| UniProt ID | MILT_DROME | |
|---|---|---|
| UniProt AC | Q960V3 | |
| Protein Name | Trafficking kinesin-binding protein milt {ECO:0000303|PubMed:12495622} | |
| Gene Name | milt | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 1122 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | Required for kinesin-mediated axonal transport of mitochondria to nerve terminals. The oocyte acquires the majority of its mitochondria by competitive bidirectional transport along microtubules mediated by the Milton adapter. Mitochondria enter the young oocyte en mass from interconnected germ cells to generate the large aggregate known as the Balbiani body. Milt and Miro form an essential protein complex that links Khc to mitochondria for light chain-independent, anterograde transport of mitochondria.. | |
| Protein Sequence | MTHVNNGEVMEKEMEPTGERERDRETAAGSGVHHRFLASASERDANSGNALEAAATKTKTGTTITNLEDLAFEACQNWSDLHQDFFITDDELEYEDELSLGSSIGGNIATTTTADAAVEGLITGEHQNEQLLMEVLCGNRVSQMTRAYDDIEAVTRLLEEKEKDLELTVQIGKELLTQNNALEARVADLETDLKASNDDRAQLVHELHKKNELISVLTNDADDGTDTDTPTMSKSITLDLLQRKVNSLLDENKSLKCEATQLAHQTDEVEEHERQLMADISAQLNDANSQYDNLSLELERQREENRLQHEQIVNLTARLAEAEMRLHQLTQDNDEHLSLLHVTKENQNALALELVEFKQRYEEVLALLHSAQDQLKQQRKRSQPQARSSFLGGLGTSGAGMGGSLFPPDSLHCELMESSLYSENSLDSGISGDSQRSADRISRMMMHMPSGGMSSSTMGGSVYAGAGNVPPYKRVFDTVRCAGKSGNYMDSGNVSMTQLGAMSMSSSSGPRMASMAYPAGSYYRGGSNQSLGVKTLSSESLNSQSDDGYPAQPSGVPGAPGAKELEAALKRLTPAEVLARRAMLSYAPAGTYNYDEPMGHGTGNVRNSDLPLGVRTPDSIMSTGSSGMSGSTNHMSASMTHQWRLPEKLQIIKPMEGSQTLHHWSRLATPTLSGLLDERPGVTIRGGRGLDDLGMQIYTLSDVEEDVSDDLPGKQFEAPGCTFTYTNSMVMHPDDGFVNDLSFLSQSQMSSRMASTSTSRQPSCPATPRAGLSRKNSCSTFSVNLGLAGMLNERGIKAVTPSALNTPAGPNFSPTVTPCNSPEGSPPRAQSPEPLFGLLSCGADLIRRKIVGDQHQQQQQKQRSSLSKQQQQKIMLSHLERRALRSLNLIEKVESIGLENIISAQRGLGSGIANRSSSPLSSGSLQSLHTSSNSIVDDIHFDRAQIKGVLHRGLKSPTPATASTSAAAAASGPGISTSSSTSAYNSDDSDDQGLVMKIKPSKSATPTTTGAAQSQPSSATTSNGTASETRLKQMQRQKSRRQLKNGMANQRPDLGTISGAGGGGRVRPDLGKVADSGSSSKLSTKRSEAKPAEEEEATPQTITQAFVGSVSSLLFGRKGGWL | |
| 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 |
|---|---|---|---|---|---|
| 229 | Phosphorylation | DDGTDTDTPTMSKSI CCCCCCCCCCCCHHH | 23.81 | 27794539 | |
| 235 | Phosphorylation | DTPTMSKSITLDLLQ CCCCCCHHHHHHHHH | 17.31 | 19429919 | |
| 237 | Phosphorylation | PTMSKSITLDLLQRK CCCCHHHHHHHHHHH | 22.70 | 19429919 | |
| 330 | Phosphorylation | EMRLHQLTQDNDEHL HHHHHHHHCCCHHHE | 27.57 | 19429919 | |
| 338 | Phosphorylation | QDNDEHLSLLHVTKE CCCHHHEEEEEECHH | 30.69 | 19429919 | |
| 343 | Phosphorylation | HLSLLHVTKENQNAL HEEEEEECHHHHCCH | 23.15 | 19429919 | |
| 831 | Phosphorylation | GSPPRAQSPEPLFGL CCCCCCCCCCCCHHH | 30.19 | 17372656 | |
| 918 | Phosphorylation | GIANRSSSPLSSGSL CCCCCCCCCCCCCCC | 30.98 | 12495622 |
| 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 MILT_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MILT_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 MILT_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PAX6_DROME | ey | physical | 14605208 | |
| MIRO_DROME | Miro | physical | 14605208 |
| 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 SER-918, 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 SER-831, AND MASSSPECTROMETRY. | |
