UniProt ID | MY61F_DROME | |
---|---|---|
UniProt AC | Q23979 | |
Protein Name | Myosin-IB | |
Gene Name | Myo61F | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 1035 | |
Subcellular Localization | Cytoplasm . Protein shifts from the basolateral to apical domain in enterocytes and follicle cells. | |
Protein Description | Involved in directing the movement of organelles along actin filaments.. | |
Protein Sequence | MASFNSQLKMETGLHERDRAGVQDFVLLENYQSEEAFIGNLKKRFQEDLIYTYIGQVLISVNPYKQLPIYTDDHVKAYRNKHFYEMPPHIFAVTDNAFRSLIEENRGQCVLISGESGSGKTEASKKVLQFIAACSGNQTTVEGVKDKLLKSNPVLEAFGNAKTNRNDNSSRFGKYMDIQFDFKGAPIGGNILNYLLEKSRVVAQMGGERNFHIFYQLLAGADEALLQELRLERALDTYSYLTDGLNGTVTRINDADSFKQVQQALTVIDFTKEEQREIFGIVASILHLGNVGFTEVEGNAKVNSRDLVVTAARLLGVNASELEAALTHRTIDARGDVVTSPLNQELAIYARDALAKAVYDRLFSWLVQRLNISLQAKETRASRNNVMGILDIYGFEIFQKNSFEQFCINFCNEKLQQLFIELTLKSEQDEYRREGIEWIPVEYFDNKVICNLIEEKHKGIISILDEECLRPGEPTDKTFLEKLTQKLAQHHHYVCHEKAPAHIKKIMLRDEFRLVHYAGEVTYSVNGFLDKNNDLLFRDLKETLSKAGNGIVRNCFPEKELRSLKRPETAITQFRASLNNLMDILMCKEPSYIRCIKPNDLQTANVFNDELVLHQVKYLGLMENLRVRRAGFAYRRTYELFLERYKSLSKSTWPNYKGPGGPKAGVQQLVKDLGWDEEKYRVGETKLFIRWPRTLFDTEDAYQEKKHEIAAIIQAHWKGLMQRRKYLKLRAQVIIMQSYCRRKLAQQAAKKRREAADKIRAFIKGFITRNDAPNGFNEEFIANAKRMWLLRLAKELPTKVLDKSWPHAPGHCEEASGILHRLHRLHLARIYRLKLTPQQKRQFELKVLAEKVFKGKKNNYASSVSTWFQEDRIPKEHIQRVNDFVASTFGSEQLKYQSFCTKFDRHGYKSRDRFILLSNKAIYVLDGKTYKQKHRLPLDKIDFTLTNHNDDLMVIRIPLDLKKDKGDLILIIPRIIEFSTYIIDTVGTASIVSIVDRNSLEHNVVKGKGGVIDIQTGAEPGVVRDKGHLVIIGTQ | |
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 |
---|---|---|---|---|---|
2 (in isoform 3) | Phosphorylation | - | 33.85 | 19429919 | |
7 (in isoform 3) | Phosphorylation | - | 46.32 | 19429919 | |
18 (in isoform 3) | Phosphorylation | - | 41.62 | 19429919 | |
304 | Phosphorylation | EGNAKVNSRDLVVTA ECCCEECHHHHHHHH | 30.11 | 17372656 | |
310 | Phosphorylation | NSRDLVVTAARLLGV CHHHHHHHHHHHHCC | 13.71 | 8201616 | |
999 | Phosphorylation | VSIVDRNSLEHNVVK EEEECCCCCCCCEEC | 35.71 | 19429919 | |
1034 | Phosphorylation | GHLVIIGTQ------ CEEEEEECC------ | 22.24 | 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 MY61F_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MY61F_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 MY61F_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
EFHD2_DROME | Swip-1 | physical | 22036573 | |
OPS5_DROME | Rh5 | physical | 22036573 | |
MY31D_DROME | Myo31DF | genetic | 22491943 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-304 AND THR-310, ANDMASS SPECTROMETRY. |