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camkii found in these Models |
| Name / Accession No. | Accession Type / Entry Date | Model Type | Accession Statistics | camkii Statistic | Species / Tissue | Cell Compartment / Source | Methodology / Model_Implementation | Model in which camkii acting as a molecule or reaction or enzyme are listed here. 6 | Osc_Ca_ IP3metabolism/ Accession No. : 24 | Network / 2002-01-08 00:00:00 | Chemical | Molecule = 137 Enzyme = 49 Reaction = 82
| Molecule = 8 Enzyme = 8 Reaction = 1
| Generic mammalian / Brain - Neuronal | Cytosol / Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. ( peer-reviewed publication ) | Quantitative match to experiments, Qualitative / Approximate implementation | | This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It differs from the NonOsc_Ca_IP3metabolism network in the CaRegulation module and in InsP3 receptor kinetics. Details of InsP3 receptor kinetics have been adapted from the Othmer-Tang model for oscillatory Ca dynamics. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. | 7 | NonOsc_Ca_ IP3metabolism/ Accession No. : 31 | Network / 2002-04-03 00:00:00 | Chemical | Molecule = 135 Enzyme = 42 Reaction = 90
| Molecule = 8 Enzyme = 8 Reaction = 1
| Generic mammalian / Brain - Neuronal | Cytosol / Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. ( peer-reviewed publication ) | Quantitative match to experiments, Qualitative / Exact GENESIS implementation | | This network models detailed metabolism of Ins(145)P3, integrated with GPCR mediated PLCbeta activation and Ca release by the InsP3 receptor in the neuron. It is similar to the NonOsc_Ca_IP3metab model (accession 23) except that some enzymes have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. These modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. | 8 | Osc_Ca_ IP3metabolism/ Accession No. : 32 | Network / 2002-04-03 00:00:00 | Chemical | Molecule = 138 Enzyme = 43 Reaction = 91
| Molecule = 8 Enzyme = 8 Reaction = 1
| Generic mammalian / Brain - Neuronal | Cytosol / Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. ( peer-reviewed publication ) | Quantitative match to experiments, Qualitative / Exact GENESIS implementation | | This network models an oscillatory calcium response to GPCR mediated PLCbeta activation, alongwith detailed InsP3 metabolism in the neuron. It is similar to the Osc_Ca_IP3metab model (accession 24) except that some enzymes in the InsP3 metabolism network have been modified to have reversible kinetics rather than Michaelis-Menten kinetics. The modified enzymes belong to the groups: IP4-system, IP3-3K, 145_dephos and 134_dephos. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. | 9 | CaMKII/ Accession No. : 33 | Network / 2002-08-21 00:00:00 | Chemical | Molecule = 23 Enzyme = 2 Reaction = 27
| Molecule = 8 Enzyme = 2 Reaction = 9
| Generic mammalian / Brain - Neuronal | Synapse / William R. Holmes J Comput Neurosci. (2000) 8(1):65-85 ( peer-reviewed publication ) | Qualitative / Approximate implementation | | This is a deterministic, point kinetics approximation to the dendritic spine CaMKII model described in William R. Holmes J Comput Neurosci. (2000) 8(1):65-85. Rates are the same but the responses differ somewhat because this model does not include the stochastic and diffusive calculations of the original. | 10 | CaMKII_2003/ Accession No. : 49 | Network / 2003-04-28 00:00:00 | Chemical | Molecule = 31 Enzyme = 18 Reaction = 15
| Molecule = 7 Enzyme = 4 Reaction = 1
| Generic mammalian / Brain - Neuronal | Synapse / Bhalla US. Biophys J. 2004 Aug;87(2):733-44. ( peer-reviewed publication ). | Qualitative / Exact GENESIS implementation | | Model of regulation of CaMKII by Calcium, including parallel excitatory input from CaM and inhibitory input from PP1 as regulated by Calcineurin and PKA. Cell type: neuronal. Bhalla US. Biophys J. 2004 Aug;87(2):733-44. |
