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Molecule Parameter List for SHP-2

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
SHP-2 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000044

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.

SHP-2 acting as a Molecule in  
SOCS1_knockout Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
SHP-2SOCS1_knockout
Accession No. : 67
SOCS1_knockout
Pathway No. : 294
0.10.0016667No
SHP-2: SH2 domain-containing tyrosine phosphatase 2 SHP-2 = 100nM = 0.1uM Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196

SHP-2 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
  • SHP-2_
    binding[1]
  • 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
    SHP-2
  • SOCS1-IFNRJ2*-ST
    AT1c


    Product
  • SOCS1-IFNRJ2*-ST
    AT1c-SHP-2

  •   Binding of SHP-2 to JAK-IFNR phosphorylated dimer complexed with SOCS1 and STAT1c Kf = 1*10e+06 /M/sec = 1/uM/sec Kb = 0.2 /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.
    3SHP2_binding[2]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
    SHP-2
    SOCS1-IFNRJ2*

    Product
  • SOCS1-IFNR2*-SHP
    2

  •   SHP2 binding reaction kf = 1/sec/uM kb = 0.2/sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534;190-196.
    4
  • SHP-2_
    binding[3]
  • 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*
    SHP-2

    Product
    IFNRJ2*-SHP-2
      Binding of SHP-2 to JAK-IFNR phosphorylated dimer Kf = 1*10e+06 /M/sec = 1/uM/sec Kb = 0.2 /sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196

    SHP-2 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
    1
  • IFNRJ2*_
    dephosphorylatio
    n
  • SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    0.003
    (s^-1)
    0
    (uM^-1 s^-1)
    --Substrate
    IFNRJ2*-SHP-2

    Product
    IFNRJ2
    SHP-2
      SHP-2 dephosphorylates JAK-IFNR dimer Kf = 0.003 /sec Kb = 0 /uM/sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196
    2
  • dephospo_
    IFNRJ2*
  • SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    0.003
    (s^-1)
    0
    (uM^-2 s^-1)
    --Substrate
  • IFNRJ2*-STAT1c-S
    HP2


    Product
    IFNRJ2
    SHP-2
    STAT1c
  •   Dephosphoryaltion of IFNRJ2* kf = 0.003/sec kb = 0/sec/uM^2 Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196.
    3
  • Disso_
    SOCS1-IFNRJ2*-SH
    P2
  • SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    0.003
    (s^-1)
    0
    (uM^-2 s^-1)
    --Substrate
  • SOCS1-IFNR2*-SHP
    2


    Product
    IFNRJ2
    SHP-2
    SOCS1
  •   Dissociation reaction of SOCS1-IFNRJ2*-SHP2 kf = 0.003/sec kb = 0/sec/uM^2 Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196.
    4
  • IFNRJ2*_
    dephospo
  • SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    0.003
    (s^-1)
    0
    (uM^-3 s^-1)
    --Substrate
  • SOCS1-IFNRJ2*-ST
    AT1c-SHP-2


    Product
    IFNRJ2
    SHP-2
    SOCS1
    STAT1c
  •   SHP-2 dephosphorylates JAK-IFNR dimer complexed with SOCS1 and STAT1c Kf = 0.003 /sec Kb = 0 /sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196



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