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Entry version 217 (16 Oct 2019)
Sequence version 3 (21 Jun 2005)
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Protein

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Gene

OGT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc) (PubMed:26678539, PubMed:23103939, PubMed:21240259, PubMed:21285374, PubMed:15361863). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, EZH2, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing (PubMed:21285374). Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination (PubMed:26678539). Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling (By similarity). Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity (PubMed:22923583). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3) (PubMed:22121020, PubMed:23353889). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (PubMed:24474760). Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver. Stabilizes clock proteins ARNTL/BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation. Promotes the CLOCK-ARNTL/BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2 (PubMed:12150998, PubMed:19451179, PubMed:20018868, PubMed:20200153, PubMed:21285374, PubMed:15361863). O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity (PubMed:21285374, PubMed:28584052, PubMed:28302723). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Glycosylates HOXA1 (By similarity).By similarity16 Publications
Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.1 Publication

Caution

Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203).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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Subject to product inhibition by UDP.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=1.8 µM for UDP-N-acetyl-D-glucosamine1 Publication

    <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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei508Proton acceptor2 Publications1
    <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 sitei849UDPCombined sources1 Publication1
    Binding sitei852UDPCombined sources1 Publication1
    Binding sitei935UDPCombined 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 bindingi906 – 908UDPCombined sources1 Publication3
    Nucleotide bindingi911 – 914UDPCombined sources1 Publication4
    Nucleotide bindingi930 – 932UDPCombined sources1 Publication3

    <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 functionChromatin regulator, Glycosyltransferase, Transferase
    Biological processApoptosis, Biological rhythms, Host-virus interaction, Ubl conjugation pathway
    LigandLipid-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:ENSG00000147162-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.4.1.255 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-3214847 HATs acetylate histones
    R-HSA-5689603 UCH proteinases

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    O15294

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

    More...
    SignaLinki
    O15294

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    O15294

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

    More...
    UniPathwayi
    UPA00378

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    GT41 Glycosyltransferase Family 41

    <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:
    UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC:2.4.1.2551 Publication3 Publications)
    Alternative name(s):
    O-GlcNAc transferase subunit p110
    O-linked N-acetylglucosamine transferase 110 kDa subunit
    Short name:
    OGT
    <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:OGT
    <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 X

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:8127 OGT

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    300255 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_O15294

    <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

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Membrane, Mitochondrion, Nucleus

    <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

    Regulation of OGT activity and altered O-GlcNAcylations are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of AKT1 affects insulin signaling and, possibly diabetes. Reduced O-GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are observed in Alzheimer disease (AD) brain cerebrum.
    Mental retardation, X-linked 106 (MRX106)3 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations.
    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_079254254L → F in MRX106; decreased protein abundance; reduced protein stability. 1 PublicationCorresponds to variant dbSNP:rs1131692155EnsemblClinVar.1
    Natural variantiVAR_079183284R → P in MRX106; decreased protein abundance; decreased enzyme activity; reduced protein stability. 1 PublicationCorresponds to variant dbSNP:rs1114167891EnsemblClinVar.1
    Natural variantiVAR_074019319A → T in MRX106; unknown pathological significance. 1 Publication1

    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>Mutagenesisi208W → E: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with D-211. 1 Publication1
    Mutagenesisi211I → D: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with E-208. 1 Publication1
    Mutagenesisi508H → A: Loss of enzyme activity. Moderate increase in KMT2E ubiquitination. Moderate increase in KMT2E ubiquitination; when associated with A-508. 2 Publications1
    Mutagenesisi568H → A: Reduces enzyme activity by about 95%. Moderate increase in KMT2E ubiquitination; when associated with A-508. 2 Publications1
    Mutagenesisi911H → A: Reduces enzyme activity by over 90%. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    8473

    MalaCards human disease database

    More...
    MalaCardsi
    OGT
    MIMi300997 phenotype

    NIAGADS Genomics Database

    More...
    NIAGADSi
    ENSG00000147162

    Open Targets

    More...
    OpenTargetsi
    ENSG00000147162

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA31914

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    O15294

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5955

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    OGT

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
    <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_00001917722 – 1046UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunitAdd BLAST1045

    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 residuei2N-acetylalanineCombined sources1 Publication1
    Modified residuei3Phosphoserine; by GSK3-beta; alternateBy similarity1
    <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>Glycosylationi3O-linked (GlcNAc) serine; alternateBy similarity1
    Modified residuei4Phosphoserine; by GSK3-beta; alternateBy similarity1
    Glycosylationi4O-linked (GlcNAc) serine; alternateBy similarity1
    Modified residuei20PhosphoserineCombined sources1
    Modified residuei989PhosphotyrosineBy similarity1

