UniProt ID | KAPS_YEAST | |
---|---|---|
UniProt AC | Q02196 | |
Protein Name | Adenylyl-sulfate kinase | |
Gene Name | MET14 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 202 | |
Subcellular Localization | ||
Protein Description | Catalyzes the synthesis of activated sulfate.. | |
Protein Sequence | MATNITWHPNLTYDERKALRKQDGCTIWLTGLSASGKSTIACALEQLLLQKNLSAYRLDGDNIRFGLNKDLGFSEKDRNENIRRISEVSKLFADSCAISITSFISPYRVDRDRARELHKEAGLKFIEIFVDVPLEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPKAPELHLRTDQKTVEECATIIYEYLISEKIIRKHL | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MATNITWHPNLTY --CCCCCCCCCCCCH | 21.57 | 28889911 | |
12 | Phosphorylation | ITWHPNLTYDERKAL CCCCCCCCHHHHHHH | 35.25 | 28889911 | |
13 | Phosphorylation | TWHPNLTYDERKALR CCCCCCCHHHHHHHH | 20.97 | 28889911 | |
51 | Acetylation | LEQLLLQKNLSAYRL HHHHHHHCCCCCEEC | 60.88 | 25381059 | |
69 | Acetylation | NIRFGLNKDLGFSEK CEEECCCCCCCCCHH | 60.41 | 22865919 | |
76 | Succinylation | KDLGFSEKDRNENIR CCCCCCHHHHCHHHH | 61.87 | 23954790 |
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 KAPS_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KAPS_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 KAPS_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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