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Molecule Parameter List for Transcription_comp2 | 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 |
| Transcription_comp2 participated as | Molecule | Sum total of | Enzyme | Substrate of an enzyme | Product of an enzyme | Substrate in Reaction | Product in Reaction | | No. of occurrences | 1 | 0 | 1 | 0 | 0 | 0 | 0 |
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. |
Transcription_comp2 acting as a Molecule in Jak-Stat_Pathway Network
| Name | Accession Name | Pathway Name | Initial Conc.
(uM) | Volume
(fL) | Buffered | | Transcription_comp2 | Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 0.001 | 0.0016667 | Yes | | DNA to which STAT1*D and other transcription factors bound. Appendix, Sattoshi Yamada et al 2003 FEBS Letters 534;190-196. |
Transcription_comp2 acting as an Enzyme in Jak-Stat_Pathway Network
Enzyme Molecule /
Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | Transcription_
comp2 /
DNA
| Jak-Stat_
Pathway
Accession No. : 66 | Jak-Stat_
Pathway
Pathway No. : 293 | 0.4 | 0.01 | 4 | Classical Michaelis-Menten
V = Etot.S.Kcat/Km+S | Substrate
dup_
STAT1n*-STAT1n*
Product
mRNAVn
| | Translation of mRNAVn Km = 400nM = 0.4uM kcat = 0.01/sec Appendix, Satoshi Yamada 2003 FEBS Letters 534:190-196. |
| Database compilation and code copyright (C) 2022, Upinder S. Bhalla and NCBS/TIFR
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