| UniProt ID | HSE1_YEAST | |
|---|---|---|
| UniProt AC | P38753 | |
| Protein Name | Class E vacuolar protein-sorting machinery protein HSE1 | |
| Gene Name | HSE1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 452 | |
| Subcellular Localization |
Endosome membrane Peripheral membrane protein Cytoplasmic side . |
|
| Protein Description | Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.. | |
| Protein Sequence | MSSSAIKIRNALLKATDPKLRSDNWQYILDVCDLVKEDPEDNGQEVMSLIEKRLEQQDANVILRTLSLTVSLAENCGSRLRQEISSKNFTSLLYALIESHSVHITLKKAVTDVVKQLSDSFKDDPSLRAMGDLYDKIKRKAPYLVQPNVPEKHNMSTQADNSDDEELQKALKMSLFEYEKQKKLQEQEKESAEVLPQQQQQHQQQNQAPAHKIPAQTVVRRVRALYDLTTNEPDELSFRKGDVITVLEQVYRDWWKGALRGNMGIFPLNYVTPIVEPSKEEIEKEKNKEAIVFSQKTTIDQLHNSLNAASKTGNSNEVLQDPHIGDMYGSVTPLRPQVTRMLGKYAKEKEDMLSLRQVLANAERSYNQLMDRAANAHISPPVPGPALYAGMTHANNTPVMPPQRQSYQSNEYSPYPSNLPIQHPTNSANNTPQYGYDLGYSVVSQPPPGYEQ | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSSSAIKIR ------CCHHHHHHH | 32.76 | 22814378 | |
| 4 | Phosphorylation | ----MSSSAIKIRNA ----CCHHHHHHHHH | 27.06 | 30377154 | |
| 14 | Ubiquitination | KIRNALLKATDPKLR HHHHHHHHHCCCCCC | 50.52 | 23749301 | |
| 122 | Ubiquitination | KQLSDSFKDDPSLRA HHHHHHCCCCHHHHH | 66.24 | 23749301 | |
| 136 | Acetylation | AMGDLYDKIKRKAPY HHHHHHHHHHHHCCC | 36.25 | 24489116 | |
| 138 | Acetylation | GDLYDKIKRKAPYLV HHHHHHHHHHCCCCC | 54.29 | 24489116 | |
| 140 | Ubiquitination | LYDKIKRKAPYLVQP HHHHHHHHCCCCCCC | 49.03 | 17644757 | |
| 152 | Ubiquitination | VQPNVPEKHNMSTQA CCCCCCCCCCCCCCC | 33.92 | 23749301 | |
| 156 | Phosphorylation | VPEKHNMSTQADNSD CCCCCCCCCCCCCCC | 23.76 | 22890988 | |
| 157 | Phosphorylation | PEKHNMSTQADNSDD CCCCCCCCCCCCCCH | 19.60 | 25371407 | |
| 162 | Phosphorylation | MSTQADNSDDEELQK CCCCCCCCCHHHHHH | 47.16 | 22369663 | |
| 189 | Ubiquitination | KKLQEQEKESAEVLP HHHHHHHHHHHHHCH | 57.58 | 23749301 | |
| 212 | Ubiquitination | QNQAPAHKIPAQTVV HHCCCHHHCCHHHHH | 53.11 | 24961812 | |
| 240 | Ubiquitination | PDELSFRKGDVITVL CCCCCCCCCCHHHHH | 58.41 | 17644757 | |
| 312 | Phosphorylation | SLNAASKTGNSNEVL HHHHHHHHCCCCHHH | 38.82 | 22369663 | |
| 315 | Phosphorylation | AASKTGNSNEVLQDP HHHHHCCCCHHHCCC | 35.39 | 21551504 | |
| 328 | Phosphorylation | DPHIGDMYGSVTPLR CCCHHHCCCCCCCCH | 15.81 | 22369663 | |
| 330 | Phosphorylation | HIGDMYGSVTPLRPQ CHHHCCCCCCCCHHH | 12.82 | 21440633 | |
| 332 | Phosphorylation | GDMYGSVTPLRPQVT HHCCCCCCCCHHHHH | 20.50 | 22369663 | |
| 339 | Phosphorylation | TPLRPQVTRMLGKYA CCCHHHHHHHHHHHH | 12.71 | 22369663 | |
| 365 | Phosphorylation | VLANAERSYNQLMDR HHHHHHHHHHHHHHH | 21.68 | 28889911 | |
| 379 | Phosphorylation | RAANAHISPPVPGPA HHHHCCCCCCCCCCH | 17.18 | 28152593 | |
| 397 | Phosphorylation | GMTHANNTPVMPPQR CCCCCCCCCCCCCCC | 19.64 | 21082442 |
| 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 HSE1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HSE1_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 HSE1_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-162 AND SER-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-162, 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-162, AND MASSSPECTROMETRY. | |
