Protein O-GlcNAc transferase

OGT
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1W3B, 3PE3, 3PE4, 3TAX, 4AY5, 4AY6, 4CDR, 4GYW, 4GYY, 4GZ3, 4GZ5, 4GZ6, 4N39, 4N3A, 4N3B, 4XI9, 4XIF, 5BNW, 5C1D
Identifiers
Aliases	OGT, HRNT1, O-GLCNAC, HINCUT-1, O-linked N-acetylglucosamine (GlcNAc) transferase, OGT1, MRX106, XLID106
External IDs	OMIM: 300255; MGI: 1339639; HomoloGene: 9675; GeneCards: OGT; OMA:OGT - orthologs
Gene location (Human)
Chr.	X chromosome (human)
End	71,575,892 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	100,727,957 bp
RNA expression pattern
	Top expressed in
	middle temporal gyrus; ; Brodmann area 23; ; skin of hip; ; right uterine tube; ; tibia; ; visceral pleura; ; epithelium of nasopharynx; ; skin of thigh; ; parietal pleura; ; trabecular bone;
	Top expressed in
	medullary collecting duct; ; genital tubercle; ; utricle; ; granulocyte; ; olfactory bulb; ; iris; ; cerebellar cortex; ; dorsal striatum; ; vas deferens; ; lobe of cerebellum;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	lipid binding; transferase activity; acetylglucosaminyltransferase activity; glycosyltransferase activity; histone acetyltransferase activity (H4-K8 specific); histone acetyltransferase activity (H4-K5 specific); protein O-GlcNAc transferase activity; protein binding; histone acetyltransferase activity (H4-K16 specific); phosphatidylinositol-3,4,5-trisphosphate binding; protein N-acetylglucosaminyltransferase activity;
Cellular component	cytoplasm; membrane; plasma membrane; mitochondrion; histone acetyltransferase complex; nucleus; cytosol; nucleoplasm; protein-containing complex; mitochondrial membranes; cell projection; protein N-acetylglucosaminyltransferase complex;
Biological process	response to nutrient; rhythmic process; histone H3-K4 trimethylation; protein O-linked glycosylation; regulation of Rac protein signal transduction; circadian regulation of gene expression; regulation of glycolytic process; histone H4-K5 acetylation; response to insulin; protein glycosylation; positive regulation of proteolysis; positive regulation of histone H3-K27 methylation; histone H4-K16 acetylation; histone H4-K8 acetylation; phosphatidylinositol-mediated signaling; signal transduction; positive regulation of transcription by RNA polymerase II; regulation of insulin receptor signaling pathway; apoptotic process; protein deubiquitination; protein processing; regulation of transcription by RNA polymerase II; negative regulation of protein ubiquitination; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; chromatin organization; regulation of gluconeogenesis; viral process; positive regulation of cold-induced thermogenesis;
	Sources:Amigo / QuickGO
Orthologs
	8473
	108155
	ENSG00000147162
	ENSMUSG00000034160
	O15294
	Q8CGY8
	NM_003605; NM_181672; NM_181673; NM_025192
	NM_001290535; NM_139144
	NP_858058; NP_858059
	NP_001277464; NP_631883
	Wikidata
View/Edit Human	View/Edit Mouse

Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme (EC 2.4.1.255) that in humans is encoded by the OGT gene.^[5]^[6] OGT catalyzes the addition of the O-GlcNAc post-translational modification to proteins.^[7]^[8]^[9]^[10]^[5]^[11]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000147162 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000034160 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b Lubas WA, Frank DW, Krause M, Hanover JA (April 1997). "O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats". The Journal of Biological Chemistry. 272 (14): 9316–24. doi:10.1074/jbc.272.14.9316. PMID 9083068.
^ "Entrez Gene: OGT O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)".
^ Banerjee S, Robbins PW, Samuelson J (April 2009). "Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum". Glycobiology. 19 (4): 331–6. doi:10.1093/glycob/cwn107. PMC 2733775. PMID 18948359.
^ Clarke AJ, Hurtado-Guerrero R, Pathak S, Schüttelkopf AW, Borodkin V, Shepherd SM, et al. (October 2008). "Structural insights into mechanism and specificity of O-GlcNAc transferase". The EMBO Journal. 27 (20): 2780–8. doi:10.1038/emboj.2008.186. PMC 2556091. PMID 18818698.
^ Rao FV, Dorfmueller HC, Villa F, Allwood M, Eggleston IM, van Aalten DM (April 2006). "Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis". The EMBO Journal. 25 (7): 1569–78. doi:10.1038/sj.emboj.7601026. PMC 1440316. PMID 16541109.
^ Haltiwanger RS, Blomberg MA, Hart GW (May 1992). "Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase". The Journal of Biological Chemistry. 267 (13): 9005–13. doi:10.1016/S0021-9258(19)50380-5. PMID 1533623.
^ Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S (January 2011). "Structure of human O-GlcNAc transferase and its complex with a peptide substrate". Nature. 469 (7331): 564–7. Bibcode:2011Natur.469..564L. doi:10.1038/nature09638. PMC 3064491. PMID 21240259.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000147162 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000034160 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9083068-5] Lubas WA, Frank DW, Krause M, Hanover JA (April 1997). "O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats". The Journal of Biological Chemistry. 272 (14): 9316–24. doi:10.1074/jbc.272.14.9316. PMID 9083068.

[entrez-6] "Entrez Gene: OGT O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase)".

[7] Banerjee S, Robbins PW, Samuelson J (April 2009). "Molecular characterization of nucleocytosolic O-GlcNAc transferases of Giardia lamblia and Cryptosporidium parvum". Glycobiology. 19 (4): 331–6. doi:10.1093/glycob/cwn107. PMC 2733775. PMID 18948359.

[8] Clarke AJ, Hurtado-Guerrero R, Pathak S, Schüttelkopf AW, Borodkin V, Shepherd SM, et al. (October 2008). "Structural insights into mechanism and specificity of O-GlcNAc transferase". The EMBO Journal. 27 (20): 2780–8. doi:10.1038/emboj.2008.186. PMC 2556091. PMID 18818698.

[9] Rao FV, Dorfmueller HC, Villa F, Allwood M, Eggleston IM, van Aalten DM (April 2006). "Structural insights into the mechanism and inhibition of eukaryotic O-GlcNAc hydrolysis". The EMBO Journal. 25 (7): 1569–78. doi:10.1038/sj.emboj.7601026. PMC 1440316. PMID 16541109.

[pmid1533623-10] Haltiwanger RS, Blomberg MA, Hart GW (May 1992). "Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase". The Journal of Biological Chemistry. 267 (13): 9005–13. doi:10.1016/S0021-9258(19)50380-5. PMID 1533623.

[Lazarus-11] Lazarus MB, Nam Y, Jiang J, Sliz P, Walker S (January 2011). "Structure of human O-GlcNAc transferase and its complex with a peptide substrate". Nature. 469 (7331): 564–7. Bibcode:2011Natur.469..564L. doi:10.1038/nature09638. PMC 3064491. PMID 21240259.

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