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Accession Type:
Network
Ajay_Bhalla_
2007_ReacDiff3
Shared_Object_
Ajay_Bhalla_
2007_ReacDiff3
PKC
PLA2
MAPK
PLA2
Ras
CaM
chain
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3
PKC
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[1]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[2]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[3]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[4]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[5]
PKC
PLA2
MAPK
Ras
MAPK
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[6]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[7]
PKC
PLA2
MAPK
Ras
CaM
PKC
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[8]
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[9]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[10]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[11]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[12]
PKC
PLA2
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[13]
PKC
PLA2
MAPK
Ras
 Molecule
 Enzyme
 Reaction
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[14]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[15]
PKC
PLA2
MAPK
Ras
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[16]
CaM
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[17]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[18]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[19]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[20]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[21]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[22]
PKC
PLA2
MAPK
Ras
CaM
Shared Object_
Ajay_Bhalla_
2007_ReacDiff3_
[23]
PKC
PLA2
MAPK
Ras
CaM

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Molecule List for pathway Ras (Pathway Number 1007)

 Name Initial Conc. (uM) Volume (fL) Buffered
1CaM-GEF0125.7No
    See Farnsworth et al Nature 376 524-527 1995
2GAP0.01125.7No
    GTPase-activating proteins. See Boguski and McCormick. Turn off Ras by helping to hydrolyze bound GTP. This one is probably NF1, ie., Neurofibromin as it is inhibited by AA and lipids, and expressed in neural cells. p120-GAP is also a possible candidate, but is less regulated. Both may exist at similar levels. See Eccleston et al JBC 268(36) pp27012-19 Level=.002 16 May 2003: Increased level to 0.0036, in line with other concentration raises at the synapse.
3GAP*0125.7No
4GDP-Ras0.5125.7No
    GDP bound form. See Rosen et al Neuron 12 1207-1221 June 1994. the activation loop is based on Boguski and McCormick Nature 366 643-654 93 Assume Ras is present at about the same level as craf-1, 0.2 uM. Hallberg et al JBC 269:6 3913-3916 1994 estimate upto 5-10% of cellular Raf is assoc with Ras. Given that only 5-10% of Ras is GTP-bound, we need similar amounts of Ras as Raf.
5GEF*0125.7No
    phosphorylated and thereby activated form of GEF. See, e.g. Orita et al JBC 268:34 25542-25546 1993, Gulbins et al. It is not clear whether there is major specificity for tyr or ser/thr.
6GTP-Ras0125.7No
    Only a very small fraction (7% unstim, 15% stim) of ras is GTP-bound. Gibbs et al JBC 265(33) 20437
7inact-GEF0.1125.7No
    Assume that SoS is present only at 50 nM. Revised to 100 nM to get equil to experimentally known levels.


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