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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-Experimental evidence at protein leveli

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). 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. 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. 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:18288188, PubMed:19377461, PubMed:19451179, PubMed:20018868, PubMed:20200153, PubMed:21285374, PubMed:15361863).13 Publications
Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.

Catalytic activityi

UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine.
UDP-N-acetyl-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine.

Enzyme regulationi

Subject to product inhibition by UDP.1 Publication

Kineticsi

  1. KM=1.8 µM for UDP-N-acetyl-D-glucosamine1 Publication

    Pathway:iprotein glycosylation

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei508 – 5081Proton acceptor1 Publication
    Binding sitei849 – 8491UDP
    Binding sitei852 – 8521UDP
    Binding sitei935 – 9351UDP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi905 – 9084UDP
    Nucleotide bindingi911 – 9144UDP
    Nucleotide bindingi929 – 9313UDP

    GO - Molecular functioni

    • acetylglucosaminyltransferase activity Source: ProtInc
    • enzyme activator activity Source: BHF-UCL
    • phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
    • protein N-acetylglucosaminyltransferase activity Source: UniProtKB
    • protein O-GlcNAc transferase activity Source: UniProtKB

    GO - Biological processi

    • apoptotic process Source: UniProtKB
    • cellular response to retinoic acid Source: BHF-UCL
    • chromatin organization Source: Reactome
    • circadian regulation of gene expression Source: UniProtKB
    • histone H3-K4 trimethylation Source: UniProtKB
    • histone H4-K16 acetylation Source: UniProtKB
    • histone H4-K5 acetylation Source: UniProtKB
    • histone H4-K8 acetylation Source: UniProtKB
    • negative regulation of protein ubiquitination Source: UniProtKB
    • phosphatidylinositol-mediated signaling Source: UniProtKB
    • positive regulation of catalytic activity Source: GOC
    • positive regulation of granulocyte differentiation Source: BHF-UCL
    • positive regulation of histone H3-K27 methylation Source: UniProtKB
    • positive regulation of histone H3-K4 methylation Source: BHF-UCL
    • positive regulation of proteolysis Source: UniProtKB
    • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    • protein O-linked glycosylation Source: UniProtKB
    • regulation of gluconeogenesis involved in cellular glucose homeostasis Source: UniProtKB
    • regulation of glycolytic process Source: UniProtKB
    • regulation of insulin receptor signaling pathway Source: UniProtKB
    • regulation of Rac protein signal transduction Source: UniProtKB
    • response to insulin Source: UniProtKB
    • response to nutrient Source: ProtInc
    • signal transduction Source: ProtInc
    Complete GO annotation...

    Keywords - Molecular functioni

    Chromatin regulator, Glycosyltransferase, Transferase

    Keywords - Biological processi

    Apoptosis, Biological rhythms

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000147162-MONOMER.
    BRENDAi2.4.1.255. 2681.
    ReactomeiREACT_264245. HATs acetylate histones.
    SABIO-RKO15294.
    SignaLinkiO15294.
    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiGT41. Glycosyltransferase Family 41.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (EC:2.4.1.255)
    Alternative name(s):
    O-GlcNAc transferase subunit p110
    O-linked N-acetylglucosamine transferase 110 kDa subunit
    Short name:
    OGT
    Gene namesi
    Name:OGT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8127. OGT.

    Subcellular locationi

    Isoform 2 :
    Isoform 3 :
    • Cytoplasm
    • Nucleus
    • Cell membrane

    • Note: Mostly in the nucleus. Retained in the nucleus via interaction with HCFC1. After insulin induction, translocated from the nucleus to the cell membrane via phophatidylinisotide binding. Colocalizes with AKT1 at the plasma membrane.

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: UniProtKB
    • histone acetyltransferase complex Source: UniProtKB
    • microtubule organizing center Source: HPA
    • mitochondrion Source: UniProtKB-SubCell
    • MLL5-L complex Source: UniProtKB
    • nucleoplasm Source: HPA
    • nucleus Source: UniProtKB
    • plasma membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi208 – 2081W → E: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with D-211. 1 Publication
    Mutagenesisi211 – 2111I → D: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with E-208. 1 Publication
    Mutagenesisi508 – 5081H → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi568 – 5681H → A: Reduces enzyme activity by about 95%. 1 Publication
    Mutagenesisi911 – 9111H → A: Reduces enzyme activity by over 90%. 1 Publication
    Mutagenesisi991 – 9922KK → AA: Abolishes phosphatidylinisitol binding, no translocation to the cell membrane, and no effect on phosphorylation of AKT1 nor IRS1. 1 Publication
    Mutagenesisi994 – 9941R → A: No effect on phosphatidylinisitol binding. 1 Publication
    Mutagenesisi996 – 9961K → A: Reduced phosphatidylinisitol binding. 1 Publication
    Mutagenesisi999 – 9991K → A: Reduced phosphatidylinisitol binding. 1 Publication
    Mutagenesisi1001 – 10011R → A: No effect on phosphatidylinisitol binding. 1 Publication
    Mutagenesisi1010 – 10101K → A: No effect on phosphatidylinisitol binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA31914.