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

    Ubiquitinated, leading to its proteasomal degradation.1 Publication
    Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    The CPTAC Assay portal

    More...
    CPTACi
    CPTAC-1261
    CPTAC-1262

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    O15294

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    O15294

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    O15294

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    O15294

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

    More...
    PaxDbi
    O15294

    PeptideAtlas

    More...
    PeptideAtlasi
    O15294

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O15294

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    48562 [O15294-1]
    48563 [O15294-2]
    48564 [O15294-3]
    48565 [O15294-4]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    O15294

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

    More...
    PhosphoSitePlusi
    O15294

    <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

    Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver.1 Publication

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induction of the nucleocytoplasmic OGT (ncOGT) isoform in the liver on glucose deprivation is mediated by the decreased hexosamine biosynthesis pathway (HBP) flux.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000147162 Expressed in 240 organ(s), highest expression level in middle temporal gyrus

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    O15294 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    O15294 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB034099
    HPA030751
    HPA030752
    HPA030753
    HPA030754

    <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

    Monomer; may exist in different oligomerization states in cells (PubMed:21240259). Homotrimer, oligomerizes via TPR repeats 6 and 7. Trimerization is not necessary for activity in vitro, however it increases affinity for UDP-GlcNAc (By similarity).

    Component of a THAP1/THAP3-HCFC1-OGT complex (PubMed:20200153).

    Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:20018852).

    Interacts directly with HCFC1; the interaction O-glycosylates HCFC1, regulates its proteolytic processing and transcriptional activity and, in turn, stabilizes OGT in the nucleus (PubMed:12670868, PubMed:20200153, PubMed:21285374, PubMed:23353889).

    Interacts (via TPRs 1-6) with SIN3A; the interaction mediates transcriptional repression in parallel with histone deacetylase (PubMed:12150998).

    Interacts (via TPR 5-6) with TET1, TET2 and TET3 (PubMed:23353889, PubMed:23222540).

    Interacts (via TPR repeats 6 and 7) with ATXN10 (By similarity).

    Interacts with histone H2B (PubMed:22121020).

    Interacts with ARNTL/BMAL1.

    Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1.

    Interacts with SINHCAF (By similarity).

    Component of a complex composed of KMT2E/MLL5 (isoform 3), OGT (isoform 1) and USP7; the complex stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination and proteosomal-mediated degradation (PubMed:26678539). Isoform 1 interacts (via TRP repeats) with isoform 3 KMT2E/MLL5 (via N-terminus) (PubMed:26678539, PubMed:23629655).

    Isoform 1 interacts with USP7 (PubMed:26678539).

    Interacts with TRAK1; this interaction is not required for glycosylation of TRAK1 by this protein.

    Found in a complex with KIF5B, RHOT1, RHOT2 and TRAK1 (PubMed:24995978).

    Interacts (via TPR repeats domain) with HOXA1; the interaction takes place mainly in the nucleus (By similarity).

    By similarity12 Publications

    (Microbial infection) Interacts with human T-cell leukemia virus 1/HTLV-1 protein Tax; this interaction increases Tax interacting partner CREB1 O-GlcNAcylation.

    1 Publication

    <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
    114049, 154 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-3323 SIN3A histone deacetylase complex, ES cell-specific variant
    CPX-809 NSL histone acetyltransferase complex

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    O15294

    Database of interacting proteins

    More...
    DIPi
    DIP-33491N

    Protein interaction database and analysis system

    More...
    IntActi
    O15294, 115 interactors

    Molecular INTeraction database

    More...
    MINTi
    O15294

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000362824

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    O15294

    <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

    11046
    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
    O15294

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    O15294

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati21 – 54TPR 1Add BLAST34
    Repeati89 – 122TPR 2Add BLAST34
    Repeati123 – 156TPR 3Add BLAST34
    Repeati157 – 190TPR 4Add BLAST34
    Repeati191 – 224TPR 5Add BLAST34
    Repeati225 – 258TPR 6Add BLAST34
    Repeati259 – 292TPR 7Add BLAST34
    Repeati293 – 326TPR 8Add BLAST34
    Repeati327 – 360TPR 9Add BLAST34
    Repeati361 – 394TPR 10Add BLAST34
    Repeati395 – 428TPR 11Add BLAST34
    Repeati429 – 462TPR 12Add BLAST34
    Repeati463 – 473TPR 13; truncatedAdd BLAST11

    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>Regioni991 – 1010Required for phosphatidylinositol 3,4,5-triphosphate bindingAdd BLAST20

