| UniProt ID | TCTP_DROME | |
|---|---|---|
| UniProt AC | Q9VGS2 | |
| Protein Name | Translationally-controlled tumor protein homolog | |
| Gene Name | Tctp | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 172 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Involved in calcium binding and microtubule stabilization.. | |
| Protein Sequence | MKIYKDIITGDEMFADTYKMKLVDDVIYEVYGKLITRQGDDIKLEGANASAEEADEGTDITSESGVDVVLNHRLTECFAFGDKKSYTLYLKDYMKKVLAKLEEKSPDQVDIFKTNMNKAMKDILGRFKELQFFTGESMDCDGMVALVEYREINGDSVPVLMFFKHGLEEEKC | |
| 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 |
|---|---|---|---|---|---|
| 19 | Acetylation | EMFADTYKMKLVDDV HHHHHHHHCCCHHHH | 31.48 | 21791702 | |
| 21 | Acetylation | FADTYKMKLVDDVIY HHHHHHCCCHHHHHH | 41.00 | 21791702 | |
| 28 | Phosphorylation | KLVDDVIYEVYGKLI CCHHHHHHHHHHHHH | 10.13 | 19429919 | |
| 31 | Phosphorylation | DDVIYEVYGKLITRQ HHHHHHHHHHHHHCC | 9.15 | 19429919 | |
| 50 | Phosphorylation | KLEGANASAEEADEG EEECCCCCHHHCCCC | 35.70 | 22817900 | |
| 58 | Phosphorylation | AEEADEGTDITSESG HHHCCCCCCCCCCCC | 23.37 | 30478224 | |
| 61 | Phosphorylation | ADEGTDITSESGVDV CCCCCCCCCCCCCCE | 29.29 | 22817900 | |
| 62 | Phosphorylation | DEGTDITSESGVDVV CCCCCCCCCCCCCEE | 30.05 | 29892262 | |
| 84 | Acetylation | CFAFGDKKSYTLYLK EEECCCCCEEEEEHH | 54.13 | 21791702 | |
| 91 | Acetylation | KSYTLYLKDYMKKVL CEEEEEHHHHHHHHH | 33.00 | 21791702 | |
| 100 | Acetylation | YMKKVLAKLEEKSPD HHHHHHHHHHHHCHH | 52.88 | 21791702 | |
| 104 | Acetylation | VLAKLEEKSPDQVDI HHHHHHHHCHHHHHH | 58.89 | 21791702 | |
| 105 | Phosphorylation | LAKLEEKSPDQVDIF HHHHHHHCHHHHHHH | 36.67 | 22817900 | |
| 113 | Acetylation | PDQVDIFKTNMNKAM HHHHHHHHHHHHHHH | 39.05 | 21791702 | |
| 121 | Acetylation | TNMNKAMKDILGRFK HHHHHHHHHHHHHHH | 46.61 | 21791702 |
| 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 TCTP_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TCTP_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 TCTP_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| DYL1_DROME | ctp | physical | 14605208 | |
| SAP47_DROME | Sap47 | physical | 14605208 | |
| C1GLT_DROME | C1GalTA | physical | 14605208 | |
| CCNE_DROME | CycE | genetic | 17301792 | |
| ATM_DROME | tefu | genetic | 24352200 | |
| RHEB_DROME | Rheb | physical | 17301792 | |
| RPB1_DROME | RpII215 | physical | 27687497 | |
| RAD50_DROME | rad50 | physical | 24352200 | |
| BRM_DROME | brm | physical | 27687497 | |
| ATM_DROME | tefu | physical | 24352200 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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 SER-50; THR-58 AND THR-61,AND MASS SPECTROMETRY. | |
| "An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells."; Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.; Mol. Biosyst. 3:275-286(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASSSPECTROMETRY. | |