NCBS Home page
Accession List
Pathway List
Search
Authorized Users
Help
News archives

Enter a Search String

Special character and space not allowed in the query term. Search string should be at least 2 characters long.
Search in: Search for Match By

Molecule Parameter List for IFNRJ2*-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
IFNRJ2*-SHP-2 participated asMoleculeSum total ofEnzymeSubstrate of an enzymeProduct of an enzymeSubstrate in ReactionProduct in Reaction
No. of occurrences1000022

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*-SHP-2 acting as a Molecule in  
SOCS1_knockout Network
NameAccession NamePathway NameInitial Conc.
(uM)
Volume
(fL)
Buffered
IFNRJ2*-SHP-2SOCS1_knockout
Accession No. : 67
SOCS1_knockout
Pathway No. : 294
00.0016667No
Phosphorylated IFNRJ dimer bound to SH2 domain containing tyrosine phosphatase 2 Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196

IFNRJ2*-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
  • 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
  • SOCS1_
    binding[3]
  • 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*-SHP-2
    SOCS1

    Product
  • SOCS1-IFNR2*-SHP
    2

  •   Binding reaction of SOCS1 kf = 20/sec/uM kb = 0.1/sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-194.

    IFNRJ2*-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
    1SOCS1_unbind[1]SOCS1_knockout
    Accession No. : 67
    SOCS1_knockout
    Pathway No. : 294
    0.0005
    (s^-1)
    0
    (s^-1)
    --Substrate
  • SOCS1-IFNR2*-SHP
    2


    Product
    IFNRJ2*-SHP-2
  •   Unbinding reaction of SOCS1 kf = 0.0005/sec kb = 0/sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196.
    2
  • 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



    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.