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Molecule Parameter List for IFNRJ2*-STAT1c

The statistics table lists the distribution of a molecule acting either as a substrate, product, enzyme or as a molecule within the network.
The text color of a molecule is highlighted by color.
Statistics
IFNRJ2*-STAT1c participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000032

Accession and Pathway Details
Accession NameAccession No.Accession TypePathway Link
SOCS1_knockout67Pathway
SOCS1_knockout 
This model was taken from the Yamada S et al. FEBS Letters 2003 Jan 16;534(1-3):190-6
This model shows the control mechanism of Jak-Stat pathway, here SOCS1 (Suppressor of cytokine signaling-I) was identified as the negative regulator of Jak and STAT signal transduction pathway. This is the knockout version of Jak-Stat pathway in this model the SOCS1 has been knocked out i.e it formation is not shown.
The graphs are almost similar to the graphs as shown in the paper but STAT1n graph has some ambiguities. Thanks to Dr Satoshi Yamada for clarifying some of those ambiguities and providing the values used in the simulations.

IFNRJ2*-STAT1c acting as a Molecule in  
SOCS1_knockout Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
IFNRJ2*-STAT1cSOCS1_knockout
Accession No. : 67
SOCS1_knockout
Pathway No. : 294
00.0016667No
STAT1c complexed with phosphorylated IFNRJ dimer Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196

IFNRJ2*-STAT1c acting as a Substrate in a reaction in  
SOCS1_knockout Network
Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reaction are not consider.
 NameAccession NamePathway NameKfKbKdtauReagents
1
  • STAT1c_
    activation
  • SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    0.4
    (s^-1)
    0
    (uM^-1 s^-1)
    --Substrate
    IFNRJ2*-STAT1c

    Product
    IFNRJ2*
    STAT1c*
      Dimerisation of the RJ complex leads to the phosphorylation of several tyrosine residues by JAK Kf = 0.4 /sec Kb = 0 /M/sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196
    2
  • IFNRJ2*-STAT1c_
    bind_SHP2
  • SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    1
    (uM^-1 s^-1)
    0.2
    (s^-1)
    Kd(bf) = 0.2(uM)-Substrate
    IFNRJ2*-STAT1c
    SHP-2

    Product
  • IFNRJ2*-STAT1c-S
    HP2

  •   Binding of IFNRJ2*-STAT1c to SHP2 kf = 1/sec/uM kb = 0.2/sec Appendix, Satoshi Yamada 2003 FEBS Letters 534:190-196.
    3
  • SOCS1c_
    binding[2]
  • SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    20
    (uM^-1 s^-1)
    0.1
    (s^-1)
    Kd(bf) = 0.005(uM)-Substrate
    IFNRJ2*-STAT1c
    SOCS1

    Product
  • SOCS1-IFNRJ2*-ST
    AT1c

  •   Binding reaction of SOCS1 kf = 20/sec/uM kb = 0.1/sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196.

    IFNRJ2*-STAT1c acting as a Product in a reaction in  
    SOCS1_knockout Network
    Kd is calculated only for second order reactions, like nA+nB <->nC or nA<->nC+nD, where n is number and A,B,C,D are molecules, where as for first order reactions Keq is calculated. Kd for higher order reaction are not consider.
     NameAccession NamePathway NameKfKbKdtauReagents
    1SOCS1_unbindSOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    0.0005
    (s^-1)
    0
    (s^-1)
    --Substrate
  • SOCS1-IFNRJ2*-ST
    AT1c


    Product
    IFNRJ2*-STAT1c
  •   Ubinding reaction of SOCS1 kf = 0.0005/sec kb = 0/sec Appendix, Satoshi Yamada et al 2003 FEBS Letters, 534:190-196.
    2
  • STAT1c_
    binding[1]
  • SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    8
    (uM^-1 s^-1)
    0.8
    (s^-1)
    Kd(bf) = 0.1(uM)-Substrate
    IFNRJ2*
    STAT1c

    Product
    IFNRJ2*-STAT1c
      Binding of STAT1c to JAK-IFNR phosphorylated dimer Kf = 8*10e+06 /M/sec = 8/uM/sec Kb = 0.8 /sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196



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