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camkii found in these Pathways |
| Pathway Name | Accession Name | Model Type / Accession Type | Pathway Statistics | camkii Statistics | Source / Entry Date | Pathway in which camkii acting as a molecule or reaction or enzyme are listed here. 6 | CaMKII
Pathway No. : 13 | fig3_CaMKII
Accession No. : 2 | Chemical / Network | Molecule = 9 Enzyme = 4 Reaction = 3
| Molecule = 8 Enzyme = 4 Reaction = 1
| Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. ( peer-reviewed publication ) / 2001-11-07 00:00:00 | | Related Pathway : 26, 80, 106, 121, 145, 159, 174, 202, 216, 235, 245, 258, 264, 272, 282, 322, 339, 357 | | This is the model file for figure 3 from Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. It is a model of the Ca activation of CaMKII and other CaM-activated enzymes. It includes the regulatory phosphatases PP1 and PP2B (Calcineurin) acting on CaMKII and also includes CaM-activated adenylyl cyclase and PKA in the synapse. Demonstration script files for generating the figures in the paper, including figure 3, are available here. | 7 | Shared_Object_ fig3_CaMKII Pathway No. : 12 | fig3_CaMKII
Accession No. : 2 | Chemical / Network | Molecule = 15 Enzyme = 16 Reaction = 0
| Molecule = 1 Enzyme = 0 Reaction = 0
| Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. ( peer-reviewed publication ) / 2001-11-07 00:00:00 | | Related Pathway :
| | This is the model file for figure 3 from Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. It is a model of the Ca activation of CaMKII and other CaM-activated enzymes. It includes the regulatory phosphatases PP1 and PP2B (Calcineurin) acting on CaMKII and also includes CaM-activated adenylyl cyclase and PKA in the synapse. Demonstration script files for generating the figures in the paper, including figure 3, are available here. | 8 | CaMKII
Pathway No. : 26 | fig4_synapse
Accession No. : 3 | Chemical / Network | Molecule = 9 Enzyme = 4 Reaction = 3
| Molecule = 8 Enzyme = 4 Reaction = 1
| Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. ( peer-reviewed publication ) / 2001-11-07 00:00:00 | | Related Pathway : 13, 80, 106, 121, 145, 159, 174, 202, 216, 235, 245, 258, 264, 272, 282, 322, 339, 357 | | This is the composite model of 4 kinases: PKC, MAPK, PKA and CaMKII and numerous regulatory pathways involved in synaptic signaling. From Bhalla US and Iyengar R. Science (1999) 283(5400):381-7.This model comes from figure 4 of that paper. Demonstration script files for generating the figures in the paper, including figure 4, are available here. | 9 | Shared_Object_ fig4_synapse Pathway No. : 19 | fig4_synapse
Accession No. : 3 | Chemical / Network | Molecule = 28 Enzyme = 28 Reaction = 2
| Molecule = 1 Enzyme = 0 Reaction = 0
| Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. ( peer-reviewed publication ) / 2001-11-07 00:00:00 | | Related Pathway :
| | This is the composite model of 4 kinases: PKC, MAPK, PKA and CaMKII and numerous regulatory pathways involved in synaptic signaling. From Bhalla US and Iyengar R. Science (1999) 283(5400):381-7.This model comes from figure 4 of that paper. Demonstration script files for generating the figures in the paper, including figure 4, are available here. | 10 | CaMKII
Pathway No. : 80 | Synaptic_ Network Accession No. : 16 | Chemical / Network | Molecule = 9 Enzyme = 4 Reaction = 3
| Molecule = 8 Enzyme = 4 Reaction = 1
| Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. ( peer-reviewed publication ) / 2001-12-12 00:00:00 | | Related Pathway : 13, 26, 106, 121, 145, 159, 174, 202, 216, 235, 245, 258, 264, 272, 282, 322, 339, 357 | | This model is an annotated version of the synaptic signaling network. The primary reference is Bhalla US and Iyengar R. Science (1999) 283(5400):381-7 but several of the model pathways have been updated. Bhalla US Biophys J. 2002 Aug;83(2):740-52 Bhalla US J Comput Neurosci. 2002 Jul-Aug;13(1):49-62 |
