UniProt ID | YHR2_YEAST | |
---|---|---|
UniProt AC | P38716 | |
Protein Name | Uncharacterized trans-sulfuration enzyme YHR112C | |
Gene Name | YHR112C | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 378 | |
Subcellular Localization | ||
Protein Description | ||
Protein Sequence | MVDLSTALIHGDDKDNRVTDVAPPINVSTTFRYDDDDLIPWTERENLDFMEKKPVYSRLAHPNSTRLESIFSEILDGYAVIYSSGLAAFYAAMVHYNPKKIFIGQSYHGVRAIANILTRNYGIEQHPLEDIEKCASEGDIVHLESPVNPYGTSSDIESLARRAHAKGALLIVDSTFASPPLQYAWNFGADIVLYSATKYFGGHSDLLSGVLVVKEEATSRQLKDDRIYLGTNVANLESFMLLRSLRTYEMRITKQSENATKLVRFLSDHQSEFDKVLKTIYHSSLQTEEFVKKQLVGGYGPVFAITLYTKEQCKQLPLKLKYFHHATSLGGIESLVEWRAMTDPYIDQTLIRVSVGCESANDLIKDLASALKELQDAA | |
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 |
---|---|---|---|---|---|
42 | Phosphorylation | DDDLIPWTERENLDF CCCCCCCCHHCCCCH | 21.58 | 28889911 | |
198 | N6-(pyridoxal phosphate)lysine | IVLYSATKYFGGHSD EEEEECCCCCCCCCC | 37.99 | - | |
198 | Other | IVLYSATKYFGGHSD EEEEECCCCCCCCCC | 37.99 | - | |
228 | Phosphorylation | QLKDDRIYLGTNVAN CCCCCEEEECCCCCH | 10.44 | 21126336 |
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 YHR2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YHR2_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 YHR2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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