UniProt ID | PSP2_YEAST | |
---|---|---|
UniProt AC | P50109 | |
Protein Name | Protein PSP2 | |
Gene Name | PSP2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 593 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | DNA polymerase alpha mutation suppressor. Suppressor of group II intron splicing defects of a mutation in MRS2. May play a role in mitochondrial mRNA splicing.. | |
Protein Sequence | MGTNNTSNNNGTTKKMSLEEFLGNDTLGESVWDEEDINLDAISNTTNIDILKQTKAGEHQRDGHQQHPHGGHGPMNRSRFSNAGPFGGGSMGDFANHHHPLQHQQGPPYIVKFSDLPPRFSNFDIEDLFQAKFTKFIKFKLFWEINKNPSISTLKSGSIFDQNFKRDSKVAFVELYTSRDMDKILNYWTTPLKEIYHITTAPAEFEDFKDYSTKVKLLTDPKDDAGKPFITKTQRSKSNPFGSAKPVDTQSKILDIEEKMENLHVEDTTTLRASLIPSSDSMATTATGSKITILKKQTPTEEESHSATPTPKPLSYSEVVERSVVNETSKKGTPLSKLDSPALELQSKPDKSDEFKGGDEQGFEKGGDDKAQLDVSNDKDKGSETDVDKQFTFKNVEREHSMSRTKYNGNHNNNNGNFRGSNRYRGGPNGSSYKGGHNNRGNRGGYRGGSSYNNNNNNTNDNNNNNNNSSSNNNNGSRYHDRQNNEEGLTSDSSLDASGNKKNDFTNSTSNTQQYSIFKPASGFLGQGNNDSIRNNGRGNYNSSGMNGGSRGRGFGRGRGFGRGAYNNRGSRGGRGSSGNYSNYNNRTTDMPL | |
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 |
---|---|---|---|---|---|
147 | Ubiquitination | KLFWEINKNPSISTL EEEEECCCCCCCEEE | 75.73 | 24961812 | |
150 | Phosphorylation | WEINKNPSISTLKSG EECCCCCCCEEECCC | 38.27 | 21440633 | |
152 | Phosphorylation | INKNPSISTLKSGSI CCCCCCCEEECCCCC | 31.83 | 24961812 | |
153 | Phosphorylation | NKNPSISTLKSGSIF CCCCCCEEECCCCCC | 36.21 | 24961812 | |
155 | Ubiquitination | NPSISTLKSGSIFDQ CCCCEEECCCCCCCC | 53.51 | 24961812 | |
178 | Phosphorylation | AFVELYTSRDMDKIL EEEEEEECCCHHHHH | 16.84 | 28889911 | |
183 | Acetylation | YTSRDMDKILNYWTT EECCCHHHHHHHHCC | 42.32 | 24489116 | |
209 | Acetylation | PAEFEDFKDYSTKVK CCCCCCCCCCCCEEE | 68.99 | 24489116 | |
216 | Ubiquitination | KDYSTKVKLLTDPKD CCCCCEEEECCCCCC | 39.06 | 15699485 | |
222 | Acetylation | VKLLTDPKDDAGKPF EEECCCCCCCCCCCC | 71.67 | 24489116 | |
222 | Ubiquitination | VKLLTDPKDDAGKPF EEECCCCCCCCCCCC | 71.67 | 15699485 | |
227 | Ubiquitination | DPKDDAGKPFITKTQ CCCCCCCCCCCCCCC | 38.18 | 15699485 | |
232 | Ubiquitination | AGKPFITKTQRSKSN CCCCCCCCCCCCCCC | 37.53 | 15699485 | |
233 | Phosphorylation | GKPFITKTQRSKSNP CCCCCCCCCCCCCCC | 22.14 | 21551504 | |
236 | Phosphorylation | FITKTQRSKSNPFGS CCCCCCCCCCCCCCC | 30.53 | 22369663 | |
237 | Ubiquitination | ITKTQRSKSNPFGSA CCCCCCCCCCCCCCC | 57.34 | 15699485 | |
238 | Phosphorylation | TKTQRSKSNPFGSAK CCCCCCCCCCCCCCC | 51.48 | 22369663 | |
243 | Phosphorylation | SKSNPFGSAKPVDTQ CCCCCCCCCCCCCCH | 33.23 | 20377248 | |
245 | Ubiquitination | SNPFGSAKPVDTQSK CCCCCCCCCCCCHHH | 47.47 | 15699485 | |
249 | Phosphorylation | GSAKPVDTQSKILDI CCCCCCCCHHHCCCH | 34.67 | 21440633 | |
251 | Phosphorylation | AKPVDTQSKILDIEE CCCCCCHHHCCCHHH | 24.61 | 19823750 | |
252 | Ubiquitination | KPVDTQSKILDIEEK CCCCCHHHCCCHHHH | 37.15 | 15699485 | |
