HUMAN:OGT1

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	OGT
Protein Name(s)	UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit O-GlcNAc transferase subunit p110 O-linked N-acetylglucosamine transferase 110 kDa subunit OGT
External Links
UniProt	O15294
EMBL	U77413 AJ315767 AJ315767 AJ315767 AL050366 AL833085 BX537844 BC014434 BC038180
CCDS	CCDS14414.1 CCDS35502.1
RefSeq	NP_858058.1 NP_858059.1 XP_005262365.1
UniGene	Hs.405410
PDB	1W3B 3PE3 3PE4 3TAX 4AY5 4AY6 4CDR 4GYW 4GYY 4GZ3 4GZ5 4GZ6 4N39 4N3A 4N3B 4N3C
PDBsum	1W3B 3PE3 3PE4 3TAX 4AY5 4AY6 4CDR 4GYW 4GYY 4GZ3 4GZ5 4GZ6 4N39 4N3A 4N3B 4N3C
ProteinModelPortal	O15294
SMR	O15294
BioGrid	114049
DIP	DIP-33491N
IntAct	O15294
MINT	MINT-2998811
STRING	9606.ENSP00000362824
BindingDB	O15294
ChEMBL	CHEMBL5955
CAZy	GT41
PhosphoSite	O15294
MaxQB	O15294
PaxDb	O15294
PRIDE	O15294
DNASU	8473
Ensembl	ENST00000373701 ENST00000373719
GeneID	8473
KEGG	hsa:8473
UCSC	uc004eaa.2 uc004eab.2
CTD	8473
GeneCards	GC0XP070752
HGNC	HGNC:8127
HPA	CAB034099 HPA030751 HPA030752 HPA030753
MIM	300255
neXtProt	NX_O15294
PharmGKB	PA31914
eggNOG	COG3914
GeneTree	ENSGT00550000074327
HOGENOM	HOG000003765
HOVERGEN	HBG000351
InParanoid	O15294
KO	K09667
OMA	KLAYMPN
OrthoDB	EOG71K624
PhylomeDB	O15294
TreeFam	TF105785
BioCyc	MetaCyc:ENSG00000147162-MONOMER
Reactome	REACT_172610
SABIO-RK	O15294
SignaLink	O15294
UniPathway	UPA00378
EvolutionaryTrace	O15294
GeneWiki	OGT_(gene)
GenomeRNAi	8473
NextBio	31706
PRO	PR:O15294
Proteomes	UP000005640
Bgee	O15294
CleanEx	HS_OGT
ExpressionAtlas	O15294
Genevestigator	O15294
GO	GO:0005737 GO:0005829 GO:0000123 GO:0005815 GO:0005739 GO:0070688 GO:0005654 GO:0005634 GO:0005886 GO:0008375 GO:0008047 GO:0005547 GO:0016262 GO:0097363 GO:0006915 GO:0071300 GO:0006325 GO:0032922 GO:0080182 GO:0043984 GO:0043981 GO:0043982 GO:0031397 GO:0048015 GO:0043085 GO:0030854 GO:0061087 GO:0051571 GO:0045862 GO:0045944 GO:0006493 GO:0090526 GO:0006110 GO:0046626 GO:0035020 GO:0032868 GO:0007584 GO:0007165
Gene3D	1.25.40.10
InterPro	IPR029489 IPR013026 IPR011990 IPR001440 IPR019734
Pfam	PF13844 PF00515
SMART	SM00028
PROSITE	PS50005 PS50293