    Polymorphism and mutation databases

    BioMutaiOGT.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 10461045UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunitPRO_0000191772Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei3 – 31Phosphoserine; by GSK3-beta; alternateBy similarity
    Glycosylationi3 – 31O-linked (GlcNAc); alternateBy similarity
    Modified residuei4 – 41Phosphoserine; by GSK3-beta; alternateBy similarity
    Glycosylationi4 – 41O-linked (GlcNAc); alternateBy similarity

    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

    MaxQBiO15294.
    PaxDbiO15294.
    PRIDEiO15294.

    PTM databases

    PhosphoSiteiO15294.

    Expressioni

    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

    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

    BgeeiO15294.
    CleanExiHS_OGT.
    ExpressionAtlasiO15294. baseline and differential.
    GenevisibleiO15294. HS.

    Organism-specific databases

    HPAiCAB034099.
    HPA030751.
    HPA030752.
    HPA030753.

    Interactioni

    Subunit structurei

    Heterotrimer; consists of one 78 kDa subunit and two 110 kDa subunits dimerized via TPR repeats 6 and 7. Interacts (via TPR repeats 6 and 7) with ATXN10 (By similarity). Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, HCFC1, PPP1CC and ACTB. 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. Interacts (via TPR 5-6) with TET1, TET2 and TET3. Interacts with ARNTL/BMAL1 (By similarity).By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HCFC1P516109EBI-539828,EBI-396176
    Hoxa1P090223EBI-539828,EBI-3957603From a different organism.
    NFATC1O956442EBI-539828,EBI-6907210
    NUP62CLQ9H1M04EBI-539828,EBI-751933
    PHC3Q8NDX53EBI-539828,EBI-1223801
    PSG1P114643EBI-539828,EBI-716740
    RELAQ042062EBI-539828,EBI-73886
    TET2E7EQS83EBI-539828,EBI-10177000
    TET2Q6N0217EBI-539828,EBI-310727
    TET3O431514EBI-539828,EBI-2831148
    Tet3Q8BG872EBI-539828,EBI-9031997From a different organism.
    TRAK1Q9UPV92EBI-539828,EBI-1105048

    Protein-protein interaction databases

    BioGridi114049. 69 interactions.
    DIPiDIP-33491N.
    IntActiO15294. 40 interactions.
    MINTiMINT-2998811.
    STRINGi9606.ENSP00000362824.

