| UniProt ID | CYM1_YEAST | |
|---|---|---|
| UniProt AC | P32898 | |
| Protein Name | Mitochondrial presequence protease | |
| Gene Name | CYM1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 989 | |
| Subcellular Localization | Mitochondrion intermembrane space . May also be present in the mitochondrial matrix. | |
| Protein Description | ATP-independent protease that degrades mitochondrial transit peptides after their cleavage both in intermembrane space and in matrix. Also degrades other unstructured peptides (By similarity).. | |
| Protein Sequence | MLRFQRFASSYAQAQAVRKYPVGGIFHGYEVRRILPVPELRLTAVDLVHSQTGAEHLHIDRDDKNNVFSIAFKTNPPDSTGVPHILEHTTLCGSVKYPVRDPFFKMLNKSLANFMNAMTGPDYTFFPFSTTNPQDFANLRGVYLDSTLNPLLKQEDFDQEGWRLEHKNITDPESNIVFKGVVYNEMKGQISNANYYFWSKFQQSIYPSLNNSGGDPMKITDLRYGDLLDFHHKNYHPSNAKTFTYGNLPLVDTLKQLNEQFSGYGKRARKDKLLMPIDLKKDIDVKLLGQIDTMLPPEKQTKASMTWICGAPQDTYDTFLLKVLGNLLMDGHSSVMYQKLIESGIGLEFSVNSGVEPTTAVNLLTVGIQGVSDIEIFKDTVNNIFQNLLETEHPFDRKRIDAIIEQLELSKKDQKADFGLQLLYSILPGWTNKIDPFESLLFEDVLQRFRGDLETKGDTLFQDLIRKYIVHKPCFTFSIQGSEEFSKSLDDEEQTRLREKITALDEQDKKNIFKRGILLQEKQNEKEDLSCLPTLQIKDIPRAGDKYSIEQKNNTMSRITDTNGITYVRGKRLLNDIIPFELFPYLPLFAESLTNLGTTTESFSEIEDQIKLHTGGISTHVEVTSDPNTTEPRLIFGFDGWSLNSKTDHIFEFWSKILLETDFHKNSDKLKVLIRLLASSNTSSVADAGHAFARGYSAAHYRSSGAINETLNGIEQLQFINRLHSLLDNEETFQREVVDKLTELQKYIVDTNNMNFFITSDSDVQAKTVESQISKFMERLPHGSCLPNGPKTSDYPLIGSKCKHTLIKFPFQVHYTSQALLGVPYTHKDGSALQVMSNMLTFKHLHREVREKGGAYGGGASYSALAGIFSFYSYRDPQPLKSLETFKNSGRYILNDAKWGVTDLDEAKLTIFQQVDAPKSPKGEGVTYFMSGVTDDMKQARREQLLDVSLLDVHRVAEKYLLNKEGVSTVIGPGIEGKTVSPNWEVKEL | |
| 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 |
|---|---|---|---|---|---|
| 29 | Phosphorylation | VGGIFHGYEVRRILP CCCEECCEEEEEEEE | 11.59 | 28889911 | |
| 105 | Acetylation | PVRDPFFKMLNKSLA CCCCHHHHHHHHHHH | 42.74 | 24489116 | |
| 167 | Acetylation | EGWRLEHKNITDPES CCCEEEECCCCCCCC | 40.44 | 24489116 | |
| 665 | Acetylation | LLETDFHKNSDKLKV HHHCCCCCCHHHHHH | 59.13 | 24489116 | |
| 775 | Acetylation | TVESQISKFMERLPH HHHHHHHHHHHHCCC | 50.81 | 24489116 | |
| 831 | Phosphorylation | PYTHKDGSALQVMSN CCCCCCCCHHHHHHH | 35.62 | 27017623 | |
| 887 | Acetylation | LKSLETFKNSGRYIL CCCHHHHHHCCCEEE | 58.59 | 22865919 | |
| 920 | Phosphorylation | QQVDAPKSPKGEGVT EECCCCCCCCCCCCE | 30.68 | 17330950 | |
| 927 | Phosphorylation | SPKGEGVTYFMSGVT CCCCCCCEEEECCCC | 23.15 | 21440633 | |
| 928 | Phosphorylation | PKGEGVTYFMSGVTD CCCCCCEEEECCCCH | 8.55 | 20377248 | |
| 938 | Acetylation | SGVTDDMKQARREQL CCCCHHHHHHHHHHH | 48.04 | 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 CYM1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CYM1_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 CYM1_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-920, AND MASSSPECTROMETRY. | |
| "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-920, 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-920, AND MASSSPECTROMETRY. | |