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0017122	protein N-acetylglucosaminyltransferase complex	PMID:21240259^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0120162	positive regulation of cold-induced thermogenesis	PMID:28637651^[2]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CGY8	P		Seeded From UniProt	complete
involved_in	GO:0032435	negative regulation of proteasomal ubiquitin-dependent protein catabolic process	PMID:26678539^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006357	regulation of transcription by RNA polymerase II	PMID:26678539^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031397	negative regulation of protein ubiquitination	PMID:26678539^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q8IZD2)	Seeded From UniProt	complete
enables	GO:0016262	protein N-acetylglucosaminyltransferase activity	PMID:26678539^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:26678539^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:26678539^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097363	protein O-GlcNAc transferase activity	PMID:28584052^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0016485	protein processing	PMID:28584052^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0097363	protein O-GlcNAc transferase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CGY8	F		Seeded From UniProt	complete
involved_in	GO:0006111	regulation of gluconeogenesis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CGY8	P		Seeded From UniProt	complete
involved_in	GO:0080182	histone H3-K4 trimethylation	PMID:23353889^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0061087	positive regulation of histone H3-K27 methylation	PMID:24474760^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048015	phosphatidylinositol-mediated signaling	PMID:18288188^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
contributes_to	GO:0046972	histone acetyltransferase activity (H4-K16 specific)	PMID:20018852^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0046626	regulation of insulin receptor signaling pathway	PMID:18288188^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:23352454^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:23222540^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:23353889^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045862	positive regulation of proteolysis	PMID:21285374^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
contributes_to	GO:0043996	histone acetyltransferase activity (H4-K8 specific)	PMID:20018852^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
contributes_to	GO:0043995	histone acetyltransferase activity (H4-K5 specific)	PMID:20018852^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0043984	histone H4-K16 acetylation	PMID:20018852^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043982	histone H4-K8 acetylation	PMID:20018852^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043981	histone H4-K5 acetylation	PMID:20018852^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035020	regulation of Rac protein signal transduction	PMID:18288188^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CGY8	P		Seeded From UniProt	complete
involved_in	GO:0032868	response to insulin	PMID:18288188^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031397	negative regulation of protein ubiquitination	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q8CGY8	P		Seeded From UniProt	complete
enables	GO:0016262	protein N-acetylglucosaminyltransferase activity	PMID:24474760^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016262	protein N-acetylglucosaminyltransferase activity	PMID:22923583^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016262	protein N-acetylglucosaminyltransferase activity	PMID:23352454^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016262	protein N-acetylglucosaminyltransferase activity	PMID:23222540^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016262	protein N-acetylglucosaminyltransferase activity	PMID:23353889^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016262	protein N-acetylglucosaminyltransferase activity	PMID:21240259^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016262	protein N-acetylglucosaminyltransferase activity	PMID:21285374^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:20824293^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	PMID:23353889^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	PMID:24474760^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	PMID:22923583^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	PMID:23352454^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	PMID:23222540^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	PMID:21285374^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	PMID:21240259^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006110	regulation of glycolytic process	PMID:22923583^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:18288188^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21285374^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21285374^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005547	phosphatidylinositol-3,4,5-trisphosphate binding	PMID:18288188^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000123	histone acetyltransferase complex	PMID:20018852^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097363	protein O-GlcNAc transferase activity	PMID:23777819^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0120162	positive regulation of cold-induced thermogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8CGY8 ensembl:ENSMUSP00000045409	P		Seeded From UniProt	complete
enables	GO:0097363	protein O-GlcNAc transferase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8CGY8 ensembl:ENSMUSP00000045409	F		Seeded From UniProt	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8CGY8 ensembl:ENSMUSP00000045409	P		Seeded From UniProt	complete
involved_in	GO:0031397	negative regulation of protein ubiquitination	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8CGY8 ensembl:ENSMUSP00000045409	P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8CGY8 ensembl:ENSMUSP00000045409	P		Seeded From UniProt	complete
involved_in	GO:0006111	regulation of gluconeogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q8CGY8 ensembl:ENSMUSP00000045409	P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR037919	P		Seeded From UniProt	complete
enables	GO:0016757	transferase activity, transferring glycosyl groups	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR037919	F		Seeded From UniProt	complete
enables	GO:0008375	acetylglucosaminyltransferase activity	PMID:9083068^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007584	response to nutrient	PMID:9083068^[15]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007165	signal transduction	PMID:9083067^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006493	protein O-linked glycosylation	PMID:9083067^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:9083067^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:9083067^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-5689630 Reactome:R-HSA-3321805	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
involved_in	GO:0006325	chromatin organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0156	P		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966 UniProtKB-SubCell:SL-0280	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472 UniProtKB-SubCell:SL-0162	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P		Seeded From UniProt	complete
enables	GO:0016757	transferase activity, transferring glycosyl groups	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0328	F		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496 UniProtKB-SubCell:SL-0173	C		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
enables	GO:0008289	lipid binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0446	F		Seeded From UniProt	complete
part_of	GO:0031966	mitochondrial membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0171	C		Seeded From UniProt	complete
involved_in	GO:0006486	protein glycosylation	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00378	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Lazarus, MB et al. (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469 564-7 PubMed GONUTS page
↑ Ohashi, N et al. (2017) Pivotal Role of -GlcNAc Modification in Cold-Induced Thermogenesis by Brown Adipose Tissue Through Mitochondrial Biogenesis. Diabetes 66 2351-2362 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Ding, X et al. (2015) Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7). PLoS ONE 10 e0145023 PubMed GONUTS page
↑ ^4.0 ^4.1 Willems, AP et al. (2017) Mutations in -acetylglucosamine (-GlcNAc) transferase in patients with X-linked intellectual disability. J. Biol. Chem. 292 12621-12631 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Deplus, R et al. (2013) TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS. EMBO J. 32 645-55 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Chu, CS et al. (2014) O-GlcNAcylation regulates EZH2 protein stability and function. Proc. Natl. Acad. Sci. U.S.A. 111 1355-60 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 Yang, X et al. (2008) Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 451 964-9 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 Cai, Y et al. (2010) Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J. Biol. Chem. 285 4268-72 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Vella, P et al. (2013) Tet proteins connect the O-linked N-acetylglucosamine transferase Ogt to chromatin in embryonic stem cells. Mol. Cell 49 645-56 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Chen, Q et al. (2013) TET2 promotes histone O-GlcNAcylation during gene transcription. Nature 493 561-4 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 Daou, S et al. (2011) Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway. Proc. Natl. Acad. Sci. U.S.A. 108 2747-52 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Yi, W et al. (2012) Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science 337 975-80 PubMed GONUTS page
↑ Shin, SH et al. (2011) Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis. Amino Acids 40 885-93 PubMed GONUTS page
↑ Mizuguchi-Hata, C et al. (2013) Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation. Biochim. Biophys. Acta 1833 2682-9 PubMed GONUTS page
↑ ^15.0 ^15.1 Lubas, WA et al. (1997) O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272 9316-24 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Kreppel, LK et al. (1997) Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272 9308-15 PubMed GONUTS page

