| UniProt ID | YG36_YEAST | |
|---|---|---|
| UniProt AC | P53274 | |
| Protein Name | Uncharacterized protein YGR126W | |
| Gene Name | YGR126W | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 230 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MPVPSVTVTTDNEYEDISSFSSIDSYKPEPFTGFKDSEAPEQPLLKNDTIVGKGQLEDDSNVDDQHRHSDVHSHHSSSTLKRPTSNSIEKMVTHNALEGNSETVDSLKEDGLNLNKKALPDITAPVTNSAHDAAFPEEYRLETETGLVKLKTLESLKREDSRVSSTKKEHINDHTDMHSTRSKVTTNSQGSSLEPNKLNMAVEKNKKRIEKYQKHKSEKGIKGFFHRIFD | |
| 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 |
|---|---|---|---|---|---|
| 46 | Ubiquitination | APEQPLLKNDTIVGK CCCCCCCCCCEEECC | 61.53 | 23749301 | |
| 49 | Phosphorylation | QPLLKNDTIVGKGQL CCCCCCCEEECCCCC | 27.27 | 28889911 | |
| 60 | Phosphorylation | KGQLEDDSNVDDQHR CCCCCCCCCCCCCCC | 51.58 | 28889911 | |
| 69 | Phosphorylation | VDDQHRHSDVHSHHS CCCCCCCCCCCCCCC | 41.08 | 24961812 | |
| 73 | Phosphorylation | HRHSDVHSHHSSSTL CCCCCCCCCCCCCCC | 23.81 | 28889911 | |
| 76 | Phosphorylation | SDVHSHHSSSTLKRP CCCCCCCCCCCCCCC | 22.14 | 24961812 | |
| 77 | Phosphorylation | DVHSHHSSSTLKRPT CCCCCCCCCCCCCCC | 24.00 | 24961812 | |
| 78 | Phosphorylation | VHSHHSSSTLKRPTS CCCCCCCCCCCCCCC | 40.55 | 24961812 | |
| 79 | Phosphorylation | HSHHSSSTLKRPTSN CCCCCCCCCCCCCCC | 37.94 | 24961812 | |
| 81 | Acetylation | HHSSSTLKRPTSNSI CCCCCCCCCCCCCCH | 57.32 | 25381059 | |
| 84 | Phosphorylation | SSTLKRPTSNSIEKM CCCCCCCCCCCHHHH | 44.57 | 19823750 | |
| 85 | Phosphorylation | STLKRPTSNSIEKMV CCCCCCCCCCHHHHH | 31.12 | 19823750 | |
| 87 | Phosphorylation | LKRPTSNSIEKMVTH CCCCCCCCHHHHHHH | 31.71 | 21551504 | |
| 90 | Ubiquitination | PTSNSIEKMVTHNAL CCCCCHHHHHHHHHH | 36.68 | 24961812 | |
| 93 | Phosphorylation | NSIEKMVTHNALEGN CCHHHHHHHHHHCCC | 13.10 | 22369663 | |
| 101 | Phosphorylation | HNALEGNSETVDSLK HHHHCCCCHHHHHHH | 45.56 | 22369663 | |
| 103 | Phosphorylation | ALEGNSETVDSLKED HHCCCCHHHHHHHHH | 29.45 | 22369663 | |
| 106 | Phosphorylation | GNSETVDSLKEDGLN CCCHHHHHHHHHCCC | 36.68 | 22369663 | |
| 152 | Phosphorylation | TGLVKLKTLESLKRE CCCEEHHHHHHHHHC | 46.31 | 24930733 | |
| 155 | Phosphorylation | VKLKTLESLKREDSR EEHHHHHHHHHCCCC | 42.16 | 25704821 | |
| 157 | Ubiquitination | LKTLESLKREDSRVS HHHHHHHHHCCCCCC | 64.12 | 24961812 | |
| 161 | Phosphorylation | ESLKREDSRVSSTKK HHHHHCCCCCCCCCH | 29.81 | 19823750 | |
| 164 | Phosphorylation | KREDSRVSSTKKEHI HHCCCCCCCCCHHHC | 31.05 | 21440633 | |
| 165 | Phosphorylation | REDSRVSSTKKEHIN HCCCCCCCCCHHHCC | 41.19 | 21440633 | |
| 166 | Phosphorylation | EDSRVSSTKKEHIND CCCCCCCCCHHHCCC | 38.33 | 19823750 | |
| 167 | Ubiquitination | DSRVSSTKKEHINDH CCCCCCCCHHHCCCC | 59.10 | 24961812 | |
| 168 | Ubiquitination | SRVSSTKKEHINDHT CCCCCCCHHHCCCCC | 55.39 | 24961812 | |
| 175 | Phosphorylation | KEHINDHTDMHSTRS HHHCCCCCCCCCCCC | 37.57 | 28132839 | |
| 179 | Phosphorylation | NDHTDMHSTRSKVTT CCCCCCCCCCCCEEC | 20.91 | 28132839 | |
| 180 | Phosphorylation | DHTDMHSTRSKVTTN CCCCCCCCCCCEECC | 25.04 | 28889911 | |
| 182 | Phosphorylation | TDMHSTRSKVTTNSQ CCCCCCCCCEECCCC | 31.40 | 24961812 | |
| 183 | Ubiquitination | DMHSTRSKVTTNSQG CCCCCCCCEECCCCC | 40.07 | 24961812 | |
| 185 | Phosphorylation | HSTRSKVTTNSQGSS CCCCCCEECCCCCCC | 24.81 | 22369663 | |
| 186 | Phosphorylation | STRSKVTTNSQGSSL CCCCCEECCCCCCCC | 35.54 | 22369663 | |
| 188 | Phosphorylation | RSKVTTNSQGSSLEP CCCEECCCCCCCCCC | 33.55 | 22369663 | |
| 191 | Phosphorylation | VTTNSQGSSLEPNKL EECCCCCCCCCCCHH | 24.90 | 22369663 | |
| 192 | Phosphorylation | TTNSQGSSLEPNKLN ECCCCCCCCCCCHHH | 43.51 | 22369663 | |
| 197 | Ubiquitination | GSSLEPNKLNMAVEK CCCCCCCHHHHHHHH | 52.53 | 24961812 | |
| 211 | Acetylation | KNKKRIEKYQKHKSE HHHHHHHHHHHHHHH | 51.08 | 25381059 | |
| 219 | Acetylation | YQKHKSEKGIKGFFH HHHHHHHHCCCHHHH | 73.38 | 25381059 | |
| 222 | Acetylation | HKSEKGIKGFFHRIF HHHHHCCCHHHHHHC | 59.33 | 25381059 |
| 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 YG36_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YG36_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 YG36_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RRP8_YEAST | RRP8 | genetic | 19061648 | |
| NGR1_YEAST | NGR1 | genetic | 19061648 | |
| LTV1_YEAST | LTV1 | genetic | 19061648 |
| 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-85 AND SER-87, AND MASSSPECTROMETRY. | |
| "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-85 AND SER-87, 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 SER-106, AND MASSSPECTROMETRY. | |