| UniProt ID | HSP60_YEAST | |
|---|---|---|
| UniProt AC | P19882 | |
| Protein Name | Heat shock protein 60, mitochondrial | |
| Gene Name | HSP60 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 572 | |
| Subcellular Localization | Mitochondrion matrix . | |
| Protein Description | May participate in assembly and/or disassembly of proteins imported into the mitochondrion. HSP60 are ATPases and have affinity for unfolded proteins.. | |
| Protein Sequence | MLRSSVVRSRATLRPLLRRAYSSHKELKFGVEGRASLLKGVETLAEAVAATLGPKGRNVLIEQPFGPPKITKDGVTVAKSIVLKDKFENMGAKLLQEVASKTNEAAGDGTTSATVLGRAIFTESVKNVAAGCNPMDLRRGSQVAVEKVIEFLSANKKEITTSEEIAQVATISANGDSHVGKLLASAMEKVGKEGVITIREGRTLEDELEVTEGMRFDRGFISPYFITDPKSSKVEFEKPLLLLSEKKISSIQDILPALEISNQSRRPLLIIAEDVDGEALAACILNKLRGQVKVCAVKAPGFGDNRKNTIGDIAVLTGGTVFTEELDLKPEQCTIENLGSCDSITVTKEDTVILNGSGPKEAIQERIEQIKGSIDITTTNSYEKEKLQERLAKLSGGVAVIRVGGASEVEVGEKKDRYDDALNATRAAVEEGILPGGGTALVKASRVLDEVVVDNFDQKLGVDIIRKAITRPAKQIIENAGEEGSVIIGKLIDEYGDDFAKGYDASKSEYTDMLATGIIDPFKVVRSGLVDASGVASLLATTEVAIVDAPEPPAAAGAGGMPGGMPGMPGMM | |
| 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 |
|---|---|---|---|---|---|
| 22 | Phosphorylation | PLLRRAYSSHKELKF HHHHHHHHCCCCHHH | 25.61 | 28889911 | |
| 23 | Phosphorylation | LLRRAYSSHKELKFG HHHHHHHCCCCHHHC | 26.38 | 28889911 | |
| 28 | Acetylation | YSSHKELKFGVEGRA HHCCCCHHHCCCHHH | 40.96 | 24489116 | |
| 28 | 2-Hydroxyisobutyrylation | YSSHKELKFGVEGRA HHCCCCHHHCCCHHH | 40.96 | - | |
| 39 | Acetylation | EGRASLLKGVETLAE CHHHHHHHHHHHHHH | 67.23 | 24489116 | |
| 55 | Ubiquitination | VAATLGPKGRNVLIE HHHHHCCCCCCEEEE | 69.57 | 24961812 | |
| 55 | Succinylation | VAATLGPKGRNVLIE HHHHHCCCCCCEEEE | 69.57 | 23954790 | |
| 69 | Acetylation | EQPFGPPKITKDGVT ECCCCCCCCCCCCEE | 67.17 | 24489116 | |
| 72 | 2-Hydroxyisobutyrylation | FGPPKITKDGVTVAK CCCCCCCCCCEEEEH | 56.83 | - | |
| 72 | Acetylation | FGPPKITKDGVTVAK CCCCCCCCCCEEEEH | 56.83 | 25381059 | |
| 84 | Acetylation | VAKSIVLKDKFENMG EEHHHHHHHHHHHHH | 48.23 | 24489116 | |
| 86 | Acetylation | KSIVLKDKFENMGAK HHHHHHHHHHHHHHH | 53.65 | 24489116 | |
| 93 | Acetylation | KFENMGAKLLQEVAS HHHHHHHHHHHHHHH | 43.96 | 24489116 | |
| 100 | Phosphorylation | KLLQEVASKTNEAAG HHHHHHHHHCCCCCC | 45.23 | 22369663 | |
| 101 | Acetylation | LLQEVASKTNEAAGD HHHHHHHHCCCCCCC | 45.70 | 24489116 | |
| 102 | Phosphorylation | LQEVASKTNEAAGDG HHHHHHHCCCCCCCC | 35.48 | 28889911 | |
| 141 | Phosphorylation | PMDLRRGSQVAVEKV HHHCCCCCHHHHHHH | 21.48 | 24603354 | |
| 147 | Ubiquitination | GSQVAVEKVIEFLSA CCHHHHHHHHHHHHC | 41.75 | 24961812 | |
| 147 | Acetylation | GSQVAVEKVIEFLSA CCHHHHHHHHHHHHC | 41.75 | 24489116 | |
| 156 | Succinylation | IEFLSANKKEITTSE HHHHHCCCCCCCCHH | 52.04 | 23954790 | |
| 156 | 2-Hydroxyisobutyrylation | IEFLSANKKEITTSE HHHHHCCCCCCCCHH | 52.04 | - | |
| 189 | Acetylation | LLASAMEKVGKEGVI HHHHHHHHHCCCCEE | 43.11 | 24489116 | |
| 192 | Acetylation | SAMEKVGKEGVITIR HHHHHHCCCCEEEEE | 55.04 | 24489116 | |
| 203 | Phosphorylation | ITIREGRTLEDELEV EEEECCCCCCCCEEE | 45.41 | 28889911 | |
