| UniProt ID | HS104_YEAST | |
|---|---|---|
| UniProt AC | P31539 | |
| Protein Name | Heat shock protein 104 | |
| Gene Name | HSP104 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 908 | |
| Subcellular Localization | Cytoplasm. Nucleus. Shuttles between the cytoplasm and the nucleus in an importin KAP95- and KAP121-dependent and an exportin XPO1-dependent manner. Accumulation in the nucleus is enhanced by severe heat shock. In the cytoplasm, concentrates on a per | |
| Protein Description | Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].. | |
| Protein Sequence | MNDQTQFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETPEDGSVPYLQNLIEKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGKVLQDAAKIQKQQKDSFIAQDHILFALFNDSSIQQIFKEAQVDIEAIKQQALELRGNTRIDSRGADTNTPLEYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIEESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIGATTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKPEELDSKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKHGHEELTQAKKKLDELENKALDAERRYDTATAADLRYFAIPDIKKQIEKLEDQVAEEERRAGANSMIQNVVDSDTISETAARLTGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQGSKIQESTKNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIEERFEQNDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLKKGKSRDENVPEEAEECLEVLPNHEATIGADTLGDDDNEDSMEIDDDLD | |
| 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 | -------MNDQTQFT -------CCHHHHHH | 12.92 | 22814378 | |
| 20 | Ubiquitination | TILTLAQKLASDHQH HHHHHHHHHHCCCCC | 40.17 | 17644757 | |
| 57 | Ubiquitination | YLQNLIEKGRYDYDL HHHHHHHCCCCCHHH | 41.51 | 17644757 | |
| 87 | Phosphorylation | QPAPAEITPSYALGK CCCCCCCCHHHHHHH | 9.55 | 28889911 | |
| 94 | Ubiquitination | TPSYALGKVLQDAAK CHHHHHHHHHHHHHH | 40.39 | 17644757 | |
| 94 | Acetylation | TPSYALGKVLQDAAK CHHHHHHHHHHHHHH | 40.39 | 24489116 | |
| 101 | Acetylation | KVLQDAAKIQKQQKD HHHHHHHHHHHHHHH | 47.60 | 22865919 | |
| 131 | Ubiquitination | SSIQQIFKEAQVDIE HHHHHHHHHCCCCHH | 54.49 | 15699485 | |
| 141 | Ubiquitination | QVDIEAIKQQALELR CCCHHHHHHHHHHHC | 43.32 | 15699485 | |
| 155 | Phosphorylation | RGNTRIDSRGADTNT CCCCCCCCCCCCCCC | 30.18 | 22369663 | |
| 160 | Phosphorylation | IDSRGADTNTPLEYL CCCCCCCCCCHHHHH | 40.22 | 22369663 | |
| 162 | Phosphorylation | SRGADTNTPLEYLSK CCCCCCCCHHHHHHH | 31.20 | 25752575 | |
| 169 | Ubiquitination | TPLEYLSKYAIDMTE CHHHHHHHHHHHHHH | 35.79 | 17644757 | |
| 169 | Acetylation | TPLEYLSKYAIDMTE CHHHHHHHHHHHHHH | 35.79 | 24489116 | |
| 182 | Acetylation | TEQARQGKLDPVIGR HHHHHCCCCCCCCCC | 41.18 | 24489116 | |
| 205 | Ubiquitination | RVLARRIKSNPCLIG HHHHHHHHCCCCEEC | 42.23 | 15699485 | |
| 206 | Phosphorylation | VLARRIKSNPCLIGE HHHHHHHCCCCEECC | 43.57 | 22369663 | |
| 218 | Ubiquitination | IGEPGIGKTAIIEGV ECCCCCCHHHHHHHH | 32.63 | 23749301 | |
| 242 | Ubiquitination | PTILQGAKLFSLDLA HHHHHHCCHHHHHHH | 57.81 | 17644757 | |
| 256 | Ubiquitination | AALTAGAKYKGDFEE HHHHCCCCCCCCHHH | 46.72 | 22817900 | |
| 256 | Acetylation | AALTAGAKYKGDFEE HHHHCCCCCCCCHHH | 46.72 | 24489116 | |
