| UniProt ID | CY24A_MOUSE | |
|---|---|---|
| UniProt AC | Q61462 | |
| Protein Name | Cytochrome b-245 light chain | |
| Gene Name | Cyba {ECO:0000312|MGI:MGI:1316658} | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 192 | |
| Subcellular Localization | Cell membrane. | |
| Protein Description | Critical component of the membrane-bound oxidase of phagocytes that generates superoxide. Associates with NOX3 to form a functional NADPH oxidase constitutively generating superoxide.. | |
| Protein Sequence | MGQIEWAMWANEQALASGLILITGGIVATAGRFTQWYFGAYSIAAGVLICLLEYPRGKRKKGSTMERCGQKYLTSVVKLFGPLTRNYYVRAALHFLLSVPAGFLLATILGTVCLAIASVIYLLAAIRGEQWTPIEPKPKERPQVGGTIKQPPTNPPPRPPAEVRKKPSEGEEEAASAGGPQVNPMPVTDEVV | |
| 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 |
|---|---|---|---|---|---|
| 139 | Ubiquitination | TPIEPKPKERPQVGG CCCCCCCCCCCCCCC | 72.91 | - | |
| 147 | Phosphorylation | ERPQVGGTIKQPPTN CCCCCCCCCCCCCCC | 21.05 | 26824392 | |
| 149 | Ubiquitination | PQVGGTIKQPPTNPP CCCCCCCCCCCCCCC | 57.50 | 26194095 | |
| 153 | Phosphorylation | GTIKQPPTNPPPRPP CCCCCCCCCCCCCCC | 68.02 | 23140645 | |
| 168 | Phosphorylation | AEVRKKPSEGEEEAA HHHCCCCCCCHHHHH | 68.09 | 25521595 | |
| 176 | Phosphorylation | EGEEEAASAGGPQVN CCHHHHHHCCCCCCC | 34.20 | 27742792 | |
| 188 | Phosphorylation | QVNPMPVTDEVV--- CCCCCCCCCCCC--- | 22.14 | 25367039 |
| 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 CY24A_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 147 | T | Oxidation |
| - |
| 147 | T | Phosphorylation |
| - |
| 149 | K | ubiquitylation |
| 26194095 |
* 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 CY24A_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of CY24A_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-176, ANDMASS SPECTROMETRY. | |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND MASSSPECTROMETRY. | |