| UniProt ID | SHEP_DROME | |
|---|---|---|
| UniProt AC | Q8MSV2 | |
| Protein Name | Protein alan shepard | |
| Gene Name | shep {ECO:0000312|FlyBase:FBgn0052423} | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 590 | |
| Subcellular Localization | ||
| Protein Description | Has a role in the perception of gravity.. | |
| Protein Sequence | MHPRYSPAPPPQQQQQMGGPPHQQQGGGGGGGVSMRGPSNAQQLPPQIPRSQNYSNGSSSSAAAAPLTSRSAFPGAPLTASAVALKGALPQRPPAMTSPAAAAAGAALAAGAPYRGAASWTPQGYAPAAAAAAAAVAQQAAYRYTAPLPQPAYAAYTPHTATTPATTTVSFLSQPVDYYWYGQRVPTAASPSNTNSSSSSNTGSQSGTLSTSLSNTTNTNTNMGPNGTVQNQNQQGGEQLSKTNLYIRGLQQGTTDKDLVNMCAQYGTIISTKAILDKTTNKCKGYGFVDFEQPAFAECAVKGLQGKGVQAQMAKQQEQDPTNLYIANLPPHFKETDLEAMLSKYGQVVSTRILRDQQMNSKGVGFARMESREKCEQIIQMFNGNTIPGAKDPLLVKFADGGPKKKNLFKTPDPNARAWRDVSAEGIPVAYDPTMQQNGVSVNVGTPIGVPYSRFSAPQVGGYPVAGSQWIPGYMMTQVDDQTSYSPQYMQMAAAPPLGVTSYKPEAVNQVQPRGISMMVSGDTGVPYGTMMPQLATLQIGNSYISPTYPYYAPPPTIIPTMPMTDSEQASTAASPDEAYTQYPHQAAPK | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MHPRYSPAPPPQ ---CCCCCCCCCCHH | 24.37 | 18327897 | |
| 67 (in isoform 2) | Phosphorylation | - | 6.11 | 21082442 | |
| 81 | Phosphorylation | PGAPLTASAVALKGA CCCCCCHHHHHHHCC | 20.31 | 21082442 | |
| 97 | Phosphorylation | PQRPPAMTSPAAAAA CCCCCCCCCHHHHHH | 33.39 | 21082442 | |
| 121 | Phosphorylation | YRGAASWTPQGYAPA CCCCCCCCCCCHHHH | 11.84 | 22817900 | |
| 125 | Phosphorylation | ASWTPQGYAPAAAAA CCCCCCCHHHHHHHH | 12.26 | 17372656 | |
| 142 | Phosphorylation | AVAQQAAYRYTAPLP HHHHHHHHHHCCCCC | 13.73 | 10731132 | |
| 162 (in isoform 1) | Phosphorylation | - | 34.17 | 21082442 | |
| 186 | Acetylation | YWYGQRVPTAASPSN EECCCCCCCCCCCCC | 37.29 | - | |
| 385 | Acetylation | IIQMFNGNTIPGAKD HHHHHCCCCCCCCCC | 34.50 | 19608861 | |
| 397 | Acetylation | AKDPLLVKFADGGPK CCCCEEEEECCCCCC | 13.32 | 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 SHEP_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SHEP_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 SHEP_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| SUHW_DROME | su(Hw) | physical | 23209434 | |
| CP190_DROME | Cp190 | physical | 23209434 | |
| MMD4_DROME | mod(mdg4) | physical | 23209434 |
| 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 TYR-5, AND MASSSPECTROMETRY. | |
| "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 TYR-125 AND TYR-142, ANDMASS SPECTROMETRY. | |