281 | Phosphorylation | SLIPSSDSMATTATG ECCCCCCCCCEECCC | 16.56 | 19779198 | |
292 | Phosphorylation | TATGSKITILKKQTP ECCCCEEEEEECCCC | 24.80 | 19779198 | |
296 | Ubiquitination | SKITILKKQTPTEEE CEEEEEECCCCCCCC | 56.83 | 24961812 | |
298 | Phosphorylation | ITILKKQTPTEEESH EEEEECCCCCCCCCC | 40.85 | 20377248 | |
300 | Phosphorylation | ILKKQTPTEEESHSA EEECCCCCCCCCCCC | 60.46 | 20377248 | |
304 | Phosphorylation | QTPTEEESHSATPTP CCCCCCCCCCCCCCC | 26.48 | 21440633 | |
306 | Phosphorylation | PTEEESHSATPTPKP CCCCCCCCCCCCCCC | 43.02 | 28889911 | |
308 | Phosphorylation | EEESHSATPTPKPLS CCCCCCCCCCCCCCC | 30.61 | 28889911 | |
312 | Ubiquitination | HSATPTPKPLSYSEV CCCCCCCCCCCHHHH | 62.15 | 24961812 | |
315 | Phosphorylation | TPTPKPLSYSEVVER CCCCCCCCHHHHHHH | 34.83 | 30377154 | |
317 | Phosphorylation | TPKPLSYSEVVERSV CCCCCCHHHHHHHHH | 22.12 | 30377154 | |
329 | Phosphorylation | RSVVNETSKKGTPLS HHHHCCCCCCCCCHH | 26.62 | 28889911 | |
333 | Phosphorylation | NETSKKGTPLSKLDS CCCCCCCCCHHHCCC | 29.90 | 27214570 | |
340 | Phosphorylation | TPLSKLDSPALELQS CCHHHCCCCCHHHCC | 23.62 | 22369663 | |
347 | Phosphorylation | SPALELQSKPDKSDE CCCHHHCCCCCCCCC | 59.80 | 20377248 | |
348 | Ubiquitination | PALELQSKPDKSDEF CCHHHCCCCCCCCCC | 44.25 | 24961812 | |
351 | Ubiquitination | ELQSKPDKSDEFKGG HHCCCCCCCCCCCCC | 69.22 | 24961812 | |
356 | Ubiquitination | PDKSDEFKGGDEQGF CCCCCCCCCCCHHCC | 60.99 | 24961812 | |
376 | Phosphorylation | DKAQLDVSNDKDKGS CCCEECCCCCCCCCC | 38.69 | 25704821 | |
383 | Phosphorylation | SNDKDKGSETDVDKQ CCCCCCCCCCCCHHH | 42.96 | 28889911 | |
385 | Phosphorylation | DKDKGSETDVDKQFT CCCCCCCCCCHHHCE | 42.91 | 28889911 | |
401 | Phosphorylation | KNVEREHSMSRTKYN CCHHHCCCCCCEECC | 17.44 | 17287358 | |
405 | Phosphorylation | REHSMSRTKYNGNHN HCCCCCCEECCCCCC | 30.49 | 21440633 | |
491 | Phosphorylation | NNEEGLTSDSSLDAS CCCCCCCCCCCCCCC | 40.30 | 28889911 | |
494 | Phosphorylation | EGLTSDSSLDASGNK CCCCCCCCCCCCCCC | 34.95 | 28889911 | |
516 | Phosphorylation | TSNTQQYSIFKPASG CCCCCEEEEECCCCC | 19.74 | 30377154 | |
519 | Ubiquitination | TQQYSIFKPASGFLG CCEEEEECCCCCCCC | 37.69 | 24961812 | |
522 | Phosphorylation | YSIFKPASGFLGQGN EEEECCCCCCCCCCC | 38.31 | 24909858 | |
577 | Phosphorylation | GSRGGRGSSGNYSNY CCCCCCCCCCCCCCC | 33.44 | 28889911 | |
584 | Phosphorylation | SSGNYSNYNNRTTDM CCCCCCCCCCCCCCC | 14.10 | 27017623 |
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 PSP2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSP2_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 PSP2_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 SER-236; SER-238 ANDSER-340, AND MASS 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-238, 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-401, 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-238 AND SER-340, ANDMASS SPECTROMETRY. |