| UniProt ID | YKT6_YEAST | |
|---|---|---|
| UniProt AC | P36015 | |
| Protein Name | Synaptobrevin homolog YKT6 | |
| Gene Name | YKT6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 200 | |
| Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side . |
|
| Protein Description | ||
| Protein Sequence | MRIYYIGVFRSGGEKALELSEVKDLSQFGFFERSSVGQFMTFFAETVASRTGAGQRQSIEEGNYIGHVYARSEGICGVLITDKEYPVRPAYTLLNKILDEYLVAHPKEEWADVTETNDALKMKQLDTYISKYQDPSQADAIMKVQQELDETKIVLHKTIENVLQRGEKLDNLVDKSESLTASSKMFYKQAKKSNSCCIIM | |
| 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 | Succinylation | VFRSGGEKALELSEV EEECCCHHEEEHHHC | 62.64 | 23954790 | |
| 15 | Ubiquitination | VFRSGGEKALELSEV EEECCCHHEEEHHHC | 62.64 | 23749301 | |
| 20 | Phosphorylation | GEKALELSEVKDLSQ CHHEEEHHHCCCHHH | 30.85 | 21440633 | |
| 23 | Ubiquitination | ALELSEVKDLSQFGF EEEHHHCCCHHHCCC | 49.23 | 24961812 | |
| 123 | Acetylation | TNDALKMKQLDTYIS CCHHHHHHHHHHHHH | 46.23 | 24489116 | |
| 123 | Ubiquitination | TNDALKMKQLDTYIS CCHHHHHHHHHHHHH | 46.23 | 23749301 | |
| 131 | Acetylation | QLDTYISKYQDPSQA HHHHHHHHCCCHHHH | 37.05 | 24489116 | |
| 131 | Ubiquitination | QLDTYISKYQDPSQA HHHHHHHHCCCHHHH | 37.05 | 23749301 | |
| 143 | Ubiquitination | SQADAIMKVQQELDE HHHHHHHHHHHHHHC | 30.68 | 23749301 | |
| 143 | Acetylation | SQADAIMKVQQELDE HHHHHHHHHHHHHHC | 30.68 | 24489116 | |
| 152 | Ubiquitination | QQELDETKIVLHKTI HHHHHCCEEEHHHHH | 28.86 | 23749301 | |
| 152 | Acetylation | QQELDETKIVLHKTI HHHHHCCEEEHHHHH | 28.86 | 24489116 | |
| 157 | Acetylation | ETKIVLHKTIENVLQ CCEEEHHHHHHHHHH | 47.22 | 24489116 | |
| 158 | Phosphorylation | TKIVLHKTIENVLQR CEEEHHHHHHHHHHH | 23.83 | 17330950 | |
| 168 | Ubiquitination | NVLQRGEKLDNLVDK HHHHHHHHHHHHCCH | 65.06 | 23749301 | |
| 168 | Acetylation | NVLQRGEKLDNLVDK HHHHHHHHHHHHCCH | 65.06 | 24489116 | |
| 175 | Ubiquitination | KLDNLVDKSESLTAS HHHHHCCHHHHCCHH | 48.95 | 23749301 | |
| 175 | Acetylation | KLDNLVDKSESLTAS HHHHHCCHHHHCCHH | 48.95 | 24489116 | |
| 176 | Phosphorylation | LDNLVDKSESLTASS HHHHCCHHHHCCHHH | 28.14 | 22369663 | |
| 178 | Phosphorylation | NLVDKSESLTASSKM HHCCHHHHCCHHHHH | 37.80 | 22369663 | |
| 180 | Phosphorylation | VDKSESLTASSKMFY CCHHHHCCHHHHHHH | 33.50 | 25521595 | |
| 182 | Phosphorylation | KSESLTASSKMFYKQ HHHHCCHHHHHHHHH | 25.84 | 22369663 | |
| 183 | Phosphorylation | SESLTASSKMFYKQA HHHCCHHHHHHHHHH | 26.19 | 22369663 | |
| 196 | S-palmitoylation | QAKKSNSCCIIM--- HHHHCCCEEEEC--- | 1.95 | - | |
| 197 | Farnesylation | AKKSNSCCIIM---- HHHCCCEEEEC---- | 2.07 | - | |
| 197 | Methylation | AKKSNSCCIIM---- HHHCCCEEEEC---- | 2.07 | - |
| 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 YKT6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YKT6_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 YKT6_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 THR-158; SER-176; SER-178;THR-180 AND SER-182, AND MASS SPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-182, 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 THR-158, AND MASSSPECTROMETRY. | |
