| UniProt ID | TMOD3_MOUSE | |
|---|---|---|
| UniProt AC | Q9JHJ0 | |
| Protein Name | Tropomodulin-3 | |
| Gene Name | Tmod3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 352 | |
| Subcellular Localization | Cytoplasm, cytoskeleton. | |
| Protein Description | Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity).. | |
| Protein Sequence | MALPFRKDLGDYKDLDEDELLGKLSESELKQLETVLDDLDPENALLPAGFRQKNQTSKSATGPFDRERLLSYLEKQALEHKDRDDYVPYTGEKKGKIFIPKQKPAQTLTEETISLDPELEEALTSASDTELCDLAAILGMHNLIADTPFCDVLGSSNGVNQERFPNVVKGEKILPVFDEPPNPTNVEESLKRIRENDARLVEVNLNNIKNIPIPTLKDFAKTLEANTHVKHFSLAATRSNDPVAVAFADMLKVNKTLKSLNMESNFITGAGVLALIDALRDNETLMELKIDNQRQQLGTSVELEMAKMLEENTNILKFGYQFTQQGPRTRAANAITKNNDLVRKRRIEGDHQ | |
| 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 |
|---|---|---|---|---|---|
| 12 | Phosphorylation | FRKDLGDYKDLDEDE CCCCCCCCCCCCHHH | 12.47 | 25159016 | |
| 23 | Ubiquitination | DEDELLGKLSESELK CHHHHHHHCCHHHHH | 49.13 | - | |
| 25 | Phosphorylation | DELLGKLSESELKQL HHHHHHCCHHHHHHH | 42.43 | 26824392 | |
| 27 | Phosphorylation | LLGKLSESELKQLET HHHHCCHHHHHHHHH | 44.87 | 26745281 | |
| 71 | Phosphorylation | FDRERLLSYLEKQAL CCHHHHHHHHHHHHH | 32.06 | 26824392 | |
| 72 | Phosphorylation | DRERLLSYLEKQALE CHHHHHHHHHHHHHH | 20.89 | 28833060 | |
| 75 | Ubiquitination | RLLSYLEKQALEHKD HHHHHHHHHHHHCCC | 37.97 | - | |
| 86 | Phosphorylation | EHKDRDDYVPYTGEK HCCCCCCCCCCCCCC | 13.96 | 25367039 | |
| 172 | Acetylation | PNVVKGEKILPVFDE CCCCCCCEEEECCCC | 59.20 | 23236377 | |
| 299 | Phosphorylation | NQRQQLGTSVELEMA HHHHHHCCHHHHHHH | 37.89 | 28066266 | |
| 300 | Phosphorylation | QRQQLGTSVELEMAK HHHHHCCHHHHHHHH | 16.28 | 28833060 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 71 | S | Phosphorylation | Kinase | AKT2 | P31751 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TMOD3_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 TMOD3_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASSSPECTROMETRY. | |