| UniProt ID | FUS2_YEAST | |
|---|---|---|
| UniProt AC | Q05670 | |
| Protein Name | Nuclear fusion protein FUS2 | |
| Gene Name | FUS2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 677 | |
| Subcellular Localization | Cell tip. Localizes at the mating projection tip (shmoo). | |
| Protein Description | Promotes cell fusion during zygote formation.. | |
| Protein Sequence | MFKTSYNLYDLNYPKNDSLTPIRDYKNDYFHKNDDKLPEIVRKPTRKLSKHENKLNDKKFTNKRPASLDLHSIVESLSNKKIYSPINTEIFQNVVRLNLSPQIPNSPHEGCKFYKIVQEFYLSEVEYYNNLLTANNVYRKALNSDPRFKNKLVKLDSSDELLLFGNIDTIASISKILVTAIKDLLLAKQRGKMLDANEWQKIFTKNEVQQQLYSTFDISEAFEQHLLRIKSTYTSYFVSHQKQMELFTTLRMNKNHFFNKWYEYCLKESGCIKLEDILKSPMKRLTQWIDTLETLESCYEDILSPELGLKLSPTRRKYSLFSNKLETEVSEYKSNSMYNFSLTPSEIIQSYDEDQFTHLLKPPDKQNKNICNASRQESNLDNSRVPSLLSGSSSYYSDVSGLEIVTNTSTASAEMINLKMDEETEFFTLADHISKFKKVMKGLLELKKNLLKNDLSGIIDISLRRINAWKKVIECERPSGAFFAHDNLISTMCSSYIDKLHEQKNQVTILKLTELETDVMNPLERIIAHCTTVKSKLKDLQALKKDYMLFLQEKKANVRDIKRDLLGMHFQNLQNQMKRELPVFITLIHDTIECILLNYIKVFLKYLEIIAGGKKYLQKDLENMSLNDSIATGQIKNLDILQCYSKSRYMTKRMVRKDWPFPGDPSGSRVVRKLFEL | |
| 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 |
|---|---|---|---|---|---|
| 20 | Phosphorylation | YPKNDSLTPIRDYKN CCCCCCCCCHHHCCC | 22.18 | 17330950 | |
| 67 | Phosphorylation | FTNKRPASLDLHSIV CCCCCCCCCCHHHHH | 25.71 | 17330950 | |
| 72 | Phosphorylation | PASLDLHSIVESLSN CCCCCHHHHHHHHCC | 35.31 | 17330950 | |
| 76 | Phosphorylation | DLHSIVESLSNKKIY CHHHHHHHHCCCCCC | 26.63 | 17330950 | |
| 78 | Phosphorylation | HSIVESLSNKKIYSP HHHHHHHCCCCCCCC | 56.75 | 28889911 | |
| 83 | Phosphorylation | SLSNKKIYSPINTEI HHCCCCCCCCCCHHH | 19.78 | 17330950 | |
| 84 | Phosphorylation | LSNKKIYSPINTEIF HCCCCCCCCCCHHHH | 23.83 | 19188495 | |
| 88 | Phosphorylation | KIYSPINTEIFQNVV CCCCCCCHHHHHCHH | 31.04 | 17330950 | |
| 100 | Phosphorylation | NVVRLNLSPQIPNSP CHHHCCCCCCCCCCC | 17.43 | 19188495 | |
| 106 | Phosphorylation | LSPQIPNSPHEGCKF CCCCCCCCCCCCCHH | 23.45 | 17330950 | |
| 254 | Acetylation | FTTLRMNKNHFFNKW HHHHCCCCHHHHHHH | 42.32 | 25381059 | |
| 319 | Phosphorylation | SPTRRKYSLFSNKLE CCCHHHHHHHCCCCC | 26.44 | 17330950 | |
| 341 | Phosphorylation | SNSMYNFSLTPSEII CCCCCCCCCCHHHHH | 27.91 | 27017623 | |
| 343 | Phosphorylation | SMYNFSLTPSEIIQS CCCCCCCCHHHHHHH | 24.46 | 27017623 | |
| 357 | Phosphorylation | SYDEDQFTHLLKPPD HCCCCCCHHHCCCCC | 13.14 | 27017623 |
| 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 FUS2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FUS2_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 FUS2_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-106, 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 THR-20; SER-67; SER-72;SER-84; THR-88; SER-100 AND SER-106, AND MASS SPECTROMETRY. | |