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camkii acting as a Molecule |
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camkii acting as Summed Molecule |
| Accession Name Accession No. | Pathway Name Pathway No. | Target | Input | 6 | fig4_synapse Accession No. 3 | CaMKII Pathway No. 26 | tot_autonomous_ CaMKII
| CaMKII-thr286 CaMKII***
| 7 | Synaptic_ Network Accession No. 16 | CaMKII Pathway No. 80 | tot_CaM_CaMKII
| CaMKII-CaM CaMKII-thr286*-C aM
| | This pool sums the levels of the CaM-bound forms of CaMKII: CaMKII-CaM + CaMKII-thr286*-CaM. Although their phosphorylation states are different, the level of activity is about the same so it makes sense to sum the levels. Hanson et al 1994 Neuron 12:943-956 | 8 | Synaptic_ Network Accession No. 16 | CaMKII Pathway No. 80 | tot_autonomous_ CaMKII
| CaMKII-thr286 CaMKII***
| | This is the sum total of the various CaM-independent forms of the kinase. There are actually several possible states here, but I only consider the forms thr-286 phosphorylated form and the doubly/triply phosphorylated form including the thr305/306, represented here as CaMKII*** | 9 | NonOsc_Ca_ IP3metabolism Accession No. 23 | CaMKII Pathway No. 106 | tot_CaM_CaMKII
| CaMKII-CaM CaMKII-thr286*-C aM
| | This pool sums the levels of the CaM-bound forms of CaMKII: CaMKII-CaM + CaMKII-thr286*-CaM. Although their phosphorylation states are different, the level of activity is about the same so it makes sense to sum the levels. Hanson et al 1994 Neuron 12:943-956 | 10 | NonOsc_Ca_ IP3metabolism Accession No. 23 | CaMKII Pathway No. 106 | tot_autonomous_ CaMKII
| CaMKII-thr286 CaMKII***
| | This is the sum total of the various CaM-independent forms of the kinase. There are actually several possible states here, but I only consider the forms thr-286 phosphorylated form and the doubly/triply phosphorylated form including the thr305/306, represented here as CaMKII*** |
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camkii acting as an Enzyme |
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camkii acting as a Subtrate for an Enzyme |
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camkii acting as a Product for an Enzyme |
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camkii acting as a Reaction |
| Name | Accession Name Accession No. | Pathway Name Pathway No. | Kf | Kb | Kd | tau | Reagents | Keq is calculated only for first order reactions.
Kd is calculated only for second order reactions. [ nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules] 6 | CaMKII-bind-CaM | NonOsc_Ca_ IP3metabolism Accession No. 31 | CaMKII Pathway No. 145 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | 7 | CaMKII-bind-CaM | Osc_Ca_ IP3metabolism Accession No. 32 | CaMKII Pathway No. 159 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | 8 | CaMKII-bind-CaM | CaMKII Accession No. 33 | CaMKII Pathway No. 174 | 0.2 uM^-1 s^-1 | 2700 s^-1 | Kd(bf) = 13500(uM) | - | Substrate: CaM CaMKII
Product: CaMKII-CaM
| 9 | CaMKII-bind-CaM | CaMKII_2003 Accession No. 49 | CaMKII Pathway No. 202 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kb/Kf = 6e4 #/cell. Rate is fast (see Hanson et al Neuron 12 943-956 1994) so lets say kb = 10. This gives kf = 1.6667e-4 H&S AnnRev Biochem 92 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | 10 | CaMKII-bind-CaM | MAPK_network_ 2003 Accession No. 50 | CaMKII Pathway No. 216 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kb/Kf = 6e4 #/cell. Rate is fast (see Hanson et al Neuron 12 943-956 1994) so lets say kb = 10. This gives kf = 1.6667e-4 H&S AnnRev Biochem 92 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. |
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camkii acting as a Substrate in a Reaction |
| Name | Accession Name Accession No. | Pathway Name Pathway No. | Kf | Kb | Kd | tau | Reagents | Keq is calculated only for first order reactions.