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi487 – 503Nuclear localization signalSequence analysisAdd BLAST17

    <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

    The TPR repeat domain is required for substrate binding and oligomerization.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

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1124 Eukaryota
    KOG4626 Eukaryota
    COG3914 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155085

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000003765

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O15294

    KEGG Orthology (KO)

    More...
    KOi
    K09667

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    PLTHEFR

    Database of Orthologous Groups

    More...
    OrthoDBi
    142546at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    O15294

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105785

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.25.40.10, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR037919 OGT
    IPR029489 OGT/SEC/SPY_C
    IPR013026 TPR-contain_dom
    IPR011990 TPR-like_helical_dom_sf
    IPR001440 TPR_1
    IPR019734 TPR_repeat

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR44366 PTHR44366, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF13844 Glyco_transf_41, 1 hit
    PF00515 TPR_1, 2 hits
    PF13181 TPR_8, 2 hits

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00028 TPR, 12 hits

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF48452 SSF48452, 2 hits

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50005 TPR, 12 hits
    PS50293 TPR_REGION, 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 (4+)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.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 <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 4 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

    Isoform 3 (identifier: O15294-1) [UniParc]FASTAAdd to basket
    Also known as: Nucleocytoplasmic isoform, ncOGT

    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
    MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ
    60 70 80 90 100
    EPDNTGVLLL LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK
    110 120 130 140 150
    ERGQLQEAIE HYRHALRLKP DFIDGYINLA AALVAAGDME GAVQAYVSAL
    160 170 180 190 200
    QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF AVAWSNLGCV
    210 220 230 240 250
    FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAAYLR
    260 270 280 290 300
    ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA
    310 320 330 340 350
    NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY
    360 370 380 390 400
    RKALEVFPEF AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN
    410 420 430 440 450
    MGNTLKEMQD VQGALQCYTR AIQINPAFAD AHSNLASIHK DSGNIPEAIA
    460 470 480 490 500
    SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV SIVADQLEKN
    510 520 530 540 550
    RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK PPYEHPKDLK
    560 570 580 590 600
    LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN
    610 620 630 640 650
    FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL
    660 670 680 690 700
    FALRPAPIQA MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP
    710 720 730 740 750
    HTFFIGDHAN MFPHLKKKAV IDFKSNGHIY DNRIVLNGID LKAFLDSLPD
    760 770 780 790 800
    VKIVKMKCPD GGDNADSSNT ALNMPVIPMN TIAEAVIEMI NRGQIQITIN
    810 820 830 840 850
    GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL
    860 870 880 890 900
    YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI
    910 920 930 940 950
    IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET
    960 970 980 990 1000
    LASRVAASQL TCLGCLELIA KNRQEYEDIA VKLGTDLEYL KKVRGKVWKQ
    1010 1020 1030 1040
    RISSPLFNTK QYTMELERLY LQMWEHYAAG NKPDHMIKPV EVTESA
    Length:1,046
    Mass (Da):116,925
    Last modified:June 21, 2005 - v3
    <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:i852ED68BDDE63363
    GO
    Isoform 2 (identifier: O15294-2) [UniParc]FASTAAdd to basket
    Also known as: Mitochondrial isoform, mOGT

    The sequence of this isoform differs from the canonical sequence as follows:
         1-176: MASSVGNVAD...LKALGRLEEA → MLQGHFWLVR...PSHLLSLTPP

    Show »
    Length:920
    Mass (Da):103,012
    Checksum:i766BF416ABD547C4
    GO
    Isoform 1 (identifier: O15294-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         13-22: Missing.

    Show »
    Length:1,036
    Mass (Da):115,706
    Checksum:iC3BD67340925A2C2
    GO
    Isoform 4 (identifier: O15294-4) [UniParc]FASTAAdd to basket
    Also known as: Short isoform, sOGT

