| UniProt ID | ACON_YEAST | |
|---|---|---|
| UniProt AC | P19414 | |
| Protein Name | Aconitate hydratase, mitochondrial | |
| Gene Name | ACO1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 778 | |
| Subcellular Localization | Mitochondrion. Cytoplasm. Mainly mitochondrial, small amounts are also detected in the cytosol with a ratio of 94:6. | |
| Protein Description | Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle. Can also provide minor contributions to the reversible dehydration of (R)-homocitrate to cis-homoaconitate, a step in the alpha-aminoadipate pathway for lysine biosynthesis. Plays also an essential role in mtDNA maintenance. May directly protect mtDNA from accumulation of point mutations and ssDNA breaks as a component of mitochondrial nucleoids, or by preventing accumulation of iron citrate thereby alleviating its detrimental effects in mitochondria.. | |
| Protein Sequence | MLSARSAIKRPIVRGLATVSNLTRDSKVNQNLLEDHSFINYKQNVETLDIVRKRLNRPFTYAEKILYGHLDDPHGQDIQRGVSYLKLRPDRVACQDATAQMAILQFMSAGLPQVAKPVTVHCDHLIQAQVGGEKDLKRAIDLNKEVYDFLASATAKYNMGFWKPGSGIIHQIVLENYAFPGALIIGTDSHTPNAGGLGQLAIGVGGADAVDVMAGRPWELKAPKILGVKLTGKMNGWTSPKDIILKLAGITTVKGGTGKIVEYFGDGVDTFSATGMGTICNMGAEIGATTSVFPFNKSMIEYLEATGRGKIADFAKLYHKDLLSADKDAEYDEVVEIDLNTLEPYINGPFTPDLATPVSKMKEVAVANNWPLDVRVGLIGSCTNSSYEDMSRSASIVKDAAAHGLKSKTIFTVTPGSEQIRATIERDGQLETFKEFGGIVLANACGPCIGQWDRRDIKKGDKNTIVSSYNRNFTSRNDGNPQTHAFVASPELVTAFAIAGDLRFNPLTDKLKDKDGNEFMLKPPHGDGLPQRGYDAGENTYQAPPADRSTVEVKVSPTSDRLQLLKPFKPWDGKDAKDMPILIKAVGKTTTDHISMAGPWLKYRGHLENISNNYMIGAINAENKKANCVKNVYTGEYKGVPDTARDYRDQGIKWVVIGDENFGEGSSREHAALEPRFLGGFAIITKSFARIHETNLKKQGLLPLNFKNPADYDKINPDDRIDILGLAELAPGKPVTMRVHPKNGKPWDAVLTHTFNDEQIEWFKYGSALNKIKADEKK | |
| 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 |
|---|---|---|---|---|---|
| 9 | Acetylation | LSARSAIKRPIVRGL CCHHHHCCCHHHHHH | 52.41 | 25381059 | |
| 27 | Acetylation | SNLTRDSKVNQNLLE HHHCCCCCCCHHHHH | 49.87 | 24489116 | |
| 37 | Phosphorylation | QNLLEDHSFINYKQN HHHHHCCCCCCHHCC | 39.89 | 21440633 | |
| 41 | Phosphorylation | EDHSFINYKQNVETL HCCCCCCHHCCCHHH | 14.77 | 27017623 | |
| 42 | Acetylation | DHSFINYKQNVETLD CCCCCCHHCCCHHHH | 30.79 | 24489116 | |
| 47 | Phosphorylation | NYKQNVETLDIVRKR CHHCCCHHHHHHHHH | 26.00 | 27017623 | |
| 83 | Phosphorylation | QDIQRGVSYLKLRPD CCCHHCCCEEECCCC | 27.80 | 20377248 | |
| 86 | Acetylation | QRGVSYLKLRPDRVA HHCCCEEECCCCCCC | 33.93 | 24489116 | |
