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Molecule List for Accession CaMKII_model3 (Accession Number63)

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The entries are grouped according to Pathway Number and are alternately color coded using  and  color.
  NamePathway Name / 
Pathway No.
Accession
Type
Initial
Conc.

(uM)
Volume
(fL)
BufferedSum Total Of
1 CaM-Ca4
  • Shared_Object_
    CaMKII_model3

    Pathway No. 263
  • Network00.09No
    2 PP1-active
  • Shared_Object_
    CaMKII_model3

    Pathway No. 263
  • Network1.80.09No
        Cohen et al Meth Enz 159 390-408 is main source of info conc = 1.8 uM
    3 Ca
  • Shared_Object_
    CaMKII_model3

    Pathway No. 263
  • Network0.080.09No
    4 PKA-active
  • Shared_Object_
    CaMKII_model3

    Pathway No. 263
  • Network00.09No
    5 CaMKII CaMKII

    Pathway No. 264
    Network200.09No
        Huge conc of CaMKII. In PSD it is 20-40% of protein, so we assume it is around 2.5% of protein in spine as a whole. This level is so high it is unlikely to matter much if we are off a bit.
    6 CaMKII-CaM CaMKII

    Pathway No. 264
    Network00.09No
    7 
  • CaMKII-thr286*-C
    aM
  •  CaMKII

    Pathway No. 264
    Network00.09No
        From Hanson and Schulman, the thr286 is responsible for autonomous activation of CaMKII.
    8 CaMKII*** CaMKII

    Pathway No. 264
    Network00.09No
        From Hanson and Schulman, the CaMKII does a lot of autophosphorylation just after the CaM is released. This prevents further CaM binding and renders the enzyme quite independent of Ca.
    9 CaMKII-thr286 CaMKII

    Pathway No. 264
    Network00.09No
        I am not sure if we need to endow this one with a lot of enzs. It is likely to be a short-lived intermediate, since it will be phosphorylated further as soon as the CAM falls off.
    10 CaMK-thr305 CaMKII

    Pathway No. 264
    Network00.09No
        This forms due to basal autophosphorylation, but I think it has to be considered as a pathway even if some CaM is floating around. In either case it will tend to block further binding of CaM, and will not display any enzyme activity. See Hanson and Schulman JBC 267:24 pp17216-17224 1992
    11 CaM CaM

    Pathway No. 265
    Network26.33330.09No
        There is a LOT of this in the cell: upto 1% of total protein mass. (Alberts et al) Say 25 uM. Meyer et al Science 256 1199-1202 1992 refer to studies saying it is comparable to CaMK levels.
    12 CaM-PSD CaM

    Pathway No. 265
    Network26.33330.01No
        There is a LOT of this in the cell: upto 1% of total protein mass. (Alberts et al) Say 25 uM. Meyer et al Science 256 1199-1202 1992 refer to studies saying it is comparable to CaMK levels.
    13 CaM-Ca3
  • Shared_Object_
    CaMKII_model3

    Pathway No. 263
  • Network00.09No
    14 CaM-TR2-Ca2
  • Shared_Object_
    CaMKII_model3

    Pathway No. 263
  • Network00.09No
        This is the intermediate where the TR2 end (the high-affinity end) has bound the Ca but the TR1 end has not.
    15 I1 PP1

    Pathway No. 266
    Network1.80.09No
        I1 is a 'mixed' inhibitor, but at high enz concs it looks like a non-compet inhibitor (Foulkes et al Eur J Biochem 132 309-313 9183). We treat it as non-compet, so it just turns the enz off without interacting with the binding site. Cohen et al ann rev bioch refer to results where conc is 1.5 to 1.8 uM. In order to get complete inhib of PP1, which is at 1.8 uM, we need >= 1.8 uM.
    16 I1* PP1

    Pathway No. 266
    Network00.09No
        Dephosph is mainly by PP2B
    17 PP1-I1* PP1

    Pathway No. 266
    Network00.09No
    18 PP1-I1 PP1

    Pathway No. 266
    Network00.09No
    19 PP2A
  • Shared_Object_
    CaMKII_model3

    Pathway No. 263
  • Network0.11110.09No
    20 CaNAB-Ca4
  • Shared_Object_
    CaMKII_model3

    Pathway No. 263
  • Network00.09No

     
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