UniProt ID | PP2A2_YEAST | |
---|---|---|
UniProt AC | P23595 | |
Protein Name | Serine/threonine-protein phosphatase PP2A-2 catalytic subunit | |
Gene Name | PPH22 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 377 | |
Subcellular Localization | ||
Protein Description | Exact function not known, phosphatase 2A performs an essential cellular function.. | |
Protein Sequence | MDMEIDDPMHGSDEDQLSPTLDEDMNSDDGKNNTKARSNDEDTDEELEDFNFKPGSSGIADHKSSKPLKLTNTNINQLDQWIEHLSKCEPLSEDDVARLCKMAVDVLQFEENVKPINVPVTICGDVHGQFHDLLELFKIGGPCPDTNYLFMGDYVDRGYYSVETVSYLVAMKVRYPHRITILRGNHESRQITQVYGFYDECLRKYGSANVWKMFTDLFDYFPVTALVDNKIFCLHGGLSPMIETIDQVRDLNRIQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGFTFGQDISEQFNHTNDLSLIARAHQLVMEGYSWSHQQNVVTIFSAPNYCYRCGNQAAIMEVDENHNRQFLQYDPSVRPGEPTVTRKTPDYFL | |
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 |
---|---|---|---|---|---|
12 | Phosphorylation | IDDPMHGSDEDQLSP CCCCCCCCCHHHCCC | 24.13 | 28152593 | |
18 | Phosphorylation | GSDEDQLSPTLDEDM CCCHHHCCCCCCCCC | 15.37 | 28152593 | |
27 | Phosphorylation | TLDEDMNSDDGKNNT CCCCCCCCCCCCCCC | 30.37 | 28889911 | |
38 | Phosphorylation | KNNTKARSNDEDTDE CCCCCCCCCCCCCHH | 54.19 | 22369663 | |
43 | Phosphorylation | ARSNDEDTDEELEDF CCCCCCCCHHHHHHC | 43.17 | 22369663 | |
53 | Acetylation | ELEDFNFKPGSSGIA HHHHCCCCCCCCCCC | 49.96 | 24489116 | |
56 | Phosphorylation | DFNFKPGSSGIADHK HCCCCCCCCCCCCCC | 33.64 | 17563356 | |
57 | Phosphorylation | FNFKPGSSGIADHKS CCCCCCCCCCCCCCC | 39.88 | 29136822 | |
64 | Phosphorylation | SGIADHKSSKPLKLT CCCCCCCCCCCCCCC | 39.93 | 25704821 | |
73 | Phosphorylation | KPLKLTNTNINQLDQ CCCCCCCCCHHHHHH | 32.04 | 21440633 | |
239 | Phosphorylation | FCLHGGLSPMIETID EEECCCCHHHHHHHH | 18.72 | 28889911 | |
280 | Phosphorylation | DRGGWGISPRGAGFT CCCCCCCCCCCCCCC | 12.47 | 22369663 | |
371 | Ubiquitination | GEPTVTRKTPDYFL- CCCCCCCCCCCCCC- | 55.85 | 23749301 | |
372 | Phosphorylation | EPTVTRKTPDYFL-- CCCCCCCCCCCCC-- | 20.36 | 27214570 | |
377 | Methylation | RKTPDYFL------- CCCCCCCC------- | 5.81 | 11060018 |
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 PP2A2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PP2A2_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 PP2A2_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-43 AND SER-56, AND MASSSPECTROMETRY. | |
"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-56, 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 THR-43, 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 THR-43, AND MASSSPECTROMETRY. |