| UniProt ID | IRS4_YEAST | |
|---|---|---|
| UniProt AC | P36115 | |
| Protein Name | Increased rDNA silencing protein 4 | |
| Gene Name | IRS4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 615 | |
| Subcellular Localization | ||
| Protein Description | With TAX4, acts as a positive regulator of INP51 activity and phosphatidylinositol 4,5-bisphosphate turnover. Negatively regulates signaling through the cell integrity pathway, including the MAP kinase SLT2. Seems also to be involved in rDNA silencing.. | |
| Protein Sequence | MRLSFGKQRYHGGTTVTLTEQGASDSLRAAQAIFQNHSNEVSSPCPPVTVSRNPQTRLSEPSLQKSGRKQEQKKARIRTKQVPKIKTTAPNDVELSKKHRSSPAGKDNVSSTAQMAAALAHSQSKLSSDNNSSHSSALDTLKVLETPNLNGLLGIHSRSSSRNGSNESLTPGQRTPDNRSQENLLTSFSSGRRLSSSSMEPATNKDSNKALPKRRPSPPLQSSLVGSGQLHENENLSSISIDSRHSLNPDTSDVISNRSQTSLSQTINQLSLCESEPSIASSNTTTTTSNQGSGLPNLVPNYSSDMRKKKLVNKFKRKVFGSKPKHLSSQYEMDASSEELGQHEQQPSMRFKTTLRKTSVSTNAENDHASSLHEGNLRYKYNPSNDTYDVYDDTDSDSESDQNQDALTKPRKRDRIKRKIRNSANKTAHHRPIHRTRDRKFNEDKPWKSHTDITFVTDNERKRYESMWVSNRHRHLNLLSWWPSITGDSGAINTLPEDGLILGIIVRDIWKRSNLPNSLLAEIYTKVDTRKDGTLDRKSFIVGMWLVDQCLYGRKLPNVVEQCVWDSVDRYASTTVVPVSTLKAMAKQKRKQMKEEIKNIKKENRVVLVDHNSSS | |
| 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 |
|---|---|---|---|---|---|
| 102 | Phosphorylation | LSKKHRSSPAGKDNV HHHHHCCCCCCCCCH | 20.80 | 21551504 | |
| 110 | Phosphorylation | PAGKDNVSSTAQMAA CCCCCCHHHHHHHHH | 28.38 | 21551504 | |
| 128 | Phosphorylation | HSQSKLSSDNNSSHS HHHHHHCCCCCCCCC | 55.59 | 21551504 | |
| 132 | Phosphorylation | KLSSDNNSSHSSALD HHCCCCCCCCCHHHH | 35.36 | 21440633 | |
| 133 | Phosphorylation | LSSDNNSSHSSALDT HCCCCCCCCCHHHHH | 29.52 | 21440633 | |
| 135 | Phosphorylation | SDNNSSHSSALDTLK CCCCCCCCHHHHHHH | 21.18 | 21440633 | |
| 136 | Phosphorylation | DNNSSHSSALDTLKV CCCCCCCHHHHHHHH | 27.68 | 21440633 | |
| 157 | Phosphorylation | NGLLGIHSRSSSRNG CCCCEEECCCCCCCC | 31.75 | 22369663 | |
| 165 | Phosphorylation | RSSSRNGSNESLTPG CCCCCCCCCCCCCCC | 40.76 | 28889911 | |
| 168 | Phosphorylation | SRNGSNESLTPGQRT CCCCCCCCCCCCCCC | 41.62 | 28889911 | |
| 175 | Phosphorylation | SLTPGQRTPDNRSQE CCCCCCCCCCCCCHH | 27.40 | 28889911 | |
| 180 | Phosphorylation | QRTPDNRSQENLLTS CCCCCCCCHHHHHHH | 48.37 | 29650682 | |
| 195 | Phosphorylation | FSSGRRLSSSSMEPA HCCCCCCCCCCCCCC | 26.77 | 22369663 | |
| 196 | Phosphorylation | SSGRRLSSSSMEPAT CCCCCCCCCCCCCCC | 30.90 | 22369663 | |
| 197 | Phosphorylation | SGRRLSSSSMEPATN CCCCCCCCCCCCCCC | 30.26 | 22369663 | |
| 198 | Phosphorylation | GRRLSSSSMEPATNK CCCCCCCCCCCCCCC | 29.16 | 22369663 | |
| 203 | Phosphorylation | SSSMEPATNKDSNKA CCCCCCCCCCCCCCC | 54.22 | 22369663 | |
| 246 | Phosphorylation | ISIDSRHSLNPDTSD CEECCCCCCCCCHHH | 28.82 | 28889911 | |
| 256 | Phosphorylation | PDTSDVISNRSQTSL CCHHHHHCCCCHHHH | 26.49 | 28889911 | |
| 331 | Phosphorylation | PKHLSSQYEMDASSE CCCCCHHHCCCCCHH | 18.37 | 27017623 | |
| 336 | Phosphorylation | SQYEMDASSEELGQH HHHCCCCCHHHHHHH | 33.74 | 24961812 | |
| 337 | Phosphorylation | QYEMDASSEELGQHE HHCCCCCHHHHHHHC | 36.49 | 24961812 | |
| 348 | Phosphorylation | GQHEQQPSMRFKTTL HHHCCCCCHHCCCEE | 20.46 | 24961812 | |
| 353 | Phosphorylation | QPSMRFKTTLRKTSV CCCHHCCCEEECCCC | 28.49 | 24961812 | |
| 354 | Phosphorylation | PSMRFKTTLRKTSVS CCHHCCCEEECCCCC | 25.75 | 24961812 | |
| 358 | Phosphorylation | FKTTLRKTSVSTNAE CCCEEECCCCCCCCC | 28.11 | 28889911 | |
| 359 | Phosphorylation | KTTLRKTSVSTNAEN CCEEECCCCCCCCCC | 19.67 | 25005228 | |
| 361 | Phosphorylation | TLRKTSVSTNAENDH EEECCCCCCCCCCCC | 18.73 | 21440633 | |
| 362 | Phosphorylation | LRKTSVSTNAENDHA EECCCCCCCCCCCCC | 35.97 | 28889911 | |
| 370 | Phosphorylation | NAENDHASSLHEGNL CCCCCCCCCCCCCCE | 29.97 | 21440633 | |
| 371 | Phosphorylation | AENDHASSLHEGNLR CCCCCCCCCCCCCEE | 34.23 | 21440633 | |
| 394 | Phosphorylation | TYDVYDDTDSDSESD CEEECCCCCCCCCCH | 34.21 | 21551504 | |
| 396 | Phosphorylation | DVYDDTDSDSESDQN EECCCCCCCCCCHHC | 45.16 | 21551504 | |
| 400 | Phosphorylation | DTDSDSESDQNQDAL CCCCCCCCHHCHHHH | 48.74 | 21551504 | |
| 613 | Phosphorylation | VVLVDHNSSS----- EEEEECCCCC----- | 28.65 | 20377248 | |
| 614 | Phosphorylation | VLVDHNSSS------ EEEECCCCC------ | 45.44 | 22369663 | |
| 615 | Phosphorylation | LVDHNSSS------- EEECCCCC------- | 44.02 | 20377248 |
| 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 IRS4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IRS4_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 IRS4_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-180, 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 SER-614, AND MASSSPECTROMETRY. | |