KCNAE_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCNAE_DROME
• UniProt AC: Q02280
• Protein Name: Potassium voltage-gated channel protein eag
• Gene Name: eag
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1174
• Subcellular Localization: Membrane ; Multi-pass membrane protein . Eag recruits CASK to the plasma membrane.
• Protein Description: Structural component of a potassium channel. Mediates the potassium permeability of membranes; potassium current is regulated by CaMKII and CASK. Has a role in growth of the perineurial glial layer of the larval peripheral nerve..
• Protein Sequence: MPGGRRGLVAPQNTFLENIIRRSNSQPDSSFLLANAQIVDFPIVYCNESFCKISGYNRAEVMQKSCRYVCGFMYGELTDKETVGRLEYTLENQQQDQFEILLYKKNNLQCGCALSQFGKAQTQETPLWLLLQVAPIRNERDLVVLFLLTFRDITALKQPIDSEDTKGVLGLSKFAKLARSVTRSRQFSAHLPTLKDPTKQSNLAHMMSLSADIMPQYRQEAPKTPPHILLHYCAFKAIWDWVILCLTFYTAIMVPYNVAFKNKTSEDVSLLVVDSIVDVIFFIDIVLNFHTTFVGPGGEVVSDPKVIRMNYLKSWFIIDLLSCLPYDVFNAFDRDEDGIGSLFSALKVVRLLRLGRVVRKLDRYLEYGAAMLILLLCFYMLVAHWLACIWYSIGRSDADNGIQYSWLWKLANVTQSPYSYIWSNDTGPELVNGPSRKSMYVTALYFTMTCMTSVGFGNVAAETDNEKVFTICMMIIAALLYATIFGHVTTIIQQMTSATAKYHDMLNNVREFMKLHEVPKALSERVMDYVVSTWAMTKGLDTEKVLNYCPKDMKADICVHLNRKVFNEHPAFRLASDGCLRALAMHFMMSHSAPGDLLYHTGESIDSLCFIVTGSLEVIQDDEVVAILGKGDVFGDQFWKDSAVGQSAANVRALTYCDLHAIKRDKLLEVLDFYSAFANSFARNLVLTYNLRHRLIFRKVADVKREKELAERRKNEPQLPQNQDHLVRKIFSKFRRTPQVQAGSKELVGGSGQSDVEKGDGEVERTKVFPKAPKLQASQATLARQDTIDEGGEVDSSPPSRDSRVVIEGAAVSSATVGPSPPVATTSSAAAGAGVSGGPGSGGTVVAIVTKADRNLALERERQIEMASSRATTSDTYDTGLRETPPTLAQRDLIATVLDMKVDVRLELQRMQQRIGRIEDLLGELVKRLAPGAGSGGNAPDNSSGQTTPGDEICAGCGAGGGGTPTTQAPPTSAVTSPVDTVITISSPGASGSGSGTGAGAGSAVAGAGGAGLLNPGATVVSSAGGNGLGPLMLKKRRSKSRKAPAPPKQTLASTAGTATAAPAGVAGSGMTSSAPASADQQQQHQSTADQSPTTPGAELLHLRLLEEDFTAAQLPSTSSGGAGGGGGSGSGATPTTPPPTTAGGSGSGTPTSTTATTTPTGSGTATRGKLDFL

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
262	N-linked_Glycosylation	PYNVAFKNKTSEDVS CHHHHCCCCCCCCHH	46.51	-
412	N-linked_Glycosylation	SWLWKLANVTQSPYS EHHHHHHCCCCCCCC	48.05	-
424	N-linked_Glycosylation	PYSYIWSNDTGPELV CCCEECCCCCCHHHH	35.55	-
787	Phosphorylation	ATLARQDTIDEGGEV HHHCCCCCCCCCCCC	23.22	11980904

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
787	T	Phosphorylation	Kinase	KCC2A	Q00168	PhosphoELM
787	T	Phosphorylation	Kinase	CAMK2B	-	GPS
787	T	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
787	T	Phosphorylation	Kinase	CAMK2	-	Uniprot

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KCNAE_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCNAS_DROME	Sh	genetic	10934243
KINH_DROME	Khc	genetic	8770597
QVR_DROME	qvr	genetic	10934243

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Calcium/calmodulin-dependent protein kinase II phosphorylates andregulates the Drosophila eag potassium channel.";
Wang Z., Wilson G.F., Griffith L.C.;
J. Biol. Chem. 277:24022-24029(2002).
Cited for: FUNCTION, PHOSPHORYLATION AT THR-787, MUTAGENESIS OF THR-787, ANDTISSUE SPECIFICITY.
PubMed: 11980904