| 258 | Ubiquitination | LTAGAKYKGDFEERF HHCCCCCCCCHHHHH | 51.82 | 23749301 | |
| 258 | 2-Hydroxyisobutyrylation | LTAGAKYKGDFEERF HHCCCCCCCCHHHHH | 51.82 | - | |
| 270 | Acetylation | ERFKGVLKEIEESKT HHHHHHHHHHHHCCE | 54.99 | 24489116 | |
| 302 | Succinylation | DDAANILKPALSRGQ CCHHHHHHHHHHCCC | 25.17 | 23954790 | |
| 302 | 2-Hydroxyisobutyrylation | DDAANILKPALSRGQ CCHHHHHHHHHHCCC | 25.17 | - | |
| 302 | Acetylation | DDAANILKPALSRGQ CCHHHHHHHHHHCCC | 25.17 | 24489116 | |
| 306 | Phosphorylation | NILKPALSRGQLKVI HHHHHHHHCCCEEEE | 36.15 | 28889911 | |
| 311 | 2-Hydroxyisobutyrylation | ALSRGQLKVIGATTN HHHCCCEEEEEECCC | 24.74 | - | |
| 311 | Ubiquitination | ALSRGQLKVIGATTN HHHCCCEEEEEECCC | 24.74 | 17644757 | |
| 327 | Acetylation | EYRSIVEKDGAFERR HHHHHHHHCCHHHHH | 51.04 | 24489116 | |
| 327 | 2-Hydroxyisobutyrylation | EYRSIVEKDGAFERR HHHHHHHHCCHHHHH | 51.04 | - | |
| 327 | Ubiquitination | EYRSIVEKDGAFERR HHHHHHHHCCHHHHH | 51.04 | 23749301 | |
| 337 | Acetylation | AFERRFQKIEVAEPS HHHHHHEEEEECCHH | 37.82 | 24489116 | |
| 358 | Acetylation | ILRGLQPKYEIHHGV HHHCCCCCCEEECCC | 42.42 | 24489116 | |
| 358 | Ubiquitination | ILRGLQPKYEIHHGV HHHCCCCCCEEECCC | 42.42 | 22817900 | |
| 380 | Acetylation | VTAAQLAKRYLPYRR HHHHHHHHHHCCHHC | 50.60 | 24489116 | |
| 380 | Ubiquitination | VTAAQLAKRYLPYRR HHHHHHHHHHCCHHC | 50.60 | 17644757 | |
| 410 | Ubiquitination | VAVARDSKPEELDSK HHHHCCCCHHHCCHH | 61.82 | 23749301 | |
| 417 | 2-Hydroxyisobutyrylation | KPEELDSKERQLQLI CHHHCCHHHHHHHHH | 57.49 | - | |
| 417 | Ubiquitination | KPEELDSKERQLQLI CHHHCCHHHHHHHHH | 57.49 | 22817900 | |
| 439 | Phosphorylation | ERDEDADSTTKDRLK HCCCCCCCCHHHHHH | 39.43 | 29136822 | |
| 440 | Phosphorylation | RDEDADSTTKDRLKL CCCCCCCCHHHHHHH | 38.11 | 28889911 | |
| 441 | Phosphorylation | DEDADSTTKDRLKLA CCCCCCCHHHHHHHH | 34.59 | 29136822 | |
| 442 | Succinylation | EDADSTTKDRLKLAR CCCCCCHHHHHHHHH | 40.72 | 23954790 | |
| 442 | Ubiquitination | EDADSTTKDRLKLAR CCCCCCHHHHHHHHH | 40.72 | 22106047 | |
| 442 | 2-Hydroxyisobutyrylation | EDADSTTKDRLKLAR CCCCCCHHHHHHHHH | 40.72 | - | |
| 442 | Acetylation | EDADSTTKDRLKLAR CCCCCCHHHHHHHHH | 40.72 | 24489116 | |
| 451 | 2-Hydroxyisobutyrylation | RLKLARQKEASLQEE HHHHHHHHHHHHHHH | 50.09 | - | |
| 470 | Ubiquitination | RQRYNEEKHGHEELT HHHHHHHHHCHHHHH | 49.02 | 23749301 | |
| 470 | Acetylation | RQRYNEEKHGHEELT HHHHHHHHHCHHHHH | 49.02 | 22865919 | |
| 480 | 2-Hydroxyisobutyrylation | HEELTQAKKKLDELE HHHHHHHHHHHHHHH | 40.39 | - | |
| 482 | Acetylation | ELTQAKKKLDELENK HHHHHHHHHHHHHHH | 61.54 | 24489116 | |
| 489 | Acetylation | KLDELENKALDAERR HHHHHHHHHHHHHHH | 40.74 | 24489116 | |
| 499 | Phosphorylation | DAERRYDTATAADLR HHHHHHCCCCHHHHH | 19.57 | 25752575 | |
| 501 | Phosphorylation | ERRYDTATAADLRYF HHHHCCCCHHHHHHH | 25.19 | 21440633 | |
| 514 | Acetylation | YFAIPDIKKQIEKLE HHCCHHHHHHHHHHH | 46.11 | 24489116 | |
| 514 | 2-Hydroxyisobutyrylation | YFAIPDIKKQIEKLE HHCCHHHHHHHHHHH | 46.11 | - | |
| 519 | Acetylation | DIKKQIEKLEDQVAE HHHHHHHHHHHHHHH | 59.82 | 24489116 | |
| 535 | Phosphorylation | ERRAGANSMIQNVVD HHHHCHHHHHHHHCC | 19.41 | 9624144 | |
