UniProt ID | PEA2_YEAST | |
---|---|---|
UniProt AC | P40091 | |
Protein Name | Protein PEA2 | |
Gene Name | PEA2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 420 | |
Subcellular Localization | ||
Protein Description | Localized to sites of polarized growth and is required for efficient mating and bipolar budding.. | |
Protein Sequence | MHKFDLELSRRANPLLFSAERYEEYPLKYDELKQYLLSQNPSHPHHNSRPYTSIDYFDYLLYRSKNDESEIDLDKKLVSEFALYYVQKEHLNSDDLNPTLNELLKLQPKSADWYEMMLRILESINTTGIDQLTKENNNSFPNSKRARSSTNMGGTDKFNKGAYHTDKADDDKNEILQELTSFLMSNSIQKGIDIKPIPLDDPVKFLKNGINSILDTCVSLEKNTSSPPISPNAAAIQEEDSSKKLEELETAFSDLQLAHNFLTKQFENDRAEYVQDIEKLTRTNRELQDKLLNNHSNLSKTEKKLHELEQENKELEKANNKLNSSRHNFGMSSPASSPVTWDPSSPSSVGSPTSGSGSRSLSIMTSEFKKVLTSTQRKYEKELSDEREHRFKLERELALLKNAEANTSLALNRDDPPDML | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
148 | Phosphorylation | PNSKRARSSTNMGGT CCCCHHCCCCCCCCC | 40.30 | 25521595 | |
149 | Phosphorylation | NSKRARSSTNMGGTD CCCHHCCCCCCCCCC | 20.46 | 29136822 | |
150 | Phosphorylation | SKRARSSTNMGGTDK CCHHCCCCCCCCCCC | 30.39 | 19823750 | |
160 | Ubiquitination | GGTDKFNKGAYHTDK CCCCCCCCCCCCCCC | 48.31 | 22106047 | |
163 | Phosphorylation | DKFNKGAYHTDKADD CCCCCCCCCCCCCCC | 17.58 | 19823750 | |
165 | Phosphorylation | FNKGAYHTDKADDDK CCCCCCCCCCCCCCH | 26.90 | 19823750 | |
180 | Phosphorylation | NEILQELTSFLMSNS HHHHHHHHHHHHHCC | 19.38 | 19823750 | |
181 | Phosphorylation | EILQELTSFLMSNSI HHHHHHHHHHHHCCC | 29.07 | 19823750 | |
185 | Phosphorylation | ELTSFLMSNSIQKGI HHHHHHHHCCCCCCC | 29.58 | 19823750 | |
187 | Phosphorylation | TSFLMSNSIQKGIDI HHHHHHCCCCCCCCC | 21.06 | 19823750 | |
224 | Phosphorylation | CVSLEKNTSSPPISP HHHHCCCCCCCCCCC | 41.47 | 22369663 | |
225 | Phosphorylation | VSLEKNTSSPPISPN HHHCCCCCCCCCCCC | 50.68 | 25521595 | |
226 | Phosphorylation | SLEKNTSSPPISPNA HHCCCCCCCCCCCCH | 32.43 | 22369663 | |
230 | Phosphorylation | NTSSPPISPNAAAIQ CCCCCCCCCCHHHHC | 20.20 | 22369663 | |
241 | Phosphorylation | AAIQEEDSSKKLEEL HHHCCCHHHHHHHHH | 47.54 | 22890988 | |
242 | Phosphorylation | AIQEEDSSKKLEELE HHCCCHHHHHHHHHH | 46.24 | 22890988 | |
332 | Phosphorylation | SRHNFGMSSPASSPV HHHCCCCCCCCCCCC | 33.28 | 22369663 | |
333 | Phosphorylation | RHNFGMSSPASSPVT HHCCCCCCCCCCCCC | 18.65 | 22369663 | |
336 | Phosphorylation | FGMSSPASSPVTWDP CCCCCCCCCCCCCCC | 38.26 | 21440633 | |
337 | Phosphorylation | GMSSPASSPVTWDPS CCCCCCCCCCCCCCC | 26.04 | 23749301 | |
340 | Phosphorylation | SPASSPVTWDPSSPS CCCCCCCCCCCCCCC | 27.77 | 22369663 | |
344 | Phosphorylation | SPVTWDPSSPSSVGS CCCCCCCCCCCCCCC | 53.02 | 22369663 | |
345 | Phosphorylation | PVTWDPSSPSSVGSP CCCCCCCCCCCCCCC | 33.90 | 22369663 | |
347 | Phosphorylation | TWDPSSPSSVGSPTS CCCCCCCCCCCCCCC | 39.33 | 22369663 | |
348 | Phosphorylation | WDPSSPSSVGSPTSG CCCCCCCCCCCCCCC | 33.60 | 22369663 | |
351 | Phosphorylation | SSPSSVGSPTSGSGS CCCCCCCCCCCCCCC | 23.89 | 22369663 | |
353 | Phosphorylation | PSSVGSPTSGSGSRS CCCCCCCCCCCCCCC | 47.63 | 22369663 | |
354 | Phosphorylation | SSVGSPTSGSGSRSL CCCCCCCCCCCCCCC | 34.05 | 22369663 | |
356 | Phosphorylation | VGSPTSGSGSRSLSI CCCCCCCCCCCCCEE | 33.10 | 22369663 | |
358 | Phosphorylation | SPTSGSGSRSLSIMT CCCCCCCCCCCEECC | 22.01 | 22369663 | |
360 | Phosphorylation | TSGSGSRSLSIMTSE CCCCCCCCCEECCHH | 28.32 | 28132839 | |
362 | Phosphorylation | GSGSRSLSIMTSEFK CCCCCCCEECCHHHH | 16.15 | 21440633 | |
373 | Phosphorylation | SEFKKVLTSTQRKYE HHHHHHHHHHHHHHH | 32.49 | 30377154 | |
407 | Phosphorylation | LKNAEANTSLALNRD HHCCHHHHHHCCCCC | 31.97 | 27017623 | |
408 | Phosphorylation | KNAEANTSLALNRDD HCCHHHHHHCCCCCC | 16.08 | 21551504 |
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 PEA2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PEA2_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 PEA2_YEAST !! |
Kegg Drug | ||||||
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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-150; THR-224; SER-225;SER-226; SER-230 AND SER-345, 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-230, AND MASSSPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-230, ANDMASS SPECTROMETRY. |