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Molecule Parameter List for IFNRJ2* | 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 |
Accession and Pathway Details | |
| Accession Name | Accession No. | Accession Type | Pathway Link | Jak-Stat_
Pathway | 66 | Pathway |
Jak-Stat_Pathway | 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.
Note: There are a few ambiguities in the paper like initial concentration of IFN and some reactions were missing in the paper that were employed for obtaining the results. The graphs are almost similar to the graphs as shown in the paper but still some ambiguities regarding the concentration are there. Thanks to Dr Satoshi Yamada for clarifying some of those ambiguities and providing the values used in the simulations. |
IFNRJ2* acting as a Molecule in Jak-Stat_Pathway Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | IFNRJ2* | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 0 | 0.0016667 | No | | Phosphorylated dimer of IFN gamma liganding to the IFN gamma receptor that has JAK bound to its intracellular domain Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196 |
IFNRJ2* acting as a Substrate in a reaction in Jak-Stat_Pathway 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. |
| | Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | | 1 | STAT1c*_binding | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 5
(uM^-1 s^-1) | 0.5
(s^-1) | Kd(bf) = 0.1(uM) | - | Substrate
IFNRJ2*
STAT1c*
Product
IFNRJ2*-STAT1c*
| | | Binding of phosphorylated STAT1c to JAK-IFNR phosphorylated dimer Kf = 5*10e+06 /M/sec = 5/uM/sec Kb = 0.5 /sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196 | | 2 | STAT1c_
binding[1] | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 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 | | 3 | SOCS1_
binding[1] | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 20
(uM^-1 s^-1) | 0.1
(s^-1) | Kd(bf) = 0.005(uM) | - | Substrate
IFNRJ2*
SOCS1
Product
SOCS1-IFNRJ2*
| | | Binding of SOCS1 to phosphorylated dimer of IFN gamma liganding to the IFN gamma receptor that has JAK bound to its intracellular domain Kf = 20*10e+06 /M/sec = 20/uM/sec Kb = 0.1 /sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196 | | 4 | SHP-2_
binding[3] | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 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 |
IFNRJ2* acting as a Product in a reaction in Jak-Stat_Pathway 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. |
| | Name | Accession Name | Pathway Name | Kf | Kb | Kd | tau | Reagents | | 1 | IFNRJ_
activation | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 0.005
(s^-1) | 0
(s^-1) | - | - | Substrate
IFNRJ2
Product
IFNRJ2*
| | | Dimerisation of the RJ complex leads to the phosphorylation of several tyrosine residues by JAK Kf = 0.005*10e+06 /M/sec = 0.005/uM/sec Kb = 0 /sec Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196 | | 2 | STAT1c_
activation | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 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 | | 3 | unbind_SOCS1[1] | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 0.0005
(s^-1) | 0
(s^-1) | - | - | Substrate
SOCS1-IFNRJ2*
Product
IFNRJ2*
| | | The unbinding reactoion of SOCS1 from SOCS1-IFNRJ2* kf = 0.0005/sec kb = 0/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
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