UniProt ID | COTL1_MOUSE | |
---|---|---|
UniProt AC | Q9CQI6 | |
Protein Name | Coactosin-like protein | |
Gene Name | Cotl1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 142 | |
Subcellular Localization | Cytoplasm . Cytoplasm, cytoskeleton . Nucleus . | |
Protein Description | Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity).. | |
Protein Sequence | MATKIDKEACRAAYNLVRDDGSAVIWVTFRYDGATIVPGDQGADYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGEDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIRSELKKAGGANYDAQSE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MATKIDKEA ------CCCHHCHHH | 20.01 | - | |
7 | Ubiquitination | -MATKIDKEACRAAY -CCCHHCHHHHHHHH | 51.16 | - | |
7 | Acetylation | -MATKIDKEACRAAY -CCCHHCHHHHHHHH | 51.16 | 22826441 | |
45 | Phosphorylation | PGDQGADYQHFIQQC CCCCCCCHHHHHHHC | 11.89 | 26026062 | |
52 | S-palmitoylation | YQHFIQQCTDDVRLF HHHHHHHCCCCCEEE | 2.30 | 28680068 | |
71 | Phosphorylation | FTTGDAMSKRSKFAL EECCCHHCHHHCEEE | 27.00 | 29176673 | |
75 | Acetylation | DAMSKRSKFALITWI CHHCHHHCEEEEEEC | 38.39 | 22826441 | |
102 | Acetylation | GTDKTLVKEVVQNFA CCCHHHHHHHHHHHH | 48.15 | 22826441 | |
102 | Ubiquitination | GTDKTLVKEVVQNFA CCCHHHHHHHHHHHH | 48.15 | - | |
110 | Acetylation | EVVQNFAKEFVISDR HHHHHHHHHHHCCCH | 47.77 | 22826441 | |
118 | Ubiquitination | EFVISDRKELEEDFI HHHCCCHHHHHHHHH | 72.19 | - | |
137 | Phosphorylation | KKAGGANYDAQSE-- HHHCCCCCCCCCC-- | 16.48 | 19854140 | |
141 | Phosphorylation | GANYDAQSE------ CCCCCCCCC------ | 47.17 | 25521595 |
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 COTL1_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of COTL1_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 COTL1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
LOX5_HUMAN | ALOX5 | physical | 11785969 | |
ACTG_MOUSE | Actg1 | physical | 11785969 | |
ACTB_MOUSE | Actb | physical | 11785969 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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 SER-141, AND MASSSPECTROMETRY. |