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 | ||
* 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 | ||||||
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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. |