    The sequence of this isoform differs from the canonical sequence as follows:
         1-381: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:665
    Mass (Da):74,536
    Checksum:i181B846A6B09E63A
    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
    C9JZL3C9JZL3_HUMAN
    UDP-N-acetylglucosamine--peptide N-...
    OGT
    156Annotation 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 conflicti308S → Q in CAB62528 (PubMed:17974005).Curated1
    Sequence conflicti663L → P in CAD97853 (PubMed:17974005).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_079254254L → F in MRX106; decreased protein abundance; reduced protein stability. 1 PublicationCorresponds to variant dbSNP:rs1131692155EnsemblClinVar.1
    Natural variantiVAR_079183284R → P in MRX106; decreased protein abundance; decreased enzyme activity; reduced protein stability. 1 PublicationCorresponds to variant dbSNP:rs1114167891EnsemblClinVar.1
    Natural variantiVAR_074019319A → T in MRX106; unknown pathological significance. 1 Publication1
    Natural variantiVAR_064736538L → P Found in a renal cell carcinoma sample; somatic mutation. 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_0407641 – 381Missing in isoform 4. 1 PublicationAdd BLAST381
    Alternative sequenceiVSP_0065531 – 176MASSV…RLEEA → MLQGHFWLVREGIMISPSSP PPPNLFFFPLQIFPFPFTSF PSHLLSLTPP in isoform 2. 1 PublicationAdd BLAST176
    Alternative sequenceiVSP_01416413 – 22Missing in isoform 1. 2 Publications10

    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
    U77413 mRNA Translation: AAB63466.1
    AJ315767 Genomic DNA Translation: CAC86127.1
    AJ315767 Genomic DNA Translation: CAC86128.1
    AJ315767 Genomic DNA Translation: CAC86129.1
    AL050366 mRNA Translation: CAB62528.1
    AL833085 mRNA Translation: CAD89970.1
    BX537844 mRNA Translation: CAD97853.1
    BC014434 mRNA Translation: AAH14434.1
    BC038180 mRNA Translation: AAH38180.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS14414.1 [O15294-1]
    CCDS35502.1 [O15294-3]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_858058.1, NM_181672.2 [O15294-1]
    NP_858059.1, NM_181673.2 [O15294-3]
    XP_016885396.1, XM_017029907.1
    XP_016885397.1, XM_017029908.1 [O15294-4]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000373701; ENSP00000362805; ENSG00000147162 [O15294-3]
    ENST00000373719; ENSP00000362824; ENSG00000147162 [O15294-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    8473

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:8473

    UCSC genome browser

    More...
    UCSCi
    uc004eaa.3 human [O15294-1]

    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

    UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110kDa subunit

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U77413 mRNA Translation: AAB63466.1
    AJ315767 Genomic DNA Translation: CAC86127.1
    AJ315767 Genomic DNA Translation: CAC86128.1
    AJ315767 Genomic DNA Translation: CAC86129.1
    AL050366 mRNA Translation: CAB62528.1
    AL833085 mRNA Translation: CAD89970.1
    BX537844 mRNA Translation: CAD97853.1
    BC014434 mRNA Translation: AAH14434.1
    BC038180 mRNA Translation: AAH38180.1
    CCDSiCCDS14414.1 [O15294-1]
    CCDS35502.1 [O15294-3]
    RefSeqiNP_858058.1, NM_181672.2 [O15294-1]
    NP_858059.1, NM_181673.2 [O15294-3]
    XP_016885396.1, XM_017029907.1
    XP_016885397.1, XM_017029908.1 [O15294-4]

    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
    1W3BX-ray2.85A/B26-410[»]
    3PE3X-ray2.78A/B/C/D323-1041[»]
    3PE4X-ray1.95A/C323-1041[»]
    3TAXX-ray1.88A/C323-1041[»]
    4AY5X-ray3.15A/B/C/D323-1041[»]
    4AY6X-ray3.30A/B/C/D323-1041[»]
    4CDRX-ray3.15A/B/C/D323-1041[»]
    4GYWX-ray1.70A/C323-1041[»]
    4GYYX-ray1.85A/C323-1041[»]
    4GZ3X-ray1.90A/C323-1041[»]
    4GZ5X-ray3.08A/B/C/D323-1041[»]
    4GZ6X-ray2.98A/B/C/D323-1041[»]
    4N39X-ray1.76A323-1041[»]
    4N3AX-ray1.88A323-1041[»]
    4N3BX-ray2.17A323-1041[»]
    4N3CX-ray2.55A323-1041[»]
    4XI9X-ray3.10A/B/C/D323-1041[»]
    4XIFX-ray3.20A/B/C/D323-1041[»]
    5BNWX-ray2.40A323-1041[»]
    5C1DX-ray2.05A323-1041[»]
    5HGVX-ray2.05A/C323-1041[»]
    5LVVX-ray2.54A325-1046[»]
    5LWVX-ray1.90A325-1046[»]
    5NPRX-ray1.85A325-1041[»]
    5NPSX-ray1.68A324-1041[»]
    5VIEX-ray2.60A/C323-1041[»]
    5VIFX-ray2.25A323-1041[»]
    6EOUX-ray1.75A26-410[»]
    6IBOX-ray2.17A323-1041[»]
    6MA1X-ray2.75A323-1041[»]
    6MA2X-ray2.10A323-1041[»]
    6MA3X-ray2.00A323-1041[»]
    6MA4X-ray2.00A323-1041[»]
    6MA5X-ray2.00A323-1041[»]
    SMRiO15294
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi114049, 154 interactors
    ComplexPortaliCPX-3323 SIN3A histone deacetylase complex, ES cell-specific variant
    CPX-809 NSL histone acetyltransferase complex
    CORUMiO15294
    DIPiDIP-33491N
    IntActiO15294, 115 interactors
    MINTiO15294
    STRINGi9606.ENSP00000362824

