         624-660: VGVPASPYSV...EGAPGAPEQT → SEEATLSHPN...LLFVQISKAG

    Note: No experimental confirmation available.Curated
    Show »
    Length:748
    Mass (Da):84,700
    Checksum:iB88BFD957237FEFD
    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
    Q68CV6Q68CV6_HUMAN
    Protein O-linked-mannose beta-1,2-N...
    POMGNT1 DKFZp761B182
    200Annotation score:

    Annotation score:1 out of 5

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

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence BAB14207 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    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 conflicti636P → L in BAA91053 (PubMed:12975309).Curated1
    Isoform 2 (identifier: Q8WZA1-2)
    Sequence conflicti636G → K in AK056186 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_077054120L → R in RP76; no effect on protein abundance; reduced acetylglucosaminyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs886037949EnsemblClinVar.1
    Natural variantiVAR_076524156E → K in RP76; reduced acetylglucosaminyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs886037947EnsemblClinVar.1
    Natural variantiVAR_065021176T → P in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs386834030EnsemblClinVar.1
    Natural variantiVAR_065022198S → R in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs386834032EnsemblClinVar.1
    Natural variantiVAR_023101223E → K in MDDGA3; specific activity abolished in the membrane bound form but not the soluble form. 3 PublicationsCorresponds to variant dbSNP:rs386834036EnsemblClinVar.1
    Natural variantiVAR_030645250E → V1 PublicationCorresponds to variant dbSNP:rs17855359Ensembl.1
    Natural variantiVAR_023102265R → H in MDDGA3; found on the same allele as Q-311; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs386834010EnsemblClinVar.1
    Natural variantiVAR_023103269C → Y in MDDGA3; specific activity abolished of the membrane bound form but not the soluble form. 3 PublicationsCorresponds to variant dbSNP:rs386834037EnsemblClinVar.1
    Natural variantiVAR_076525287I → S in RP76; reduced acetylglucosaminyltransferase activity. 1 PublicationCorresponds to variant dbSNP:rs200863680EnsemblClinVar.1
    Natural variantiVAR_023104311R → Q in MDDGA3 and MDDGB3. 2 PublicationsCorresponds to variant dbSNP:rs193919336EnsemblClinVar.1
    Natural variantiVAR_065023367R → H in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs762972459Ensembl.1
    Natural variantiVAR_023105425W → S in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs386834011EnsemblClinVar.1
    Natural variantiVAR_065024427D → H in MDDGA3. 1 Publication1
    Natural variantiVAR_023106442R → C in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs28940869EnsemblClinVar.1
    Natural variantiVAR_023107490C → Y in MDDGA3 and MDDGB3. 3 PublicationsCorresponds to variant dbSNP:rs267606960EnsemblClinVar.1
    Natural variantiVAR_023108493P → R in MDDGA3; specific activity abolished. 2 PublicationsCorresponds to variant dbSNP:rs28942068EnsemblClinVar.1
    Natural variantiVAR_076526502G → A in RP76. 1 PublicationCorresponds to variant dbSNP:rs886037948EnsemblClinVar.1
    Natural variantiVAR_030646504V → I. Corresponds to variant dbSNP:rs17102066EnsemblClinVar.1
    Natural variantiVAR_023109550S → N in MDDGA3. 1 PublicationCorresponds to variant dbSNP:rs193919335EnsemblClinVar.1
    Natural variantiVAR_065025556D → N in MDDGC3; normal enzyme activity but altered kinetic properties. 1 PublicationCorresponds to variant dbSNP:rs74374973EnsemblClinVar.1
    Natural variantiVAR_065026605R → P in MDDGB3. 1 PublicationCorresponds to variant dbSNP:rs267606962EnsemblClinVar.1
    Natural variantiVAR_023110623M → V7 PublicationsCorresponds to variant dbSNP:rs6659553Ensembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_054029624 – 660VGVPA…APEQT → SEEATLSHPNFPGATPKGGG SPRSPRTDMRPPPGPCGAGP GSESNLFIDCPEGLENRPNL EGLDFFLGWNAALRVGLALT QETAVPNPWTGPAGAHMLTQ THSETLRHWTRPPLSLLFVQ ISKAG in isoform 2. 1 PublicationAdd BLAST37

    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
    AB057356 mRNA Translation: BAB71960.1
    AY358592 mRNA Translation: AAQ88955.1
    AK000284 mRNA Translation: BAA91053.1
    AK022727 mRNA Translation: BAB14207.1 Different initiation.
    AK056186 mRNA No translation available.
    AL672043 Genomic DNA No translation available.
    CH471059 Genomic DNA Translation: EAX06932.1
    CH471059 Genomic DNA Translation: EAX06933.1
    CH471059 Genomic DNA Translation: EAX06935.1
    BC001471 mRNA Translation: AAH01471.1
    AF250859 mRNA Translation: AAF71270.2

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS531.1 [Q8WZA1-1]
    CCDS57995.1 [Q8WZA1-2]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_060209.3, NM_017739.3
    XP_006710819.1, XM_006710756.1 [Q8WZA1-2]
    XP_016857179.1, XM_017001690.1 [Q8WZA1-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000371984; ENSP00000361052; ENSG00000085998 [Q8WZA1-1]
    ENST00000371992; ENSP00000361060; ENSG00000085998 [Q8WZA1-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    55624

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:55624

    UCSC genome browser

    More...
    UCSCi
    uc001cpe.4 human [Q8WZA1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, 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