    Structurei

    Secondary structure

    1
    1046
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 348Combined sources
    Helixi37 – 5014Combined sources
    Helixi55 – 6713Combined sources
    Helixi71 – 8414Combined sources
    Helixi89 – 10214Combined sources
    Helixi105 – 11814Combined sources
    Helixi123 – 13614Combined sources
    Helixi141 – 15212Combined sources
    Helixi158 – 16811Combined sources
    Helixi173 – 18614Combined sources
    Helixi191 – 20212Combined sources
    Turni203 – 2053Combined sources
    Helixi207 – 22014Combined sources
    Helixi225 – 23612Combined sources
    Turni237 – 2393Combined sources
    Helixi243 – 25412Combined sources
    Helixi259 – 27113Combined sources
    Helixi275 – 28713Combined sources
    Helixi293 – 30614Combined sources
    Helixi309 – 32214Combined sources
    Helixi325 – 33915Combined sources
    Helixi343 – 35614Combined sources
    Helixi361 – 37313Combined sources
    Helixi377 – 39014Combined sources
    Helixi395 – 40713Combined sources
    Helixi411 – 42414Combined sources
    Helixi429 – 44113Combined sources
    Helixi445 – 45814Combined sources
    Helixi463 – 47513Combined sources
    Helixi482 – 49817Combined sources
    Helixi509 – 5124Combined sources
    Helixi517 – 53620Combined sources
    Turni537 – 5393Combined sources
    Beta strandi547 – 5493Combined sources
    Turni550 – 5545Combined sources
    Beta strandi556 – 5638Combined sources
    Beta strandi565 – 5684Combined sources
    Helixi569 – 5746Combined sources
    Helixi577 – 5804Combined sources
    Turni583 – 5853Combined sources
    Beta strandi586 – 5949Combined sources
    Helixi600 – 6089Combined sources
    Beta strandi609 – 6146Combined sources
    Helixi615 – 6173Combined sources
    Helixi621 – 63010Combined sources
    Beta strandi634 – 6396Combined sources
    Beta strandi641 – 6433Combined sources
    Helixi649 – 6524Combined sources
    Beta strandi656 – 6616Combined sources
    Beta strandi676 – 6794Combined sources
    Turni681 – 6833Combined sources
    Helixi686 – 6916Combined sources
    Beta strandi693 – 6986Combined sources
    Helixi708 – 7114Combined sources
    Helixi713 – 7153Combined sources
    Beta strandi719 – 7213Combined sources
    Beta strandi731 – 7377Combined sources
    Helixi741 – 7466Combined sources
    Beta strandi748 – 7503Combined sources
    Beta strandi752 – 7543Combined sources
    Beta strandi774 – 7774Combined sources
    Helixi781 – 79212Combined sources
    Beta strandi796 – 7994Combined sources
    Beta strandi802 – 8065Combined sources
    Helixi807 – 8093Combined sources
    Helixi810 – 8134Combined sources
    Helixi815 – 8184Combined sources
    Beta strandi820 – 8223Combined sources
    Beta strandi826 – 8316Combined sources
    Helixi832 – 8354Combined sources
    Beta strandi841 – 8455Combined sources
    Helixi850 – 8523Combined sources
    Helixi855 – 86713Combined sources
    Beta strandi869 – 8779Combined sources
    Helixi880 – 8823Combined sources
    Helixi883 – 89210Combined sources
    Helixi897 – 8993Combined sources
    Beta strandi900 – 9045Combined sources
    Helixi908 – 9147Combined sources
    Helixi915 – 9173Combined sources
    Beta strandi919 – 9224Combined sources
    Beta strandi925 – 9273Combined sources
    Helixi931 – 9388Combined sources
    Beta strandi943 – 9453Combined sources
    Helixi951 – 9533Combined sources
    Helixi955 – 9639Combined sources
    Helixi966 – 9683Combined sources
    Helixi973 – 98513Combined sources
    Helixi987 – 100317Combined sources
    Helixi1005 – 10073Combined sources
    Helixi1009 – 102820Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliO15294.
    SMRiO15294. Positions 23-1038.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15294.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati21 – 5434TPR 1Add
    BLAST
    Repeati89 – 12234TPR 2Add
    BLAST
    Repeati123 – 15634TPR 3Add
    BLAST
    Repeati157 – 19034TPR 4Add
    BLAST
    Repeati191 – 22434TPR 5Add
    BLAST
    Repeati225 – 25834TPR 6Add
    BLAST
    Repeati259 – 29234TPR 7Add
    BLAST
    Repeati293 – 32634TPR 8Add
    BLAST
    Repeati327 – 36034TPR 9Add
    BLAST
    Repeati361 – 39434TPR 10Add
    BLAST
    Repeati395 – 42834TPR 11Add
    BLAST
    Repeati429 – 46234TPR 12Add
    BLAST
    Repeati463 – 47311TPR 13; truncatedAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni991 – 101020Required for phosphatidylinositol 3,4,5-triphosphate bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi487 – 50317Nuclear localization signalSequence AnalysisAdd
    BLAST

    Domaini

    The TPR repeat domain is required for substrate binding and oligomerization.1 Publication

    Sequence similaritiesi

    Contains 13 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG3914.
    GeneTreeiENSGT00550000074327.
    HOGENOMiHOG000003765.
    HOVERGENiHBG000351.
    InParanoidiO15294.
    KOiK09667.
    OMAiKLAYMPN.
    OrthoDBiEOG71K624.
    PhylomeDBiO15294.
    TreeFamiTF105785.

