UniProt ID | SEC15_YEAST | |
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UniProt AC | P22224 | |
Protein Name | Exocyst complex component SEC15 | |
Gene Name | SEC15 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 910 | |
Subcellular Localization |
Cytoplasm. Cell membrane Peripheral membrane protein. 25% cytoplasmic. 75% is associated with the cell membrane. |
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Protein Description | Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.. | |
Protein Sequence | MDQEGQPLLSKDFQQVLLATASGNNSSWTERAVLNNESTDAVKHEPALGQNDVFDLDPLSFDKWVPFLRRALDKNQLDPVIDELENSIEDNFQGLELQLLQDSQMNDKLETSIDEIANIQGMVQDTLSSEISKFQIRLSESANELIVKKQMYVNNKKISLKISEATILITKVVRILELSSKCQELITERKFFKVLQNLDSLEKLYLQEFKNYNFQFLIEIYNSIPFLQKVTKDECINLIRNSLNLNLGKNLIKVGQEFVAIYENELLPQWLETRSKMKLTNFKFNSPIEISMRDESFLAKLNLGEFFQLDDFHDSIMIFQNLNELSVLSGEFNKEYELRKTKLMYPLIWKKNKTAAYQMDSLLRGTGTTPGSTAHDVSTDDPFTQSLSLHFLQDYFLKILGFLLYDINLNKATEFILVDNNYNSTNEFWDGLMDRLSPYLSYFIDEKLKTEEDMIKLKDFLCIYVAILENFKLNIEPLYKILVSIFEKFCSVSLRAFDDEFQILLNDDDFMPLSINDKTLYEKVLKICWMKEGEHLSLPDPTNGEPFAVTLPFSPLYPMTCTLAKKTYSKITAFLSIFYRHELHTLNNILVKTMDDIFNDIVNKKIRSKLESTSREEIAQILVNLDYFIIAAKEFSNFMTRENILQNPDMEIRLSSIKYLAESRKLAETKLIELIDSKISDILETIEIDWQITEVRQDPDISIIDLAQFLEMMFASTLQNLPYSVQTLLIFREFDSLTRQFMGLLLHDTPSTITHESIMNFEVDVNYLESIIPRIFPSTPGTIDSNGYQSPMTPSTPTFPNANGVDAPTLFENNIKSLEATFMELKQCIELLKTQGKDYNEPEIRLRKYSRIRQEDAALLLSKIQHFVSSVEGANGDDTSVMDSSSIFNSESASVIDSNTSRIAKFFNRR | |
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 |
---|---|---|---|---|---|
26 | Phosphorylation | ATASGNNSSWTERAV HHHCCCCCCHHHHHH | 31.11 | 30377154 | |
27 | Phosphorylation | TASGNNSSWTERAVL HHCCCCCCHHHHHHH | 39.89 | 30377154 | |
29 | Phosphorylation | SGNNSSWTERAVLNN CCCCCCHHHHHHHCC | 19.96 | 30377154 | |
286 | Phosphorylation | LTNFKFNSPIEISMR CCCCCCCCCEEEECC | 30.32 | 28889911 | |
342 | Acetylation | EYELRKTKLMYPLIW HHHHHHCCCHHHHHH | 34.00 | 24489116 | |
361 | Phosphorylation | TAAYQMDSLLRGTGT CHHHHHHHHHHCCCC | 24.78 | 30377154 | |
523 | Acetylation | NDKTLYEKVLKICWM CCHHHHHHHHHHHCC | 39.03 | 24489116 | |
537 | Phosphorylation | MKEGEHLSLPDPTNG CCCCCCCCCCCCCCC | 39.50 | 19779198 | |
550 | Phosphorylation | NGEPFAVTLPFSPLY CCCCEEEEECCCCCC | 25.86 | 19779198 | |
817 | Phosphorylation | LFENNIKSLEATFME HHHHHHHHHHHHHHH | 27.87 | 28889911 | |
880 | Phosphorylation | GANGDDTSVMDSSSI CCCCCCCCCCCHHHC | 23.57 | 19779198 | |
884 | Phosphorylation | DDTSVMDSSSIFNSE CCCCCCCHHHCCCCC | 14.11 | 19779198 | |
885 | Phosphorylation | DTSVMDSSSIFNSES CCCCCCHHHCCCCCC | 24.16 | 19779198 | |
886 | Phosphorylation | TSVMDSSSIFNSESA CCCCCHHHCCCCCCC | 34.84 | 19779198 | |
890 | Phosphorylation | DSSSIFNSESASVID CHHHCCCCCCCEEEC | 23.37 | 19779198 | |
894 | Phosphorylation | IFNSESASVIDSNTS CCCCCCCEEECCCHH | 28.96 | 19779198 | |
905 | Acetylation | SNTSRIAKFFNRR-- CCHHHHHHHHCCC-- | 48.38 | 25381059 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of SEC15_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of SEC15_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 SEC15_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 SER-286, AND MASSSPECTROMETRY. |