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Index > Protein center > OGT(Gene name) > Human
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  • OGT (Gene name),
  • UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (Protein name ),  OGT1_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • 3D
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  • Predicted Eptitope
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  • Vaild Sequence
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  • Gene name:
    OGT;
    Protein name:
    UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit;
    Alternative:
    O-linked N-acetylglucosamine transferase 110 kDa subunit(OGT);O-GlcNAc transferase subunit p110;
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Heterotrimer of two 110 kDa and one 70 kDa subunits. It is not known if the 70 kDa subunit is encoded by a separate gene or is the product of either of a proteolytic degradation or an alternative initiation of the 110 kDa subunit (By similarity). Interacts with ATXN10 (By similarity). Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts directly with HCFC1.
    Function:
    Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Mediates the O-glycosylation of MLL5 and HCFC1. Promotes proteolytic maturation of HCFC1.
    Subcellular Location:
    Cytoplasm Nucleus Mostly in the nucleus.
    Protein Attributes:
    Sequence length:
    1046
    Sequence:
    50:
    MASSVGNVAD | STEPTKRMLS | FQGLAELAHR | EYQAGDFEAA | ERHCMQLWRQ | 
    100:
    EPDNTGVLLL | LSSIHFQCRR | LDRSAHFSTL | AIKQNPLLAE | AYSNLGNVYK | 
    150:
    ERGQLQEAIE | HYRHALRLKP | DFIDGYINLA | AALVAAGDME | GAVQAYVSAL | 
    200:
    QYNPDLYCVR | SDLGNLLKAL | GRLEEAKACY | LKAIETQPNF | AVAWSNLGCV | 
    250:
    FNAQGEIWLA | IHHFEKAVTL | DPNFLDAYIN | LGNVLKEARI | FDRAVAAYLR | 
    300:
    ALSLSPNHAV | VHGNLACVYY | EQGLIDLAID | TYRRAIELQP | HFPDAYCNLA | 
    350:
    NALKEKGSVA | EAEDCYNTAL | RLCPTHADSL | NNLANIKREQ | GNIEEAVRLY | 
    400:
    RKALEVFPEF | AAAHSNLASV | LQQQGKLQEA | LMHYKEAIRI | SPTFADAYSN | 
    450:
    MGNTLKEMQD | VQGALQCYTR | AIQINPAFAD | AHSNLASIHK | DSGNIPEAIA | 
    500:
    SYRTALKLKP | DFPDAYCNLA | HCLQIVCDWT | DYDERMKKLV | SIVADQLEKN | 
    550:
    RLPSVHPHHS | MLYPLSHGFR | KAIAERHGNL | CLDKINVLHK | PPYEHPKDLK | 
    600:
    LSDGRLRVGY | VSSDFGNHPT | SHLMQSIPGM | HNPDKFEVFC | YALSPDDGTN | 
    650:
    FRVKVMAEAN | HFIDLSQIPC | NGKAADRIHQ | DGIHILVNMN | GYTKGARNEL | 
    700:
    FALRPAPIQA | MWLGYPGTSG | ALFMDYIITD | QETSPAEVAE | QYSEKLAYMP | 
    750:
    HTFFIGDHAN | MFPHLKKKAV | IDFKSNGHIY | DNRIVLNGID | LKAFLDSLPD | 
    800:
    VKIVKMKCPD | GGDNADSSNT | ALNMPVIPMN | TIAEAVIEMI | NRGQIQITIN | 
    850:
    GFSISNGLAT | TQINNKAATG | EEVPRTIIVT | TRSQYGLPED | AIVYCNFNQL | 
    900:
    YKIDPSTLQM | WANILKRVPN | SVLWLLRFPA | VGEPNIQQYA | QNMGLPQNRI | 
    950:
    IFSPVAPKEE | HVRRGQLADV | CLDTPLCNGH | TTGMDVLWAG | TPMVTMPGET | 
    1000:
    LASRVAASQL | TCLGCLELIA | KNRQEYEDIA | VKLGTDLEYL | KKVRGKVWKQ | 
    1046:
    RISSPLFNTK | QYTMELERLY | LQMWEHYAAG | NKPDHMIKPV | EVTESA
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    UniGene:
    String:
    Pfam:
    KEGG:
    MIM:
    SMR:
    Uniprot:
     
    FOR
    ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    ELISA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    CLIA Kit for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Polyclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Monoclonal Antibody for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
    Protein for Human UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

    R&D Technical Data
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    Precision
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    Recovery
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    Linearity
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    References
    1. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2);PROTEIN SEQUENCE OF 227-236 AND 955-971;TISSUE SPECIFICITY
      tissue: Liver.
    2. 2.
      "Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1."
      Nolte D. , Muller U.
      Mamm. Genome13:62-64(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3)
    3. 3.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4)
      tissue: Endometrium.
      tissue: Fetal brain.
      tissue: Spinal cord.
    4. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3)
      tissue: Colon.
      tissue: Pancreas.
    5. 5.
      Bienvenut W.V. , Dhillon A.S. , Kolch W.
      Submitted (2008-02) to the UniProtKB
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) 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. 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.
      Cell110:69-80(2002) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH SIN3A;FUNCTION
    7. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH HCFC1
    8. 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.
      Nature451:964-969(2008) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) 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. 9.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Cervix carcinoma.
    10. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    11. 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.
      Brain132:1820-1832(2009) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;ASSOCIATION WITH ALZHEIMER DISEASE
    12. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INDUCTION
    13. 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.
      Nature459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;CATALYTIC ACTIVITY;IDENTIFICATION IN THE MLL5-L COMPLEX
    14. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN HISTONE H4 ACETYLATION;IDENTIFICATION IN NSL COMPLEX;SUBCELLULAR LOCATION
    15. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;POSSIBLE ASSOCIATION WITH DIABETES
    16. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY IN A THAP1/THAP3-HCFC1-OGT COMPLEX;INTERACTION WITH HCFC1; THAP1 AND THAP3;FUNCTION
    17. 17.
      "Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis."
      Shin S.H. , Love D.C. , Hanover J.A.
      Amino Acids40:885-893(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION (ISOFORM 2)
    18. 18.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    19. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;CATALYTIC ACTIVITY;SUBCELLULAR LOCATION;UBIQUITINATION;INTERACTION WITH HCFC1
    20. 20.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH H2B
    21. 21.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    22. 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.
      Science337:975-980(2012) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION
    23. 23.
      "TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS."
      Deplus R. , Delatte B. , Schwinn M.K. , Defrance M. , Mendez J. , Murphy N. , Dawson M.A. , Volkmar M. , Putmans P. , Calonne E. , Shih A.H. , Levine R.L. , Bernard O. , Mercher T. , Solary E. , Urh M. , Daniels D.L. , Fuks F.
      EMBO J.32:645-655(2013) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH HCFC1; TET2 AND TET3
    24. 24.
      "TET2 promotes histone O-GlcNAcylation during gene transcription."
      Chen Q. , Chen Y. , Bian C. , Fujiki R. , Yu X.
      Nature493:561-564(2013) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH TET2 AND TET3
    25. 25.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION
    26. 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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 26-400;FUNCTION;CATALYTIC ACTIVITY;DOMAIN;MUTAGENESIS OF TRP-208 AND ILE-211
    27. 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.
      Nature469:564-567(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) 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
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