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O15294

- OGT1_HUMAN

UniProt

O15294 - OGT1_HUMAN

Protein

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

Gene

OGT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 3 (21 Jun 2005)
      Previous versions | rss
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    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

    Pathwayi

    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

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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cellular response to retinoic acid Source: BHF-UCL
    3. chromatin organization Source: Reactome
    4. circadian regulation of gene expression Source: UniProtKB
    5. histone H3-K4 trimethylation Source: UniProtKB
    6. histone H4-K16 acetylation Source: UniProtKB
    7. histone H4-K5 acetylation Source: UniProtKB
    8. histone H4-K8 acetylation Source: UniProtKB
    9. negative regulation of protein ubiquitination Source: UniProtKB
    10. phosphatidylinositol-mediated signaling Source: UniProtKB
    11. positive regulation of catalytic activity Source: GOC
    12. positive regulation of granulocyte differentiation Source: BHF-UCL
    13. positive regulation of histone H3-K27 methylation Source: UniProtKB
    14. positive regulation of histone H3-K4 methylation Source: BHF-UCL
    15. positive regulation of proteolysis Source: UniProtKB
    16. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    17. protein O-linked glycosylation Source: UniProtKB
    18. regulation of gluconeogenesis involved in cellular glucose homeostasis Source: UniProtKB
    19. regulation of glycolytic process Source: UniProtKB
    20. regulation of insulin receptor signaling pathway Source: UniProtKB
    21. regulation of Rac protein signal transduction Source: UniProtKB
    22. response to insulin Source: UniProtKB
    23. response to nutrient Source: ProtInc
    24. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Chromatin regulator, Glycosyltransferase, Transferase

    Keywords - Biological processi

    Apoptosis, Biological rhythms

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000147162-MONOMER.
    ReactomeiREACT_172610. 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: Chromosome X

    Organism-specific databases

    HGNCiHGNC:8127. OGT.

    Subcellular locationi

    Isoform 2 : Mitochondrion. Membrane
    Note: Associates with the mitochondrial inner membrane.
    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

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. histone acetyltransferase complex Source: UniProtKB
    4. microtubule organizing center Source: HPA
    5. mitochondrion Source: UniProtKB-SubCell
    6. MLL5-L complex Source: UniProtKB
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProtKB
    9. plasma membrane Source: UniProtKB

    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.
    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.

    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-betaBy similarity
    Glycosylationi3 – 31O-linked (GlcNAc)By similarity
    Modified residuei4 – 41Phosphoserine; by GSK3-betaBy similarity
    Glycosylationi4 – 41O-linked (GlcNAc)By 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

    ArrayExpressiO15294.
    BgeeiO15294.
    CleanExiHS_OGT.
    GenevestigatoriO15294.

    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
    RELAQ042062EBI-539828,EBI-73886
    TET2Q6N0217EBI-539828,EBI-310727
    TET3O431514EBI-539828,EBI-2831148
    Tet3Q8BG872EBI-539828,EBI-9031997From a different organism.

    Protein-protein interaction databases

    BioGridi114049. 59 interactions.
    DIPiDIP-33491N.
    IntActiO15294. 34 interactions.
    MINTiMINT-2998811.
    STRINGi9606.ENSP00000362824.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000003765.
    HOVERGENiHBG000351.
    InParanoidiO15294.
    KOiK09667.
    OMAiLAYMPNT.
    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.
    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. Align

