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UDP-GlcNAc + CKII peptide
UDP + N-acetylglucosaminyl-CKII alpha-peptide
PGGSTPVSSANMM
-
-
?
UDP-GlcNAc + dynamin-related protein 1
UDP + dynamin-related protein 1-GlcNAc
dynamin-related protein 1 is O-linked-N-acetyl-glucosamine-glycosylated at threonine 585 and 586
-
-
?
UDP-GlcNAc + p62 protein
UDP + N-acetyl-D-glucosaminyl-[p62 protein]
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + GlcNAc-YSDSPSTST
-
-
-
?
casein kinase II peptide + UDP-GlcNAc
? + UDP
-
-
-
-
?
mitochondrial motor-adaptor protein milton + UDP-GlcNAc
? + UDP
-
-
mitochondrial motor-adaptor protein Milton is a required substrate for OGT to arrest mitochondrial motility by mapping and mutating the key O-GlcNAcylated serine residues
-
?
nucleoporin p62 + UDP-GlcNAc
? + UDP
-
high affinity substrate
-
-
?
OIP106 protein + UDP-GlcNAc
O-GlcNAc-OIP106 protein + UDP
-
N-terminal deletions of OIP106 are generated as S-tagged constructs: DELTAnCC, DELTA491, DELTA639, DELTA859
-
-
?
UDP-GlcNAc + AIPVSREEK
UDP + AIPV-(GlcNAc)SREEK
-
-
-
-
?
UDP-GlcNAc + beta-amyloid associated protein
GlcNAc-beta-amyloid associated protein + UDP
-
-
-
-
?
UDP-GlcNAc + DELTA639 protein
UDP + N-acetyl-D-glucosaminyl-[DELTA639 protein]
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
UDP-GlcNAc + DELTAnCC protein
UDP + N-acetyl-D-glucosaminyl-[DELTAnCC protein]
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
UDP-GlcNAc + glutathione S-transferase
glutathione S-transferase-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-CARM1
glutathione S-transferase-CARM1-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + glutathione S-transferase-MYPT1
glutathione S-transferase-MYPT1-GlcNAc + UDP
-
-
-
-
?
UDP-GlcNAc + ITISETPSSTTTTQITK
UDP + ITI-(GlcNAc)SETPSSTTTTQITK
-
-
-
-
?
UDP-GlcNAc + KKFELLPTPPLSPSRR
UDP + KKFELLP-(GlcNAc)TPPLSPSRR
-
-
-
-
?
UDP-GlcNAc + PGGSTPVS(PO3)-SANMM
? + UDP
-
-
-
-
?
UDP-GlcNAc + PGGSTPVSSANMM
UDP + PGGSTPV-(GlcNAc)SSANMM
-
PGGSTPVSSANMM is the best acceptor
-
-
?
UDP-GlcNAc + tau protein
GlcNAc-tau protein + UDP
-
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + ?
UDP-GlcNAc + YSPTSPSYSPTSPS
UDP + Y-(GlcNAc)SPT-(GlcNAc)SPSYSPT-(GlcNAc)SPS
-
YSPTSPSYSPTSPS is a poor substrate
-
-
?
UDP-GlcNAc + [YSPTSPSYSPTSPS]5
UDP + [Y-(GlcNAc)SP-(GlcNAc)TSPSYSP-(GlcNAc)TSPS]5
-
-
-
-
?
UDP-GlcNAc DELTA491 protein
UDP + N-acetyl-D-glucosaminyl-[DELTA491 protein]
-
N-terminal truncation of OIP106, able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
additional information
?
-
UDP-GlcNAc + YSDSPSTST
UDP + ?
-
-
-
-
?
UDP-GlcNAc + YSDSPSTST
UDP + ?
-
highly specific synthetic peptide assay, affinity of the enzyme for UDP-GlcNAc is high and for the peptide substrate, YSDSPSTST, is only moderate
-
-
?
additional information
?
-
catalyses the O-linked attachment of single GlcNAc moieties to serine and threonine residues on many cytosolic or nuclear proteins
-
-
?
additional information
?
