| UniProt ID | 2A5D_YEAST | |
|---|---|---|
| UniProt AC | P38903 | |
| Protein Name | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform | |
| Gene Name | RTS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 757 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.; Multicopy suppressor of ROX3 and HSP60.. | |
| Protein Sequence | MMRGFKQRLIKKTTGSSSSSSSKKKDKEKEKEKSSTTSSTSKKPASASSSSHGTTHSSASSTGSKSTTEKGKQSGSVPSQGKHHSSSTSKTKTATTPSSSSSSSRSSSVSRSGSSSTKKTSSRKGQEQSKQSQQPSQSQKQGSSSSSAAIMNPTPVLTVTKDDKSTSGEDHAHPTLLGAVSAVPSSPISNASGTAVSSDVENGNSNNNNMNINTSNTQDANHASSQSIDIPRSSHSFERLPTPTKLNPDTDLELIKTPQRHSSSRFEPSRYTPLTKLPNFNEVSPEERIPLFIAKVDQCNTMFDFNDPSFDIQGKEIKRSTLDELIEFLVTNRFTYTNEMYAHVVNMFKINLFRPIPPPVNPVGDIYDPDEDEPVNELAWPHMQAVYEFFLRFVESPDFNHQIAKQYIDQDFILKLLELFDSEDIRERDCLKTTLHRIYGKFLSLRSFIRRSMNNIFLQFIYETEKFNGVAELLEILGSIINGFALPLKEEHKVFLVRILIPLHKVRCLSLYHPQLAYCIVQFLEKDPLLTEEVVMGLLRYWPKINSTKEIMFLNEIEDIFEVIEPLEFIKVEVPLFVQLAKCISSPHFQVAEKVLSYWNNEYFLNLCIENAEVILPIIFPALYELTSQLELDTANGEDSISDPYMLVEQAINSGSWNRAIHAMAFKALKIFLETNPVLYENCNALYLSSVKETQQRKVQREENWSKLEEYVKNLRINNDKDQYTIKNPELRNSFNTASENNTLNEENENDCDSEIQ | |
| 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 |
|---|---|---|---|---|---|
| 6 | Acetylation | --MMRGFKQRLIKKT --CCCCHHHHHHHHC | 37.01 | 25381059 | |
| 14 | Phosphorylation | QRLIKKTTGSSSSSS HHHHHHCCCCCCCCC | 43.90 | 28889911 | |
| 19 | Phosphorylation | KTTGSSSSSSSKKKD HCCCCCCCCCCCCCH | 35.87 | 28889911 | |
| 20 | Phosphorylation | TTGSSSSSSSKKKDK CCCCCCCCCCCCCHH | 40.35 | 28889911 | |
| 21 | Phosphorylation | TGSSSSSSSKKKDKE CCCCCCCCCCCCHHH | 48.39 | 28889911 | |
| 22 | Phosphorylation | GSSSSSSSKKKDKEK CCCCCCCCCCCHHHH | 50.90 | 28889911 | |
| 62 | Phosphorylation | THSSASSTGSKSTTE CCCCCCCCCCCCCCC | 42.87 | 27017623 | |
| 76 | Phosphorylation | EKGKQSGSVPSQGKH CCCCCCCCCCCCCCC | 35.78 | 21551504 | |
| 79 | Phosphorylation | KQSGSVPSQGKHHSS CCCCCCCCCCCCCCC | 49.78 | 28889911 | |
| 82 | Acetylation | GSVPSQGKHHSSSTS CCCCCCCCCCCCCCC | 30.43 | 25381059 | |
| 91 | Phosphorylation | HSSSTSKTKTATTPS CCCCCCCCEEECCCC | 33.13 | 21551504 | |
| 93 | Phosphorylation | SSTSKTKTATTPSSS CCCCCCEEECCCCCC | 34.17 | 22369663 | |
| 95 | Phosphorylation | TSKTKTATTPSSSSS CCCCEEECCCCCCCC | 44.46 | 22369663 | |
| 96 | Phosphorylation | SKTKTATTPSSSSSS CCCEEECCCCCCCCC | 20.79 | 22369663 | |
| 98 | Phosphorylation | TKTATTPSSSSSSSR CEEECCCCCCCCCCC | 40.54 | 22369663 | |
| 99 | Phosphorylation | KTATTPSSSSSSSRS EEECCCCCCCCCCCC | 35.13 | 22369663 | |
| 100 | Phosphorylation | TATTPSSSSSSSRSS EECCCCCCCCCCCCC | 38.28 | 22369663 | |
| 101 | Phosphorylation | ATTPSSSSSSSRSSS ECCCCCCCCCCCCCC | 35.87 | 22369663 | |
| 102 | Phosphorylation | TTPSSSSSSSRSSSV CCCCCCCCCCCCCCC | 33.99 | 22369663 | |
| 103 | Phosphorylation | TPSSSSSSSRSSSVS CCCCCCCCCCCCCCC | 31.55 | 20377248 | |
| 104 | Phosphorylation | PSSSSSSSRSSSVSR CCCCCCCCCCCCCCC | 37.82 | 20377248 | |
| 106 | Phosphorylation | SSSSSSRSSSVSRSG CCCCCCCCCCCCCCC | 28.98 | 20377248 | |
| 107 | Phosphorylation | SSSSSRSSSVSRSGS CCCCCCCCCCCCCCC | 33.38 | 21551504 | |
| 108 | Phosphorylation | SSSSRSSSVSRSGSS CCCCCCCCCCCCCCC | 25.92 | 20377248 | |
