| UniProt ID | TRIP6_MOUSE | |
|---|---|---|
| UniProt AC | Q9Z1Y4 | |
| Protein Name | Thyroid receptor-interacting protein 6 | |
| Gene Name | Trip6 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 480 | |
| Subcellular Localization | Cytoplasm, cytoskeleton . Cell junction, focal adhesion . Nucleus . Cytoplasm . Shuttles between nucleus and cytoplasm. Colocalizes with actin. | |
| Protein Description | Relays signals from the cell surface to the nucleus to weaken adherens junction and promote actin cytoskeleton reorganization and cell invasiveness. Involved in lysophosphatidic acid-induced cell adhesion and migration. Acts as a transcriptional coactivator for NF-kappa-B and JUN, and mediates the transrepression of these transcription factors induced by glucocorticoid receptor (By similarity).. | |
| Protein Sequence | MSGPTWLPPKQPEPSRLPQGRSLPRGALGPPTAHGATLQPHPRVNFCPLPPEHCYQPPGVPEDRGPTWVGSHGTPQRLQGLPPDRGIIRPGSLDAEIDSLTSMLADLDGGRSHAPRRPDRQAFEAPPPHAYRGGSLKPSGGAVPTPMLPASHYGGPTPASYATASTPAGPAFPVQVKVAQPVRGCGLPRRGASQASGPLPGPHFPLTGRGEVWGAGYRSHREPGPGVPEGPSGVHIPAGGGRGGGHEPQGPLGQPPEEELERLTKKLVHDMSHPPSGEYFGRCGGCGEDVVGDGAGVVALDRVFHIGCFVCSTCRAQLRGQHFYAVERRAYCESCYVATLEKCSTCSEPILDRILRAMGKAYHPGCFTCVVCHRGLDGIPFTVDATSQIHCIEDFHRKFAPRCSVCGGAIMPEPGQEETVRIVALDRSFHIGCYKCEECGLLLSSEGECQGCYPLDGHILCKACSAWRIQELSATVTTDC | |
| 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 |
|---|---|---|---|---|---|
| 22 | Phosphorylation | SRLPQGRSLPRGALG CCCCCCCCCCCCCCC | 49.93 | 29514104 | |
| 25 | Methylation | PQGRSLPRGALGPPT CCCCCCCCCCCCCCC | 48.59 | 24129315 | |
| 25 | Asymmetric dimethylarginine | PQGRSLPRGALGPPT CCCCCCCCCCCCCCC | 48.59 | - | |
| 55 | Phosphorylation | PLPPEHCYQPPGVPE CCCHHHCCCCCCCCC | 26.43 | 22817900 | |
| 92 | Phosphorylation | RGIIRPGSLDAEIDS CCCCCCCCCHHHHHH | 26.26 | 26239621 | |
| 99 | Phosphorylation | SLDAEIDSLTSMLAD CCHHHHHHHHHHHHH | 38.93 | 23984901 | |
| 101 | Phosphorylation | DAEIDSLTSMLADLD HHHHHHHHHHHHHCC | 18.95 | 23984901 | |
| 102 | Phosphorylation | AEIDSLTSMLADLDG HHHHHHHHHHHHCCC | 19.66 | 23984901 | |
| 111 | Methylation | LADLDGGRSHAPRRP HHHCCCCCCCCCCCC | 30.69 | - | |
| 183 | Methylation | VKVAQPVRGCGLPRR EEEECCCCCCCCCCC | 41.17 | 12019297 | |
| 190 | Methylation | RGCGLPRRGASQASG CCCCCCCCCCCCCCC | 42.99 | 24129315 | |
| 193 | Phosphorylation | GLPRRGASQASGPLP CCCCCCCCCCCCCCC | 29.15 | 22817900 | |
| 196 | Phosphorylation | RRGASQASGPLPGPH CCCCCCCCCCCCCCC | 33.05 | 18846507 | |
| 207 | Phosphorylation | PGPHFPLTGRGEVWG CCCCCCCCCCCCCCC | 25.68 | 18846507 | |
| 209 | Methylation | PHFPLTGRGEVWGAG CCCCCCCCCCCCCCC | 32.63 | 24129315 | |
| 218 | Methylation | EVWGAGYRSHREPGP CCCCCCCCCCCCCCC | 25.68 | 12019327 | |
| 242 | Methylation | HIPAGGGRGGGHEPQ CCCCCCCCCCCCCCC | 43.81 | 24129315 | |
| 279 | Phosphorylation | SHPPSGEYFGRCGGC CCCCCCCCCCCCCCC | 18.17 | 29514104 | |
| 344 | Phosphorylation | VATLEKCSTCSEPIL EEEHHHHCCCCHHHH | 43.44 | 21454597 | |
| 345 | Phosphorylation | ATLEKCSTCSEPILD EEHHHHCCCCHHHHH | 29.53 | 21454597 | |
| 347 | Phosphorylation | LEKCSTCSEPILDRI HHHHCCCCHHHHHHH | 46.63 | 21454597 | |
| 419 | Phosphorylation | PEPGQEETVRIVALD CCCCCCCCEEEEEEE | 17.84 | - | |
| 428 | Phosphorylation | RIVALDRSFHIGCYK EEEEEECCEEEECEE | 22.35 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRIP6_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 TRIP6_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of TRIP6_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY. | |