    Chemistry databases

    BindingDBiO15294
    ChEMBLiCHEMBL5955

    Protein family/group databases

    CAZyiGT41 Glycosyltransferase Family 41

    PTM databases

    iPTMnetiO15294
    PhosphoSitePlusiO15294

    Polymorphism and mutation databases

    BioMutaiOGT

    Proteomic databases

    CPTACiCPTAC-1261
    CPTAC-1262
    EPDiO15294
    jPOSTiO15294
    MassIVEiO15294
    MaxQBiO15294
    PaxDbiO15294
    PeptideAtlasiO15294
    PRIDEiO15294
    ProteomicsDBi48562 [O15294-1]
    48563 [O15294-2]
    48564 [O15294-3]
    48565 [O15294-4]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    8473

    Genome annotation databases

    EnsembliENST00000373701; ENSP00000362805; ENSG00000147162 [O15294-3]
    ENST00000373719; ENSP00000362824; ENSG00000147162 [O15294-1]
    GeneIDi8473
    KEGGihsa:8473
    UCSCiuc004eaa.3 human [O15294-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    8473
    DisGeNETi8473

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    OGT
    HGNCiHGNC:8127 OGT
    HPAiCAB034099
    HPA030751
    HPA030752
    HPA030753
    HPA030754
    MalaCardsiOGT
    MIMi300255 gene
    300997 phenotype
    neXtProtiNX_O15294
    NIAGADSiENSG00000147162
    OpenTargetsiENSG00000147162
    PharmGKBiPA31914

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG1124 Eukaryota
    KOG4626 Eukaryota
    COG3914 LUCA
    GeneTreeiENSGT00940000155085
    HOGENOMiHOG000003765
    InParanoidiO15294
    KOiK09667
    OMAiPLTHEFR
    OrthoDBi142546at2759
    PhylomeDBiO15294
    TreeFamiTF105785

    Enzyme and pathway databases

    UniPathwayiUPA00378
    BioCyciMetaCyc:ENSG00000147162-MONOMER
    BRENDAi2.4.1.255 2681
    ReactomeiR-HSA-3214847 HATs acetylate histones
    R-HSA-5689603 UCH proteinases
    SABIO-RKiO15294
    SignaLinkiO15294
    SIGNORiO15294

    Miscellaneous databases

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

    More...
    ChiTaRSi
    OGT human
    EvolutionaryTraceiO15294

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    OGT_(gene)

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

    More...
    GenomeRNAii
    8473
    PharosiO15294

    Protein Ontology

    More...
    PROi
    PR:O15294

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000147162 Expressed in 240 organ(s), highest expression level in middle temporal gyrus
    ExpressionAtlasiO15294 baseline and differential
    GenevisibleiO15294 HS

    Family and domain databases

    Gene3Di1.25.40.10, 2 hits
    InterProiView protein in InterPro
    IPR037919 OGT
    IPR029489 OGT/SEC/SPY_C
    IPR013026 TPR-contain_dom
    IPR011990 TPR-like_helical_dom_sf
    IPR001440 TPR_1
    IPR019734 TPR_repeat
    PANTHERiPTHR44366 PTHR44366, 1 hit
    PfamiView protein in Pfam
    PF13844 Glyco_transf_41, 1 hit
    PF00515 TPR_1, 2 hits
    PF13181 TPR_8, 2 hits
    SMARTiView protein in SMART
    SM00028 TPR, 12 hits
    SUPFAMiSSF48452 SSF48452, 2 hits
    PROSITEiView protein in PROSITE
    PS50005 TPR, 12 hits
    PS50293 TPR_REGION, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

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

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiOGT1_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: O15294
    Secondary accession number(s): Q7Z3K0
    , Q8WWM8, Q96CC1, Q9UG57
    <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: May 30, 2000
    Last sequence update: June 21, 2005
    Last modified: October 16, 2019
    This is version 217 of the entry and version 3 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, Direct protein sequencing, 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 X
      Human chromosome X: 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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