-
catalyzes the attachment of GlcNAc monosaccharides to the hydroxyl group of serine or threonine residues of intracellular proteins and may play an important role in the hexosamine pathway
-
-
?
additional information
?
-
-
enzyme catalyzes the abundant and dynamic posttranslational modification of nuclear and cytosolic proteins by beta-O-linked N-acetylglucosamine (O-GlcNAc)
-
-
?
additional information
?
-
-
O-GlcNAc transferase, the enzyme that adds O-GlcNAc to proteins, exists in stable and active complexes with the serine/threonine phosphatases PP1beta and PP1gamma, enzymes that remove phosphate from proteins
-
-
?
additional information
?
-
-
p110 subunit of the enzyme forms both homo- and heterotrimers that appear to have different binding affinities for UDP-GlcNAc
-
-
?
additional information
?
-
-
DELTA859 is not able to bind and pull down OGT, indicates that the potential OGT-binding domain localized to within residues 639-859 in the C-terminus of OIP106
-
-
?
additional information
?
-
-
OGT-interacting proteins interact strongly with the tetratricopeptide repeat (TPR) domain of OGT, they are modified by O-GlcNAc and are excellent substrates of OGT
-
-
?
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3-[2-adamantanylethyl]-2-[[4-chlorophenyl]azamethylene]-4-oxo-1,3-thiazaperhyd roine-6-carboxylic acid
-
endothelin 1 effects are not observed when vessels are previously instilled with anti-O-GlcNAc transferase antibody or after incubation with an O-GlcNAc transferase inhibitor (100 microMol)
ATP
-
has a much lower affinity for OGT
thiouridine diphosphate
-
SUDP
UDP
-
UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
UDP-galactose
-
much lower affinity for OGT compared with UDP-GlcNAc
UDP-glucose
-
much lower affinity for OGT compared with UDP-GlcNAc
UMP
-
UMP and UDP-GalNAc are 100fold less potent than UDP, UTP, and UDP-GlcNAc
additional information
-
the isolated tetratricopeptide repeat domain of OGT competitively inhibits glycosylation of the OID protein, but does not inhibit glycosylation of small peptides, providing kinetic evidence for the role of the tetratricopeptide repeat domain as a protein substrate docking site
-
KCl
-
lowers OGT activity by reducing enzyme affinity for UDP-GlcNAc
KCl
-
50 mM causes 66% inhibition
NaCl
-
-
NaCl
-
50 mM causes 66% inhibition
UDP-GalNAc
-
-
UDP-GalNAc
-
UMP and UDP-GalNAc are 100fold less potent than UDP, UTP, and UDP-GlcNAc
UDP-GlcNAc
-
-
UDP-GlcNAc
-
UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
UTP
-
has a high affinity for OGT
UTP
-
UDP, UTP, and UDP-GlcNAc are all equally potent inhibitors of the activity
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Haltiwanger, R.S.; Blomberg, M.A.; Hart, G.W.
Glycosylation of nuclear and cytoplasmic proteins. Purification and characterization of a uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase
J. Biol. Chem.
267
9005-9013
1992
Rattus norvegicus
brenda
Kreppel, L.K.; Blomberg, M.A.; Hart, G.W.
Dynamic glycosylation of nuclear and cytosolic proteins. Cloning and characterization of a unique O-GlcNAc transferase with multiple tetratricopeptide repeats
J. Biol. Chem.
272
9308-9315
1997
Rattus norvegicus (P56558)
brenda
Konrad, R.J.; Tolar, J.F.; Hale, J.E.; Knierman, M.D.; Becker, G.W.; Kudlow, J.E.
Purification of the O-glycosylated protein p135 and identification as O-GlcNAc transferase
Biochem. Biophys. Res. Commun.
288
1136-1140
2001
Rattus norvegicus
brenda
Akimoto, Y.; Comer, F.I.; Cole, R.N.; Kudo, A.; Kawakami, H.; Hirano, H.; Hart, G.W.
Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex
Brain Res.
