| UniProt ID | CAP_YEAST | |
|---|---|---|
| UniProt AC | P17555 | |
| Protein Name | Adenylyl cyclase-associated protein | |
| Gene Name | SRV2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 526 | |
| Subcellular Localization | Cytoplasm, cytoskeleton, actin patch . Cortical actin patches. | |
| Protein Description | The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control.. | |
| Protein Sequence | MPDSKYTMQGYNLVKLLKRLEEATARLEDVTIYQEGYIQNKLEASKNNKPSDSGADANTTNEPSAENAPEVEQDPKCITAFQSYIGENIDPLVELSGKIDTVVLDALQLLKGGFQSQLTFLRAAVRSRKPDYSSQTFADSLRPINENIIKLGQLKESNRQSKYFAYLSALSEGAPLFSWVAVDTPVSMVTDFKDAAQFWTNRILKEYRESDPNAVEWVKKFLASFDNLKAYIKEYHTTGVSWKKDGMDFADAMAQSTKNTGATSSPSPASATAAPAPPPPPPAPPASVFEISNDTPATSSDANKGGIGAVFAELNQGENITKGLKKVDKSQQTHKNPELRQSSTVSSTGSKSGPPPRPKKPSTLKTKRPPRKELVGNKWFIENYENETESLVIDANKDESIFIGKCSQVLVQIKGKVNAISLSETESCSVVLDSSISGMDVIKSNKFGIQVNHSLPQISIDKSDGGNIYLSKESLNTEIYTSCSTAINVNLPIGEDDDYVEFPIPEQMKHSFADGKFKSAVFEHAG | |
| 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 |
|---|---|---|---|---|---|
| 15 | Acetylation | MQGYNLVKLLKRLEE HHHHHHHHHHHHHHH | 51.79 | 24489116 | |
| 49 | Ubiquitination | LEASKNNKPSDSGAD HHHHCCCCCCCCCCC | 56.12 | 23749301 | |
| 59 | Phosphorylation | DSGADANTTNEPSAE CCCCCCCCCCCCCHH | 32.49 | 26447709 | |
| 60 | Phosphorylation | SGADANTTNEPSAEN CCCCCCCCCCCCHHC | 37.07 | 23749301 | |
| 64 | Phosphorylation | ANTTNEPSAENAPEV CCCCCCCCHHCCCCH | 41.87 | 23749301 | |
| 155 | Ubiquitination | IIKLGQLKESNRQSK HHHHHHHHHCCCCHH | 51.73 | 23749301 | |
| 205 | Acetylation | FWTNRILKEYRESDP HHHHHHHHHHHHHCC | 50.78 | 22865919 | |
| 219 | Acetylation | PNAVEWVKKFLASFD CCHHHHHHHHHHCCH | 38.59 | 24489116 | |
| 219 | Succinylation | PNAVEWVKKFLASFD CCHHHHHHHHHHCCH | 38.59 | 23954790 | |
| 220 | Ubiquitination | NAVEWVKKFLASFDN CHHHHHHHHHHCCHH | 35.67 | 24961812 | |
| 229 | Acetylation | LASFDNLKAYIKEYH HHCCHHHHHHHHHHH | 45.45 | 24489116 | |
| 233 | Acetylation | DNLKAYIKEYHTTGV HHHHHHHHHHHCCCC | 39.27 | 24489116 | |
| 237 | Phosphorylation | AYIKEYHTTGVSWKK HHHHHHHCCCCCCCC | 25.09 | 21440633 | |
| 256 | Phosphorylation | FADAMAQSTKNTGAT HHHHHHHHCCCCCCC | 31.63 | 28889911 | |
| 260 | Phosphorylation | MAQSTKNTGATSSPS HHHHCCCCCCCCCCC | 29.74 | 30377154 | |
| 263 | Phosphorylation | STKNTGATSSPSPAS HCCCCCCCCCCCCCC | 30.96 | 21551504 | |
| 265 | Phosphorylation | KNTGATSSPSPASAT CCCCCCCCCCCCCCC | 25.66 | 19779198 | |
| 267 | Phosphorylation | TGATSSPSPASATAA CCCCCCCCCCCCCCC | 34.74 | 28889911 | |
| 270 | Phosphorylation | TSSPSPASATAAPAP CCCCCCCCCCCCCCC | 29.54 | 30377154 | |
| 272 | Phosphorylation | SPSPASATAAPAPPP CCCCCCCCCCCCCCC | 22.36 | 19779198 | |
| 299 | Phosphorylation | SNDTPATSSDANKGG ECCCCCCCCCCCCCC | 28.47 | 27017623 | |
| 300 | Phosphorylation | NDTPATSSDANKGGI CCCCCCCCCCCCCCC | 36.07 | 27017623 | |
| 322 | Acetylation | NQGENITKGLKKVDK CCCCCHHHHHHHCCH | 59.45 | 24489116 | |
| 335 | Acetylation | DKSQQTHKNPELRQS CHHHHCCCCHHHHHC | 77.05 | 25381059 | |
| 342 | Phosphorylation | KNPELRQSSTVSSTG CCHHHHHCCCCCCCC | 22.88 | 20377248 | |
| 343 | Phosphorylation | NPELRQSSTVSSTGS CHHHHHCCCCCCCCC | 25.21 | 20377248 | |
| 344 | Phosphorylation | PELRQSSTVSSTGSK HHHHHCCCCCCCCCC | 29.65 | 20377248 | |
| 346 | Phosphorylation | LRQSSTVSSTGSKSG HHHCCCCCCCCCCCC | 23.44 | 20377248 | |
| 347 | Phosphorylation | RQSSTVSSTGSKSGP HHCCCCCCCCCCCCC | 32.24 | 20377248 | |
| 348 | Phosphorylation | QSSTVSSTGSKSGPP HCCCCCCCCCCCCCC | 37.66 | 21440633 | |
| 350 | Phosphorylation | STVSSTGSKSGPPPR CCCCCCCCCCCCCCC | 24.60 | 20377248 | |
| 352 | Phosphorylation | VSSTGSKSGPPPRPK CCCCCCCCCCCCCCC | 59.22 | 23749301 | |
| 454 | Phosphorylation | FGIQVNHSLPQISID EEEEECCCCCEEEEE | 36.22 | 21440633 | |
| 459 | Phosphorylation | NHSLPQISIDKSDGG CCCCCEEEEECCCCC | 21.35 | 28889911 | |
| 469 | Phosphorylation | KSDGGNIYLSKESLN CCCCCCEEECCCCCC | 14.66 | 28889911 | |
| 471 | Phosphorylation | DGGNIYLSKESLNTE CCCCEEECCCCCCCE | 19.87 | 28889911 | |
| 516 | Acetylation | KHSFADGKFKSAVFE HHHCCCCCHHHHHHH | 50.60 | 22865919 | |
| 519 | Phosphorylation | FADGKFKSAVFEHAG CCCCCHHHHHHHCCC | 32.56 | 21440633 |
| 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 CAP_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CAP_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 CAP_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-454, AND MASSSPECTROMETRY. | |
