KCNAS_DROME - dbPTM
KCNAS_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCNAS_DROME
UniProt AC P08510
Protein Name Potassium voltage-gated channel protein Shaker
Gene Name Sh
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 655
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Forms rapidly inactivating tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient and may contribute to A-type currents. [PubMed: 2448636 Plays a role in the regulation of sleep need or efficiency]
Protein Sequence MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGYGSLPKLSSQDEEGGAGHGFGGGPQHFEPIPHDHDFCERVVINVSGLRFETQLRTLNQFPDTLLGDPARRLRYFDPLRNEYFFDRSRPSFDAILYYYQSGGRLRRPVNVPLDVFSEEIKFYELGDQAINKFREDEGFIKEEERPLPDNEKQRKVWLLFEYPESSQAARVVAIISVFVILLSIVIFCLETLPEFKHYKVFNTTTNGTKIEEDEVPDITDPFFLIETLCIIWFTFELTVRFLACPNKLNFCRDVMNVIDIIAIIPYFITLATVVAEEEDTLNLPKAPVSPQDKSSNQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGRTLKASMRELGLLIFFLFIGVVLFSSAVYFAEAGSENSFFKSIPDAFWWAVVTMTTVGYGDMTPVGVWGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDQEEMQSQNFNHVTSCPYLPGTLGQHMKKSSLSESSSDMMDLDDGVESTPGLTETHPGRSAVAPFLGAQQQQQQPVASSLSMSIDKQLQHPLQQLTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQLQQQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV
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
3Sulfoxidation-----MAAVAGLYGL
-----CCHHHHHHHC
7.159923602
259N-linked_GlycosylationFKHYKVFNTTTNGTK
HCCCEEEEECCCCCC
39.2317893096
263N-linked_GlycosylationKVFNTTTNGTKIEED
EEEEECCCCCCCCCC
54.7817893096

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

Oops, there are no upstream regulatory protein records of KCNAS_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCNAS_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 KCNAS_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_DROMEPCNAphysical
14605208
A4_DROMEApplgenetic
10322116
CYA1_DROMErutgenetic
14960616
KCNAE_DROMEeaggenetic
10934243
KCNAE_DROMEeaggenetic
16452147
SCNA_DROMEparagenetic
11567611
SCNA_DROMEparagenetic
2155153
MLE_DROMEmlegenetic
15728380
KINH_DROMEKhcgenetic
8770597
KCNAB_DROMEShabgenetic
16525044
QVR_DROMEqvrgenetic
10934243
QVR_DROMEqvrphysical
20010822
QVR_DROMEqvrphysical
24613312
QVR_DROMEqvrphysical
26828958
DLG1_DROMEdlg1physical
17666528
DLG1_DROMEdlg1physical
25813388
DLG1_DROMEdlg1physical
9390515

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

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster.";
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.;
Glycobiology 17:1388-1403(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259 AND ASN-263, AND MASSSPECTROMETRY.

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