| 545 | Phosphorylation | QNVVDSDTISETAAR HHHCCCCCHHHHHHH | 30.29 | 21440633 | |
| 547 | Phosphorylation | VVDSDTISETAARLT HCCCCCHHHHHHHHH | 30.87 | 25752575 | |
| 560 | 2-Hydroxyisobutyrylation | LTGIPVKKLSESENE HHCCCHHHCCHHHCH | 58.44 | - | |
| 568 | Acetylation | LSESENEKLIHMERD CCHHHCHHHEEEECC | 65.41 | 24489116 | |
| 577 | Phosphorylation | IHMERDLSSEVVGQM EEEECCCCHHHHHHH | 28.83 | 22369663 | |
| 578 | Phosphorylation | HMERDLSSEVVGQMD EEECCCCHHHHHHHH | 41.53 | 22369663 | |
| 588 | Acetylation | VGQMDAIKAVSNAVR HHHHHHHHHHHHHHH | 44.44 | 24489116 | |
| 620 | Ubiquitination | LGLSGSGKTELAKKV EECCCCCHHHHHHHH | 40.29 | 14557538 | |
| 625 | 2-Hydroxyisobutyrylation | SGKTELAKKVAGFLF CCHHHHHHHHHHHHC | 61.48 | - | |
| 649 | Ubiquitination | DCSELSEKYAVSKLL EHHHHHHHHHHHHHH | 34.82 | 23749301 | |
| 649 | Acetylation | DCSELSEKYAVSKLL EHHHHHHHHHHHHHH | 34.82 | 24489116 | |
| 654 | Ubiquitination | SEKYAVSKLLGTTAG HHHHHHHHHHCCCCE | 40.92 | 22817900 | |
| 710 | Phosphorylation | LDDGRITSGQGKTID HCCCCCCCCCCCEEE | 27.09 | 27214570 | |
| 747 | Ubiquitination | SKIQESTKNLVMGAV CCHHHHHHHHHHHHH | 58.52 | 24961812 | |
| 768 | Phosphorylation | EFLNRISSIVIFNKL HHHHHCHHHHHCCCC | 20.64 | 25752575 | |
| 774 | Acetylation | SSIVIFNKLSRKAIH HHHHHCCCCCHHHHH | 36.77 | 24489116 | |
| 782 | Acetylation | LSRKAIHKIVDIRLK CCHHHHHHHHHHHHH | 38.01 | 24489116 | |
| 789 | 2-Hydroxyisobutyrylation | KIVDIRLKEIEERFE HHHHHHHHHHHHHHH | 46.96 | - | |
| 800 | Acetylation | ERFEQNDKHYKLNLT HHHHHCCCEEECCCH | 57.28 | 25381059 | |
| 800 | 2-Hydroxyisobutyrylation | ERFEQNDKHYKLNLT HHHHHCCCEEECCCH | 57.28 | - | |
| 803 | 2-Hydroxyisobutyrylation | EQNDKHYKLNLTQEA HHCCCEEECCCHHHH | 30.53 | - | |
| 803 | Acetylation | EQNDKHYKLNLTQEA HHCCCEEECCCHHHH | 30.53 | 24489116 | |
| 811 | Acetylation | LNLTQEAKDFLAKYG CCCHHHHHHHHHHCC | 48.54 | 24489116 | |
| 811 | Ubiquitination | LNLTQEAKDFLAKYG CCCHHHHHHHHHHCC | 48.54 | 24961812 | |
| 816 | Acetylation | EAKDFLAKYGYSDDM HHHHHHHHCCCCCCC | 41.16 | 24489116 | |
| 839 | Ubiquitination | IQNEILNKLALRILK HHHHHHHHHHHHHHH | 31.52 | 23749301 | |
| 839 | Acetylation | IQNEILNKLALRILK HHHHHHHHHHHHHHH | 31.52 | 24489116 | |
| 864 | Phosphorylation | VVLKKGKSRDENVPE EEEECCCCCCCCCCH | 54.34 | 19795423 | |
| 886 | Phosphorylation | VLPNHEATIGADTLG HCCCCCCEECCCCCC | 19.57 | 19823750 | |
| 891 | Phosphorylation | EATIGADTLGDDDNE CCEECCCCCCCCCCC | 31.91 | 19823750 | |
| 900 | Phosphorylation | GDDDNEDSMEIDDDL CCCCCCCCCCCCCCC | 16.49 | 19795423 |
| 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 HS104_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HS104_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 HS104_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 THR-87; SER-155; THR-162;SER-206; SER-306; THR-499; SER-535; SER-577; SER-578 AND SER-768, 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-206, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery."; Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.; Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-620, AND MASSSPECTROMETRY. | |
