| UniProt ID | PIL1_YEAST | |
|---|---|---|
| UniProt AC | P53252 | |
| Protein Name | Sphingolipid long chain base-responsive protein PIL1 | |
| Gene Name | PIL1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 339 | |
| Subcellular Localization | Lipid droplet . | |
| Protein Description | Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.. | |
| Protein Sequence | MHRTYSLRNSRAPTASQLQNPPPPPSTTKGRFFGKGGLAYSFRRSAAGAFGPELSRKLSQLVKIEKNVLRSMELTANERRDAAKQLSIWGLENDDDVSDITDKLGVLIYEVSELDDQFIDRYDQYRLTLKSIRDIEGSVQPSRDRKDKITDKIAYLKYKDPQSPKIEVLEQELVRAEAESLVAEAQLSNITRSKLRAAFNYQFDSIIEHSEKIALIAGYGKALLELLDDSPVTPGETRPAYDGYEASKQIIIDAESALNEWTLDSAQVKPTLSFKQDYEDFEPEEGEEEEEEDGQGRWSEDEQEDGQIEEPEQEEEGAVEEHEQVGHQQSESLPQQTTA | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MHRTYSLRNSR ----CCCCCCCCCCC | 11.64 | 21440633 | |
| 5 | Phosphorylation | ---MHRTYSLRNSRA ---CCCCCCCCCCCC | 12.98 | 19823750 | |
| 6 | Phosphorylation | --MHRTYSLRNSRAP --CCCCCCCCCCCCC | 21.90 | 28152593 | |
| 10 | Phosphorylation | RTYSLRNSRAPTASQ CCCCCCCCCCCCHHH | 24.32 | 28152593 | |
| 14 | Phosphorylation | LRNSRAPTASQLQNP CCCCCCCCHHHHCCC | 37.65 | 19823750 | |
| 16 | Phosphorylation | NSRAPTASQLQNPPP CCCCCCHHHHCCCCC | 33.62 | 19823750 | |
| 26 | Phosphorylation | QNPPPPPSTTKGRFF CCCCCCCCCCCCCCC | 55.25 | 27214570 | |
| 27 | Phosphorylation | NPPPPPSTTKGRFFG CCCCCCCCCCCCCCC | 38.00 | 28152593 | |
| 28 | Phosphorylation | PPPPPSTTKGRFFGK CCCCCCCCCCCCCCC | 35.52 | 25752575 | |
| 29 | Ubiquitination | PPPPSTTKGRFFGKG CCCCCCCCCCCCCCC | 48.45 | 23749301 | |
| 35 | Acetylation | TKGRFFGKGGLAYSF CCCCCCCCCCHHHHH | 44.65 | 24489116 | |
| 35 | Ubiquitination | TKGRFFGKGGLAYSF CCCCCCCCCCHHHHH | 44.65 | 22817900 | |
| 40 | Phosphorylation | FGKGGLAYSFRRSAA CCCCCHHHHHHHHHC | 17.24 | 21440633 | |
| 41 | Phosphorylation | GKGGLAYSFRRSAAG CCCCHHHHHHHHHCH | 13.48 | 22369663 | |
| 45 | Phosphorylation | LAYSFRRSAAGAFGP HHHHHHHHHCHHHCH | 20.43 | 25533186 | |
| 55 | Phosphorylation | GAFGPELSRKLSQLV HHHCHHHHHHHHHHH | 26.21 | 25704821 | |
| 57 | Ubiquitination | FGPELSRKLSQLVKI HCHHHHHHHHHHHHH | 49.46 | 23749301 | |
| 59 | Phosphorylation | PELSRKLSQLVKIEK HHHHHHHHHHHHHHH | 25.22 | 25533186 | |
| 63 | Acetylation | RKLSQLVKIEKNVLR HHHHHHHHHHHHHHH | 54.46 | 24489116 | |
| 63 | Ubiquitination | RKLSQLVKIEKNVLR HHHHHHHHHHHHHHH | 54.46 | 22817900 | |
| 66 | Acetylation | SQLVKIEKNVLRSME HHHHHHHHHHHHHCC | 56.69 | 24489116 | |
| 66 | Ubiquitination | SQLVKIEKNVLRSME HHHHHHHHHHHHHCC | 56.69 | 23749301 | |
| 84 | Ubiquitination | NERRDAAKQLSIWGL HHHHHHHHHHHEECC | 54.19 | 23749301 | |
| 98 | Phosphorylation | LENDDDVSDITDKLG CCCCCCHHHHHHHHC | 30.23 | 21440633 | |
| 101 | Phosphorylation | DDDVSDITDKLGVLI CCCHHHHHHHHCEEE | 31.88 | 28889911 | |
| 130 | Ubiquitination | DQYRLTLKSIRDIEG HHHHEHHHHHHHCCC | 38.30 | 23749301 | |
| 130 | Acetylation | DQYRLTLKSIRDIEG HHHHEHHHHHHHCCC | 38.30 | 24489116 | |
| 131 | Phosphorylation | QYRLTLKSIRDIEGS HHHEHHHHHHHCCCC | 26.43 | 19779198 | |
| 138 | Phosphorylation | SIRDIEGSVQPSRDR HHHHCCCCCCCCCCC | 12.56 | 23749301 | |
