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O15294 (OGT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:OGT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1046 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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, 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. 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). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues. O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex. 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. Ref.6 Ref.8 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Isoform 2:the mitochondrial isoform (mOGT)is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line (Ref.17). Ref.6 Ref.8 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Catalytic activity

UDP-N-acetyl-D-glucosamine + [protein]-L-serine = UDP + [protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine. Ref.13 Ref.19 Ref.26 Ref.27

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

Enzyme regulation

Subject to product inhibition by UDP. Ref.27

Pathway

Protein modification; protein glycosylation.

Subunit structure

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. Ref.6 Ref.7 Ref.13 Ref.14 Ref.16 Ref.19 Ref.20 Ref.23 Ref.24

Subcellular location

Isoform 2: Mitochondrion. Membrane. Note: Associates with the mitochondrial inner membrane. Ref.8 Ref.14 Ref.19

Isoform 3: Cytoplasm. Nucleus Ref.8 Ref.14 Ref.19. 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. Ref.8 Ref.14 Ref.19

Isoform 4: Cytoplasm. Nucleus Ref.8 Ref.14 Ref.19.

Tissue specificity

Highly expressed in pancreas and to a lesser extent in skeletal muscle, heart, brain and placenta. Present in trace amounts in lung and liver. Ref.1

Induction

Induction of the nucleocytoplasmic OGT (ncOGT) isoform inthe liver on glucose deprivation is mediated by the decreased hexosamine biosynthesis pathway (HBP) flux. Ref.12 Ref.27

Domain

The TPR repeat domain is required for substrate binding and oligomerization. Ref.26

Post-translational modification

Ubiquitinated, leading to its proteasomal degradation. Ref.19

Phosphorylation on Ser-3 or Ser-4 by GSK3-beta positively regulates its activity By similarity.

Involvement in disease

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. Ref.11

Sequence similarities

Belongs to the O-GlcNAc transferase family.

Contains 13 TPR repeats.

Biophysicochemical properties

Kinetic parameters:

KM=1.8 µM for UDP-N-acetyl-D-glucosamine Ref.27

Ontologies

Keywords
   Biological processApoptosis
Biological rhythms
   Cellular componentCell membrane
Cytoplasm
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
TPR repeat
   LigandLipid-binding
   Molecular functionChromatin regulator
Glycosyltransferase
Transferase
   PTMAcetylation
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from direct assay Ref.17. Source: UniProtKB

cellular response to retinoic acid

Inferred from mutant phenotype Ref.13. Source: BHF-UCL

chromatin organization

Traceable author statement. Source: Reactome

histone H3-K4 trimethylation

Inferred from mutant phenotype Ref.23. Source: UniProtKB

histone H4-K16 acetylation

Inferred from direct assay Ref.14. Source: UniProtKB

histone H4-K5 acetylation

Inferred from direct assay Ref.14. Source: UniProtKB

histone H4-K8 acetylation

Inferred from direct assay Ref.14. Source: UniProtKB

phosphatidylinositol-mediated signaling

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of catalytic activity

Inferred from direct assay Ref.13. Source: GOC

positive regulation of granulocyte differentiation

Inferred from mutant phenotype Ref.13. Source: BHF-UCL

positive regulation of histone H3-K4 methylation

Inferred from direct assay Ref.13. Source: BHF-UCL

positive regulation of proteolysis

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.24Ref.23. Source: UniProtKB

protein O-linked glycosylation

Inferred from direct assay Ref.27Ref.19Ref.22Ref.24PubMed 23352454Ref.25. Source: UniProtKB

regulation of Rac protein signal transduction

Inferred from direct assay Ref.8. Source: UniProtKB

regulation of glycolysis

Inferred from direct assay Ref.22. Source: UniProtKB

regulation of insulin receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

response to insulin

Inferred from direct assay Ref.8. Source: UniProtKB

response to nutrient

Traceable author statement Ref.1. Source: ProtInc

signal transduction

Traceable author statement PubMed 9083067. Source: ProtInc

   Cellular_componentMLL5-L complex

Inferred from direct assay Ref.13. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.19. Source: UniProtKB

histone acetyltransferase complex

Inferred from direct assay Ref.14. Source: UniProtKB

microtubule organizing center

Inferred from direct assay. Source: HPA

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.19. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionacetylglucosaminyltransferase activity

Traceable author statement Ref.1. Source: ProtInc

enzyme activator activity

Inferred from direct assay Ref.13. Source: BHF-UCL

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay Ref.8. Source: UniProtKB

protein N-acetylglucosaminyltransferase activity

Inferred from direct assay Ref.13Ref.27Ref.19Ref.22Ref.24PubMed 23352454Ref.23Ref.25. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HCFC1P516109EBI-539828,EBI-396176
Hoxa1P090223EBI-539828,EBI-3957603From a different organism.
NFATC1O956442EBI-539828,EBI-6907210
RELAQ042062EBI-539828,EBI-73886

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: O15294-1)

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.
Isoform 2 (identifier: O15294-2)

Also known as: Mitochondrial isoform; mOGT;