    Family and domain databases

    Gene3Di1.25.40.10. 5 hits.
    InterProiIPR029489. OGT/SEC/SPY_C.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical_dom.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF13844. Glyco_transf_41. 1 hit.
    PF00515. TPR_1. 9 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 12 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 12 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 3 (identifier: O15294-1) [UniParc]FASTAAdd to basket

    Also known as: Nucleocytoplasmic isoform, ncOGT

    This isoform has been chosen as the 'canonical' 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
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti308 – 3081S → Q in CAB62528 (PubMed:17974005).Curated
    Sequence conflicti663 – 6631L → P in CAD97853 (PubMed:17974005).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti538 – 5381L → P Found in a renal cell carcinoma sample; somatic mutation.
    VAR_064736

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 381381Missing in isoform 4. 1 PublicationVSP_040764Add
    BLAST
    Alternative sequencei1 – 176176MASSV…RLEEA → MLQGHFWLVREGIMISPSSP PPPNLFFFPLQIFPFPFTSF PSHLLSLTPP in isoform 2. 1 PublicationVSP_006553Add
    BLAST
    Alternative sequencei13 – 2210Missing in isoform 1. 2 PublicationsVSP_014164

    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_005262365.1. XM_005262308.1. [O15294-4]
    UniGeneiHs.405410.

    Genome annotation databases

    EnsembliENST00000373701; ENSP00000362805; ENSG00000147162. [O15294-3]
    ENST00000373719; ENSP00000362824; ENSG00000147162.
    GeneIDi8473.
    KEGGihsa:8473.
    UCSCiuc004eaa.2. human. [O15294-1]
    uc004eab.2. human. [O15294-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    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_005262365.1. XM_005262308.1. [O15294-4]
    UniGeneiHs.405410.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliO15294.
    SMRiO15294. Positions 23-1038.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114049. 69 interactions.
    DIPiDIP-33491N.
    IntActiO15294. 40 interactions.
    MINTiMINT-2998811.
    STRINGi9606.ENSP00000362824.

    Chemistry

    BindingDBiO15294.
    ChEMBLiCHEMBL5955.

    Protein family/group databases

    CAZyiGT41. Glycosyltransferase Family 41.

    PTM databases

    PhosphoSiteiO15294.

    Polymorphism and mutation databases

    BioMutaiOGT.

    Proteomic databases

    MaxQBiO15294.
    PaxDbiO15294.
    PRIDEiO15294.

    Protocols and materials databases

    DNASUi8473.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000373701; ENSP00000362805; ENSG00000147162. [O15294-3]
    ENST00000373719; ENSP00000362824; ENSG00000147162.
    GeneIDi8473.
    KEGGihsa:8473.
    UCSCiuc004eaa.2. human. [O15294-1]
    uc004eab.2. human. [O15294-3]

    Organism-specific databases

    CTDi8473.
    GeneCardsiGC0XP070752.
    HGNCiHGNC:8127. OGT.
    HPAiCAB034099.
    HPA030751.
    HPA030752.
    HPA030753.
    MIMi300255. gene.
    neXtProtiNX_O15294.
    PharmGKBiPA31914.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3914.
    GeneTreeiENSGT00550000074327.
    HOGENOMiHOG000003765.
    HOVERGENiHBG000351.
    InParanoidiO15294.
    KOiK09667.
    OMAiKLAYMPN.
    OrthoDBiEOG71K624.
    PhylomeDBiO15294.
    TreeFamiTF105785.

    Enzyme and pathway databases

    UniPathwayiUPA00378.
    BioCyciMetaCyc:ENSG00000147162-MONOMER.
    BRENDAi2.4.1.255. 2681.
    ReactomeiREACT_264245. HATs acetylate histones.
    SABIO-RKO15294.
    SignaLinkiO15294.

    Miscellaneous databases

    EvolutionaryTraceiO15294.
    GeneWikiiOGT_(gene).
    GenomeRNAii8473.
    NextBioi31706.
    PROiO15294.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO15294.
    CleanExiHS_OGT.
    ExpressionAtlasiO15294. baseline and differential.
    GenevisibleiO15294. HS.