| 142 | Phosphorylation | IEGSVQPSRDRKDKI CCCCCCCCCCCCCHH | 29.71 | 28889911 | |
| 148 | Acetylation | PSRDRKDKITDKIAY CCCCCCCHHCCEEEH | 51.01 | 24489116 | |
| 152 | Acetylation | RKDKITDKIAYLKYK CCCHHCCEEEHHHCC | 22.15 | 24489116 | |
| 152 | Ubiquitination | RKDKITDKIAYLKYK CCCHHCCEEEHHHCC | 22.15 | 23749301 | |
| 157 | Acetylation | TDKIAYLKYKDPQSP CCEEEHHHCCCCCCC | 37.26 | 24489116 | |
| 158 | Phosphorylation | DKIAYLKYKDPQSPK CEEEHHHCCCCCCCC | 20.30 | 22369663 | |
| 159 | Acetylation | KIAYLKYKDPQSPKI EEEHHHCCCCCCCCC | 62.44 | 24489116 | |
| 163 | Phosphorylation | LKYKDPQSPKIEVLE HHCCCCCCCCCHHHH | 33.28 | 22369663 | |
| 165 | Ubiquitination | YKDPQSPKIEVLEQE CCCCCCCCCHHHHHH | 57.66 | 24961812 | |
| 165 | Acetylation | YKDPQSPKIEVLEQE CCCCCCCCCHHHHHH | 57.66 | 24489116 | |
| 180 | Phosphorylation | LVRAEAESLVAEAQL HHHHHHHHHHHHHHH | 34.88 | 25752575 | |
| 188 | Phosphorylation | LVAEAQLSNITRSKL HHHHHHHHHCCHHHH | 17.69 | 19823750 | |
| 191 | Phosphorylation | EAQLSNITRSKLRAA HHHHHHCCHHHHHHH | 32.89 | 19823750 | |
| 193 | Phosphorylation | QLSNITRSKLRAAFN HHHHCCHHHHHHHHH | 27.65 | 19823750 | |
| 212 | Ubiquitination | SIIEHSEKIALIAGY HHHHCHHHHHHHCCH | 35.97 | 23749301 | |
| 221 | Ubiquitination | ALIAGYGKALLELLD HHHCCHHHHHHHHHC | 27.64 | 23749301 | |
| 230 | Phosphorylation | LLELLDDSPVTPGET HHHHHCCCCCCCCCC | 22.42 | 22369663 | |
| 233 | Phosphorylation | LLDDSPVTPGETRPA HHCCCCCCCCCCCCC | 29.03 | 22369663 | |
| 237 | Phosphorylation | SPVTPGETRPAYDGY CCCCCCCCCCCCCCC | 48.11 | 22369663 | |
| 241 | Phosphorylation | PGETRPAYDGYEASK CCCCCCCCCCCHHHC | 16.75 | 22369663 | |
| 244 | Phosphorylation | TRPAYDGYEASKQII CCCCCCCCHHHCEEE | 12.86 | 21440633 | |
| 247 | Phosphorylation | AYDGYEASKQIIIDA CCCCCHHHCEEEEEH | 17.10 | 22369663 | |
| 256 | Phosphorylation | QIIIDAESALNEWTL EEEEEHHHHHCCCCC | 39.51 | 22369663 | |
| 262 | Phosphorylation | ESALNEWTLDSAQVK HHHHCCCCCCHHHCC | 17.95 | 22369663 | |
| 265 | Phosphorylation | LNEWTLDSAQVKPTL HCCCCCCHHHCCCCC | 24.58 | 22369663 | |
| 271 | Phosphorylation | DSAQVKPTLSFKQDY CHHHCCCCCCCCCCH | 29.35 | 22369663 | |
| 273 | Phosphorylation | AQVKPTLSFKQDYED HHCCCCCCCCCCHHH | 32.64 | 22369663 | |
| 278 | Phosphorylation | TLSFKQDYEDFEPEE CCCCCCCHHHCCCCC | 18.20 | 28889911 | |
| 299 | Phosphorylation | EDGQGRWSEDEQEDG CCCCCCCCHHHCCCC | 33.53 | 28889911 |
| 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 PIL1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PIL1_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 PIL1_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-14; SER-16; SER-41;SER-45; SER-163; SER-180; SER-230; THR-233; THR-237 AND SER-273, 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-59; SER-163; SER-230 ANDTHR-233, AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, 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-163 AND THR-233, ANDMASS SPECTROMETRY. | |
| "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-233, 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-233, AND MASSSPECTROMETRY. | |
