| UniProt ID | MYL9_MOUSE | |
|---|---|---|
| UniProt AC | Q9CQ19 | |
| Protein Name | Myosin regulatory light polypeptide 9 | |
| Gene Name | Myl9 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 172 | |
| Subcellular Localization | ||
| Protein Description | Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion.. | |
| Protein Sequence | MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASLGKNPTDEYLEGMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSSKRAKAK ------CCCHHHHCC | 44.56 | - | |
| 19 | Phosphorylation | KKRPQRATSNVFAMF CCCCHHHHHHHHHHC | 24.03 | 27087446 | |
| 20 | Phosphorylation | KRPQRATSNVFAMFD CCCHHHHHHHHHHCC | 29.97 | 27087446 | |
| 29 | Phosphorylation | VFAMFDQSQIQEFKE HHHHCCHHHHHHHHH | 30.97 | 24925903 | |
| 51 | Ubiquitination | NRDGFIDKEDLHDML CCCCCCCHHHHHHHH | 48.59 | - | |
| 135 | Phosphorylation | TTMGDRFTDEEVDEM HHHHCCCCHHHHHHH | 43.31 | 17242355 | |
| 150 | Ubiquitination | YREAPIDKKGNFNYV HHHCCCCCCCCCCCC | 64.40 | 27667366 | |
| 151 | Ubiquitination | REAPIDKKGNFNYVE HHCCCCCCCCCCCCH | 56.17 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 19 | T | Phosphorylation | Kinase | CIT | P49025 | Uniprot |
| 19 | T | Phosphorylation | Kinase | DAPK3 | O43293 | PSP |
| 19 | T | Phosphorylation | Kinase | MYLK | P11799 | GPS |
| 19 | T | Phosphorylation | Kinase | ROCK2 | P70336 | Uniprot |
| 19 | T | Phosphorylation | Kinase | MLCK | - | Uniprot |
| 20 | S | Phosphorylation | Kinase | CIT | P49025 | Uniprot |
| 20 | S | Phosphorylation | Kinase | DAPK1 | Q80YE7 | Uniprot |
| 20 | S | Phosphorylation | Kinase | DAPK2 | Q8VDF3 | Uniprot |
| 20 | S | Phosphorylation | Kinase | DAPK3 | O43293 | PSP |
| 20 | S | Phosphorylation | Kinase | DAPK3 | O54784 | Uniprot |
| 20 | S | Phosphorylation | Kinase | MYLK | P11799 | GPS |
| 20 | S | Phosphorylation | Kinase | PAK1 | O88643 | Uniprot |
| 20 | S | Phosphorylation | Kinase | ROCK1 | P70335 | Uniprot |
| 20 | S | Phosphorylation | Kinase | ROCK2 | P70336 | Uniprot |
| 20 | S | Phosphorylation | Kinase | CDC42BP | - | Uniprot |
| 20 | S | Phosphorylation | Kinase | MLCK | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MYL9_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 MYL9_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of MYL9_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-20; SER-29 ANDTHR-135, AND MASS 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-19 AND SER-20, AND MASSSPECTROMETRY. | |