| UniProt ID | IPYR_YEAST | |
|---|---|---|
| UniProt AC | P00817 | |
| Protein Name | Inorganic pyrophosphatase | |
| Gene Name | IPP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 287 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | ||
| Protein Sequence | MTYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKENNIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFVRNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPIDVLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDINDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPENQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGIDLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWFFISGSV | |
| 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 |
|---|---|---|---|---|---|
| 11 | Succinylation | TTRQIGAKNTLEYKV ECEECCCCCEEEEEE | 45.30 | 23954790 | |
| 11 | 2-Hydroxyisobutyrylation | TTRQIGAKNTLEYKV ECEECCCCCEEEEEE | 45.30 | - | |
| 11 | Ubiquitination | TTRQIGAKNTLEYKV ECEECCCCCEEEEEE | 45.30 | 23749301 | |
| 13 | Phosphorylation | RQIGAKNTLEYKVYI EECCCCCEEEEEEEE | 21.91 | 21126336 | |
| 17 | Acetylation | AKNTLEYKVYIEKDG CCCEEEEEEEECCCC | 21.13 | 24489116 | |
| 17 | Ubiquitination | AKNTLEYKVYIEKDG CCCEEEEEEEECCCC | 21.13 | 22817900 | |
| 17 | Succinylation | AKNTLEYKVYIEKDG CCCEEEEEEEECCCC | 21.13 | 23954790 | |
| 22 | Ubiquitination | EYKVYIEKDGKPVSA EEEEEECCCCEEEEE | 63.32 | 24961812 | |
| 22 | Acetylation | EYKVYIEKDGKPVSA EEEEEECCCCEEEEE | 63.32 | 24489116 | |
| 22 | Succinylation | EYKVYIEKDGKPVSA EEEEEECCCCEEEEE | 63.32 | 23954790 | |
| 25 | Ubiquitination | VYIEKDGKPVSAFHD EEECCCCEEEEEEEC | 52.99 | 24961812 | |
| 25 | Acetylation | VYIEKDGKPVSAFHD EEECCCCEEEEEEEC | 52.99 | 24489116 | |
| 25 | Succinylation | VYIEKDGKPVSAFHD EEECCCCEEEEEEEC | 52.99 | 23954790 | |
| 39 | Acetylation | DIPLYADKENNIFNM CCCEEEECCCCEEEE | 54.92 | 24489116 | |
| 57 | Acetylation | IPRWTNAKLEITKEE ECCHHCCEEEECHHH | 49.04 | 24489116 | |
| 57 | Succinylation | IPRWTNAKLEITKEE ECCHHCCEEEECHHH | 49.04 | 23954790 | |
| 57 | Ubiquitination | IPRWTNAKLEITKEE ECCHHCCEEEECHHH | 49.04 | 24961812 | |
| 57 | 2-Hydroxyisobutyrylation | IPRWTNAKLEITKEE ECCHHCCEEEECHHH | 49.04 | - | |
| 61 | Phosphorylation | TNAKLEITKEETLNP HCCEEEECHHHHCCC | 24.03 | 22369663 | |
| 62 | Acetylation | NAKLEITKEETLNPI CCEEEECHHHHCCCC | 60.25 | 24489116 | |
| 62 | Succinylation | NAKLEITKEETLNPI CCEEEECHHHHCCCC | 60.25 | 23954790 | |
| 62 | Ubiquitination | NAKLEITKEETLNPI CCEEEECHHHHCCCC | 60.25 | 23749301 | |
| 65 | Phosphorylation | LEITKEETLNPIIQD EEECHHHHCCCCEEC | 32.69 | 22369663 | |
| 74 | Succinylation | NPIIQDTKKGKLRFV CCCEECCCCCCEEEE | 68.75 | 23954790 | |
| 74 | Ubiquitination | NPIIQDTKKGKLRFV CCCEECCCCCCEEEE | 68.75 | 24961812 | |
| 74 | Acetylation | NPIIQDTKKGKLRFV CCCEECCCCCCEEEE | 68.75 | 24489116 | |
| 75 | 2-Hydroxyisobutyrylation | PIIQDTKKGKLRFVR CCEECCCCCCEEEEE | 64.47 | - | |
| 168 | Acetylation | INDPLAPKLNDIEDV CCCCCCCCCCCHHHH | 55.07 | 24489116 | |
