INT272486

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Context Info
Confidence 0.66
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 10
Total Number 30
Disease Relevance 4.63
Pain Relevance 0.08

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

mRNA binding (Celf1) mRNA processing (Celf1) RNA binding (Celf1)
nucleus (Celf1) cytoplasm (Celf1)
Anatomy Link Frequency
myoblasts 4
myotubes 4
muscle cells 1
muscle 1
nucleus 1
Celf1 (Mus musculus)
Pain Link Frequency Relevance Heat
Kinase C 18 98.24 Very High Very High Very High
cytokine 42 64.88 Quite High
Central nervous system 42 5.00 Very Low Very Low Very Low
spastic colon 21 5.00 Very Low Very Low Very Low
depression 21 5.00 Very Low Very Low Very Low
Inflammation 21 5.00 Very Low Very Low Very Low
tolerance 9 5.00 Very Low Very Low Very Low
abdominal pain 9 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Targeted Disruption 471 99.20 Very High Very High Very High
Myotonic Dystrophy 534 98.76 Very High Very High Very High
Disease 390 96.16 Very High Very High Very High
Stress 21 82.68 Quite High
Cataract 183 74.04 Quite High
Arrhythmias 2 Under Development 51 73.60 Quite High
Hypopituitarism 99 72.48 Quite High
Frailty 174 72.08 Quite High
Congenital Anomalies 231 70.20 Quite High
Cancer 21 37.92 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Although there are several predicted sites for the phosphorylation of CUGBP1 by PKC, additional studies are needed to identify phosphorylation sites for PKC and DMPK kinases within the CUGBP1 molecule.
Phosphorylation (phosphorylation) of CUGBP1
1) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.21 Pain Relevance 0
As noted above, CUGBP1-eIF2 complexes are increased in DM2 differentiating myotubes similar to normal myotubes (Fig. 6); suggesting that in DM2 myotubes, phosphorylation of CUGBP1 at Ser302 is normal.
Phosphorylation (phosphorylation) of CUGBP1 in myotubes
2) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.05 Pain Relevance 0.03
During DM1 myogenesis, phosphorylation of CUGBP1 and CUGBP1 interactions with its RNA targets are altered.
Phosphorylation (phosphorylation) of CUGBP1
3) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.06 Pain Relevance 0
Thus, stabilization of CUGBP1 in DM1 is achieved by a complex mechanism involving specific phosphorylation of CUGBP1, its interactions with un-aggregated CUG repeats, and possibly some other factors.
Phosphorylation (phosphorylation) of CUGBP1
4) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.07 Pain Relevance 0
In addition, the phosphorylation of CUGBP1 on the putative PKC sites might stabilize CUGBP1 in DM1 cells leading to the enhancement of CUGBP1 functions.
Phosphorylation (phosphorylation) of CUGBP1
5) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.10 Pain Relevance 0
Recent data revealed that phosphorylation of CUGBP1 by PKC kinase also plays a significant role in the stabilization of CUGBP1 in DM1 cells [63].
Phosphorylation (phosphorylation) of CUGBP1
6) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.07 Pain Relevance 0
As noted above, in normal myotubes, CUGBP1 interacts with cyclin D3/cdk4 complex which phosphorylates CUGBP1 at Ser302 [68].
Phosphorylation (phosphorylates) of CUGBP1 in myotubes
7) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.07 Pain Relevance 0
In DM1 myoblasts, CUGBP1 is hyperphosphorylated by Akt; whereas in DM1 myotubes CUGBP1 phosphorylation by cyclinD3/cdk4 is reduced due to low levels of cytoplasmic cyclin D3 [68].
Phosphorylation (phosphorylation) of CUGBP1 in myotubes
8) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.12 Pain Relevance 0
During DM1 myogenesis, phosphorylation of CUGBP1 and CUGBP1 interactions with its RNA targets are altered.
Phosphorylation (phosphorylation) of CUGBP1
9) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.11 Pain Relevance 0
These changes of CUGBP1 phosphorylation in DM1 myogenesis lead to the increase of cyclin D1 in DM1 myoblasts and to the reduction p21 in DM1 myotubes [68] (Fig. 7).
Phosphorylation (phosphorylation) of CUGBP1 in myoblasts
10) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.12 Pain Relevance 0
Interactions of CUGBP1 with eIF2 require site-specific phosphorylation of CUGBP1 at Ser302 by cyclin D3-cdk4 kinase [75,76,78].
Phosphorylation (phosphorylation) of CUGBP1
11) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.21 Pain Relevance 0
In proliferating myoblasts CUGBP1 is phosphorylated by Akt and the ph-S28-CUGBP1 has increased binding activity toward mRNA encoding cyclin D1 [78].
Phosphorylation (phosphorylated) of CUGBP1 in myoblasts
12) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.13 Pain Relevance 0
CUGBP1 phosphorylated isoforms are increased in cytoplasm of DM2 myoblasts with elevated levels of CUGBP1; thus phosphorylation may also play a role in the stabilization of CUGBP1 in DM2 cells [52].
Phosphorylation (phosphorylated) of CUGBP1 in myoblasts
13) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0 Pain Relevance 0
In DM1 myoblasts, CUGBP1 is hyperphosphorylated by Akt; whereas in DM1 myotubes CUGBP1 phosphorylation by cyclinD3/cdk4 is reduced due to low levels of cytoplasmic cyclin D3 [68].
Phosphorylation (hyperphosphorylated) of CUGBP1 in myotubes
14) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.12 Pain Relevance 0
Examination of CUGBP1 phosphorylation status in the DMPK knock out mice suggested that CUGBP1 is a possible substrate for DMPK kinase [86].
Phosphorylation (phosphorylation) of CUGBP1 associated with targeted disruption
15) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.45 Pain Relevance 0
These data suggest that a lack of CDM in patients with DM2 may be, at least in part, due to normal phosphorylation of CUGBP1 at Ser302.


Phosphorylation (phosphorylation) of CUGBP1 associated with myotonic dystrophy
16) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.53 Pain Relevance 0
It has been shown that the site-specific phosphorylation of CUGBP1 by Akt and cyclinD3/cdk4 kinase regulates CUGBP1 function during normal myogenesis (Fig. 7).
Phosphorylation (phosphorylation) of CUGBP1
17) Confidence 0.66 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.14 Pain Relevance 0
Although there are several predicted sites for the phosphorylation of CUGBP1 by PKC, additional studies are needed to identify phosphorylation sites for PKC and DMPK kinases within the CUGBP1 molecule.
Phosphorylation (phosphorylation) of CUGBP1
18) Confidence 0.65 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.20 Pain Relevance 0
In proliferating myoblasts CUGBP1 is phosphorylated by Akt and the ph-S28-CUGBP1 has increased binding activity toward mRNA encoding cyclin D1 [78].
Phosphorylation (phosphorylated) of CUGBP1 in myoblasts
19) Confidence 0.51 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.13 Pain Relevance 0
In addition, the phosphorylation of CUGBP1 on the putative PKC sites might stabilize CUGBP1 in DM1 cells leading to the enhancement of CUGBP1 functions.
Phosphorylation (phosphorylation) of CUGBP1
20) Confidence 0.44 Published 2010 Journal Current Genomics Section Body Doc Link PMC2874224 Disease Relevance 0.10 Pain Relevance 0

General Comments

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