The sequence of this isoform differs from the canonical sequence as follows:
     1-176: MASSVGNVAD...LKALGRLEEA → MLQGHFWLVR...PSHLLSLTPP
Isoform 1 (identifier: O15294-3)

The sequence of this isoform differs from the canonical sequence as follows:
     13-22: Missing.
Isoform 4 (identifier: O15294-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 10461045UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
PRO_0000191772

Regions

Repeat21 – 5434TPR 1
Repeat89 – 12234TPR 2
Repeat123 – 15634TPR 3
Repeat157 – 19034TPR 4
Repeat191 – 22434TPR 5
Repeat225 – 25834TPR 6
Repeat259 – 29234TPR 7
Repeat293 – 32634TPR 8
Repeat327 – 36034TPR 9
Repeat361 – 39434TPR 10
Repeat395 – 42834TPR 11
Repeat429 – 46234TPR 12
Repeat463 – 47311TPR 13; truncated
Nucleotide binding905 – 9084UDP
Nucleotide binding911 – 9144UDP
Nucleotide binding929 – 9313UDP
Region991 – 101020Required for phosphatidylinositol 3,4,5-triphosphate binding
Motif487 – 50317Nuclear localization signal Potential

Sites

Active site5081Proton acceptor Probable
Binding site8491UDP
Binding site8521UDP
Binding site9351UDP

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.10 Ref.21
Modified residue31Phosphoserine; by GSK3-beta By similarity
Modified residue41Phosphoserine; by GSK3-beta By similarity
Glycosylation31O-linked (GlcNAc) By similarity
Glycosylation41O-linked (GlcNAc) By similarity

Natural variations

Alternative sequence1 – 381381Missing in isoform 4.
VSP_040764
Alternative sequence1 – 176176MASSV…RLEEA → MLQGHFWLVREGIMISPSSP PPPNLFFFPLQIFPFPFTSF PSHLLSLTPP in isoform 2.
VSP_006553
Alternative sequence13 – 2210Missing in isoform 1.
VSP_014164
Natural variant5381L → P Found in a renal cell carcinoma sample; somatic mutation.
VAR_064736

Experimental info

Mutagenesis2081W → E: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with D-211. Ref.26
Mutagenesis2111I → D: Abolishes homodimerization of the TPR domain. Slightly reduced enzyme activity; when associated with E-208. Ref.26
Mutagenesis5081H → A: Loss of enzyme activity. Ref.27
Mutagenesis5681H → A: Reduces enzyme activity by about 95%. Ref.27
Mutagenesis9111H → A: Reduces enzyme activity by over 90%. Ref.27
Mutagenesis991 – 9922KK → AA: Abolishes phosphatidylinisitol binding, no translocation to the cell membrane, and no effect on phosphorylation of AKT1 nor IRS1.
Mutagenesis9941R → A: No effect on phosphatidylinisitol binding. Ref.8
Mutagenesis9961K → A: Reduced phosphatidylinisitol binding. Ref.8
Mutagenesis9991K → A: Reduced phosphatidylinisitol binding. Ref.8
Mutagenesis10011R → A: No effect on phosphatidylinisitol binding. Ref.8
Mutagenesis10101K → A: No effect on phosphatidylinisitol binding. Ref.8
Sequence conflict3081S → Q in CAB62528. Ref.3
Sequence conflict6631L → P in CAD97853. Ref.3

Secondary structure

......................................................................................................................................................................... 1046
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (Nucleocytoplasmic isoform) (ncOGT) [UniParc].

Last modified June 21, 2005. Version 3.
Checksum: 852ED68BDDE63363

FASTA1,046116,925
        10         20         30         40         50         60 
MASSVGNVAD STEPTKRMLS FQGLAELAHR EYQAGDFEAA ERHCMQLWRQ EPDNTGVLLL 

        70         80         90        100        110        120 
LSSIHFQCRR LDRSAHFSTL AIKQNPLLAE AYSNLGNVYK ERGQLQEAIE HYRHALRLKP 

       130        140        150        160        170        180 
DFIDGYINLA AALVAAGDME GAVQAYVSAL QYNPDLYCVR SDLGNLLKAL GRLEEAKACY 

       190        200        210        220        230        240 
LKAIETQPNF AVAWSNLGCV FNAQGEIWLA IHHFEKAVTL DPNFLDAYIN LGNVLKEARI 

       250        260        270        280        290        300 
FDRAVAAYLR ALSLSPNHAV VHGNLACVYY EQGLIDLAID TYRRAIELQP HFPDAYCNLA 

       310        320        330        340        350        360 
NALKEKGSVA EAEDCYNTAL RLCPTHADSL NNLANIKREQ GNIEEAVRLY RKALEVFPEF 

       370        380        390        400        410        420 
AAAHSNLASV LQQQGKLQEA LMHYKEAIRI SPTFADAYSN MGNTLKEMQD VQGALQCYTR 

       430        440        450        460        470        480 
AIQINPAFAD AHSNLASIHK DSGNIPEAIA SYRTALKLKP DFPDAYCNLA HCLQIVCDWT 

