UniProt ID | PSR1_YEAST | |
---|---|---|
UniProt AC | Q07800 | |
Protein Name | Phosphatase PSR1 | |
Gene Name | PSR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 427 | |
Subcellular Localization | Cell membrane . | |
Protein Description | Has phosphatase activity in vitro. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR2. Also involved in the general stress response; acts together with WHI2 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2.. | |
Protein Sequence | MGFISSILCCSSETTQSNSNSAYRQQQSSSLNKNRSVKHSNTKSRTRGVHQTNSPPSKTNSAATFSSTERSTGKSGISTNDNEKKKPSSPTAAVTATTTNNMTKVEKRISKDDLYEEKYEVDEDEEIDDEDNRRSRGIVQEKGDAVKDTSRQKKQQQQQQQQSQPQPQPQSQSQSQSQSQSQQRGPTVQVSSDHLIQDMNLSRVSSSSQASETSNDADDEDDEDEEYIDLTLLQQGQYHAPGYNTLLPPQDESTKGKKCLILDLDETLVHSSFKYLRSADFVLSVEIDDQVHNVYVIKRPGVEEFLERVGKLFEVVVFTASVSRYGDPLLDILDTDKVIHHRLFREACYNYEGNYIKNLSQIGRPLSDIIILDNSPASYIFHPQHAIPISSWFSDTHDNELLDIIPLLEDLSVKTSLDVGKILDVTI | |
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 |
---|---|---|---|---|---|
9 | S-palmitoylation | GFISSILCCSSETTQ CCCCEEEECCCCCCC | 1.70 | 10777497 | |
10 | S-palmitoylation | FISSILCCSSETTQS CCCEEEECCCCCCCC | 4.49 | 10777497 | |
30 | Phosphorylation | YRQQQSSSLNKNRSV HHHHHHHHCCCCCCC | 41.00 | 28889911 | |
52 | Phosphorylation | RTRGVHQTNSPPSKT CCCCCCCCCCCCCCC | 23.84 | 21440633 | |
54 | Phosphorylation | RGVHQTNSPPSKTNS CCCCCCCCCCCCCCC | 41.39 | 23749301 | |
57 | Phosphorylation | HQTNSPPSKTNSAAT CCCCCCCCCCCCCCC | 56.34 | 23749301 | |
58 | Ubiquitination | QTNSPPSKTNSAATF CCCCCCCCCCCCCCE | 58.46 | 23749301 | |
59 | Phosphorylation | TNSPPSKTNSAATFS CCCCCCCCCCCCCEE | 38.45 | 22369663 | |
61 | Phosphorylation | SPPSKTNSAATFSST CCCCCCCCCCCEECC | 25.22 | 22369663 | |
64 | Phosphorylation | SKTNSAATFSSTERS CCCCCCCCEECCCCC | 24.62 | 22369663 | |
66 | Phosphorylation | TNSAATFSSTERSTG CCCCCCEECCCCCCC | 31.81 | 20377248 | |
67 | Phosphorylation | NSAATFSSTERSTGK CCCCCEECCCCCCCC | 30.05 | 22369663 | |
68 | Phosphorylation | SAATFSSTERSTGKS CCCCEECCCCCCCCC | 33.93 | 22369663 | |
71 | Phosphorylation | TFSSTERSTGKSGIS CEECCCCCCCCCCCC | 34.97 | 19823750 | |
72 | Phosphorylation | FSSTERSTGKSGIST EECCCCCCCCCCCCC | 55.65 | 24961812 | |
74 | Ubiquitination | STERSTGKSGISTND CCCCCCCCCCCCCCC | 45.67 | 23749301 | |
75 | Phosphorylation | TERSTGKSGISTNDN CCCCCCCCCCCCCCC | 42.58 | 28889911 | |
78 | Phosphorylation | STGKSGISTNDNEKK CCCCCCCCCCCCCCC | 25.36 | 25521595 | |
79 | Phosphorylation | TGKSGISTNDNEKKK CCCCCCCCCCCCCCC | 44.67 | 28889911 | |
84 | Ubiquitination | ISTNDNEKKKPSSPT CCCCCCCCCCCCCCC | 72.80 | 23749301 | |
