UniProt ID | CHMP5_DROME | |
---|---|---|
UniProt AC | Q9VVI9 | |
Protein Name | Charged multivesicular body protein 5 | |
Gene Name | Vps60 {ECO:0000312|FlyBase:FBgn0036740} | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 226 | |
Subcellular Localization |
Endosome membrane Peripheral membrane protein. |
|
Protein Description | Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and are delivered to lysosomes enabling degradation of membrane proteins (By similarity). Specifically down-regulates Notch signaling activity in the germarium, probably by facilitating Notch endocytosis. [PubMed: 24762813] | |
Protein Sequence | MNRLFGRGKPKEPGPSLNDCIAGVDARATNIEEKISNLEAELRKYREQMSKMREGPAKNSVKQKALRVLKQKKAYEQQAESLRNQSFNMEQANYAAQSLKDTQATVAAMKDGVKQMKTEYKKINIDQIEDIQDDMADMFEQADEVQEALGRTYGMPEVDDDDLQAELDALGDEIALDDDTSYLDDVVKAPEAPSREPGADSIVPGKSTIETDEFGLPKIPTSLKTT | |
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 |
---|---|---|---|---|---|
86 | Phosphorylation | AESLRNQSFNMEQAN HHHHHHCCCCHHHHH | 23.33 | 19429919 | |
94 | Phosphorylation | FNMEQANYAAQSLKD CCHHHHHHHHHHHHH | 13.31 | 19429919 | |
201 | Phosphorylation | SREPGADSIVPGKST CCCCCCCCCCCCCCE | 25.58 | 22817900 | |
226 | Phosphorylation | IPTSLKTT------- CCCCCCCC------- | 34.72 | 18327897 |
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 CHMP5_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CHMP5_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 CHMP5_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NOTCH_DROME | N | genetic | 24762813 |
Kegg Drug | ||||||
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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-201, AND MASSSPECTROMETRY. | |
"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-226, AND MASSSPECTROMETRY. |