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UniProtKB - Q8CGY8 (OGT1_MOUSE)

Entry version 155 (10 Feb 2021)
Sequence version 2 (01 May 2007)
Previous versions | rss
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Protein

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

Gene

Ogt

Organism
Mus musculus (Mouse)
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:29465778). 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. Probably by glycosylating KMT2E/MLL5, stabilizes KMT2E/MLL5 by preventing its ubiquitination (By similarity).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. 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). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (By similarity). 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:23337503, PubMed:23395176). O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity (By similarity). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Glycosylates HOXA1 (PubMed:29465778). O-glycosylates FNIP1 (By similarity).By similarity3 Publications

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 acceptorBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei849UDPBy similarity1
Binding sitei852UDPBy similarity1
Binding sitei935UDPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 – 908UDPBy similarity3
Nucleotide bindingi911 – 914UDPBy similarity4
Nucleotide bindingi930 – 932UDPBy similarity3

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 processBiological rhythms
LigandLipid-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.1.255, 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-3214847, HATs acetylate histones
R-MMU-5675482, Regulation of necroptotic cell death
R-MMU-5689603, UCH proteinases

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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC:2.4.1.2551 Publication)
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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ogt
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1339639, Ogt

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2 – 473Missing : Loss of interaction with HOXA1. Loss of glycosylation of HOXA1. 1 PublicationAdd BLAST472
Mutagenesisi474 – 1046Missing : Interacts with HOXA1. Interaction is localized to the nucleus. 1 PublicationAdd BLAST573
Mutagenesisi504 – 1046Missing : Interacts with HOXA1. Interaction is localized to the nucleus. 1 PublicationAdd BLAST543
Mutagenesisi991 – 1046Missing : Impaired interaction with HOXA1. Loss of glycosylation of HOXA1. 1 PublicationAdd BLAST56

<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%5Fprocessing%5Fsection">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 methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002852162 – 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-acetylalanineBy similarity1
Modified residuei3Phosphoserine; by GSK3-beta; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi3O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei4Phosphoserine; by GSK3-beta; alternate1 Publication1
Glycosylationi4O-linked (GlcNAc) serine; alternate1 Publication1
Modified residuei20PhosphoserineCombined sources1
Modified residuei989PhosphotyrosineBy similarity1

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

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

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q8CGY8

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

More...PaxDbi		Q8CGY8

PeptideAtlas

More...PeptideAtlasi		Q8CGY8

PRoteomics IDEntifications database

More...PRIDEi		Q8CGY8

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q8CGY8, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q8CGY8

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

More...PhosphoSitePlusi		Q8CGY8

<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 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

Expression in the liver oscillates in a circadian manner.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000034160, Expressed in female gonad and 325 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q8CGY8, MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

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

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.

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

Interacts directly with HCFC1; the interaction O-glycosylates HCFC1, regulates its proteolytic processing and transcriptional activity and, in turn, stabilizes OGT in the nucleus.

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

Interacts (via TPR 5-6) with TET1, TET2 and TET3 (PubMed:23352454).

Interacts (via TPR repeats 6 and 7) with ATXN10 (PubMed:16182253).

Interacts with histone H2B (By similarity).

Interacts with ARNTL/BMAL1 (PubMed:23337503).

Found in a complex composed of at least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (PubMed:28554894).

Interacts with SINHCAF (PubMed:28554894).

Component of a complex composed of KMT2E/MLL5, OGT and USP7; the complex stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination and proteosomal-mediated degradation.

Interacts (via TRP repeats) with KMT2E/MLL5 (via N-terminus).

Interacts with USP7 (By similarity).

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 (By similarity).

Interacts (via TPR repeats domain) with HOXA1; the interaction takes place mainly in the nucleus (PubMed:29465778).

Interacts with NSD2 (PubMed:19483677).

By similarity6 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		223870, 29 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3441, SIN3A histone deacetylase complex, ES cell-specific variant
CPX-875, NSL histone acetyltransferase complex

Database of interacting proteins

More...DIPi		DIP-35700N

Protein interaction database and analysis system

More...IntActi		Q8CGY8, 9 interactors

Molecular INTeraction database

More...MINTi		Q8CGY8

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000045409

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q8CGY8, protein

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

3D structure databases

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

More...SMRi		Q8CGY8

Database of comparative protein structure models

More...ModBasei		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

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.By similarity

<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 41 family. O-GlcNAc transferase subfamily.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1124, Eukaryota
KOG4626, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155085

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001721_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q8CGY8

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		Q8CGY8

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, 3 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is 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 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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q8CGY8-1) [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
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 SIVAEQLEKN 
       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 GGDNPDSSNT 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 KSRQEYEDIA VKLGTDLEYL KKIRGKVWKQ 
      1010       1020       1030       1040 
RISSPLFNTK QYTMELERLY LQMWEHYAAG NKPDHMIKPV EVTESA
Length:1,046
Mass (Da):116,952
Last modified:May 1, 2007 - 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:iFD5EE12844E00097
GO
Isoform 2 (identifier: Q8CGY8-2) [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):115,733
Checksum:iBBCD509790239136
GO

