Enter a Search String |
| Special character and space not allowed in the query term. Search string should be at least 2 characters long. |
Molecule Parameter List for dup_STAT1n*-STAT1n* | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| dup_STAT1n*-STAT1n* 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 | 1 | 0 | 2 | 0 | 0 | 0 |
Accession and Pathway Details |
| Accession Name | Accession No. | Accession Type | Pathway Link |
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. | |||
dup_STAT1n*-STAT1n* acting as a Molecule in Jak-Stat_Pathway Network
| Name | Accession Name | Pathway Name | Initial Conc. (uM) | Volume (fL) | Buffered | |
| dup_STAT1n*-STAT1n* | Pathway Accession No. : 66 | Pathway Pathway No. : 293 | 0 | 0.0016667 | No | |
| Duplicate of the STAT1c dimer Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196 | ||||||
dup_STAT1n*-STAT1n* acting as a Summed Molecule in Jak-Stat_Pathway Network
| Accession Name | Pathway Name | Target | Input |
Pathway Accession No. : 66 | Pathway Pathway No. : 293 | dup_STAT1n*-STAT1n* | STAT1n*-STAT1n* |
| Duplicate of the STAT1c dimer Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196 | |||
dup_STAT1n*-STAT1n* acting as a Substrate for an Enzyme in Jak-Stat_Pathway Network
| Enzyme Molecule / Enzyme Activity | Accession Name | Pathway Name | Km (uM) | kcat (s^-1) | Ratio | Enzyme Type | Reagents | |
| 1 | complex / DNA | Pathway Accession No. : 66 | Pathway Pathway No. : 293 | 0.4 | 0.01 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate STAT1n*-STAT1n* Product mRNASn |
| Km = 400nM = 0.4uM Vmax = 0.01 nM/sec. Assume [enz] = 1 nM, then kcat = 0.01/sec. Appendix, Satoshi Yamada et al 2003 FEBS Letters 534:190-196 | ||||||||
| 2 | comp2 / DNA | Pathway Accession No. : 66 | Pathway Pathway No. : 293 | 0.4 | 0.01 | 4 | Classical Michaelis-Menten V = Etot.S.Kcat/Km+S | Substrate STAT1n*-STAT1n* Product mRNAVn |
| Translation of mRNAVn Km = 400nM = 0.4uM kcat = 0.01/sec Appendix, Satoshi Yamada 2003 FEBS Letters 534:190-196. | ||||||||
color.