| UniProt ID | SLM2_YEAST | |
|---|---|---|
| UniProt AC | P53955 | |
| Protein Name | Phosphatidylinositol 4,5-bisphosphate-binding protein SLM2 | |
| Gene Name | SLM2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 656 | |
| Subcellular Localization |
Cell membrane Peripheral membrane protein Cytoplasmic side . |
|
| Protein Description | Together with SLM1, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin, inhibiting interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.. | |
| Protein Sequence | MSYQRNSARASLDLRSQYQQLEGRMRSEHFNPAYQQQQQKGQNIPLSLPSSLAQRNPIPYPIDAVTSDPTIPAQLNVYDHDRQNSIVDAAAGTNTTHSLNSNNIPSSQNNNINNNNINNVGSFTDPSMLTLPKMSLHSHQKQYDSNQNDPRSPLAILIPTSAQPTDVLSARFSAWRNVIRAILVYLSETASIQDEIVRQQLRLSHAVQFPFFSIENQYQPVSNEDKSMQKFFLPLGSGSVQDLPTMLTKYHDNLASLASKSSKELTSEIIPRLEDLRRDLLVKIKEIKALQSDFKNSCNKELQQTKHLMKLFNESLKECKLGTPKSDPFLIKLQLEKQIKRQLVEENYLHEAFDNLQNSGAQLESVIVMEIQNGLTSYARILGKEAQVVFDSVISKLDSTILNKNTNLEWDSFILRNISNFVPPNLPMRRFKEISYSNQNDPFTFEVKSGFLEKRSKFLKSYSRGFYVLTPSFLHEFKTPDKHKFSTPLMSIPLVECTVTEHSKKTKSNSEQGKNKFILRTNSNGLIHRGHNWVFKVDSYDDMIEWFGNIKALSSLPNYDDKCKYVSKVAKLSKEKAKSNENTTESVTPQVTNEQHTRYDDVSSSNFPLNSIPKLDNLTITNTTSSIPETNDSQIQNRVPEFYIENVDSPRKSNQL | |
| 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 |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MSYQRNSARASLDL -CCCCHHCHHHHHHH | 22.71 | 28889911 | |
| 11 | Phosphorylation | QRNSARASLDLRSQY CHHCHHHHHHHHHHH | 19.50 | 28889911 | |
| 40 | Ubiquitination | AYQQQQQKGQNIPLS HHHHHHHCCCCCCCC | 59.11 | 17644757 | |
| 47 | Phosphorylation | KGQNIPLSLPSSLAQ CCCCCCCCCCHHHHH | 32.64 | 19684113 | |
| 50 | Phosphorylation | NIPLSLPSSLAQRNP CCCCCCCHHHHHHCC | 43.19 | 28889911 | |
| 51 | Phosphorylation | IPLSLPSSLAQRNPI CCCCCCHHHHHHCCC | 26.28 | 28889911 | |
| 226 | Ubiquitination | QPVSNEDKSMQKFFL CCCCCCCHHHHHEEE | 41.47 | 17644757 | |
| 384 | Ubiquitination | SYARILGKEAQVVFD HHHHHHCHHHHHHHH | 46.56 | 24961812 | |
| 523 | Phosphorylation | KFILRTNSNGLIHRG CEEEEECCCCCEECC | 31.49 | 27214570 | |
| 578 | Ubiquitination | KLSKEKAKSNENTTE HHCHHHHHCCCCCCC | 65.95 | 23749301 | |
| 586 | Phosphorylation | SNENTTESVTPQVTN CCCCCCCCCCCCCCC | 29.24 | 23749301 | |
| 588 | Phosphorylation | ENTTESVTPQVTNEQ CCCCCCCCCCCCCCC | 19.79 | 29136822 | |
| 592 | Phosphorylation | ESVTPQVTNEQHTRY CCCCCCCCCCCCCCC | 27.99 | 23749301 | |
| 603 | Phosphorylation | HTRYDDVSSSNFPLN CCCCCCCCCCCCCCC | 34.74 | 23749301 | |
| 604 | Phosphorylation | TRYDDVSSSNFPLNS CCCCCCCCCCCCCCC | 29.20 | 23749301 | |
| 605 | Phosphorylation | RYDDVSSSNFPLNSI CCCCCCCCCCCCCCC | 34.68 | 21440633 | |
| 611 | Phosphorylation | SSNFPLNSIPKLDNL CCCCCCCCCCCCCCE | 48.20 | 21551504 | |
| 619 | Phosphorylation | IPKLDNLTITNTTSS CCCCCCEEEECCCCC | 31.82 | 21440633 | |
| 621 | Phosphorylation | KLDNLTITNTTSSIP CCCCEEEECCCCCCC | 22.68 | 30377154 | |
| 623 | Phosphorylation | DNLTITNTTSSIPET CCEEEECCCCCCCCC | 21.29 | 27738172 | |
| 624 | Phosphorylation | NLTITNTTSSIPETN CEEEECCCCCCCCCC | 23.65 | 21440633 | |
| 625 | Phosphorylation | LTITNTTSSIPETND EEEECCCCCCCCCCH | 25.00 | 20377248 | |
| 626 | Phosphorylation | TITNTTSSIPETNDS EEECCCCCCCCCCHH | 39.82 | 19779198 | |
| 630 | Phosphorylation | TTSSIPETNDSQIQN CCCCCCCCCHHHHHH | 38.68 | 21440633 | |
| 643 | Phosphorylation | QNRVPEFYIENVDSP HHHCCEEEEECCCCC | 12.98 | 21440633 | |
| 649 | Phosphorylation | FYIENVDSPRKSNQL EEEECCCCCCCCCCC | 23.48 | 17330950 | |
| 652 | Ubiquitination | ENVDSPRKSNQL--- ECCCCCCCCCCC--- | 58.08 | 23749301 | |
| 653 | Phosphorylation | NVDSPRKSNQL---- CCCCCCCCCCC---- | 30.96 | 25752575 |
| 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 SLM2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SLM2_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 SLM2_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-624; SER-626; SER-649AND SER-653, AND MASS 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 SER-649, AND MASSSPECTROMETRY. | |