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 conflicti57V → A in AAO17363 (PubMed:12504895).Curated1
Sequence conflicti992K → R in AAK39123 (Ref. 2) Curated1

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_02484413 – 22Missing in isoform 2. Curated10

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
AF539527 Genomic DNA Translation: AAO17363.1
AF363030 mRNA Translation: AAK39123.1
AL805980 Genomic DNA No translation available.
AL806534 Genomic DNA No translation available.
BC057319 mRNA Translation: AAH57319.1
AK047095 mRNA Translation: BAC32961.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS30318.1 [Q8CGY8-1]
CCDS72415.1 [Q8CGY8-2]

NCBI Reference Sequences

More...RefSeqi		NP_001277464.1, NM_001290535.1 [Q8CGY8-2]
NP_631883.2, NM_139144.4 [Q8CGY8-1]
XP_006527799.1, XM_006527736.3 [Q8CGY8-1]
XP_011245805.1, XM_011247503.2 [Q8CGY8-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000044475; ENSMUSP00000045409; ENSMUSG00000034160 [Q8CGY8-1]
ENSMUST00000119299; ENSMUSP00000113454; ENSMUSG00000034160 [Q8CGY8-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		108155

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:108155

UCSC genome browser

More...UCSCi		uc009tyc.3, mouse [Q8CGY8-1]
uc057ask.1, mouse [Q8CGY8-2]

Keywords - Coding sequence diversityi

Alternative splicing

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

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF539527 Genomic DNA Translation: AAO17363.1
AF363030 mRNA Translation: AAK39123.1
AL805980 Genomic DNA No translation available.
AL806534 Genomic DNA No translation available.
BC057319 mRNA Translation: AAH57319.1
AK047095 mRNA Translation: BAC32961.1
CCDSiCCDS30318.1 [Q8CGY8-1]
CCDS72415.1 [Q8CGY8-2]
RefSeqiNP_001277464.1, NM_001290535.1 [Q8CGY8-2]
NP_631883.2, NM_139144.4 [Q8CGY8-1]
XP_006527799.1, XM_006527736.3 [Q8CGY8-1]
XP_011245805.1, XM_011247503.2 [Q8CGY8-2]

3D structure databases

SMRiQ8CGY8
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi223870, 29 interactors
ComplexPortaliCPX-3441, SIN3A histone deacetylase complex, ES cell-specific variant
CPX-875, NSL histone acetyltransferase complex
DIPiDIP-35700N
IntActiQ8CGY8, 9 interactors
MINTiQ8CGY8
STRINGi10090.ENSMUSP00000045409

Protein family/group databases

CAZyiGT41, Glycosyltransferase Family 41

PTM databases

GlyGeniQ8CGY8, 2 sites
iPTMnetiQ8CGY8
PhosphoSitePlusiQ8CGY8

Proteomic databases

EPDiQ8CGY8
PaxDbiQ8CGY8
PeptideAtlasiQ8CGY8
PRIDEiQ8CGY8

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		27791, 438 antibodies

Genome annotation databases

EnsembliENSMUST00000044475; ENSMUSP00000045409; ENSMUSG00000034160 [Q8CGY8-1]
ENSMUST00000119299; ENSMUSP00000113454; ENSMUSG00000034160 [Q8CGY8-2]
GeneIDi108155
KEGGimmu:108155
UCSCiuc009tyc.3, mouse [Q8CGY8-1]
uc057ask.1, mouse [Q8CGY8-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8473
MGIiMGI:1339639, Ogt

Phylogenomic databases

eggNOGiKOG1124, Eukaryota
KOG4626, Eukaryota
GeneTreeiENSGT00940000155085
HOGENOMiCLU_001721_1_0_1
InParanoidiQ8CGY8
OMAiPLTHEFR
OrthoDBi142546at2759
PhylomeDBiQ8CGY8
TreeFamiTF105785

Enzyme and pathway databases

UniPathwayiUPA00378
BRENDAi2.4.1.255, 3474
ReactomeiR-MMU-3214847, HATs acetylate histones
R-MMU-5675482, Regulation of necroptotic cell death
R-MMU-5689603, UCH proteinases

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		108155, 10 hits in 18 CRISPR screens

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

More...ChiTaRSi		Ogt, mouse

Protein Ontology

More...PROi		PR:Q8CGY8
RNActiQ8CGY8, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000034160, Expressed in female gonad and 325 other tissues
GenevisibleiQ8CGY8, MM

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, 3 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		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 nameiOGT1_MOUSE
<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: Q8CGY8
Secondary accession number(s): A2ALY1
, Q6PG10, Q8BXH6, Q91Y38
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: February 10, 2021
This is version 155 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

<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

Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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