Kd is calculated only for second order reactions. [ nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules] 6 | basal-activity | fig4_synapse Accession No. 3 | CaMKII Pathway No. 26 | 0.003 s^-1 | 0 s^-1 | - | - | Substrate: CaMKII
Product: CaMKII-thr286
| 7 | CaMKII-bind-CaM | Synaptic_ Network Accession No. 16 | CaMKII Pathway No. 80 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | 8 | CaMK-thr286-bind -CaM | Synaptic_ Network Accession No. 16 | CaMKII Pathway No. 80 | 1000.2 uM^-1 s^-1 | 0.1 s^-1 | Kd(bf) = 0.0001(uM) | - | Substrate: CaMKII-thr286 CaM-Ca4
Product: CaMKII-thr286*-C aM
| | Affinity is up 1000X over the unphosphorylated CaMKII, which makes the Kd of 0.1 nM. See Hanson et al 1994 Neuron 12:943-956. Time to release is about 20 sec, so the kb is OK at 0.1/sec. as tested by a few runs. | 9 | basal-activity | Synaptic_ Network Accession No. 16 | CaMKII Pathway No. 80 | 0.003 s^-1 | 0 s^-1 | - | - | Substrate: CaMKII
Product: CaMKII-thr286
| | This reaction represents one of the unknowns in CaMK-II biochemistry: what maintains the basal level of phosphorylation on thr 286 ? See Hanson and Schulman Ann Rev Biochem 1992 61:559-601, specially pg 580, for review. I have not been able to find any compelling mechanism in the literature, but fortunately the level of basal activity is well documented. Lisman et al propose that the levels of PP1 are very low in the postsynaptic density, and PP2A is excluded from the PSD, and this would lead to autophosphorylation at a sustained level. | 10 | CaMKII-bind-CaM | NonOsc_Ca_ IP3metabolism Accession No. 23 | CaMKII Pathway No. 106 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. |
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camkii acting as a Product in a Reaction |
| Name | Accession Name Accession No. | Pathway Name Pathway No. | Kf | Kb | Kd | tau | Reagents | Keq is calculated only for first order reactions.
Kd is calculated only for second order reactions. [ nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules] 6 | basal-activity | fig4_synapse Accession No. 3 | CaMKII Pathway No. 26 | 0.003 s^-1 | 0 s^-1 | - | - | Substrate: CaMKII
Product: CaMKII-thr286
| 7 | CaMKII-bind-CaM | Synaptic_ Network Accession No. 16 | CaMKII Pathway No. 80 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. | 8 | CaMK-thr286-bind -CaM | Synaptic_ Network Accession No. 16 | CaMKII Pathway No. 80 | 1000.2 uM^-1 s^-1 | 0.1 s^-1 | Kd(bf) = 0.0001(uM) | - | Substrate: CaMKII-thr286 CaM-Ca4
Product: CaMKII-thr286*-C aM
| | Affinity is up 1000X over the unphosphorylated CaMKII, which makes the Kd of 0.1 nM. See Hanson et al 1994 Neuron 12:943-956. Time to release is about 20 sec, so the kb is OK at 0.1/sec. as tested by a few runs. | 9 | basal-activity | Synaptic_ Network Accession No. 16 | CaMKII Pathway No. 80 | 0.003 s^-1 | 0 s^-1 | - | - | Substrate: CaMKII
Product: CaMKII-thr286
| | This reaction represents one of the unknowns in CaMK-II biochemistry: what maintains the basal level of phosphorylation on thr 286 ? See Hanson and Schulman Ann Rev Biochem 1992 61:559-601, specially pg 580, for review. I have not been able to find any compelling mechanism in the literature, but fortunately the level of basal activity is well documented. Lisman et al propose that the levels of PP1 are very low in the postsynaptic density, and PP2A is excluded from the PSD, and this would lead to autophosphorylation at a sustained level. | 10 | CaMKII-bind-CaM | NonOsc_Ca_ IP3metabolism Accession No. 23 | CaMKII Pathway No. 106 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| | This is tricky. There is some cooperativity here arising from interactions between the subunits of the CAMKII holoenzyme. However, the stoichiometry is 1. Kd = 0.1 uM. Rate is fast (see Hanson et al Neuron 12 943-956 1994) Hanson and Schulman 1992 AnnRev Biochem 61:559-601 give tau for dissoc as 0.2 sec at low Ca, 0.4 at high. Low Ca = 100 nM = physiol. |
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