| 144 | Acetylation | KRAIDLNKEVYDFLA HHHHHCCHHHHHHHH | 56.72 | 24489116 | |
| 224 | 2-Hydroxyisobutyrylation | PWELKAPKILGVKLT CCCCCCCEEEEEECC | 56.26 | - | |
| 229 | 2-Hydroxyisobutyrylation | APKILGVKLTGKMNG CCEEEEEECCCCCCC | 38.23 | - | |
| 229 | Acetylation | APKILGVKLTGKMNG CCEEEEEECCCCCCC | 38.23 | 24489116 | |
| 239 | Phosphorylation | GKMNGWTSPKDIILK CCCCCCCCHHHHHHH | 24.36 | 21440633 | |
| 246 | Acetylation | SPKDIILKLAGITTV CHHHHHHHHHCCEEE | 26.36 | 24489116 | |
| 254 | Ubiquitination | LAGITTVKGGTGKIV HHCCEEEECCCEEEE | 49.91 | 23749301 | |
| 254 | 2-Hydroxyisobutyrylation | LAGITTVKGGTGKIV HHCCEEEECCCEEEE | 49.91 | - | |
| 254 | Succinylation | LAGITTVKGGTGKIV HHCCEEEECCCEEEE | 49.91 | 23954790 | |
| 298 | Phosphorylation | SVFPFNKSMIEYLEA EEECCCHHHHHHHHH | 26.54 | 21440633 | |
| 310 | 2-Hydroxyisobutyrylation | LEATGRGKIADFAKL HHHHCCCHHHHHHHH | 33.10 | - | |
| 310 | Acetylation | LEATGRGKIADFAKL HHHHCCCHHHHHHHH | 33.10 | 25381059 | |
| 316 | Acetylation | GKIADFAKLYHKDLL CHHHHHHHHHHHHHH | 49.96 | 24489116 | |
| 320 | Acetylation | DFAKLYHKDLLSADK HHHHHHHHHHHCCCC | 36.19 | 24489116 | |
| 351 | Phosphorylation | PYINGPFTPDLATPV CCCCCCCCCCCCCCH | 21.01 | 28889911 | |
| 381 | Phosphorylation | VRVGLIGSCTNSSYE EEEEEEECCCCCCHH | 15.69 | 19779198 | |
| 383 | Phosphorylation | VGLIGSCTNSSYEDM EEEEECCCCCCHHHH | 39.57 | 28889911 | |
| 385 | Phosphorylation | LIGSCTNSSYEDMSR EEECCCCCCHHHHHH | 19.02 | 21440633 | |
| 386 | Phosphorylation | IGSCTNSSYEDMSRS EECCCCCCHHHHHHH | 34.31 | 19779198 | |
| 387 | Phosphorylation | GSCTNSSYEDMSRSA ECCCCCCHHHHHHHH | 18.77 | 21440633 | |
| 391 | Phosphorylation | NSSYEDMSRSASIVK CCCHHHHHHHHHHHH | 35.09 | 20377248 | |
| 393 | Phosphorylation | SYEDMSRSASIVKDA CHHHHHHHHHHHHHH | 21.04 | 21440633 | |
| 395 | Phosphorylation | EDMSRSASIVKDAAA HHHHHHHHHHHHHHH | 29.21 | 21440633 | |
| 398 | Succinylation | SRSASIVKDAAAHGL HHHHHHHHHHHHCCC | 39.72 | 23954790 | |
| 398 | 2-Hydroxyisobutyrylation | SRSASIVKDAAAHGL HHHHHHHHHHHHCCC | 39.72 | - | |
| 398 | Acetylation | SRSASIVKDAAAHGL HHHHHHHHHHHHCCC | 39.72 | 24489116 | |
| 407 | Phosphorylation | AAAHGLKSKTIFTVT HHHCCCCCCEEEEEC | 39.82 | 21440633 | |
| 408 | Acetylation | AAHGLKSKTIFTVTP HHCCCCCCEEEEECC | 44.01 | 24489116 | |
| 408 | 2-Hydroxyisobutyrylation | AAHGLKSKTIFTVTP HHCCCCCCEEEEECC | 44.01 | - | |
| 409 | Phosphorylation | AHGLKSKTIFTVTPG HCCCCCCEEEEECCC | 28.54 | 28889911 | |