    <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

    Functional Glycomics Gateway - GTase

    Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB057356 mRNA Translation: BAB71960.1
    AY358592 mRNA Translation: AAQ88955.1
    AK000284 mRNA Translation: BAA91053.1
    AK022727 mRNA Translation: BAB14207.1 Different initiation.
    AK056186 mRNA No translation available.
    AL672043 Genomic DNA No translation available.
    CH471059 Genomic DNA Translation: EAX06932.1
    CH471059 Genomic DNA Translation: EAX06933.1
    CH471059 Genomic DNA Translation: EAX06935.1
    BC001471 mRNA Translation: AAH01471.1
    AF250859 mRNA Translation: AAF71270.2
    CCDSiCCDS531.1 [Q8WZA1-1]
    CCDS57995.1 [Q8WZA1-2]
    RefSeqiNP_060209.3, NM_017739.3
    XP_006710819.1, XM_006710756.1 [Q8WZA1-2]
    XP_016857179.1, XM_017001690.1 [Q8WZA1-1]

    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
    5GGFX-ray2.49A/B/C92-660[»]
    5GGGX-ray3.00A92-660[»]
    5GGIX-ray2.60A/B92-660[»]
    5GGJX-ray1.42A/B92-250[»]
    5GGKX-ray1.30A/B92-250[»]
    5GGLX-ray1.27A/B92-250[»]
    5GGNX-ray1.21A/B92-250[»]
    5GGOX-ray1.50A/B92-250[»]
    5GGPX-ray1.60A/B92-250[»]
    5XFCX-ray1.40A/B92-250[»]
    SMRiQ8WZA1
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi120763, 29 interactors
    IntActiQ8WZA1, 21 interactors
    STRINGi9606.ENSP00000361060

    Chemistry databases

    ChEMBLiCHEMBL2321629

    Protein family/group databases

    CAZyiGT13 Glycosyltransferase Family 13

    PTM databases

    iPTMnetiQ8WZA1
    PhosphoSitePlusiQ8WZA1
    SwissPalmiQ8WZA1

    Polymorphism and mutation databases

    BioMutaiPOMGNT1
    DMDMi311033411

    Proteomic databases

    EPDiQ8WZA1
    jPOSTiQ8WZA1
    MassIVEiQ8WZA1
    MaxQBiQ8WZA1
    PaxDbiQ8WZA1
    PeptideAtlasiQ8WZA1
    PRIDEiQ8WZA1
    ProteomicsDBi65277
    75242 [Q8WZA1-1]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    55624

    Genome annotation databases

    EnsembliENST00000371984; ENSP00000361052; ENSG00000085998 [Q8WZA1-1]
    ENST00000371992; ENSP00000361060; ENSG00000085998 [Q8WZA1-2]
    GeneIDi55624
    KEGGihsa:55624
    UCSCiuc001cpe.4 human [Q8WZA1-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    55624
    DisGeNETi55624

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    POMGNT1
    GeneReviewsiPOMGNT1
    HGNCiHGNC:19139 POMGNT1
    HPAiHPA044518
    MalaCardsiPOMGNT1
    MIMi253280 phenotype
    606822 gene
    613151 phenotype
    613157 phenotype
    617123 phenotype
    neXtProtiNX_Q8WZA1
    OpenTargetsiENSG00000085998
    Orphaneti206564 Autosomal recessive limb-girdle muscular dystrophy type 2O
    370959 Congenital muscular dystrophy with cerebellar involvement
    588 Muscle-eye-brain disease
    791 Retinitis pigmentosa
    899 Walker-Warburg syndrome
    PharmGKBiPA142671161

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiENOG410IFXX Eukaryota
    ENOG410YMAS LUCA
    GeneTreeiENSGT00530000063632
    HOGENOMiHOG000231121
    InParanoidiQ8WZA1
    KOiK09666
    OMAiKKGGEVY
    OrthoDBi607108at2759
    PhylomeDBiQ8WZA1
    TreeFamiTF320555

    Enzyme and pathway databases

    UniPathwayiUPA00378
    BioCyciMetaCyc:ENSG00000085998-MONOMER
    ReactomeiR-HSA-5083628 Defective POMGNT1 causes MDDGA3, MDDGB3 and MDDGC3
    R-HSA-5173105 O-linked glycosylation
    SIGNORiQ8WZA1

    Miscellaneous databases

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

    More...
    ChiTaRSi
    POMGNT1 human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    POMGNT1

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

    More...
    GenomeRNAii
    55624
    PharosiQ8WZA1

    Protein Ontology

    More...
    PROi
    PR:Q8WZA1

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000085998 Expressed in 214 organ(s), highest expression level in C1 segment of cervical spinal cord
    ExpressionAtlasiQ8WZA1 baseline and differential
    GenevisibleiQ8WZA1 HS

    Family and domain databases

    CDDicd13937 PANDER_GnT-1_2_like, 1 hit
    Gene3Di3.90.550.10, 1 hit
    InterProiView protein in InterPro
    IPR004139 Glyco_trans_13
    IPR039477 ILEI/PANDER_dom
    IPR029044 Nucleotide-diphossugar_trans
    IPR039474 POMGNT1_PANDER-like
    PfamiView protein in Pfam
    PF03071 GNT-I, 1 hit
    PF15711 ILEI, 1 hit
    SUPFAMiSSF53448 SSF53448, 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 nameiPMGT1_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: Q8WZA1
    Secondary accession number(s): D3DQ16
    , Q5VST2, Q5VST3, Q9BV55, Q9H9L8, Q9NXF9, Q9NYF7
    <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: August 16, 2005
    Last sequence update: November 2, 2010
    Last modified: October 16, 2019
    This is version 159 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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