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 | ||
* 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 | ||||||
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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-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. |