+ |
OGT | up-regulates activity
glycosylation
|
YAP1 |
0.287 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276942 |
Ser109 |
KSHSRQAsTDAGTAG |
|
|
pmid |
sentence |
34155345 |
Mass spectrometry analysis showed that YAP was the effector protein modified by OGT. In details, YAP Ser109 O-GlcNAcylation promoted the malignant phenotypes in PTC cells by inducing YAP Ser127 dephosphorylation and activation. |
|
Publications: |
1 |
+ |
GSK3B | up-regulates activity
phosphorylation
|
OGT |
0.5 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276482 |
Ser3 |
sSVGNVAD |
Mus musculus |
Brain |
pmid |
sentence |
23395175 |
We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β. Interestingly, OGT activity is regulated by GSK3β; hence, OGT and GSK3β exhibit reciprocal regulation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276481 |
Ser4 |
sVGNVADS |
Mus musculus |
Brain |
pmid |
sentence |
23395175 |
We employed a circadian proteomic approach to demonstrate that circadian timing of phosphorylation is a critical factor in regulating complex GSK3β-dependent pathways and identified O-GlcNAc transferase (OGT) as a substrate of GSK3β. Interestingly, OGT activity is regulated by GSK3β; hence, OGT and GSK3β exhibit reciprocal regulation. |
|
Publications: |
2 |
Organism: |
Mus Musculus |
+ |
OGT | up-regulates activity
glycosylation
|
PYGL |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267988 |
Ser430 |
VDRLRRMsLIEEEGS |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
34939084 |
O-GlcNAcylation at Ser-430 promotes PYGL activity |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGT | down-regulates activity
glycosylation
|
PFKL |
0.281 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267585 |
Ser529 |
CVIPATIsNNVPGTD |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22923583 |
O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia. Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway| O-GlcNAc transferase (OGT) catalyzes the transfer of N-acetylglucosamine from uridine diphospho-N-acetylglucosamine (UDP-GlcNAc) to serine or threonine residues |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGT | down-regulates activity
glycosylation
|
PFKM |
0.354 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267584 |
Ser530 |
VVIPATVsNNVPGSD |
Homo sapiens |
|
pmid |
sentence |
26399441 |
Our previous investigation on O-GlcNAcylation of PFK1 has demonstrated that O-GlcNAcylation inhibits PFK1 enzyme activity|In cells, a single set of antagonistic enzymes-O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase are responsible for the addition and removal of GlcNAc moiety, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGT | down-regulates activity
glycosylation
|
PFKP |
0.26 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267583 |
Ser540 |
VMVPATVsNNVPGSD |
Homo sapiens |
A-549 Cell |
pmid |
sentence |
26399441 |
Our previous investigation on O-GlcNAcylation of PFK1 has demonstrated that O-GlcNAcylation inhibits PFK1 enzyme activity|In cells, a single set of antagonistic enzymes-O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase are responsible for the addition and removal of GlcNAc moiety, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGT | up-regulates activity
glycosylation
|
G6PD |
0.267 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267582 |
Ser84 |
VADIRKQsEPFFKAT |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
26399441 |
O-GlcNAcylation of G6PD promotes the pentose phosphate pathway and tumor growth|O-GlcNAcylation of G6PD activates enzyme activity|G6PD is dynamically modified by O-GlcNAc at serine 84|In cells, a single set of antagonistic enzymes-O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase are responsible for the addition and removal of GlcNAc moiety, respectively. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TET3 | up-regulates
binding
|
OGT |
0.455 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200729 |
|
|
Homo sapiens |
|
pmid |
sentence |
23353889 |
Tet2 and tet3 associate with the o_glcnac transferase ogt / tet2 and tet3 promote ogt_mediated glcnacylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGT | up-regulates activity
glycosylation
|
TET1 |
0.452 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259184 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
23729667 |
The DNA demethylation enzyme Tet1 interacts with Ogt and is O-GlcNAcylated. Tet1 protein stability is positively regulated by O-GlcNAcylation, and its repression function on targeting genes is dependent on Ogt. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGT | form complex
binding
|
NSL histone acetyltransferase |
0.538 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267158 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
20018852 |
Here we report an analysis of the subunit composition and substrate specificity of the NSL complex. Proteomic analyses of complexes purified through multiple candidate subunits reveal that NSL is composed of nine subunits. Two of its subunits, WD repeat domain 5 (WDR5) and host cell factor 1 (HCF1), are shared with members of the MLL/SET family of histone H3 lysine 4 (H3K4) methyltransferase complexes, and a third subunit, MCRS1, is shared with the human INO80 chromatin-remodeling complex. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
OGT | down-regulates activity
glycosylation
|
PFK |
0.354 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267586 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
22923583 |
O-GlcNAcylation was induced at serine 529 of phosphofructokinase 1 (PFK1) in response to hypoxia. Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway| O-GlcNAc transferase (OGT) catalyzes the transfer of N-acetylglucosamine from uridine diphospho-N-acetylglucosamine (UDP-GlcNAc) to serine or threonine residues |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TET2 | up-regulates
binding
|
OGT |
0.456 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-200695 |
|
|
Homo sapiens |
|
pmid |
sentence |
23353889 |
Tet2 and tet3 associate with the o_glcnac transferase ogt / tet2 and tet3 promote ogt_mediated glcnacylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |