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Identification
HMDB Protein ID HMDBP01707
Secondary Accession Numbers
  • 7045
Name UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Synonyms
  1. O-GlcNAc transferase subunit p110
  2. O-linked N-acetylglucosamine transferase 110 kDa subunit
  3. OGT
Gene Name OGT
Protein Type Enzyme
Biological Properties
General Function Involved in binding
Specific Function 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, PFKL, 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. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. Isoform 2, the mitochondrial isoform (mOGT), is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.
Pathways
  • Other types of O-glycan biosynthesis
  • protein glycosylation
Reactions
Uridine diphosphate-N-acetylglucosamine + [protein]-L-serine → Uridine 5'-diphosphate + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine details
Uridine diphosphate-N-acetylglucosamine + [protein]-L-threonine → Uridine 5'-diphosphate + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine details
UDP-N-acetyl-D-glucosamine + Protein serine → UDP + details
GO Classification
Biological Process
regulation of glycolysis
apoptotic process
regulation of insulin receptor signaling pathway
positive regulation of histone H3-K4 methylation
regulation of Rac protein signal transduction
protein O-linked glycosylation
response to insulin stimulus
response to nutrient
positive regulation of proteolysis
induction of apoptosis
phosphatidylinositol-mediated signaling
cellular response to retinoic acid
protein homotrimerization
histone H4-K5 acetylation
histone H4-K8 acetylation
histone H4-K16 acetylation
positive regulation of granulocyte differentiation
Cellular Component
cytosol
centrosome
mitochondrion
plasma membrane
histone acetyltransferase complex
MLL5-L complex
Function
binding
Molecular Function
monosaccharide binding
phosphatidylinositol-3,4,5-trisphosphate binding
enzyme activator activity
protein N-acetylglucosaminyltransferase activity
peptide binding
Cellular Location
  1. Cytoplasm
  2. Nucleus (Potential)
Gene Properties
Chromosome Location X
Locus Xq13
SNPs OGT
Gene Sequence
>3141 bp
ATGGCGTCTTCCGTGGGCAACGTGGCCGACAGCACAGAACCAACGAAACGTATGCTTTCC
TTCCAAGGGTTAGCTGAGTTGGCACATCGAGAATATCAGGCAGGAGATTTTGAGGCAGCT
GAGAGACACTGCATGCAGCTCTGGAGACAAGAGCCAGACAATACTGGTGTGCTTTTATTA
CTTTCATCTATACACTTCCAGTGTCGAAGGCTGGACAGATCTGCTCACTTTAGCACTCTG
GCAATTAAACAGAACCCCCTTCTGGCAGAAGCTTATTCGAATTTGGGGAATGTGTACAAG
GAAAGAGGGCAGTTGCAGGAGGCAATTGAGCATTATCGACATGCATTGCGTCTCAAACCT
GATTTCATCGATGGTTATATTAACCTGGCAGCCGCCTTGGTAGCAGCGGGTGACATGGAA
GGGGCAGTACAAGCTTACGTCTCTGCTCTTCAGTACAATCCTGATTTGTACTGTGTTCGC
AGTGACCTGGGGAACCTGCTCAAAGCCCTGGGTCGCTTGGAAGAAGCCAAGGCATGTTAT
TTGAAAGCAATTGAGACGCAACCGAACTTTGCAGTAGCTTGGAGTAATCTTGGCTGTGTT
TTCAATGCACAAGGGGAAATTTGGCTTGCAATTCATCACTTTGAAAAGGCTGTCACCCTT
GACCCAAACTTTCTGGATGCTTATATCAATTTAGGAAATGTCTTGAAAGAGGCACGCATT
TTTGACAGAGCTGTGGCAGCTTATCTTCGTGCCCTAAGTTTGAGTCCAAATCACGCAGTG
GTGCACGGCAACCTGGCTTGTGTATACTATGAGCAAGGCCTGATAGATCTGGCAATAGAC
ACCTACAGGCGGGCTATCGAACTACAACCACATTTCCCTGATGCTTACTGCAACCTAGCC
AATGCTCTCAAAGAGAAGGGCAGTGTTGCTGAAGCAGAAGATTGTTATAATACAGCTCTC
CGTCTGTGTCCCACCCATGCAGACTCTCTGAATAACCTAGCCAATATCAAACGAGAACAG
GGAAACATTGAAGAGGCAGTTCGCTTGTATCGTAAAGCATTAGAAGTCTTCCCAGAGTTT
GCTGCTGCCCATTCAAATTTAGCAAGTGTACTGCAGCAGCAGGGAAAACTGCAGGAAGCT
CTGATGCATTATAAGGAGGCTATTCGAATCAGTCCTACCTTTGCTGATGCCTACTCTAAT
ATGGGAAACACTCTAAAGGAGATGCAGGATGTTCAGGGAGCCTTGCAGTGTTATACGCGT
GCCATCCAAATTAATCCTGCATTTGCAGATGCACATAGCAATCTGGCTTCCATTCATAAG
GATTCAGGGAATATTCCAGAAGCCATAGCTTCTTACCGCACGGCTCTGAAACTTAAGCCT
GATTTTCCTGATGCTTATTGTAACTTGGCTCATTGCCTGCAGATTGTCTGTGATTGGACA
GACTATGATGAGCGAATGAAGAAGTTGGTCAGTATTGTGGCTGACCAGTTAGAGAAGAAT