| 110 | Phosphorylation | SSRSSSVSRSGSSST CCCCCCCCCCCCCCC | 23.76 | 22369663 | |
| 114 | Phosphorylation | SSVSRSGSSSTKKTS CCCCCCCCCCCCCCC | 23.51 | 21440633 | |
| 233 | Phosphorylation | QSIDIPRSSHSFERL CCCCCCCCCCCCCCC | 27.35 | 30377154 | |
| 234 | Phosphorylation | SIDIPRSSHSFERLP CCCCCCCCCCCCCCC | 25.16 | 30377154 | |
| 236 | Phosphorylation | DIPRSSHSFERLPTP CCCCCCCCCCCCCCC | 30.65 | 21082442 | |
| 242 | Phosphorylation | HSFERLPTPTKLNPD CCCCCCCCCCCCCCC | 48.45 | 17330950 | |
| 244 | Phosphorylation | FERLPTPTKLNPDTD CCCCCCCCCCCCCCC | 51.12 | 23607784 | |
| 245 | Ubiquitination | ERLPTPTKLNPDTDL CCCCCCCCCCCCCCH | 47.69 | 23749301 | |
| 245 | Acetylation | ERLPTPTKLNPDTDL CCCCCCCCCCCCCCH | 47.69 | 24489116 | |
| 250 | Phosphorylation | PTKLNPDTDLELIKT CCCCCCCCCHHHCCC | 43.68 | 28889911 | |
| 256 | Acetylation | DTDLELIKTPQRHSS CCCHHHCCCCCCCCC | 67.77 | 24489116 | |
| 256 | Ubiquitination | DTDLELIKTPQRHSS CCCHHHCCCCCCCCC | 67.77 | 23749301 | |
| 257 | Phosphorylation | TDLELIKTPQRHSSS CCHHHCCCCCCCCCC | 20.05 | 19823750 | |
| 262 | Phosphorylation | IKTPQRHSSSRFEPS CCCCCCCCCCCCCCC | 32.00 | 22890988 | |
| 263 | Phosphorylation | KTPQRHSSSRFEPSR CCCCCCCCCCCCCCC | 21.29 | 19823750 | |
| 264 | Phosphorylation | TPQRHSSSRFEPSRY CCCCCCCCCCCCCCC | 43.96 | ||
| 269 | Phosphorylation | SSSRFEPSRYTPLTK CCCCCCCCCCCCCCC | 30.62 | 19823750 | |
| 271 | Phosphorylation | SRFEPSRYTPLTKLP CCCCCCCCCCCCCCC | 19.63 | 24961812 | |
| 272 | Phosphorylation | RFEPSRYTPLTKLPN CCCCCCCCCCCCCCC | 15.65 | 19823750 | |
| 275 | Phosphorylation | PSRYTPLTKLPNFNE CCCCCCCCCCCCCCC | 31.57 | 29136822 | |
| 276 | Ubiquitination | SRYTPLTKLPNFNEV CCCCCCCCCCCCCCC | 70.41 | 24961812 | |
| 405 | Acetylation | DFNHQIAKQYIDQDF CCCHHHHHHHCCHHH | 45.31 | 24489116 | |
| 441 | Acetylation | TLHRIYGKFLSLRSF HHHHHHHHHHHHHHH | 26.59 | 24489116 | |
| 707 | Acetylation | QREENWSKLEEYVKN HHHHHHHHHHHHHHH | 52.08 | 24489116 | |
| 721 | Acetylation | NLRINNDKDQYTIKN HCCCCCCCCCCEECC | 49.18 | 24489116 | |
| 721 | Ubiquitination | NLRINNDKDQYTIKN HCCCCCCCCCCEECC | 49.18 | 23749301 | |
| 734 | Phosphorylation | KNPELRNSFNTASEN CCHHHHHHHCCCCCC | 17.28 | 20377248 | |
| 737 | Phosphorylation | ELRNSFNTASENNTL HHHHHHCCCCCCCCC | 29.56 | 20377248 | |
| 739 | Phosphorylation | RNSFNTASENNTLNE HHHHCCCCCCCCCCC | 38.53 | 20377248 | |
| 743 | Phosphorylation | NTASENNTLNEENEN CCCCCCCCCCCCCCC | 42.41 | 20377248 | |
| 754 | Phosphorylation | ENENDCDSEIQ---- CCCCCCCCCCC---- | 42.82 | 20377248 |
| 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 2A5D_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 2A5D_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 2A5D_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 SER-236; THR-242; THR-257AND THR-272, 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 THR-257 AND THR-272, ANDMASS SPECTROMETRY. | |
| "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-272, 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-242, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-272, AND MASSSPECTROMETRY. | |
