| UniProt ID | ENT5_YEAST | |
|---|---|---|
| UniProt AC | Q03769 | |
| Protein Name | Epsin-5 | |
| Gene Name | ENT5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 411 | |
| Subcellular Localization |
Cytoplasm. Endosome membrane Peripheral membrane protein. Found predominantly on endosomal structures. |
|
| Protein Description | Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).. | |
| Protein Sequence | MDSLSKKIQNLGIHDIRNAARFAQNVIVQYEPYQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLVVIEFLLLNVDTGDELNQIRSCLLTHKHILTREIAQFKVKFSNDGKMEIHERGIRKKGELILQYLEDSQFLKKERAKNKKNALKIRQQGESSIYNANQISTSASYDNIDDDEFDADADGFDSEMDANNVTNFNVPVETEANSNTRRRSHMEEQRRQRREILREQIKNKEQQRKRKQQQDSIPDLIDLDDSTSTTNNITIDNGNNDNKNNNINSNSDDDDDEFGDFQSETSPDTTAPKTSNSKIDDLLDWDGPKSDTDTTAAAQTSLPFAEKKQQKARPQATKDKSKGNDAFSDLFSYSKSLV | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MDSLSKKI -------CCHHHHHH | 7.73 | 22814378 | |
| 51 | Acetylation | DAWGPTPKHLAKVLR CCCCCCHHHHHHHHH | 54.45 | 24489116 | |
| 85 | Acetylation | DHIATRPKNLYEKAR HHHHHCCHHHHHHHH | 57.18 | 24489116 | |
| 95 | Phosphorylation | YEKARKDYVNYGSEW HHHHHHHHCCCCHHH | 8.14 | 21551504 | |
| 98 | Phosphorylation | ARKDYVNYGSEWRVV HHHHHCCCCHHHHHH | 16.40 | 21551504 | |
| 100 | Phosphorylation | KDYVNYGSEWRVVLK HHHCCCCHHHHHHHH | 24.51 | 21551504 | |
| 257 | Phosphorylation | NSNTRRRSHMEEQRR CCHHHCHHHHHHHHH | 25.93 | 28889911 | |
| 322 | Phosphorylation | NKNNNINSNSDDDDD CCCCCCCCCCCCCCC | 33.63 | 22369663 | |
| 324 | Phosphorylation | NNNINSNSDDDDDEF CCCCCCCCCCCCCCC | 42.09 | 22369663 | |
| 336 | Phosphorylation | DEFGDFQSETSPDTT CCCCCCCCCCCCCCC | 42.72 | 22369663 | |
| 338 | Phosphorylation | FGDFQSETSPDTTAP CCCCCCCCCCCCCCC | 51.29 | 29734811 | |
| 339 | Phosphorylation | GDFQSETSPDTTAPK CCCCCCCCCCCCCCC | 19.41 | 29734811 | |
| 342 | Phosphorylation | QSETSPDTTAPKTSN CCCCCCCCCCCCCCC | 28.39 | 22369663 | |
| 343 | Phosphorylation | SETSPDTTAPKTSNS CCCCCCCCCCCCCCC | 48.63 | 22369663 | |
| 347 | Phosphorylation | PDTTAPKTSNSKIDD CCCCCCCCCCCCHHH | 31.89 | 21440633 | |
| 348 | Phosphorylation | DTTAPKTSNSKIDDL CCCCCCCCCCCHHHH | 45.28 | 19779198 | |
| 350 | Phosphorylation | TAPKTSNSKIDDLLD CCCCCCCCCHHHHHC | 30.65 | 21440633 | |
| 351 | Acetylation | APKTSNSKIDDLLDW CCCCCCCCHHHHHCC | 55.17 | 24489116 | |
| 363 | Phosphorylation | LDWDGPKSDTDTTAA HCCCCCCCCCCCHHH | 49.21 | 22369663 | |
| 365 | Phosphorylation | WDGPKSDTDTTAAAQ CCCCCCCCCCHHHHH | 42.19 | 22369663 | |
| 367 | Phosphorylation | GPKSDTDTTAAAQTS CCCCCCCCHHHHHHC | 22.04 | 22369663 | |
| 368 | Phosphorylation | PKSDTDTTAAAQTSL CCCCCCCHHHHHHCC | 19.67 | 22369663 | |
| 373 | Phosphorylation | DTTAAAQTSLPFAEK CCHHHHHHCCCHHHH | 27.75 | 22369663 | |
| 374 | Phosphorylation | TTAAAQTSLPFAEKK CHHHHHHCCCHHHHH | 23.20 | 22369663 | |
| 380 | Acetylation | TSLPFAEKKQQKARP HCCCHHHHHHHHCCC | 53.07 | 24489116 | |
| 391 | Acetylation | KARPQATKDKSKGND HCCCCCCCCHHCCCH | 67.20 | 25381059 | |
| 394 | Phosphorylation | PQATKDKSKGNDAFS CCCCCCHHCCCHHHH | 56.80 | 17330950 | |
| 401 | Phosphorylation | SKGNDAFSDLFSYSK HCCCHHHHHHHHHHH | 34.81 | 12483220 | |
| 405 | Phosphorylation | DAFSDLFSYSKSLV- HHHHHHHHHHHCCC- | 35.48 | 28152593 | |
| 406 | Phosphorylation | AFSDLFSYSKSLV-- HHHHHHHHHHCCC-- | 16.88 | 19779198 | |
| 407 | Phosphorylation | FSDLFSYSKSLV--- HHHHHHHHHCCC--- | 17.99 | 21440633 |
| 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 ENT5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ENT5_YEAST !! | ||||||
* 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 ENT5_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND THR-365, ANDMASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASSSPECTROMETRY. | |
