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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. 1 | fig3_CaMKII/ Accession No. : 2 | Network / 2001-11-07 00:00:00 | Chemical | Molecule = 59 Enzyme = 29 Reaction = 29
| Molecule = 9 Enzyme = 4 Reaction = 1
| Generic mammalian / Neuronal | Synapse / Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. ( peer-reviewed publication ) | Quantitative match to experiments, Qualitative / Exact GENESIS implementation | | 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. | 2 | fig4_synapse/ Accession No. : 3 | Network / 2001-11-07 00:00:00 | Chemical | Molecule = 122 Enzyme = 56 Reaction = 70
| Molecule = 9 Enzyme = 4 Reaction = 1
| Generic mammalian / Neuronal | Synapse / Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. ( peer-reviewed publication ) | Quantitative match to experiments, Qualitative, Hypothetical / Exact GENESIS implementation | | 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. | 3 | Synaptic_ Network/ Accession No. : 16 | Network / 2001-12-12 00:00:00 | Chemical | Molecule = 148 Enzyme = 63 Reaction = 84
| Molecule = 8 Enzyme = 4 Reaction = 1
| Generic mammalian / Neuronal | Synapse / Bhalla US and Iyengar R. Science (1999) 283(5400):381-7. ( peer-reviewed publication ) | Quantitative match to experiments, Qualitative / Exact GENESIS implementation | | 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 | 4 | NOS_Phosph_ regulation/ Accession No. : 20 | Pathway / 2001-12-25 00:00:00 | Chemical | Molecule = 10 Enzyme = 4 Reaction = 2
| Molecule = 1 Enzyme = 1 Reaction = 0
| rat; Mammalian / Brain - Neuronal; expressed in E.coli | Cytosol / In-house | Quantitative match to experiments, Qualitative / Exact GENESIS implementation | | This model features the phosphorylation of rat brain neuronal NOS expressed in E. coli or Sf9 cells, which leads to a decrease in Vmax of the phosphorylated enzyme, with little change of both the Km for L-arginine and Kact for CaM. This is based on Hayashi Y. et al. J Biol Chem. (1999) 274(29):20597-602. They report of phosphorylatin being carried out by CaM kinases I alpha, II alpha and IV. The rates used have been obtained from their paper and from other reported experimental data. | 5 | NonOsc_Ca_ IP3metabolism/ Accession No. : 23 | Network / 2002-01-07 00:00:00 | Chemical | Molecule = 134 Enzyme = 48 Reaction = 81
| 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 detailed metabolism of Ins(145)P3, integrated with GPCR mediated PLCbeta activation and Ca release by the InsP3 receptor in the neuron. The calcium response is non-oscillatory. Mishra J, Bhalla US. Biophys J. 2002 Sep;83(3):1298-316. |
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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. 1 | CaMKII
Pathway No. : 235 | AMPAR_traff_ model0 Accession No. : 59 | Chemical / Network | Molecule = 25 Enzyme = 24 Reaction = 10
| Molecule = 21 Enzyme = 22 Reaction = 5
| Hayer A, Bhalla US PLoS Comput Biol. 2005 Jul;1(2):137-54. Epub 2005 Jul 29. ( Peer-reviewed publication ) / 2005-07-19 00:00:00 | | Related Pathway : 13, 26, 80, 106, 121, 145, 159, 174, 202, 216, 245, 258, 264, 272, 282, 322, 339, 357 | | This is model 0 from Hayer and Bhalla, PLoS Comput Biol 2005. It has a bistable model of AMPAR traffick, plus a
non-bistable model of CaMKII. This differs from the reference model (model 1) in that model0 lacks degradation and turno
ver reactions for AMPAR. | 2 | CaMKII
Pathway No. : 245 | AMPAR_traff_ model1 Accession No. : 60 | Chemical / Network | Molecule = 25 Enzyme = 24 Reaction = 10
| Molecule = 21 Enzyme = 22 Reaction = 5
| Hayer A, Bhalla US PLoS Comput Biol. 2005 Jul;1(2):137-54. Epub 2005 Jul 29. ( Peer-reviewed publication ) / 2005-07-19 00:00:00 | | Related Pathway : 13, 26, 80, 106, 121, 145, 159, 174, 202, 216, 235, 258, 264, 272, 282, 322, 339, 357 | | This is the basic model of AMPAR trafficking bistability. It is based on Hayer and Bhalla, PLoS Comput. Biol. 2005. It includes the degradation and turnover of AMPARs. The CaMKII portion of the model is not bistable. | 3 | Shared_Object_ AMPAR_CaMKII_ strong_coupling Pathway No. : 271 | AMPAR_CaMKII_ strong_coupling Accession No. : 64 | Chemical / Network | Molecule = 51 Enzyme = 148 Reaction = 16
| Molecule = 14 Enzyme = 19 Reaction = 4
| Hayer A, Bhalla US PLoS Comput Biol. 2005 Jul;1(2):137-54. Epub 2005 Jul 29. ( Peer-reviewed publication ) / 2005-07-19 00:00:00 | | Related Pathway :
| | This is a model of tight coupling between the AMPAR trafficking bistability, and the CaMKII autophosphorylation bistability. In this model, the CaMKII activity is self sustaining only when AMPAR is turned on. Further, CaMKII turns on when AMPAR is turned on. | 4 | CaMKII_PSD
Pathway No. : 292 | AMPAR_CaMKII_ weak_coupling Accession No. : 65 | Chemical / Network | Molecule = 14 Enzyme = 22 Reaction = 8
| Molecule = 11 Enzyme = 19 Reaction = 4
| Hayer A, Bhalla US PLoS Comput Biol. 2005 Jul;1(2):137-54. Epub 2005 Jul 29. ( Peer-reviewed publication ) / 2005-07-21 00:00:00 | | Related Pathway :
| | This is a model of weak coupling between the AMPAR traffikcing bistability, and the CaMKII autophosphorylation bistability. In this model, there are three stable states: Both off, AMPAR on, or both on. The fourth possible state: CaMKII on but AMPAR off, is not truly stable, since over the course of hours the AMPAR also turns on. | 5 | Shared_Object_ CaMKIII Pathway No. : 1093 | CaMKIII
Accession No. : 90 | Chemical / Network | Molecule = 15 Enzyme = 5 Reaction = 3
| Molecule = 4 Enzyme = 4 Reaction = 2
| Jain P, and Bhalla, U.S. PLoS Comput Biol. 2009 Feb;5(2). ( Peer-reviewed publication ) / 2009-02-12 00:00:00 | | Related Pathway :
| | CaMKIII is activated by Ca2+ and inactivated by S6K. Since CaMKIII inhibits eEF2, the net effect of Ca2+ on elongation is inhibitory and of S6K is excitatory |
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CamKII acting as a Molecule |
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CamKII acting as Summed Molecule |
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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] 1 | CaMKII-bind-CaM | fig3_CaMKII Accession No. 2 | CaMKII Pathway No. 13 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| 2 | CaMKII-bind-CaM | fig4_synapse Accession No. 3 | CaMKII Pathway No. 26 | 49.9998 uM^-1 s^-1 | 5 s^-1 | Kd(bf) = 0.1(uM) | - | Substrate: CaM-Ca4 CaMKII
Product: CaMKII-CaM
| 3 | 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. | 4 | 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. | 5 | CaMKII-bind-CaM | Osc_Ca_ IP3metabolism Accession No. 24 | CaMKII Pathway No. 121 | 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 Substrate in a Reaction |
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CamKII acting as a Product in a Reaction |
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| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR This Copyright is applied to ensure that the contents of this database remain freely available. Please see FAQ for details. |
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