| UniProt ID | SEC10_YEAST | |
|---|---|---|
| UniProt AC | Q06245 | |
| Protein Name | Exocyst complex component SEC10 | |
| Gene Name | SEC10 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 871 | |
| Subcellular Localization | ||
| Protein Description | Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.. | |
| Protein Sequence | MNSLYELDPKWKKLLKTDNFLGGLTVNEFVQELSKDHRNDVLIDANTKNLPTNEKDQDAIREAIWKQLDPKPYIRTFESTLKELKNLNEETLNKRQYFSEQVATQEVIHSENVIKLSKDLHTTLLTFDKLDDRLTNVTQVVSPLGDKLETAIKKKQNYIQSVELIRRYNDFYSMGKSDIVEQLRLSKNWKLNLKSVKLMKNLLILSSKLETSSIPKTINTKLVIEKYSEMMENELLENFNSAYRENNFTKLNEIAIILNNFNGGVNVIQSFINQHDYFIDTKQIDLENEFENVFIKNVKFKEQLIDFENHSVIIETSMQNLINDVETVIKNESKIVKRVFEEKATHVIQLFIQRVFAQKIEPRFEVLLRNSLSISNLAYVRILHGLFTLFGKFTKSLIDYFQLLEIDDSNQILSTTLEQCFADLFSHYLYDRSKYFGIEKRSLEAILVDMTSKFTVNYDKEINKRVLLDKYKEKLSTNVDAFMHSPRGNTHSRQDSTSRSKLSQFNSFLKTHLDKDHLSLNRTNTLSDSFNNSSSSTQYDVANNSSSLVNSSFTASDIDNSPNSPANYSLNDVDSMLKCVVESTARVMELIPNKAHLYILEILKIMFLGIVDSYMEIALEVAYWKICKVDINKTAGVVNLNFLKFISMSTEILDLLSISIKSIFLPLLNNSPEIKAQIIEMTNSQIQKMEILINIILQETITVISTKFSAILCKQKKKDFVPKSQELLDQDTLPAIEIVNILNLIFEQSSKFLKGKNLQTFLTLIGEELYGLLLSHYSHFQVNSIGGVVVTKDIIGYQTAIEDWGVASLIDKFATLRELANLFTVQPELLESLTKEGHLADIGRDIIQSYISNREDFNHDNFINSVKLNFR | |
| 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 | -----MNSLYELDPK -----CCCHHCCCHH | 30.91 | 28152593 | |
| 91 | Phosphorylation | LKNLNEETLNKRQYF HHCCCHHHHHHHHHH | 29.47 | 25704821 | |
| 142 | Phosphorylation | TNVTQVVSPLGDKLE CCHHEEECCCHHHHH | 18.62 | 17330950 | |
| 186 | Phosphorylation | IVEQLRLSKNWKLNL HHHHHHHCCCCCCCH | 19.94 | 30377154 | |
| 477 | Phosphorylation | KYKEKLSTNVDAFMH HHHHHHCCCCCHHCC | 50.09 | 30377154 | |
| 485 | Phosphorylation | NVDAFMHSPRGNTHS CCCHHCCCCCCCCCC | 12.42 | 17330950 | |
| 490 | Phosphorylation | MHSPRGNTHSRQDST CCCCCCCCCCCCCCC | 24.85 | 24961812 | |
| 492 | Phosphorylation | SPRGNTHSRQDSTSR CCCCCCCCCCCCCCH | 29.60 | 24961812 | |
| 496 | Phosphorylation | NTHSRQDSTSRSKLS CCCCCCCCCCHHHHH | 21.68 | 24961812 | |
| 497 | Phosphorylation | THSRQDSTSRSKLSQ CCCCCCCCCHHHHHH | 36.13 | 24961812 | |
| 498 | Phosphorylation | HSRQDSTSRSKLSQF CCCCCCCCHHHHHHH | 38.21 | 24961812 | |
| 500 | Phosphorylation | RQDSTSRSKLSQFNS CCCCCCHHHHHHHHH | 37.40 | 24961812 | |
| 501 | Acetylation | QDSTSRSKLSQFNSF CCCCCHHHHHHHHHH | 51.56 | 24489116 | |
| 503 | Phosphorylation | STSRSKLSQFNSFLK CCCHHHHHHHHHHHH | 36.14 | 21126336 | |
| 507 | Phosphorylation | SKLSQFNSFLKTHLD HHHHHHHHHHHHHHC | 32.99 | 25752575 | |
| 519 | Phosphorylation | HLDKDHLSLNRTNTL HHCCCCCCCCCCCCC | 21.85 | 28889911 | |
| 700 | Phosphorylation | INIILQETITVISTK HHHHHHHCHHHHHHC | 14.69 | 29688323 | |
| 702 | Phosphorylation | IILQETITVISTKFS HHHHHCHHHHHHCHH | 21.14 | 29688323 | |
| 705 | Phosphorylation | QETITVISTKFSAIL HHCHHHHHHCHHHHH | 22.62 | 29688323 | |
| 706 | Phosphorylation | ETITVISTKFSAILC HCHHHHHHCHHHHHC | 25.61 | 29688323 |
| 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 SEC10_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEC10_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 SEC10_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-485 AND SER-507, ANDMASS SPECTROMETRY. | |
| "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-142 AND SER-485, ANDMASS SPECTROMETRY. | |
| "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-142, AND MASSSPECTROMETRY. | |