| 468 | Phosphorylation | DKNTIVSSYNRNFTS CCCEEEEECCCCCCC | 18.61 | 19779198 | |
| 469 | Phosphorylation | KNTIVSSYNRNFTSR CCEEEEECCCCCCCC | 15.61 | 19779198 | |
| 510 | 2-Hydroxyisobutyrylation | RFNPLTDKLKDKDGN CCCCCCHHCCCCCCC | 52.80 | - | |
| 510 | Acetylation | RFNPLTDKLKDKDGN CCCCCCHHCCCCCCC | 52.80 | 24489116 | |
| 522 | Acetylation | DGNEFMLKPPHGDGL CCCCCCCCCCCCCCC | 44.72 | 24489116 | |
| 554 | Acetylation | DRSTVEVKVSPTSDR CCCCEEEEECCCCCC | 24.40 | 24489116 | |
| 556 | Phosphorylation | STVEVKVSPTSDRLQ CCEEEEECCCCCCCE | 19.42 | 22369663 | |
| 558 | Phosphorylation | VEVKVSPTSDRLQLL EEEEECCCCCCCEEC | 35.44 | 22369663 | |
| 559 | Phosphorylation | EVKVSPTSDRLQLLK EEEECCCCCCCEECC | 24.90 | 22369663 | |
| 566 | Acetylation | SDRLQLLKPFKPWDG CCCCEECCCCCCCCC | 57.93 | 24489116 | |
| 569 | Acetylation | LQLLKPFKPWDGKDA CEECCCCCCCCCCCC | 54.44 | 24489116 | |
| 577 | Acetylation | PWDGKDAKDMPILIK CCCCCCCCCCCEEEE | 65.77 | 24489116 | |
| 584 | Acetylation | KDMPILIKAVGKTTT CCCCEEEEECCCCCC | 33.31 | 24489116 | |
| 591 | Phosphorylation | KAVGKTTTDHISMAG EECCCCCCCCCHHCH | 30.71 | 21440633 | |
| 602 | Acetylation | SMAGPWLKYRGHLEN HHCHHCHHHCCCHHH | 29.09 | 24489116 | |
| 624 | Acetylation | GAINAENKKANCVKN EEEECCCCCCCCEEE | 44.78 | 24489116 | |
| 630 | Acetylation | NKKANCVKNVYTGEY CCCCCCEEECCCCCC | 42.78 | 24489116 | |
| 638 | 2-Hydroxyisobutyrylation | NVYTGEYKGVPDTAR ECCCCCCCCCCCCHH | 49.48 | - | |
| 638 | Succinylation | NVYTGEYKGVPDTAR ECCCCCCCCCCCCHH | 49.48 | 23954790 | |
| 638 | Acetylation | NVYTGEYKGVPDTAR ECCCCCCCCCCCCHH | 49.48 | 24489116 | |
| 697 | Succinylation | RIHETNLKKQGLLPL HHHHHCCHHCCCCCC | 45.16 | 23954790 | |
| 707 | Acetylation | GLLPLNFKNPADYDK CCCCCCCCCHHHHHH | 62.03 | 24489116 | |
| 714 | Acetylation | KNPADYDKINPDDRI CCHHHHHHCCCCCCE | 37.85 | 24489116 | |
| 767 | Phosphorylation | IEWFKYGSALNKIKA EEEEEHHHHHHHHCC | 26.88 | 21440633 | |
| 777 | Succinylation | NKIKADEKK------ HHHCCCCCC------ | 65.41 | 23954790 | |
| 777 | Acetylation | NKIKADEKK------ HHHCCCCCC------ | 65.41 | 25381059 |
| 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 ACON_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACON_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 ACON_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-556, AND MASSSPECTROMETRY. | |
| "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-351, 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-409, AND MASSSPECTROMETRY. | |
