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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-alpha-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-serine.4 Publications
UDP-N-acetyl-alpha-D-glucosamine + [protein]-L-threonine = UDP + [protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonine.4 Publications

Enzyme regulationi

Subject to product inhibition by UDP.1 Publication

Kineticsi

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

    Pathwayi: protein glycosylation

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

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei508Proton acceptor1 Publication1
    Binding sitei849UDP1
    Binding sitei852UDP1
    Binding sitei935UDP1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi905 – 908UDP4
    Nucleotide bindingi911 – 914UDP4
    Nucleotide bindingi929 – 931UDP3

    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
    • 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 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.
    ZFISH:ENSG00000147162-MONOMER.
    BRENDAi2.4.1.255. 2681.
    ReactomeiR-HSA-3214847. HATs acetylate histones.
    R-HSA-5689603. UCH proteinases.
    SABIO-RKO15294.
    SignaLinkiO15294.
    SIGNORiO15294.
    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:2.4.1.2554 Publications)
    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
    Proteomesi
    • UP000005640 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

    • cytosol Source: UniProtKB
    • histone acetyltransferase complex Source: UniProtKB
    • mitochondrion Source: UniProtKB-SubCell
    • MLL5-L complex Source: UniProtKB
    • nucleoplasm Source: Reactome
    • 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)DescriptionActionsGraphical viewLength
    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. 1 Publication1
    Mutagenesisi568H → A: Reduces enzyme activity by about 95%. 1 Publication1
    Mutagenesisi911H → A: Reduces enzyme activity by over 90%. 1 Publication1
    Mutagenesisi991 – 992KK → AA: Abolishes phosphatidylinisitol binding, no translocation to the cell membrane, and no effect on phosphorylation of AKT1 nor IRS1. 1 Publication2
    Mutagenesisi994R → A: No effect on phosphatidylinisitol binding. 1 Publication1
    Mutagenesisi996K → A: Reduced phosphatidylinisitol binding. 1 Publication1
    Mutagenesisi999K → A: Reduced phosphatidylinisitol binding. 1 Publication1
    Mutagenesisi1001R → A: No effect on phosphatidylinisitol binding. 1 Publication1
    Mutagenesisi1010K → A: No effect on phosphatidylinisitol binding. 1 Publication1

    Organism-specific databases

    DisGeNETi8473.
    OpenTargetsiENSG00000147162.
    PharmGKBiPA31914.

    Chemistry databases

    ChEMBLiCHEMBL5955.

    Polymorphism and mutation databases

    BioMutaiOGT.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources1 Publication
    ChainiPRO_00001917722 – 1046UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunitAdd BLAST1045

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineCombined sources1 Publication1
    Modified residuei3Phosphoserine; by GSK3-beta; alternateBy similarity1
    Glycosylationi3O-linked (GlcNAc); alternateBy similarity1
    Modified residuei4Phosphoserine; by GSK3-beta; alternateBy similarity1
    Glycosylationi4O-linked (GlcNAc); alternateBy similarity1
    Modified residuei20PhosphoserineCombined sources1

    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

    EPDiO15294.
    MaxQBiO15294.
    PaxDbiO15294.
    PeptideAtlasiO15294.
    PRIDEiO15294.

    PTM databases

    iPTMnetiO15294.
    PhosphoSitePlusiO15294.

    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

    BgeeiENSG00000147162.
    CleanExiHS_OGT.
    ExpressionAtlasiO15294. baseline and differential.
    GenevisibleiO15294. HS.

    Organism-specific databases

    HPAiCAB034099.
    HPA030751.
    HPA030752.
    HPA030754.

    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
    HCFC1P5161010EBI-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.
    TRAK1Q9UPV93EBI-539828,EBI-1105048

    Protein-protein interaction databases

    BioGridi114049. 98 interactors.
    DIPiDIP-33491N.
    IntActiO15294. 80 interactors.
    MINTiMINT-2998811.
    STRINGi9606.ENSP00000362824.

    Chemistry databases

    BindingDBiO15294.