       490        500        510        520        530        540 
DYDERMKKLV SIVADQLEKN RLPSVHPHHS MLYPLSHGFR KAIAERHGNL CLDKINVLHK 

       550        560        570        580        590        600 
PPYEHPKDLK LSDGRLRVGY VSSDFGNHPT SHLMQSIPGM HNPDKFEVFC YALSPDDGTN 

       610        620        630        640        650        660 
FRVKVMAEAN HFIDLSQIPC NGKAADRIHQ DGIHILVNMN GYTKGARNEL FALRPAPIQA 

       670        680        690        700        710        720 
MWLGYPGTSG ALFMDYIITD QETSPAEVAE QYSEKLAYMP HTFFIGDHAN MFPHLKKKAV 

       730        740        750        760        770        780 
IDFKSNGHIY DNRIVLNGID LKAFLDSLPD VKIVKMKCPD GGDNADSSNT ALNMPVIPMN 

       790        800        810        820        830        840 
TIAEAVIEMI NRGQIQITIN GFSISNGLAT TQINNKAATG EEVPRTIIVT TRSQYGLPED 

       850        860        870        880        890        900 
AIVYCNFNQL YKIDPSTLQM WANILKRVPN SVLWLLRFPA VGEPNIQQYA QNMGLPQNRI 

       910        920        930        940        950        960 
IFSPVAPKEE HVRRGQLADV CLDTPLCNGH TTGMDVLWAG TPMVTMPGET LASRVAASQL 

       970        980        990       1000       1010       1020 
TCLGCLELIA KNRQEYEDIA VKLGTDLEYL KKVRGKVWKQ RISSPLFNTK QYTMELERLY 

      1030       1040 
LQMWEHYAAG NKPDHMIKPV EVTESA 

« Hide

Isoform 2 (Mitochondrial isoform) (mOGT) [UniParc].

Checksum: 766BF416ABD547C4
Show »

FASTA920103,012
Isoform 1 [UniParc].

Checksum: C3BD67340925A2C2
Show »

FASTA1,036115,706
Isoform 4 (Short isoform) (sOGT) [UniParc].

Checksum: 181B846A6B09E63A
Show »

FASTA66574,536

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"GlcNAcylation of histone H2B facilitates its monoubiquitination."
Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S., Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F., Kitagawa H., Roeder R.G., Brown M., Kato S.
Nature 480:557-560(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH H2B.
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"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]
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]"O-GlcNAcylation regulates EZH2 protein stability and function."
Chu C.S., Lo P.W., Yeh Y.H., Hsu P.H., Peng S.H., Teng Y.C., Kang M.L., Wong C.H., Juan L.J.
Proc. Natl. Acad. Sci. U.S.A. 111:1355-1360(2014) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_858058.1. NM_181672.2.
NP_858059.1. NM_181673.2.
XP_005262365.1. XM_005262308.1.
UniGeneHs.405410.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO15294.
SMRO15294. Positions 23-1038.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114049. 57 interactions.
DIPDIP-33491N.
IntActO15294. 23 interactions.
MINTMINT-2998811.
STRING9606.ENSP00000362824.

Chemistry

BindingDBO15294.
ChEMBLCHEMBL5955.

Protein family/group databases

CAZyGT41. Glycosyltransferase Family 41.

PTM databases

PhosphoSiteO15294.

Proteomic databases

PaxDbO15294.
PRIDEO15294.

Protocols and materials databases

DNASU8473.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373701; ENSP00000362805; ENSG00000147162. [O15294-3]
ENST00000373719; ENSP00000362824; ENSG00000147162. [O15294-1]
GeneID8473.
KEGGhsa:8473.
UCSCuc004eaa.2. human. [O15294-1]
uc004eab.2. human. [O15294-3]

Organism-specific databases

CTD8473.
GeneCardsGC0XP070752.
HGNCHGNC:8127. OGT.
HPACAB034099.
HPA030751.
HPA030752.
HPA030753.
MIM300255. gene.
neXtProtNX_O15294.
PharmGKBPA31914.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3914.
HOGENOMHOG000003765.
HOVERGENHBG000351.
InParanoidO15294.
KOK09667.
OMALAYMPNT.
OrthoDBEOG71K624.
PhylomeDBO15294.
TreeFamTF105785.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000147162-MONOMER.
ReactomeREACT_172623. Chromatin organization.
SABIO-RKO15294.
SignaLinkO15294.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressO15294.
BgeeO15294.
CleanExHS_OGT.
GenevestigatorO15294.

Family and domain databases

Gene3D1.25.40.10. 5 hits.
InterProIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamPF00515. TPR_1. 9 hits.
[Graphical view]
SMARTSM00028. TPR. 12 hits.
[Graphical view]
PROSITEPS50005. TPR. 12 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO15294.
GeneWikiOGT_(gene).
GenomeRNAi8473.
NextBio31706.
PROO15294.
SOURCESearch...

Entry information

Entry nameOGT1_HUMAN
AccessionPrimary (citable) accession number: O15294
Secondary accession number(s): Q7Z3K0 expand/collapse secondary AC list , Q8WWM8, Q96CC1, Q9UG57
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 21, 2005
Last modified: April 16, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM