| UniProt ID | KAPR_YEAST | |
|---|---|---|
| UniProt AC | P07278 | |
| Protein Name | cAMP-dependent protein kinase regulatory subunit | |
| Gene Name | BCY1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 416 | |
| Subcellular Localization | Cytoplasm. Nucleus. Cytoplasmic when phosphorylated. Nuclear when not phosphorylated. | |
| Protein Description | Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in the absence of cAMP. cAMP activates PKA and promotes growth and proliferation in response to good nutrient conditions. Together with ZDS1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1.. | |
| Protein Sequence | MVSSLPKESQAELQLFQNEINAANPSDFLQFSANYFNKRLEQQRAFLKAREPEFKAKNIVLFPEPEESFSRPQSAQSQSRSRSSVMFKSPFVNEDPHSNVFKSGFNLDPHEQDTHQQAQEEQQHTREKTSTPPLPMHFNAQRRTSVSGETLQPNNFDDWTPDHYKEKSEQQLQRLEKSIRNNFLFNKLDSDSKRLVINCLEEKSVPKGATIIKQGDQGDYFYVVEKGTVDFYVNDNKVNSSGPGSSFGELALMYNSPRAATVVATSDCLLWALDRLTFRKILLGSSFKKRLMYDDLLKSMPVLKSLTTYDRAKLADALDTKIYQPGETIIREGDQGENFYLIEYGAVDVSKKGQGVINKLKDHDYFGEVALLNDLPRQATVTATKRTKVATLGKSGFQRLLGPAVDVLKLNDPTRH | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MVSSLPKESQ -----CCCCCCHHHH | 25.51 | 28889911 | |
| 4 | Phosphorylation | ----MVSSLPKESQA ----CCCCCCHHHHH | 36.96 | 28889911 | |
| 9 | Phosphorylation | VSSLPKESQAELQLF CCCCCHHHHHHHHHH | 40.59 | 28889911 | |
| 57 | Ubiquitination | REPEFKAKNIVLFPE CCCCHHCCCEEEECC | 48.04 | 19722269 | |
| 68 | Phosphorylation | LFPEPEESFSRPQSA EECCCHHHCCCCCHH | 27.19 | 22369663 | |
| 70 | Phosphorylation | PEPEESFSRPQSAQS CCCHHHCCCCCHHHC | 52.94 | 22369663 | |
| 74 | Phosphorylation | ESFSRPQSAQSQSRS HHCCCCCHHHCCCCC | 30.84 | 22369663 | |
| 77 | Phosphorylation | SRPQSAQSQSRSRSS CCCCHHHCCCCCCCC | 29.82 | 22369663 | |
| 79 | Phosphorylation | PQSAQSQSRSRSSVM CCHHHCCCCCCCCCC | 37.15 | 22369663 | |
| 81 | Phosphorylation | SAQSQSRSRSSVMFK HHHCCCCCCCCCCEE | 41.58 | 22369663 | |
| 83 | Phosphorylation | QSQSRSRSSVMFKSP HCCCCCCCCCCEECC | 28.65 | 22369663 | |
| 84 | Phosphorylation | SQSRSRSSVMFKSPF CCCCCCCCCCEECCC | 19.25 | 22369663 | |
| 88 | Acetylation | SRSSVMFKSPFVNED CCCCCCEECCCCCCC | 38.84 | 24489116 | |
| 89 | Phosphorylation | RSSVMFKSPFVNEDP CCCCCEECCCCCCCC | 16.59 | 25752575 | |
| 98 | Phosphorylation | FVNEDPHSNVFKSGF CCCCCCCCCCCCCCC | 39.82 | 22369663 | |
| 102 | Acetylation | DPHSNVFKSGFNLDP CCCCCCCCCCCCCCC | 45.44 | 22865919 | |
| 103 | Phosphorylation | PHSNVFKSGFNLDPH CCCCCCCCCCCCCCC | 36.83 | 30377154 | |
| 114 | Phosphorylation | LDPHEQDTHQQAQEE CCCCCCHHHHHHHHH | 22.68 | 28889911 | |
| 125 | Phosphorylation | AQEEQQHTREKTSTP HHHHHHHHHHHCCCC | 35.86 | 28889911 | |
| 129 | Phosphorylation | QQHTREKTSTPPLPM HHHHHHHCCCCCCCC | 32.83 | 22369663 | |
| 130 | Phosphorylation | QHTREKTSTPPLPMH HHHHHHCCCCCCCCC | 50.40 | 22369663 | |
| 131 | Phosphorylation | HTREKTSTPPLPMHF HHHHHCCCCCCCCCC | 33.87 | 22369663 | |
| 144 | Phosphorylation | HFNAQRRTSVSGETL CCCCCCCCCCCCCCC | 35.35 | 22369663 | |
| 145 | Phosphorylation | FNAQRRTSVSGETLQ CCCCCCCCCCCCCCC | 16.69 | 22369663 | |
| 147 | Phosphorylation | AQRRTSVSGETLQPN CCCCCCCCCCCCCCC | 30.58 | 22369663 | |
| 150 | Phosphorylation | RTSVSGETLQPNNFD CCCCCCCCCCCCCCC | 33.93 | 22369663 | |
| 160 | Phosphorylation | PNNFDDWTPDHYKEK CCCCCCCCHHHHHHH | 26.32 | 22890988 | |
| 164 | Phosphorylation | DDWTPDHYKEKSEQQ CCCCHHHHHHHHHHH | 28.37 | 22890988 | |
| 165 | Acetylation | DWTPDHYKEKSEQQL CCCHHHHHHHHHHHH | 56.07 | 24489116 | |
| 187 | Acetylation | RNNFLFNKLDSDSKR HHCCHHHCCCCCCCE | 46.46 | 24489116 | |
| 203 | Acetylation | VINCLEEKSVPKGAT EHHHHHHCCCCCCCE | 47.59 | 24489116 | |
| 285 | Phosphorylation | FRKILLGSSFKKRLM HHHHHHCCHHHHHHC | 32.35 | 30377154 | |
| 286 | Phosphorylation | RKILLGSSFKKRLMY HHHHHCCHHHHHHCH | 39.01 | 30377154 | |
| 288 | Acetylation | ILLGSSFKKRLMYDD HHHCCHHHHHHCHHH | 38.64 | 24489116 | |
| 298 | Acetylation | LMYDDLLKSMPVLKS HCHHHHHHHCHHHHH | 52.59 | 24489116 | |
| 304 | Ubiquitination | LKSMPVLKSLTTYDR HHHCHHHHHCCHHCH | 43.59 | 23749301 | |
| 305 | Phosphorylation | KSMPVLKSLTTYDRA HHCHHHHHCCHHCHH | 27.13 | 28889911 | |
| 309 | Phosphorylation | VLKSLTTYDRAKLAD HHHHCCHHCHHHHHH | 9.74 | 28889911 | |
| 313 | Acetylation | LTTYDRAKLADALDT CCHHCHHHHHHHHCC | 45.14 | 22865919 | |
| 321 | Acetylation | LADALDTKIYQPGET HHHHHCCCCCCCCCE | 38.80 | 24489116 | |
| 382 | Phosphorylation | LPRQATVTATKRTKV CCCCEEEEEECCCEE | 25.01 | 27214570 | |
| 409 | Acetylation | GPAVDVLKLNDPTRH CCCEEEEECCCCCCC | 45.13 | 24489116 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 145 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 145 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 129 | T | Phosphorylation |
| 20702584 |
| 129 | T | Phosphorylation |
| 20702584 |
| 129 | T | Phosphorylation |
| 20702584 |
| 130 | S | Phosphorylation |
| 20702584 |
| 131 | T | Phosphorylation |
| 20702584 |
| 144 | T | Phosphorylation |
| 20702584 |
| 145 | S | Phosphorylation |
| 18407956 |
| 145 | S | Phosphorylation |
| 18407956 |
| 145 | S | Phosphorylation |
| 18407956 |
| 147 | S | Phosphorylation |
| 20702584 |
| 150 | T | Phosphorylation |
| 19779198 |
| 160 | T | Phosphorylation |
| 20702584 |
* 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 KAPR_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "The rapamycin-sensitive phosphoproteome reveals that TOR controlsprotein kinase A toward some but not all substrates."; Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.; Mol. Biol. Cell 21:3475-3486(2010). Cited for: PHOSPHORYLATION AT SER-68; SER-70; SER-74; SER-77; SER-79; SER-83;SER-83; SER-84; THR-129; SER-130; THR-131; THR-144; SER-145; SER-147;THR-150 AND THR-160, AND MUTAGENESIS OF THR-129. | |
| "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-68; SER-70; SER-74;SER-77; SER-83; THR-129; SER-130; THR-131; THR-144 AND SER-145, ANDMASS 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-74; SER-79; SER-83;THR-129; SER-130 AND THR-131, AND MASS 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-83, AND MASSSPECTROMETRY. | |
| "Cloning and characterization of BCY1, a locus encoding a regulatorysubunit of the cyclic AMP-dependent protein kinase in Saccharomycescerevisiae."; Toda T., Cameron S., Sass P., Zoller M., Scott J.D., McMullen B.,Hurwitz M., Krebs E.G., Wigler M.; Mol. Cell. Biol. 7:1371-1377(1987). Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-80; 83-126;139-177; 195-203; 227-275; 291-298; 310-340; 345-377 AND 387-399,FUNCTION, AND SUBUNIT. | |
| "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-144, AND MASSSPECTROMETRY. | |
