| + |
SRC | up-regulates activity 
phosphorylation
|
SDHA |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276420 |
Tyr215 |
SLRYDTSyFVEYFAL |
Homo sapiens |
T-98G Cell |
| pmid |
sentence |
| 22823520 |
Phosphorylation-site analysis selects c-Src targets, including NDUFV2 (NADH dehydrogenase [ubiquinone] flavoprotein 2) at Tyr(193) of respiratory complex I and SDHA (succinate dehydrogenase A) at Tyr(215) of complex II. The phosphorylation of these sites by c-Src is supported by an in vivo assay using cells expressing their phosphorylation-defective mutants. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGR |
phosphorylation
|
SDHA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262872 |
Tyr543 |
CGKISKLyGDLKHLK |
in vitro |
|
| pmid |
sentence |
| 17997986 |
Here, we provide evidence that the flavoprotein of succinate dehydrogenase and aconitase are "in vitro" substrates of Fgr tyrosine kinase. Fgr phosphorylates flavoprotein of succinate dehydrogenase at Y535 and Y596 and aconitase at Y71, Y544 and Y665. Further experiments will be necessary to verify if Fgr is the tyrosine kinase responsible for the tyrosine phosphorylation of these proteins in vivo and to elucidate the role of these phosphorylations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262873 |
Tyr604 |
YKVRIDEyDYSKPIQ |
in vitro |
|
| pmid |
sentence |
| 17997986 |
Here, we provide evidence that the flavoprotein of succinate dehydrogenase and aconitase are "in vitro" substrates of Fgr tyrosine kinase. Fgr phosphorylates flavoprotein of succinate dehydrogenase at Y535 and Y596 and aconitase at Y71, Y544 and Y665. Further experiments will be necessary to verify if Fgr is the tyrosine kinase responsible for the tyrosine phosphorylation of these proteins in vivo and to elucidate the role of these phosphorylations. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
SDHA | form complex 
binding
|
Mitochondrial respiratory chain complex II |
0.95 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262188 |
|
|
|
|
| pmid |
sentence |
| 30030361 |
Complex II (EC 1.3.5.1) or succinate dehydrogenase (quinone) is shared between the TCA cycle and the ETC and has no proton pumping activity. It is composed of four nDNA-encoded subunits. The two hydrophilic catalytic subunits are SDHA/SDH1 and SDHB/SDH2. Hydrophobic subunits SDHC/SDH3 and SDHD/SDH4 constitute the cII membrane anchor, containing a haem b group and two CoQ binding sites |
|
| Publications: |
1 |
| + |
SDHA | form complex
binding
|
SDH |
0.95 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266271 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16143825 |
Mitochondrial succinate dehydrogenase (SDH) consists merely of four nuclearly encoded subunits. It participates in the electron transfer in the respiratory chain and in succinate catabolism in the Krebs cycle. The SDH enzyme, also known as respiratory chain complex II, faces the mitochondrial matrix and is bound to the inner membrane. Four nuclear genes encode the four subunits, SDHA (15 exons), SDHB (8 exons), SDHC (6 exons) and SDHD (4 exons), mapping on to chromosomes 5p15, 1p35-p36.1, 1q21 and 11q23, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Citric acid cycle |
3.0
SDHA
- 
- 