UniProt ID | KXD1_YEAST | |
---|---|---|
UniProt AC | P53158 | |
Protein Name | Biogenesis of lysosome-related organelles complex 1 subunit KXD1 | |
Gene Name | KXD1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 218 | |
Subcellular Localization | Endosome . | |
Protein Description | Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in endosomal cargo sorting.. | |
Protein Sequence | MVTGISEENDDEETFSAVHSSTPSINSQSYAIPITEEMSSSFHDSISTTSNSSGSFDSDGSNVSDVVEQNEMDNESNVDEDLFLDNDIPQSSNLLPTDAQDPGPIFDVSRYIFDSLKQSIDSADFSEALSLQTKTSAVINSKSLELKQYIDEMKSRLTQLQEKFENGEATSKKIKRDLETSRKNIDYLNAALRVDFPIEFNQAREKILERRLNEDHDC | |
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 |
---|---|---|---|---|---|
119 | Phosphorylation | IFDSLKQSIDSADFS HHHHHHHHHCCCCHH | 27.12 | 20377248 | |
122 | Phosphorylation | SLKQSIDSADFSEAL HHHHHHCCCCHHHHH | 28.24 | 20377248 | |
126 | Phosphorylation | SIDSADFSEALSLQT HHCCCCHHHHHCCHH | 23.62 | 20377248 | |
133 | Phosphorylation | SEALSLQTKTSAVIN HHHHCCHHHHCHHHC | 41.40 | 20377248 |
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 KXD1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KXD1_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 KXD1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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