UniProt ID | YB47_YEAST | |
---|---|---|
UniProt AC | P38306 | |
Protein Name | Uncharacterized protein YBR197C | |
Gene Name | YBR197C | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 217 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MGVKQTPPVQVKVSDADSTNRRKSSSQEGNPQLVQLKAKSDKDKRKGSSDSTASIMGSSNALPTKNLTTPPALNPLTTSISRGNTAYERSVNGSRITMHSNLAPTETQDVSWSEIDTLDDVKKMAKEPIVNDGFPRDFESNLTQMRKSHAQLLRLMRERNQRLKYAKLRSPPHKDQHNSATNKDQEPDEVLHDPEIALDGEKYVSQVVDTIKDVHRC | |
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 |
---|---|---|---|---|---|
14 | Phosphorylation | PPVQVKVSDADSTNR CCEEEEECCCCCCCC | 22.74 | 27017623 | |
18 | Phosphorylation | VKVSDADSTNRRKSS EEECCCCCCCCCCCC | 29.33 | 28889911 | |
19 | Phosphorylation | KVSDADSTNRRKSSS EECCCCCCCCCCCCC | 33.04 | 27017623 | |
24 | Phosphorylation | DSTNRRKSSSQEGNP CCCCCCCCCCCCCCC | 33.15 | 22369663 | |
25 | Phosphorylation | STNRRKSSSQEGNPQ CCCCCCCCCCCCCCC | 38.79 | 22369663 | |
26 | Phosphorylation | TNRRKSSSQEGNPQL CCCCCCCCCCCCCCC | 39.06 | 22369663 | |
48 | Phosphorylation | DKDKRKGSSDSTASI CCCCCCCCCCCHHHH | 33.73 | 23749301 | |
49 | Phosphorylation | KDKRKGSSDSTASIM CCCCCCCCCCHHHHH | 44.22 | 25752575 | |
51 | Phosphorylation | KRKGSSDSTASIMGS CCCCCCCCHHHHHCC | 28.02 | 21440633 | |
52 | Phosphorylation | RKGSSDSTASIMGSS CCCCCCCHHHHHCCC | 29.43 | 21440633 | |
54 | Phosphorylation | GSSDSTASIMGSSNA CCCCCHHHHHCCCCC | 17.13 | 21551504 | |
58 | Phosphorylation | STASIMGSSNALPTK CHHHHHCCCCCCCCC | 11.75 | 19823750 | |
59 | Phosphorylation | TASIMGSSNALPTKN HHHHHCCCCCCCCCC | 22.01 | 19823750 | |
64 | Phosphorylation | GSSNALPTKNLTTPP CCCCCCCCCCCCCCC | 33.15 | 19823750 | |
68 | Phosphorylation | ALPTKNLTTPPALNP CCCCCCCCCCCCCCC | 46.80 | 29688323 | |
69 | Phosphorylation | LPTKNLTTPPALNPL CCCCCCCCCCCCCCC | 30.37 | 25752575 | |
77 | Phosphorylation | PPALNPLTTSISRGN CCCCCCCCCCCCCCC | 21.54 | 29688323 | |
78 | Phosphorylation | PALNPLTTSISRGNT CCCCCCCCCCCCCCC | 31.57 | 27017623 | |
79 | Phosphorylation | ALNPLTTSISRGNTA CCCCCCCCCCCCCCC | 17.21 | 24930733 | |
81 | Phosphorylation | NPLTTSISRGNTAYE CCCCCCCCCCCCCEE | 33.62 | 24909858 | |
97 | Phosphorylation | SVNGSRITMHSNLAP CCCCCEEEEECCCCC | 14.02 | 27017623 | |
100 | Phosphorylation | GSRITMHSNLAPTET CCEEEEECCCCCCCC | 23.79 | 27017623 | |
148 | Phosphorylation | NLTQMRKSHAQLLRL HHHHHHHHHHHHHHH | 17.43 | 28889911 |
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 YB47_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YB47_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 YB47_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ATG17_YEAST | ATG17 | physical | 16554755 | |
RV161_YEAST | RVS161 | genetic | 27708008 | |
GPR1_YEAST | GPR1 | genetic | 27708008 | |
HKR1_YEAST | HKR1 | genetic | 27708008 | |
PKR1_YEAST | PKR1 | genetic | 27708008 | |
KATL1_HUMAN | KATNAL1 | physical | 27107014 |
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-26, AND MASSSPECTROMETRY. |