AGGTTGCCTTCTGTGCATCCTCATCATAGTATGCTATATCCTCTTTCTCATGGCTTCAGG
AAGGCTATTGCTGAGAGGCACGGCAACCTGTGCTTAGATAAGATTAATGTTCTTCATAAA
CCACCATATGAACATCCAAAAGACTTGAAGCTCAGTGATGGTCGGCTGCGTGTAGGATAT
GTGAGTTCCGACTTTGGGAATCATCCTACTTCTCACCTTATGCAGTCTATTCCAGGCATG
CACAATCCTGATAAATTTGAGGTGTTCTGTTATGCCCTGAGCCCAGACGATGGCACAAAC
TTCCGAGTGAAGGTGATGGCAGAAGCCAATCATTTCATTGATCTTTCTCAGATTCCATGC
AATGGAAAAGCAGCTGATCGCATCCATCAGGATGGAATTCATATCCTTGTAAATATGAAT
GGCTATACTAAGGGCGCTCGAAATGAGCTTTTTGCTCTCAGGCCAGCTCCTATTCAGGCA
ATGTGGCTGGGATACCCTGGGACGAGTGGTGCGCTTTTCATGGATTATATTATCACTGAT
CAGGAAACTTCGCCAGCTGAAGTTGCTGAGCAGTATTCCGAGAAATTGGCTTATATGCCC
CACACTTTTTTTATTGGTGATCATGCTAATATGTTCCCTCACCTGAAGAAAAAAGCAGTC
ATCGATTTTAAGTCCAATGGGCACATTTATGACAATCGGATAGTTCTGAATGGCATCGAC
CTCAAAGCATTTCTTGATAGTCTACCAGATGTGAAAATTGTCAAGATGAAGTGTCCTGAT
GGAGGAGACAATGCAGATAGCAGTAACACAGCTCTTAATATGCCTGTTATTCCTATGAAT
ACTATTGCAGAAGCAGTTATTGAAATGATTAACCGAGGACAGATTCAAATAACAATTAAT
GGATTCAGTATTAGCAATGGACTGGCAACTACTCAGATCAACAATAAGGCTGCAACTGGA
GAGGAGGTTCCCCGTACCATTATTGTAACCACCCGTTCTCAGTACGGGTTACCAGAAGAT
GCCATCGTATACTGTAACTTTAATCAGTTGTATAAAATTGACCCTTCTACTTTGCAGATG
TGGGCAAACATTCTGAAGCGTGTTCCCAATAGTGTACTCTGGCTGTTGCGTTTTCCAGCA
GTAGGAGAACCTAATATTCAACAGTATGCACAAAACATGGGCCTGCCCCAGAACCGTATC
ATTTTTTCACCTGTTGCTCCTAAAGAGGAACACGTCAGGAGAGGCCAGCTGGCTGATGTC
TGCTTGGACACTCCACTCTGTAATGGGCACACCACAGGGATGGATGTCCTCTGGGCAGGG
ACCCCCATGGTGACTATGCCAGGAGAGACTCTTGCTTCTCGAGTTGCAGCATCCCAGCTC
ACTTGCTTAGGTTGTCTTGAGCTTATTGCTAAAAACAGACAAGAATATGAAGACATAGCT
GTGAAGCTGGGAACTGATCTAGAATACCTGAAGAAAGTTCGTGGCAAAGTCTGGAAGCAA
AGAATATCTAGCCCTCTGTTCAACACCAAACAATACACAATGGAACTAGAGCGGCTCTAT
CTACAGATGTGGGAGCATTATGCAGCTGGCAACAAACCTGACCACATGATTAAGCCTGTT
GAAGTCACTGAGTCAGCATAA
Protein Properties
Number of Residues 1046
Molecular Weight 116923.515
Theoretical pI 6.693
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLL
LSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKP
DFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACY
LKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARI
FDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLA
NALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEF
AAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTR
AIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWT
DYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHK
PPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTN
FRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQA
MWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAV
IDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMN
TIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPED
AIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRI
IFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQL
TCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLY
LQMWEHYAAGNKPDHMIKPVEVTESA
GenBank ID Protein 18250915
UniProtKB/Swiss-Prot ID O15294
UniProtKB/Swiss-Prot Entry Name OGT1_HUMAN
PDB IDs
GenBank Gene ID AJ315767
GeneCard ID OGT
GenAtlas ID OGT
HGNC ID HGNC:8127
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  5. Fujiki R, Chikanishi T, Hashiba W, Ito H, Takada I, Roeder RG, Kitagawa H, Kato S: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature. 2009 May 21;459(7245):455-9. doi: 10.1038/nature07954. Epub 2009 Apr 19. [PubMed:19377461 ]
  6. Lubas WA, Frank DW, Krause M, Hanover JA: O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J Biol Chem. 1997 Apr 4;272(14):9316-24. [PubMed:9083068 ]
  7. Nolte D, Muller U: Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1. Mamm Genome. 2002 Jan;13(1):62-4. [PubMed:11773972 ]
  8. Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W: Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 2003 Apr 1;17(7):896-911. [PubMed:12670868 ]