966
194-205
2003
Rattus norvegicus
brenda
Wells, L.; Kreppel, L.K.; Comer, F.I.; Wadzinski, B.E.; Hart, G.W.
O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits
J. Biol. Chem.
279
38466-38470
2004
Rattus norvegicus
brenda
Maerz, P.; Stetefeld, J.; Bendfeldt, K.; Nitsch, C.; Reinstein, J.; Shoeman, R.L.; Dimitriades-Schmutz, B.; Schwager, M.; Leiser, D.; Ozcan, S.; Otten, U.; Ozbek, S.
Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain
J. Biol. Chem.
281
20263-20270
2006
Homo sapiens (O15294), Rattus norvegicus (P56558)
brenda
Akimoto, Y.; Kreppel, L.K.; Hirano, H.; Hart, G.W.
Hyperglycemia and the O-GlcNAc transferase in rat aortic smooth muscle cells: elevated expression and altered patterns of O-GlcNAcylation
Arch. Biochem. Biophys.
389
166-175
2001
Rattus norvegicus (P56558)
brenda
Hanover, J.A.; Yu, S.; Lubas, W.B.; Shin, S.H.; Ragano-Caracciola, M.; Kochran, J.; Love, D.C.
Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
Arch. Biochem. Biophys.
409
287-297
2003
Homo sapiens, Rattus norvegicus, Mus musculus (Q8CGY8), Mus musculus
brenda
Akimoto, Y.; Kreppel, L.K.; Hirano, H.; Hart, G.W.
Localization of the O-linked N-acetylglucosamine transferase in rat pancreas
Diabetes
48
2407-2413
1999
Rattus norvegicus (P56558)
brenda
Lima, V.V.; Giachini, F.R.; Carneiro, F.S.; Carneiro, Z.N.; Saleh, M.A.; Pollock, D.M.; Fortes, Z.B.; Carvalho, M.H.; Ergul, A.; Webb, R.C.; Tostes, R.C.
O-GlcNAcylation contributes to augmented vascular reactivity induced by endothelin 1
Hypertension
55
180-188
2010
Rattus norvegicus
brenda
Kreppel, L.K.; Hart, G.W.
Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
J. Biol. Chem.
274
32015-32022
1999
Rattus norvegicus
brenda
Iyer, S.P.; Hart, G.W.
Roles of the tetratricopeptide repeat domain in O-GlcNAc transferase targeting and protein substrate specificity
J. Biol. Chem.
278
24608-24616
2003
Rattus norvegicus
brenda
Cheung, W.D.; Sakabe, K.; Housley, M.P.; Dias, W.B.; Hart, G.W.
O-linked beta-N-acetylglucosaminyltransferase substrate specificity is regulated by myosin phosphatase targeting and other interacting proteins
J. Biol. Chem.
283
33935-33941
2008
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Okuyama, R.; Marshall, S.
UDP-N-acetylglucosaminyl transferase (OGT) in brain tissue: temperature sensitivity and subcellular distribution of cytosolic and nuclear enzyme
J. Neurochem.
86
1271-1280
2003
Rattus norvegicus
brenda
Gawlowski, T.; Suarez, J.; Scott, B.; Torres-Gonzalez, M.; Wang, H.; Schwappacher, R.; Han, X.; Yates, J.R.; Hoshijima, M.; Dillmann, W.
Modulation of dynamin-related protein 1 (DRP1) function by increased O-linked-beta-N-acetylglucosamine modification (O-GlcNAc) in cardiac myocytes
J. Biol. Chem.
287
30024-30034
2012
Rattus norvegicus (P56558)
brenda
Liu, Y.; Li, X.; Yu, Y.; Shi, J.; Liang, Z.; Run, X.; Li, Y.; Dai, C.L.; Grundke-Iqbal, I.; Iqbal, K.; Liu, F.; Gong, C.X.
Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain
PLoS ONE
7
e43724
2012
Rattus norvegicus (P56558)
brenda
Pekkurnaz, G.; Trinidad, J.C.; Wang, X.; Kong, D.; Schwarz, T.L.
Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase
Cell
158
54-68
2014
Rattus norvegicus
brenda