    Structurei

    Secondary structure

    11046
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi27 – 34Combined sources8
    Helixi37 – 50Combined sources14
    Helixi55 – 67Combined sources13
    Helixi71 – 84Combined sources14
    Helixi89 – 102Combined sources14
    Helixi105 – 118Combined sources14
    Helixi123 – 136Combined sources14
    Helixi141 – 152Combined sources12
    Helixi158 – 168Combined sources11
    Helixi173 – 186Combined sources14
    Helixi191 – 202Combined sources12
    Turni203 – 205Combined sources3
    Helixi207 – 220Combined sources14
    Helixi225 – 236Combined sources12
    Turni237 – 239Combined sources3
    Helixi243 – 254Combined sources12
    Helixi259 – 271Combined sources13
    Helixi275 – 287Combined sources13
    Helixi293 – 306Combined sources14
    Helixi309 – 322Combined sources14
    Helixi325 – 339Combined sources15
    Helixi343 – 356Combined sources14
    Helixi361 – 373Combined sources13
    Helixi377 – 390Combined sources14
    Helixi395 – 407Combined sources13
    Helixi411 – 424Combined sources14
    Helixi429 – 441Combined sources13
    Helixi445 – 458Combined sources14
    Helixi463 – 475Combined sources13
    Helixi482 – 498Combined sources17
    Helixi509 – 512Combined sources4
    Helixi517 – 536Combined sources20
    Turni537 – 539Combined sources3
    Beta strandi547 – 549Combined sources3
    Turni550 – 554Combined sources5
    Beta strandi556 – 563Combined sources8
    Beta strandi565 – 568Combined sources4
    Helixi569 – 574Combined sources6
    Helixi577 – 580Combined sources4
    Turni583 – 585Combined sources3
    Beta strandi586 – 594Combined sources9
    Helixi600 – 608Combined sources9
    Beta strandi609 – 614Combined sources6
    Helixi615 – 617Combined sources3
    Helixi621 – 630Combined sources10
    Beta strandi634 – 639Combined sources6
    Beta strandi641 – 643Combined sources3
    Helixi649 – 652Combined sources4
    Beta strandi656 – 661Combined sources6
    Beta strandi676 – 679Combined sources4
    Turni681 – 683Combined sources3
    Helixi686 – 691Combined sources6
    Beta strandi693 – 698Combined sources6
    Helixi708 – 711Combined sources4
    Helixi713 – 715Combined sources3
    Beta strandi719 – 721Combined sources3
    Beta strandi731 – 737Combined sources7
    Helixi741 – 746Combined sources6
    Beta strandi748 – 750Combined sources3
    Beta strandi752 – 754Combined sources3
    Beta strandi774 – 777Combined sources4
    Helixi781 – 792Combined sources12
    Beta strandi796 – 799Combined sources4
    Beta strandi802 – 806Combined sources5
    Helixi807 – 809Combined sources3
    Helixi810 – 813Combined sources4
    Helixi815 – 818Combined sources4
    Beta strandi820 – 822Combined sources3
    Beta strandi826 – 831Combined sources6
    Helixi832 – 835Combined sources4
    Beta strandi841 – 845Combined sources5
    Helixi850 – 852Combined sources3
    Helixi855 – 867Combined sources13
    Beta strandi869 – 877Combined sources9
    Helixi880 – 882Combined sources3
    Helixi883 – 892Combined sources10
    Helixi897 – 899Combined sources3
    Beta strandi900 – 904Combined sources5
    Helixi908 – 914Combined sources7
    Helixi915 – 917Combined sources3
    Beta strandi919 – 922Combined sources4
    Beta strandi925 – 927Combined sources3
    Helixi931 – 938Combined sources8
    Beta strandi943 – 945Combined sources3
    Helixi951 – 953Combined sources3
    Helixi955 – 963Combined sources9
    Helixi966 – 968Combined sources3
    Helixi973 – 985Combined sources13
    Helixi987 – 1003Combined sources17
    Helixi1005 – 1007Combined sources3
    Helixi1009 – 1028Combined sources20

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliO15294.
    SMRiO15294.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15294.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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
    Regioni991 – 1010Required for phosphatidylinositol 3,4,5-triphosphate bindingAdd BLAST20

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Motifi487 – 503Nuclear localization signalSequence analysisAdd BLAST17

    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

    eggNOGiKOG1124. Eukaryota.
    KOG4626. Eukaryota.
    COG3914. LUCA.
    GeneTreeiENSGT00550000074327.
    HOGENOMiHOG000003765.
    HOVERGENiHBG000351.
    InParanoidiO15294.
    KOiK09667.
    OMAiKLAYMPN.
    OrthoDBiEOG091G024Y.
    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. 2 hits.
    PF13414. TPR_11. 3 hits.
    PF13181. TPR_8. 2 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 12 hits.
    [Graphical view]
    SUPFAMiSSF48452. SSF48452. 4 hits.
    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)DescriptionActionsGraphical viewLength
    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_074019319A → T Probable disease-associated mutation found in a family with X-linked intellectual disability. 1 Publication1
    Natural variantiVAR_064736538L → P Found in a renal cell carcinoma sample; somatic mutation. 1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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:
    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. [O15294-4]
    XP_016885397.1. XM_017029908.1. [O15294-4]
    UniGeneiHs.405410.

    Genome annotation databases

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

    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_016885396.1. XM_017029907.1. [O15294-4]
    XP_016885397.1. XM_017029908.1. [O15294-4]
    UniGeneiHs.405410.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliO15294.
    SMRiO15294.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114049. 98 interactors.
    DIPiDIP-33491N.
    IntActiO15294. 80 interactors.
    MINTiMINT-2998811.
    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

    EPDiO15294.
    MaxQBiO15294.
    PaxDbiO15294.
    PeptideAtlasiO15294.
    PRIDEiO15294.

    Protocols and materials databases

    DNASUi8473.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi8473.
    DisGeNETi8473.
    GeneCardsiOGT.
    HGNCiHGNC:8127. OGT.
    HPAiCAB034099.
    HPA030751.
    HPA030752.
    HPA030754.
    MIMi300255. gene.
    neXtProtiNX_O15294.
    OpenTargetsiENSG00000147162.
    PharmGKBiPA31914.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1124. Eukaryota.
    KOG4626. Eukaryota.
    COG3914. LUCA.
    GeneTreeiENSGT00550000074327.
    HOGENOMiHOG000003765.
    HOVERGENiHBG000351.
    InParanoidiO15294.
    KOiK09667.
    OMAiKLAYMPN.
    OrthoDBiEOG091G024Y.
    PhylomeDBiO15294.
    TreeFamiTF105785.

    Enzyme and pathway databases

    UniPathwayiUPA00378.
    BioCyciMetaCyc:ENSG00000147162-MONOMER.
    ZFISH:ENSG00000147162-MONOMER.
    BRENDAi2.4.1.255. 2681.
    ReactomeiR-HSA-3214847. HATs acetylate histones.
    R-HSA-5689603. UCH proteinases.
    SABIO-RKO15294.
    SignaLinkiO15294.
    SIGNORiO15294.

    Miscellaneous databases

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

    Gene expression databases

    BgeeiENSG00000147162.
    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. 2 hits.
    PF13414. TPR_11. 3 hits.
    PF13181. TPR_8. 2 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 12 hits.
    [Graphical view]
    SUPFAMiSSF48452. SSF48452. 4 hits.
    PROSITEiPS50005. TPR. 12 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 187 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

    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 one 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.