    Family and domain databases

    Gene3Di1.25.40.10. 5 hits.
    InterProiIPR029489. OGT/SEC/SPY_C.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical_dom.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF13844. Glyco_transf_41. 1 hit.
    PF00515. TPR_1. 9 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 12 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 12 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "O-linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats."
      Lubas W.A., Frank D.W., Krause M., Hanover J.A.
      J. Biol. Chem. 272:9316-9324(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 227-236 AND 955-971, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1."
      Nolte D., Muller U.
      Mamm. Genome 13:62-64(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
      Tissue: Endometrium, Fetal brain and Spinal cord.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Colon and Pancreas.
    5. Bienvenut W.V., Dhillon A.S., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17; 31-42; 161-168; 244-250; 339-348; 734-752; 868-877 AND 1002-1010, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    6. "Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression."
      Yang X., Zhang F., Kudlow J.E.
      Cell 110:69-80(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIN3A, FUNCTION.
    7. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
      Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
      Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCFC1.
    8. "Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance."
      Yang X., Ongusaha P.P., Miles P.D., Havstad J.C., Zhang F., So W.V., Kudlow J.E., Michell R.H., Olefsky J.M., Field S.J., Evans R.M.
      Nature 451:964-969(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, FUNCTION, PHOSPHATIDYLINOSITOL-BINDING, MUTAGENESIS OF 991-LYS-LYS-992; ARG-994; LYS-996; LYS-999; ARG-1001 AND LYS-1010.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Reduced O-GlcNAcylation links lower brain glucose metabolism and tau pathology in Alzheimer's disease."
      Liu F., Shi J., Tanimukai H., Gu J., Gu J., Grundke-Iqbal I., Iqbal K., Gong C.X.
      Brain 132:1820-1832(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH ALZHEIMER DISEASE.
    12. "Up-regulation of O-GlcNAc transferase with glucose deprivation in HepG2 cells is mediated by decreased hexosamine pathway flux."
      Taylor R.P., Geisler T.S., Chambers J.H., McClain D.A.
      J. Biol. Chem. 284:3425-3432(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    13. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
      Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
      Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE MLL5-L COMPLEX.
    14. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
      Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
      J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
    15. "Regulation of insulin receptor substrate 1 (IRS-1)/AKT kinase-mediated insulin signaling by O-Linked beta-N-acetylglucosamine in 3T3-L1 adipocytes."
      Whelan S.A., Dias W.B., Thiruneelakantapillai L., Lane M.D., Hart G.W.
      J. Biol. Chem. 285:5204-5211(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, POSSIBLE ASSOCIATION WITH DIABETES.
    16. "The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias."
      Mazars R., Gonzalez-de-Peredo A., Cayrol C., Lavigne A.C., Vogel J.L., Ortega N., Lacroix C., Gautier V., Huet G., Ray A., Monsarrat B., Kristie T.M., Girard J.P.
      J. Biol. Chem. 285:13364-13371(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX, INTERACTION WITH HCFC1; THAP1 AND THAP3, FUNCTION.
    17. "Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis."
      Shin S.H., Love D.C., Hanover J.A.
      Amino Acids 40:885-893(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION (ISOFORM 2).
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway."
      Daou S., Mashtalir N., Hammond-Martel I., Pak H., Yu H., Sui G., Vogel J.L., Kristie T.M., Affar E.B.
      Proc. Natl. Acad. Sci. U.S.A. 108:2747-2752(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, INTERACTION WITH HCFC1.
    20. Cited for: FUNCTION, INTERACTION WITH H2B.
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    22. "Phosphofructokinase 1 glycosylation regulates cell growth and metabolism."
      Yi W., Clark P.M., Mason D.E., Keenan M.C., Hill C., Goddard W.A. III, Peters E.C., Driggers E.M., Hsieh-Wilson L.C.
      Science 337:975-980(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. Cited for: FUNCTION, INTERACTION WITH HCFC1; TET2 AND TET3.
    24. "TET2 promotes histone O-GlcNAcylation during gene transcription."
      Chen Q., Chen Y., Bian C., Fujiki R., Yu X.
      Nature 493:561-564(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TET2 AND TET3.
    25. Cited for: FUNCTION.
    26. "The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha."
      Jinek M., Rehwinkel J., Lazarus B.D., Izaurralde E., Hanover J.A., Conti E.
      Nat. Struct. Mol. Biol. 11:1001-1007(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 26-400, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, MUTAGENESIS OF TRP-208 AND ILE-211.
    27. "Structure of human O-GlcNAc transferase and its complex with a peptide substrate."
      Lazarus M.B., Nam Y., Jiang J., Sliz P., Walker S.
      Nature 469:564-567(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 323-1041 IN COMPLEXES WITH UDP AND PEPTIDE SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF HIS-508; HIS-568 AND HIS-911.

    Entry informationi

    Entry nameiOGT1_HUMAN
    AccessioniPrimary (citable) accession number: O15294
    Secondary accession number(s): Q7Z3K0
    , Q8WWM8, Q96CC1, Q9UG57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: June 21, 2005
    Last modified: July 22, 2015
    This is version 172 of the entry and version 3 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.