UniProt ID | HAL4_YEAST | |
---|---|---|
UniProt AC | P25333 | |
Protein Name | Serine/threonine-protein kinase HAL4/SAT4 | |
Gene Name | SAT4 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 603 | |
Subcellular Localization | ||
Protein Description | Promotes K(+) uptake, by the potassium transporter TRK1-TRK2, which leads to the subsequent cellular resistance to toxic cations such as Na(+), Li(+) and Ca(2+).. | |
Protein Sequence | MTGMNDNNAAIPQQTPRKHALSSKVMQLFRSGSRSSRQGKASSNIQPPSNINTNVPSASKSAKFGLHTPTTATPRVVSNPSNTAGVSKPGMYMPEYYQSASPSHSSSSASLNNHIDINTSKSSSAASLTSSVSALSLSPTSAINISSKSLSPKFSHHSNSNTAITPAPTPTASNINNVNKITNTSAPICGRFLVHKDGTHEHHLKNAKRQEKLSTMIKNMVGASKLRGEAKSAVPDIIMDPKTTLKSNKNPPTLFAGFMKQVVDMDDKYPEGAPTSGALNCPERDIYRSDQKDSKNNTHNITTTKKDRQCFAEKYGRCQEVLGKGAFGVVRICQKKNVSSQDGNKSEKLYAVKEFKRRTSESAEKYSKRLTSEFCISSSLHHTNIVTTLDLFQDAKGEYCEVMEYCAGGDLFTLVVAAGKLEYMEADCFFKQLIRGVVYMHEMGVCHRDLKPENLLLTHDGVLKITDFGNSECFKMAWEKNIHLSGGVCGSSPYIAPEEYIKEEFDPRPVDIWACGVIYMAMRTGRQLWSSAEKDDPFYMNYLKGRKEKGGYEPIESLKRARCRNVIYSMLDPVPYRRINGKQILNSEWGREIKCCHNGRALK | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MTGMNDNNA ------CCCCCCCCC | 45.17 | 30377154 | |
15 | Phosphorylation | NAAIPQQTPRKHALS CCCCCCCCCCHHHHH | 21.58 | 30377154 | |
61 | Phosphorylation | NVPSASKSAKFGLHT CCCCCCCCCCCCCCC | 33.91 | 21440633 | |
68 | Phosphorylation | SAKFGLHTPTTATPR CCCCCCCCCCCCCCC | 27.63 | 25752575 | |
70 | Phosphorylation | KFGLHTPTTATPRVV CCCCCCCCCCCCCEE | 30.16 | 28889911 | |
71 | Phosphorylation | FGLHTPTTATPRVVS CCCCCCCCCCCCEEC | 29.72 | 21440633 | |
73 | Phosphorylation | LHTPTTATPRVVSNP CCCCCCCCCCEECCC | 14.99 | 19779198 | |
78 | Phosphorylation | TATPRVVSNPSNTAG CCCCCEECCCCCCCC | 39.92 | 21551504 | |
123 | Phosphorylation | DINTSKSSSAASLTS ECCCCCCCCCHHHHC | 27.94 | 28889911 | |
149 | Phosphorylation | AINISSKSLSPKFSH CCCCCCCCCCCCCCC | 35.71 | 21440633 | |
151 | Phosphorylation | NISSKSLSPKFSHHS CCCCCCCCCCCCCCC | 32.89 | 21440633 | |
153 | Acetylation | SSKSLSPKFSHHSNS CCCCCCCCCCCCCCC | 57.00 | 24489116 | |
155 | Phosphorylation | KSLSPKFSHHSNSNT CCCCCCCCCCCCCCC | 26.81 | 17330950 | |
158 | Phosphorylation | SPKFSHHSNSNTAIT CCCCCCCCCCCCCEE | 36.21 | 17330950 | |
160 | Phosphorylation | KFSHHSNSNTAITPA CCCCCCCCCCCEECC | 38.27 | 21440633 | |
162 | Phosphorylation | SHHSNSNTAITPAPT CCCCCCCCCEECCCC | 21.18 | 21440633 | |
165 | Phosphorylation | SNSNTAITPAPTPTA CCCCCCEECCCCCCC | 15.78 | 28889911 | |
169 | Phosphorylation | TAITPAPTPTASNIN CCEECCCCCCCCCCC | 35.06 | 28889911 | |
171 | Phosphorylation | ITPAPTPTASNINNV EECCCCCCCCCCCCC | 45.24 | 19779198 | |
173 | Phosphorylation | PAPTPTASNINNVNK CCCCCCCCCCCCCCC | 40.49 | 24961812 | |
184 | Phosphorylation | NVNKITNTSAPICGR CCCCCCCCCCCCCCE | 20.02 | 21440633 | |
185 | Phosphorylation | VNKITNTSAPICGRF CCCCCCCCCCCCCEE | 33.83 | 21440633 | |
359 | Phosphorylation | VKEFKRRTSESAEKY HHHHHHHCHHHHHHH | 40.66 | 27717283 | |
360 | Phosphorylation | KEFKRRTSESAEKYS HHHHHHCHHHHHHHH | 27.95 | 27717283 | |
362 | Phosphorylation | FKRRTSESAEKYSKR HHHHCHHHHHHHHHH | 41.31 | 27717283 |
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 HAL4_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HAL4_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 HAL4_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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