UniProt ID | SLO_DROME | |
---|---|---|
UniProt AC | Q03720 | |
Protein Name | Calcium-activated potassium channel slowpoke | |
Gene Name | slo | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 1200 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Kinetics are determined by alternative splicing, phosphorylation status and its combination interaction with Slob and 14-3-3-zeta. While the interaction with Slob1 alone increases its activity, its interaction with both Slob1 and 14-3-3-zeta decreases its activity.. | |
Protein Sequence | MASGLIDTNFSSTLANGMSGCDQSTVESLADDPTDSPFDADDCLKVRKYWCFLLSSIFTFLAGLLVVLLWRAFAFVCCRKEPDLGPNDPKQKEQKASRNKQEFEGTFMTEAKDWAGELISGQTTTGRILVVLVFILSIASLIIYFVDASSEEVERCQKWSNNITQQIDLAFNIFFMVYFFIRFIAASDKLWFMLEMYSFVDYFTIPPSFVSIYLDRTWIGLRFLRALRLMTVPDILQYLNVLKTSSSIRLAQLVSIFISVWLTAAGIIHLLENSGDPLDFNNAHRLSYWTCVYFLIVTMSTVGYGDVYCETVLGRTFLVFFLLVGLAMFASSIPEIIELVGSGNKYGGELKREHGKRHIVVCGHITYESVSHFLKDFLHEDREDVDVEVVFLHRKPPDLELEGLFKRHFTTVEFFQGTIMNPIDLQRVKVHEADACLVLANKYCQDPDAEDAANIMRVISIKNYSDDIRVIIQLMQYHNKAYLLNIPSWDWKQGDDVICLAELKLGFIAQSCLAPGFSTMMANLFAMRSFKTSPDMQSWTNDYLRGTGMEMYTETLSPTFIGIPFAQATELCFSKLKLLLLAIEIKGAEEGADSKISINPRGAKIQANTQGFFIAQSADEVKRAWFYCKACHEDIKDETLIKKCKCKNLTVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVSGDITRDREDTNLLNRNVRRPNGTGNGTGGMHHMNNTAAAAAAAAAAGKQVNKVKPTVNVSRQVEGQVISPSQYNRPTSRSSGTGTQNQNGGVSLPAGIADDQSKDFDFEKTEMKYDSTGMFHWSPAKSLEDCILDRNQAAMTVLNGHVVVCLFADPDSPLIGLRNLVMPLRASNFHYHELKHVVIVGSVDYIRREWKMLQNLPKISVLNGSPLSRADLRAVNVNLCDMCCILSAKVPSNDDPTLADKEAILASLNIKAMTFDDTIGVLSQRGPEFDNLSATAGSPIVLQRRGSVYGANVPMITELVNDSNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSTTYFNQNALTLIRSLITGGATPELELILAEGAGLRGGYSTVESLSNRDRCRVGQISLYDGPLAQFGECGKYGDLFVAALKSYGMLCIGLYRFRDTSSSCDASSKRYVITNPPDDFSLLPTDQVFVLMQFDPGLEYKPPAVRAPAGGRGTNTQGSGVGGGGSNKDDNS | |
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 |
---|---|---|---|---|---|
978 | Phosphorylation | IVLQRRGSVYGANVP EEEEECCCCCCCCCC | 15.45 | 1497890 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
978 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
978 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SLO_DROME !! |
* 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 SLO_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SLIP1_DROME | Slip1 | physical | 9502797 | |
SLOB_DROME | Slob | physical | 9539129 | |
PDE4B_DROME | dnc | genetic | 21106821 | |
PDE4E_DROME | dnc | genetic | 21106821 | |
PDE4C_DROME | dnc | genetic | 21106821 | |
PDE4A_DROME | dnc | genetic | 21106821 | |
FAS2_DROME | Fas2 | genetic | 21106821 | |
DLG1_DROME | dlg1 | genetic | 21106821 | |
CYA1_DROME | rut | genetic | 21106821 | |
CAC1D_DROME | Ca-alpha1D | genetic | 21106821 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Simultaneous binding of two protein kinases to a calcium-dependentpotassium channel."; Wang J., Zhou Y., Wen H., Levitan I.B.; J. Neurosci. 19:RC4-RC4(1999). Cited for: INTERACTION WITH PKA AND SRC, PHOSPHORYLATION AT SER-978, ANDMUTAGENESIS OF TYR-552; SER-978 AND TYR-1012. |