UniProt ID | ODPA_YEAST | |
---|---|---|
UniProt AC | P16387 | |
Protein Name | Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial | |
Gene Name | PDA1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 420 | |
Subcellular Localization | Mitochondrion matrix. | |
Protein Description | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).. | |
Protein Sequence | MLAASFKRQPSQLVRGLGAVLRTPTRIGHVRTMATLKTTDKKAPEDIEGSDTVQIELPESSFESYMLEPPDLSYETSKATLLQMYKDMVIIRRMEMACDALYKAKKIRGFCHLSVGQEAIAVGIENAITKLDSIITSYRCHGFTFMRGASVKAVLAELMGRRAGVSYGKGGSMHLYAPGFYGGNGIVGAQVPLGAGLAFAHQYKNEDACSFTLYGDGASNQGQVFESFNMAKLWNLPVVFCCENNKYGMGTAASRSSAMTEYFKRGQYIPGLKVNGMDILAVYQASKFAKDWCLSGKGPLVLEYETYRYGGHSMSDPGTTYRTRDEIQHMRSKNDPIAGLKMHLIDLGIATEAEVKAYDKSARKYVDEQVELADAAPPPEAKLSILFEDVYVKGTETPTLRGRIPEDTWDFKKQGFASRD | |
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 |
---|---|---|---|---|---|
32 | Phosphorylation | TRIGHVRTMATLKTT CCCCCEEEEEEEECC | 15.29 | 28889911 | |
35 | Phosphorylation | GHVRTMATLKTTDKK CCEEEEEEEECCCCC | 20.26 | 26447709 | |
86 | Acetylation | ATLLQMYKDMVIIRR HHHHHHHHHHHHHHH | 33.72 | 24489116 | |
103 | Acetylation | MACDALYKAKKIRGF HHHHHHHHCHHHCCC | 55.36 | 24489116 | |
138 | Phosphorylation | LDSIITSYRCHGFTF HHHHHHHCCCCCEEC | 14.49 | 29650682 | |
152 | Acetylation | FMRGASVKAVLAELM CCCCCCHHHHHHHHH | 30.22 | 24489116 | |
247 | Phosphorylation | FCCENNKYGMGTAAS EEECCCCCCCCCHHC | 17.92 | 22369663 | |
251 | Phosphorylation | NNKYGMGTAASRSSA CCCCCCCCHHCCHHH | 15.34 | 22369663 | |
254 | Phosphorylation | YGMGTAASRSSAMTE CCCCCHHCCHHHHHH | 30.17 | 22369663 | |
264 | Acetylation | SAMTEYFKRGQYIPG HHHHHHHHCCCCCCC | 55.51 | 24489116 | |
264 | Succinylation | SAMTEYFKRGQYIPG HHHHHHHHCCCCCCC | 55.51 | 23954790 | |
268 | Phosphorylation | EYFKRGQYIPGLKVN HHHHCCCCCCCCEEC | 16.35 | 22369663 | |
287 | Acetylation | LAVYQASKFAKDWCL HHHHHHHHHHHHHHH | 52.97 | 24489116 | |
290 | Acetylation | YQASKFAKDWCLSGK HHHHHHHHHHHHCCC | 55.69 | 25381059 | |
304 | Phosphorylation | KGPLVLEYETYRYGG CCCEEEEEEEEEECC | 14.92 | 22369663 | |
306 | Phosphorylation | PLVLEYETYRYGGHS CEEEEEEEEEECCCC | 16.64 | 22369663 | |
307 | Phosphorylation | LVLEYETYRYGGHSM EEEEEEEEEECCCCC | 7.01 | 22369663 | |
309 | Phosphorylation | LEYETYRYGGHSMSD EEEEEEEECCCCCCC | 19.62 | 22369663 | |
313 | Phosphorylation | TYRYGGHSMSDPGTT EEEECCCCCCCCCCC | 24.21 | 22369663 | |
315 | Phosphorylation | RYGGHSMSDPGTTYR EECCCCCCCCCCCEE | 43.60 | 22369663 | |
319 | Phosphorylation | HSMSDPGTTYRTRDE CCCCCCCCCEECHHH | 26.49 | 22890988 | |
320 | Phosphorylation | SMSDPGTTYRTRDEI CCCCCCCCEECHHHH | 19.54 | 22890988 | |
321 | Phosphorylation | MSDPGTTYRTRDEIQ CCCCCCCEECHHHHH | 15.15 | 22890988 | |
332 | Phosphorylation | DEIQHMRSKNDPIAG HHHHHHHHCCCCCCH | 28.38 | 19779198 | |
333 | Acetylation | EIQHMRSKNDPIAGL HHHHHHHCCCCCCHH | 55.81 | 22865919 | |
341 | Acetylation | NDPIAGLKMHLIDLG CCCCCHHHHHHHHHC | 24.29 | 25381059 | |
360 | Acetylation | AEVKAYDKSARKYVD HHHHHCCHHHHHHHH | 33.08 | 24489116 | |
364 | Acetylation | AYDKSARKYVDEQVE HCCHHHHHHHHHHHH | 49.71 | 24489116 | |
395 | Phosphorylation | EDVYVKGTETPTLRG EEEEECCCCCCCCCC | 30.85 | 21126336 | |
397 | Phosphorylation | VYVKGTETPTLRGRI EEECCCCCCCCCCCC | 22.78 | 28889911 | |
399 | Phosphorylation | VKGTETPTLRGRIPE ECCCCCCCCCCCCCC | 36.19 | 27214570 | |
412 | Acetylation | PEDTWDFKKQGFASR CCCCCCHHHCCCCCC | 41.53 | 24489116 | |
413 | 2-Hydroxyisobutyrylation | EDTWDFKKQGFASRD CCCCCHHHCCCCCCC | 56.50 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
313 | S | Phosphorylation | Kinase | PDK2 | P53170 | Uniprot |
313 | S | Phosphorylation | Kinase | PDK1 | - | Uniprot |
* 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 ODPA_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 TYR-309; SER-313 ANDSER-315, 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-313 AND SER-315, 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 SER-313, AND MASSSPECTROMETRY. | |
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase."; Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.; Mol. Cell. Proteomics 6:1896-1906(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, 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-313, 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 SER-254 AND SER-313, ANDMASS SPECTROMETRY. | |
"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-313, AND MASSSPECTROMETRY. |