SLO_DROME - dbPTM
SLO_DROME - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
978PhosphorylationIVLQRRGSVYGANVP
EEEEECCCCCCCCCC
15.451497890

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
978SPhosphorylationKinasePKA-FAMILY-GPS
978SPhosphorylationKinasePKA_GROUP-PhosphoELM

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SLO_DROME !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLIP1_DROMESlip1physical
9502797
SLOB_DROMESlobphysical
9539129
PDE4B_DROMEdncgenetic
21106821
PDE4E_DROMEdncgenetic
21106821
PDE4C_DROMEdncgenetic
21106821
PDE4A_DROMEdncgenetic
21106821
FAS2_DROMEFas2genetic
21106821
DLG1_DROMEdlg1genetic
21106821
CYA1_DROMErutgenetic
21106821
CAC1D_DROMECa-alpha1Dgenetic
21106821

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SLO_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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