| 177 | Acetylation | NDIEDVEKYFPGLLR CCHHHHHHHCHHHHH | 52.63 | 24489116 | |
| 194 | 2-Hydroxyisobutyrylation | NEWFRIYKIPDGKPE CCEEEEEECCCCCCC | 45.45 | - | |
| 194 | Acetylation | NEWFRIYKIPDGKPE CCEEEEEECCCCCCC | 45.45 | 24489116 | |
| 199 | Ubiquitination | IYKIPDGKPENQFAF EEECCCCCCCCCCCC | 57.44 | 23749301 | |
| 199 | Acetylation | IYKIPDGKPENQFAF EEECCCCCCCCCCCC | 57.44 | 24489116 | |
| 214 | Acetylation | SGEAKNKKYALDIIK CCCCCCCEEHHHHHH | 45.19 | 22865919 | |
| 221 | 2-Hydroxyisobutyrylation | KYALDIIKETHDSWK EEHHHHHHHHHHHHH | 57.82 | - | |
| 221 | Acetylation | KYALDIIKETHDSWK EEHHHHHHHHHHHHH | 57.82 | 24489116 | |
| 228 | Acetylation | KETHDSWKQLIAGKS HHHHHHHHHHHCCCC | 38.90 | 24489116 | |
| 228 | 2-Hydroxyisobutyrylation | KETHDSWKQLIAGKS HHHHHHHHHHHCCCC | 38.90 | - | |
| 234 | Ubiquitination | WKQLIAGKSSDSKGI HHHHHCCCCCCCCCC | 37.45 | 23749301 | |
| 236 | Phosphorylation | QLIAGKSSDSKGIDL HHHCCCCCCCCCCCC | 49.76 | 25752575 | |
| 239 | Acetylation | AGKSSDSKGIDLTNV CCCCCCCCCCCCCCC | 65.95 | 24489116 | |
| 239 | Succinylation | AGKSSDSKGIDLTNV CCCCCCCCCCCCCCC | 65.95 | 23954790 | |
| 239 | 2-Hydroxyisobutyrylation | AGKSSDSKGIDLTNV CCCCCCCCCCCCCCC | 65.95 | - | |
| 239 | Ubiquitination | AGKSSDSKGIDLTNV CCCCCCCCCCCCCCC | 65.95 | 23749301 | |
| 244 | Phosphorylation | DSKGIDLTNVTLPDT CCCCCCCCCCCCCCC | 24.72 | 22369663 | |
| 247 | Phosphorylation | GIDLTNVTLPDTPTY CCCCCCCCCCCCCCC | 34.34 | 22369663 | |
| 251 | Phosphorylation | TNVTLPDTPTYSKAA CCCCCCCCCCCCHHH | 18.65 | 22369663 | |
| 253 | Phosphorylation | VTLPDTPTYSKAASD CCCCCCCCCCHHHHC | 42.38 | 22369663 | |
| 254 | Phosphorylation | TLPDTPTYSKAASDA CCCCCCCCCHHHHCC | 14.91 | 22369663 | |
| 255 | Phosphorylation | LPDTPTYSKAASDAI CCCCCCCCHHHHCCC | 20.49 | 22369663 | |
| 256 | Acetylation | PDTPTYSKAASDAIP CCCCCCCHHHHCCCC | 37.24 | 24489116 | |
| 256 | Ubiquitination | PDTPTYSKAASDAIP CCCCCCCHHHHCCCC | 37.24 | 23749301 | |
| 259 | Phosphorylation | PTYSKAASDAIPPAS CCCCHHHHCCCCCCC | 32.22 | 22890988 | |
| 266 | Phosphorylation | SDAIPPASPKADAPI HCCCCCCCCCCCCCC | 32.48 | 22369663 | |
| 275 | 2-Hydroxyisobutyrylation | KADAPIDKSIDKWFF CCCCCCCCCCCCEEE | 50.45 | - | |
| 275 | Acetylation | KADAPIDKSIDKWFF CCCCCCCCCCCCEEE | 50.45 | 24489116 | |
| 276 | Phosphorylation | ADAPIDKSIDKWFFI CCCCCCCCCCCEEEE | 32.07 | 21440633 | |
| 279 | Ubiquitination | PIDKSIDKWFFISGS CCCCCCCCEEEEECC | 44.20 | 23749301 | |
| 286 | Phosphorylation | KWFFISGSV------ CEEEEECCC------ | 20.19 | 15665377 |
| 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 IPYR_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IPYR_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 IPYR_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-65; THR-247; THR-251;THR-253; SER-255 AND SER-266, AND MASS 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 THR-61 AND SER-266, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251 AND SER-286, ANDMASS SPECTROMETRY. | |
| "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 THR-251, AND MASSSPECTROMETRY. | |