88 | Phosphorylation | DNEKKKPSSPTAAVT CCCCCCCCCCCEEEE | 58.80 | 21440633 | |
89 | Phosphorylation | NEKKKPSSPTAAVTA CCCCCCCCCCEEEEE | 34.49 | 21440633 | |
91 | Phosphorylation | KKKPSSPTAAVTATT CCCCCCCCEEEEEEC | 29.24 | 21440633 | |
95 | Phosphorylation | SSPTAAVTATTTNNM CCCCEEEEEECCCCC | 17.35 | 27017623 | |
103 | Phosphorylation | ATTTNNMTKVEKRIS EECCCCCHHHEEECC | 33.78 | 21440633 | |
110 | Phosphorylation | TKVEKRISKDDLYEE HHHEEECCHHHHHHH | 33.78 | 22369663 | |
111 | Ubiquitination | KVEKRISKDDLYEEK HHEEECCHHHHHHHH | 53.54 | 23749301 | |
115 | Phosphorylation | RISKDDLYEEKYEVD ECCHHHHHHHHCCCC | 29.09 | 22890988 | |
142 | Ubiquitination | SRGIVQEKGDAVKDT CCCCHHHHHHHHHHH | 45.03 | 23749301 | |
150 | Phosphorylation | GDAVKDTSRQKKQQQ HHHHHHHHHHHHHHH | 42.73 | 25533186 | |
154 | Ubiquitination | KDTSRQKKQQQQQQQ HHHHHHHHHHHHHHH | 45.03 | 23749301 | |
173 | Phosphorylation | QPQPQSQSQSQSQSQ CCCCCCHHHHHHHHH | 36.73 | 23749301 | |
177 | Phosphorylation | QSQSQSQSQSQSQQR CCHHHHHHHHHHHHC | 36.73 | 23749301 | |
181 | Phosphorylation | QSQSQSQSQQRGPTV HHHHHHHHHHCCCCE | 33.26 | 28889911 | |
187 | Phosphorylation | QSQQRGPTVQVSSDH HHHHCCCCEEECHHH | 26.79 | 22369663 | |
191 | Phosphorylation | RGPTVQVSSDHLIQD CCCCEEECHHHHHHC | 16.98 | 22369663 | |
192 | Phosphorylation | GPTVQVSSDHLIQDM CCCEEECHHHHHHCC | 30.14 | 22369663 | |
258 | Ubiquitination | DESTKGKKCLILDLD CCCCCCCEEEEEECC | 42.83 | 17644757 | |
274 | Ubiquitination | TLVHSSFKYLRSADF HHHHHHHHHHHHCCE | 45.37 | 17644757 | |
319 | Phosphorylation | LFEVVVFTASVSRYG HEEEEEEEEEHHHHC | 13.35 | 27017623 | |
323 | Phosphorylation | VVFTASVSRYGDPLL EEEEEEHHHHCCCHH | 19.79 | 27017623 | |
335 | Phosphorylation | PLLDILDTDKVIHHR CHHHHHCCCCCHHHH | 33.98 | 27017623 | |
337 | Acetylation | LDILDTDKVIHHRLF HHHHCCCCCHHHHHH | 45.22 | 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 PSR1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSR1_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 PSR1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Palmitoylation | |
Reference | PubMed |
"Psr1p/Psr2p, two plasma membrane phosphatases with an essentialDXDX(T/V) motif required for sodium stress response in yeast."; Siniossoglou S., Hurt E.C., Pelham H.R.B.; J. Biol. Chem. 275:19352-19360(2000). Cited for: FUNCTION, SUBCELLULAR LOCATION, POSSIBLE PALMITOYLATION,PHOSPHORYLATION, AND MUTAGENESIS OF GLY-2; 9-CYS-CYS-10; ASP-263 ANDASP-265. | |
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-61 AND SER-191, AND MASSSPECTROMETRY. | |
"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-110, AND MASSSPECTROMETRY. |