[PMID:21240259-1] 1.0 ^1.1 ^1.2 Lazarus, MB et al. (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469 564-7 PubMed GONUTS page

[PMID:28637651-2] Ohashi, N et al. (2017) Pivotal Role of -GlcNAc Modification in Cold-Induced Thermogenesis by Brown Adipose Tissue Through Mitochondrial Biogenesis. Diabetes 66 2351-2362 PubMed GONUTS page

[PMID:26678539-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Ding, X et al. (2015) Mixed Lineage Leukemia 5 (MLL5) Protein Stability Is Cooperatively Regulated by O-GlcNac Transferase (OGT) and Ubiquitin Specific Protease 7 (USP7). PLoS ONE 10 e0145023 PubMed GONUTS page

[PMID:28584052-4] 4.0 ^4.1 Willems, AP et al. (2017) Mutations in -acetylglucosamine (-GlcNAc) transferase in patients with X-linked intellectual disability. J. Biol. Chem. 292 12621-12631 PubMed GONUTS page

[PMID:23353889-5] 5.0 ^5.1 ^5.2 ^5.3 Deplus, R et al. (2013) TET2 and TET3 regulate GlcNAcylation and H3K4 methylation through OGT and SET1/COMPASS. EMBO J. 32 645-55 PubMed GONUTS page

[PMID:24474760-6] 6.0 ^6.1 ^6.2 Chu, CS et al. (2014) O-GlcNAcylation regulates EZH2 protein stability and function. Proc. Natl. Acad. Sci. U.S.A. 111 1355-60 PubMed GONUTS page

[PMID:18288188-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 Yang, X et al. (2008) Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance. Nature 451 964-9 PubMed GONUTS page

[PMID:20018852-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 Cai, Y et al. (2010) Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J. Biol. Chem. 285 4268-72 PubMed GONUTS page

[PMID:23352454-9] 9.0 ^9.1 ^9.2 Vella, P et al. (2013) Tet proteins connect the O-linked N-acetylglucosamine transferase Ogt to chromatin in embryonic stem cells. Mol. Cell 49 645-56 PubMed GONUTS page

[PMID:23222540-10] 10.0 ^10.1 ^10.2 Chen, Q et al. (2013) TET2 promotes histone O-GlcNAcylation during gene transcription. Nature 493 561-4 PubMed GONUTS page

[PMID:21285374-11] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 Daou, S et al. (2011) Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway. Proc. Natl. Acad. Sci. U.S.A. 108 2747-52 PubMed GONUTS page

[PMID:22923583-12] 12.0 ^12.1 ^12.2 Yi, W et al. (2012) Phosphofructokinase 1 glycosylation regulates cell growth and metabolism. Science 337 975-80 PubMed GONUTS page

[PMID:20824293-13] Shin, SH et al. (2011) Elevated O-GlcNAc-dependent signaling through inducible mOGT expression selectively triggers apoptosis. Amino Acids 40 885-93 PubMed GONUTS page

[PMID:23777819-14] Mizuguchi-Hata, C et al. (2013) Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation. Biochim. Biophys. Acta 1833 2682-9 PubMed GONUTS page

[PMID:9083068-15] 15.0 ^15.1 Lubas, WA et al. (1997) O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J. Biol. Chem. 272 9316-24 PubMed GONUTS page

[PMID:9083067-16] 16.0 ^16.1 ^16.2 ^16.3 Kreppel, LK et al. (1997) Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats. J. Biol. Chem. 272 9308-15 PubMed GONUTS page

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HUMAN:OGT1

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