INT121195

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Context Info
Confidence 0.63
First Reported 2004
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 5
Total Number 5
Disease Relevance 0.49
Pain Relevance 0.60

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

plasma membrane (KCNMA1) transmembrane transport (KCNMA1)
Anatomy Link Frequency
myometrium 1
KCNMA1 (Homo sapiens)
Pain Link Frequency Relevance Heat
bradykinin 12 100.00 Very High Very High Very High
potassium channel 3 93.60 High High
Pain 1 75.00 Quite High
antagonist 2 72.64 Quite High
COX2 1 25.00 Low Low
Dismenorea 6 5.00 Very Low Very Low Very Low
member 8 1 5.00 Very Low Very Low Very Low
chemokine 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Osteoporosis 2 93.04 High High
Pain 1 75.00 Quite High
Death 5 64.24 Quite High
Osteogenic Sarcomas 1 63.52 Quite High
Apoptosis 9 57.60 Quite High
Disease 1 37.12 Quite Low
Cancer 13 35.68 Quite Low
Breast Cancer 2 22.08 Low Low
Metastasis 1 20.16 Low Low
Pre-term Labor 3 18.44 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Previous studies provide evidence that alternate splicing effects calcium and voltage sensitivity of the maxi-K channel and thus channel function in myometrium [16], surface expression [17], and sensitivity to protein phosphorylation of the maxi-K channel [18].
Phosphorylation (phosphorylation) of maxi-K channel in myometrium
1) Confidence 0.63 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC524189 Disease Relevance 0 Pain Relevance 0
These data include evidence for splice variation effecting calcium and voltage sensitivity, surface expression, and sensitivity to protein phosphorylation of the maxi-K channel [16,17]; [18].
Phosphorylation (phosphorylation) of maxi-K channel
2) Confidence 0.63 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC524189 Disease Relevance 0 Pain Relevance 0.05
AKAP6, located on the ER/SR, acts as an adapter molecule in co-localization of the PKA, which also phosphorylates and regulates the activity of KCNMA1 [44], [45].
Phosphorylation (phosphorylates) of KCNMA1
3) Confidence 0.54 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2935366 Disease Relevance 0.18 Pain Relevance 0
However, as described above, it contains a consensus sequence for protein kinase phosphorylation; therefore, it may have important consequences for post-translational modification of channel function.
Phosphorylation (phosphorylation) of channel
4) Confidence 0.48 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC524189 Disease Relevance 0 Pain Relevance 0
BK treatment resulted in the phosphorylation of p38 MAPK and extracellular signal-regulated kinase (ERK)1/2, and 2-APB could suppress BK-induced phosphorylation of ERK1/2.
Phosphorylation (phosphorylation) of BK associated with bradykinin
5) Confidence 0.05 Published 2004 Journal Biochem. Pharmacol. Section Abstract Doc Link 15345332 Disease Relevance 0.31 Pain Relevance 0.55

General Comments

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