| UniProt ID | CISD1_MOUSE | |
|---|---|---|
| UniProt AC | Q91WS0 | |
| Protein Name | CDGSH iron-sulfur domain-containing protein 1 | |
| Gene Name | Cisd1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 108 | |
| Subcellular Localization |
Mitochondrion outer membrane Single-pass type III membrane protein . |
|
| Protein Description | Plays a key role in regulating maximal capacity for electron transport and oxidative phosphorylation. May be involved in Fe-S cluster shuttling and/or in redox reactions (By similarity).. | |
| Protein Sequence | MGLSSNSAVRVEWIAAVTFAAGTAALGYLAYKKFYAKENRTKAMVNLQIQKDNPKVVHAFDMEDLGDKAVYCRCWRSKKFPFCDGAHIKHNEETGDNVGPLIIKKKET | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MGLSSNSAVRVE ---CCCCCCCCCCHH | 39.59 | 28464351 | |
| 7 | Phosphorylation | -MGLSSNSAVRVEWI -CCCCCCCCCCHHHH | 30.04 | 28464351 | |
| 37 | Malonylation | AYKKFYAKENRTKAM HHHHHHCCCCCCCEE | 44.11 | 26320211 | |
| 37 | Acetylation | AYKKFYAKENRTKAM HHHHHHCCCCCCCEE | 44.11 | 23201123 | |
| 42 | Malonylation | YAKENRTKAMVNLQI HCCCCCCCEEEEEEE | 31.11 | 26320211 | |
| 55 | Acetylation | QIQKDNPKVVHAFDM EECCCCCCEEEEEEH | 64.24 | 23576753 | |
| 55 | Malonylation | QIQKDNPKVVHAFDM EECCCCCCEEEEEEH | 64.24 | 26320211 | |
| 55 | Ubiquitination | QIQKDNPKVVHAFDM EECCCCCCEEEEEEH | 64.24 | 27667366 | |
| 68 | Ubiquitination | DMEDLGDKAVYCRCW EHHHHCCCEEEEEEC | 37.64 | - | |
| 68 | Acetylation | DMEDLGDKAVYCRCW EHHHHCCCEEEEEEC | 37.64 | 23576753 | |
| 68 | Malonylation | DMEDLGDKAVYCRCW EHHHHCCCEEEEEEC | 37.64 | 26320211 | |
| 72 | S-nitrosocysteine | LGDKAVYCRCWRSKK HCCCEEEEEECCCCC | 2.02 | - | |
| 72 | Glutathionylation | LGDKAVYCRCWRSKK HCCCEEEEEECCCCC | 2.02 | 24333276 | |
| 72 | S-nitrosylation | LGDKAVYCRCWRSKK HCCCEEEEEECCCCC | 2.02 | 21278135 | |
| 78 | Acetylation | YCRCWRSKKFPFCDG EEEECCCCCCCCCCC | 50.27 | 24062335 | |
| 79 | Acetylation | CRCWRSKKFPFCDGA EEECCCCCCCCCCCC | 60.56 | 24062335 | |
| 79 | Malonylation | CRCWRSKKFPFCDGA EEECCCCCCCCCCCC | 60.56 | 26320211 | |
| 83 | S-nitrosocysteine | RSKKFPFCDGAHIKH CCCCCCCCCCCEEEC | 4.86 | - | |
| 83 | S-nitrosylation | RSKKFPFCDGAHIKH CCCCCCCCCCCEEEC | 4.86 | 21278135 | |
| 89 | Acetylation | FCDGAHIKHNEETGD CCCCCEEECCCCCCC | 30.43 | 24062335 | |
| 104 | Acetylation | NVGPLIIKKKET--- CCCCEEEEECCC--- | 51.29 | 23576753 | |
| 104 | Ubiquitination | NVGPLIIKKKET--- CCCCEEEEECCC--- | 51.29 | - | |
| 104 | Malonylation | NVGPLIIKKKET--- CCCCEEEEECCC--- | 51.29 | 26320211 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CISD1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CISD1_MOUSE !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CISD1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CISD1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104, AND MASS SPECTROMETRY. | |