    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

    MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ     50
    EPDNTGVLLL LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK 100
    ERGQLQEAIE HYRHALRLKP DFIDGYINLA AALVAAGDME GAVQAYVSAL 150
    QYNPDLYCVR SDLGNLLKAL GRLEEAKACY LKAIETQPNF AVAWSNLGCV 200
    FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI FDRAVAAYLR 250
    ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA 300
    NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY 350
    RKALEVFPEF AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN 400
    MGNTLKEMQD VQGALQCYTR AIQINPAFAD AHSNLASIHK DSGNIPEAIA 450
    SYRTALKLKP DFPDAYCNLA HCLQIVCDWT DYDERMKKLV SIVADQLEKN 500
    RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK PPYEHPKDLK 550
    LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN 600
    FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL 650
    FALRPAPIQA MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP 700
    HTFFIGDHAN MFPHLKKKAV IDFKSNGHIY DNRIVLNGID LKAFLDSLPD 750
    VKIVKMKCPD GGDNADSSNT ALNMPVIPMN TIAEAVIEMI NRGQIQITIN 800
    GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED AIVYCNFNQL 850
    YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI 900
    IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET 950
    LASRVAASQL TCLGCLELIA KNRQEYEDIA VKLGTDLEYL KKVRGKVWKQ 1000
    RISSPLFNTK QYTMELERLY LQMWEHYAAG NKPDHMIKPV EVTESA 1046
    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:
    EMBL
    GenBank
    DDBJ
    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. [O15294-1]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14414.1. [O15294-1 ]
    CCDS35502.1. [O15294-3 ]
    RefSeqi NP_858058.1. NM_181672.2. [O15294-1 ]
    NP_858059.1. NM_181673.2. [O15294-3 ]
    XP_005262365.1. XM_005262308.1. [O15294-4 ]
    UniGenei Hs.405410.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W3B X-ray 2.85 A/B 26-410 [» ]
    3PE3 X-ray 2.78 A/B/C/D 323-1041 [» ]
    3PE4 X-ray 1.95 A/C 323-1041 [» ]
    3TAX X-ray 1.88 A/C 323-1041 [» ]
    4AY5 X-ray 3.15 A/B/C/D 323-1041 [» ]
    4AY6 X-ray 3.30 A/B/C/D 323-1041 [» ]
    4CDR X-ray 3.15 A/B/C/D 323-1041 [» ]
    4GYW X-ray 1.70 A/C 323-1041 [» ]
    4GYY X-ray 1.85 A/C 323-1041 [» ]
    4GZ3 X-ray 1.90 A/C 323-1041 [» ]
    4GZ5 X-ray 3.08 A/B/C/D 323-1041 [» ]
    4GZ6 X-ray 2.98 A/B/C/D 323-1041 [» ]
    4N39 X-ray 1.76 A 323-1041 [» ]
    4N3A X-ray 1.88 A 323-1041 [» ]
    4N3B X-ray 2.17 A 323-1041 [» ]
    4N3C X-ray 2.55 A 323-1041 [» ]
    ProteinModelPortali O15294.
    SMRi O15294. Positions 23-1038.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114049. 59 interactions.
    DIPi DIP-33491N.
    IntActi O15294. 34 interactions.
    MINTi MINT-2998811.
    STRINGi 9606.ENSP00000362824.

    Chemistry

    BindingDBi O15294.
    ChEMBLi CHEMBL5955.

    Protein family/group databases

    CAZyi GT41. Glycosyltransferase Family 41.

    PTM databases

    PhosphoSitei O15294.

    Proteomic databases

    MaxQBi O15294.
    PaxDbi O15294.
    PRIDEi O15294.

    Protocols and materials databases

    DNASUi 8473.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373701 ; ENSP00000362805 ; ENSG00000147162 . [O15294-3 ]
    ENST00000373719 ; ENSP00000362824 ; ENSG00000147162 . [O15294-1 ]
    GeneIDi 8473.
    KEGGi hsa:8473.
    UCSCi uc004eaa.2. human. [O15294-1 ]
    uc004eab.2. human. [O15294-3 ]

    Organism-specific databases

    CTDi 8473.
    GeneCardsi GC0XP070752.
    HGNCi HGNC:8127. OGT.
    HPAi CAB034099.
    HPA030751.
    HPA030752.
    HPA030753.
    MIMi 300255. gene.
    neXtProti NX_O15294.
    PharmGKBi PA31914.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3914.
    HOGENOMi HOG000003765.
    HOVERGENi HBG000351.
    InParanoidi O15294.
    KOi K09667.
    OMAi LAYMPNT.
    OrthoDBi EOG71K624.
    PhylomeDBi O15294.
    TreeFami TF105785.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BioCyci MetaCyc:ENSG00000147162-MONOMER.
    Reactomei REACT_172610. HATs acetylate histones.
    SABIO-RK O15294.
    SignaLinki O15294.

    Miscellaneous databases

    EvolutionaryTracei O15294.
    GeneWikii OGT_(gene).
    GenomeRNAii 8473.
    NextBioi 31706.
    PROi O15294.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15294.
    Bgeei O15294.
    CleanExi HS_OGT.
    Genevestigatori O15294.

    Family and domain databases

    Gene3Di 1.25.40.10. 5 hits.
    InterProi IPR029489. OGT/SEC/SPY_C.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF13844. Glyco_transf_41. 1 hit.
    PF00515. TPR_1. 9 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 12 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 12 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    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].
    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: October 1, 2014
    This is version 164 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