| 230 | Succinylation | PYFITDPKSSKVEFE CCEECCCCCCCCEEC | 70.89 | 23954790 | |
| 230 | Acetylation | PYFITDPKSSKVEFE CCEECCCCCCCCEEC | 70.89 | 24489116 | |
| 233 | Acetylation | ITDPKSSKVEFEKPL ECCCCCCCCEECCCE | 53.53 | 24489116 | |
| 238 | Acetylation | SSKVEFEKPLLLLSE CCCCEECCCEEEEEH | 46.41 | 24489116 | |
| 246 | Succinylation | PLLLLSEKKISSIQD CEEEEEHHHHCCHHH | 52.62 | 23954790 | |
| 246 | Acetylation | PLLLLSEKKISSIQD CEEEEEHHHHCCHHH | 52.62 | 24489116 | |
| 249 | Phosphorylation | LLSEKKISSIQDILP EEEHHHHCCHHHHHH | 30.21 | 21440633 | |
| 250 | Phosphorylation | LSEKKISSIQDILPA EEHHHHCCHHHHHHH | 27.95 | 22369663 | |
| 261 | Phosphorylation | ILPALEISNQSRRPL HHHHHHHCCCCCCCE | 21.31 | 22369663 | |
| 264 | Phosphorylation | ALEISNQSRRPLLII HHHHCCCCCCCEEEE | 34.21 | 22369663 | |
| 351 | Phosphorylation | ITVTKEDTVILNGSG EEECCCCEEEECCCC | 15.55 | 28889911 | |
| 360 | Acetylation | ILNGSGPKEAIQERI EECCCCCHHHHHHHH | 64.40 | 24489116 | |
| 373 | Phosphorylation | RIEQIKGSIDITTTN HHHHHHCCCCCCCCC | 16.46 | 28889911 | |
| 377 | Phosphorylation | IKGSIDITTTNSYEK HHCCCCCCCCCHHHH | 24.66 | 22369663 | |
| 378 | Phosphorylation | KGSIDITTTNSYEKE HCCCCCCCCCHHHHH | 25.06 | 22369663 | |
| 379 | Phosphorylation | GSIDITTTNSYEKEK CCCCCCCCCHHHHHH | 17.33 | 22369663 | |
| 381 | Phosphorylation | IDITTTNSYEKEKLQ CCCCCCCHHHHHHHH | 32.35 | 22369663 | |
| 382 | Phosphorylation | DITTTNSYEKEKLQE CCCCCCHHHHHHHHH | 32.84 | 22369663 | |
| 384 | Succinylation | TTTNSYEKEKLQERL CCCCHHHHHHHHHHH | 52.49 | 23954790 | |
| 384 | Acetylation | TTTNSYEKEKLQERL CCCCHHHHHHHHHHH | 52.49 | 24489116 | |
| 386 | Acetylation | TNSYEKEKLQERLAK CCHHHHHHHHHHHHH | 67.54 | 24489116 | |
| 393 | Acetylation | KLQERLAKLSGGVAV HHHHHHHHHCCCEEE | 48.02 | 24489116 | |
| 395 | Phosphorylation | QERLAKLSGGVAVIR HHHHHHHCCCEEEEE | 32.56 | 21440633 | |
| 414 | Acetylation | SEVEVGEKKDRYDDA CEEEECCCCCCHHHH | 54.79 | 22865919 | |
| 414 | Ubiquitination | SEVEVGEKKDRYDDA CEEEECCCCCCHHHH | 54.79 | 23749301 | |
| 443 | 2-Hydroxyisobutyrylation | GGGTALVKASRVLDE CCHHHHHHHHHHCCE | 41.30 | - | |
| 474 | Acetylation | KAITRPAKQIIENAG HHCCCCHHHHHHHCC | 44.72 | 24489116 | |
| 474 | Ubiquitination | KAITRPAKQIIENAG HHCCCCHHHHHHHCC | 44.72 | 24961812 | |
| 485 | Phosphorylation | ENAGEEGSVIIGKLI HHCCCCCCEEEEEEH | 17.27 | 20377248 | |
| 501 | Acetylation | EYGDDFAKGYDASKS HHCCCCCCCCCCCHH | 58.98 | 24489116 | |
| 501 | 2-Hydroxyisobutyrylation | EYGDDFAKGYDASKS HHCCCCCCCCCCCHH | 58.98 | - | |
| 501 | Succinylation | EYGDDFAKGYDASKS HHCCCCCCCCCCCHH | 58.98 | 23954790 | |
| 507 | Acetylation | AKGYDASKSEYTDML CCCCCCCHHHHHHHH | 49.37 | 24489116 | |
| 523 | Acetylation | TGIIDPFKVVRSGLV CCCCCHHHHHHCCCC | 45.25 | 24489116 |
| 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 HSP60_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HSP60_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 HSP60_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-485, AND MASSSPECTROMETRY. | |
| "Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102, AND MASSSPECTROMETRY. | |
