| UniProt ID | AXN_DROME | |
|---|---|---|
| UniProt AC | Q9V407 | |
| Protein Name | Axin | |
| Gene Name | Axn | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 745 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Inhibitor of the WG signaling pathway. Down-regulates beta-catenin (armadillo=ARM). Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B (zeste-white 3=ZW3).. | |
| Protein Sequence | MSGHPSGIRKHDDNECSGPRPPVPGEESRVKKMTEGVADTSKNSSPSYLNWARTLNHLLEDRDGVELFKKYVEEEAPAYNDHLNFYFACEGLKQQTDPEKIKQIIGAIYRFLRKSQLSISDDLRAQIKAIKTNPEIPLSPHIFDPMQRHVEVTIRDNIYPTFLCSEMYILYIQQMSAQQERCTSSGATGSGSAGSSGSGGSSLAGACALPPTTASGKQQLPQLVPPGAFINLPVSSVSGPPAGTCSASGSVYGPSTSASSSGSISATDTLPRSSTLPTLHEDSVLSLCDDFEKVQMQEGGGSLGSGSVGAGARAPDYPIRLTRDLLIATQKRRLEIRPPGAHGYVYNPSTTNTSYVPNSRVDSERASVSSGGRTDSDTMSISSCSMDGRPYIQRRHSSTESKAIRQSAMANKETNTFQVIPRTQRLHSNEHRPLKEEELVSLLIPKLEEVKRKRDLEERARERNPGAALLTNERSSASDRAFAEAIREKFALDEDNDQDILDQHVSRVWKDQTPHRSPGTMSPCPPIPSRRRTATHDSGMVSDGAMSLSGHSMKHSKSMPDHSSCSRKLTNKWPSMNTDSGISMFSADTVTKYKDASSRSGSSTASKLEEAKRRLEDEPRRSRRYAQPPMQHLSQQPLASFSSSSSGGSISLPHQPPPLPAKPPETIVVFSFCEEPVPYRIKIPGTQPTLRQFKDYLPRRGHFRFFFKTHCEDPDSPVIQEEIVNDSDILPLFGDKAMGLVKPSD | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | VADTSKNSSPSYLNW CCCCCCCCCHHHHHH | 47.57 | 19429919 | |
| 45 | Phosphorylation | ADTSKNSSPSYLNWA CCCCCCCCHHHHHHH | 27.53 | 19429919 | |
| 302 | Phosphorylation | QMQEGGGSLGSGSVG EEECCCCCCCCCCCC | 32.60 | 25749252 | |
| 305 | Phosphorylation | EGGGSLGSGSVGAGA CCCCCCCCCCCCCCC | 32.94 | 25749252 | |
| 307 | Phosphorylation | GGSLGSGSVGAGARA CCCCCCCCCCCCCCC | 21.05 | 25749252 | |
| 428 | Phosphorylation | PRTQRLHSNEHRPLK CCCCCCCCCCCCCCC | 48.80 | 22817900 | |
| 513 | Phosphorylation | SRVWKDQTPHRSPGT HHHHHCCCCCCCCCC | 31.06 | 19429919 | |
| 517 | Phosphorylation | KDQTPHRSPGTMSPC HCCCCCCCCCCCCCC | 25.34 | 19429919 | |
| 520 | Phosphorylation | TPHRSPGTMSPCPPI CCCCCCCCCCCCCCC | 20.19 | 19429919 | |
| 522 | Phosphorylation | HRSPGTMSPCPPIPS CCCCCCCCCCCCCCC | 24.16 | 19429919 |
| 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 AXN_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AXN_DROME !! | ||||||
* 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 AXN_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RBF_DROME | Rbf | genetic | 24809668 | |
| ARM_DROME | arm | genetic | 23444354 | |
| DSH_DROME | dsh | genetic | 12781135 | |
| WNTG_DROME | wg | genetic | 12781135 | |
| SALM_DROME | salm | genetic | 23444354 | |
| TNKS_DROME | Tnks | genetic | 24768997 | |
| PYGO_DROME | pygo | genetic | 12015286 | |
| PANG1_DROME | pan | genetic | 11290291 | |
| PANG2_DROME | pan | genetic | 11290291 | |
| PANG1_DROME | pan | genetic | 19502486 | |
| PANG2_DROME | pan | genetic | 19502486 | |
| DSH_DROME | dsh | physical | 22736244 | |
| GNAO_DROME | Galphao | physical | 19705439 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-513; SER-517 ANDSER-522, AND MASS SPECTROMETRY. | |