KCNQ4_HUMAN - dbPTM
KCNQ4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCNQ4_HUMAN
UniProt AC P56696
Protein Name Potassium voltage-gated channel subfamily KQT member 4
Gene Name KCNQ4
Organism Homo sapiens (Human).
Sequence Length 695
Subcellular Localization Basal cell membrane
Multi-pass membrane protein. Situated at the basal membrane of cochlear outer hair cells..
Protein Description Probably important in the regulation of neuronal excitability. May underlie a potassium current involved in regulating the excitability of sensory cells of the cochlea. KCNQ4 channels are blocked by linopirdin, XE991 and bepridil, whereas clofilium is without significant effect. Muscarinic agonist oxotremorine-M strongly suppress KCNQ4 current in CHO cells in which cloned KCNQ4 channels were coexpressed with M1 muscarinic receptors..
Protein Sequence MAEAPPRRLGLGPPPGDAPRAELVALTAVQSEQGEAGGGGSPRRLGLLGSPLPPGAPLPGPGSGSGSACGQRSSAAHKRYRRLQNWVYNVLERPRGWAFVYHVFIFLLVFSCLVLSVLSTIQEHQELANECLLILEFVMIVVFGLEYIVRVWSAGCCCRYRGWQGRFRFARKPFCVIDFIVFVASVAVIAAGTQGNIFATSALRSMRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFASFLVYLAEKDANSDFSSYADSLWWGTITLTTIGYGDKTPHTWLGRVLAAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRMPAANLIQAAWRLYSTDMSRAYLTATWYYYDSILPSFRELALLFEHVQRARNGGLRPLEVRRAPVPDGAPSRYPPVATCHRPGSTSFCPGESSRMGIKDRIRMGSSQRRTGPSKQHLAPPTMPTSPSSEQVGEATSPTKVQKSWSFNDRTRFRASLRLKPRTSAEDAPSEEVAEEKSYQCELTVDDIMPAVKTVIRSIRILKFLVAKRKFKETLRPYDVKDVIEQYSAGHLDMLGRIKSLQTRVDQIVGRGPGDRKAREKGDKGPSDAEVVDEISMMGRVVKVEKQVQSIEHKLDLLLGFYSRCLRSGTSASLGAVQVPLFDPDITSDYHSPVDHEDISVSAQTLSISRSVSTNMD
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
31PhosphorylationVALTAVQSEQGEAGG
EEEEEEECCCCCCCC
25.8628348404
41PhosphorylationGEAGGGGSPRRLGLL
CCCCCCCCCCCCCCC
20.6428348404
223PhosphorylationRMDRRGGTWKLLGSV
HCCCCCCCCHHHEEH
23.4216319223
235PhosphorylationGSVVYAHSKELITAW
EEHHHHCCHHHHHHH
21.47-
353PhosphorylationIQAAWRLYSTDMSRA
HHHHHHHHCCCCCCH
10.8430257219
361 (in isoform 2)Phosphorylation-11.9525072903
363 (in isoform 2)Phosphorylation-14.9025072903
365 (in isoform 2)Phosphorylation-14.5725072903
367 (in isoform 2)Phosphorylation-6.4425072903
368 (in isoform 2)Phosphorylation-7.7425072903
369 (in isoform 2)Phosphorylation-6.3725072903
371 (in isoform 2)Phosphorylation-15.2025072903
460PhosphorylationKQHLAPPTMPTSPSS
CCCCCCCCCCCCCCH
34.4222210691
467PhosphorylationTMPTSPSSEQVGEAT
CCCCCCCHHHCCCCC
35.1222210691
475PhosphorylationEQVGEATSPTKVQKS
HHCCCCCCCCCCCCC
37.31-
477PhosphorylationVGEATSPTKVQKSWS
CCCCCCCCCCCCCCC
43.55-
482PhosphorylationSPTKVQKSWSFNDRT
CCCCCCCCCCCCCCC
15.7430266825
484PhosphorylationTKVQKSWSFNDRTRF
CCCCCCCCCCCCCCC
22.6623401153
494PhosphorylationDRTRFRASLRLKPRT
CCCCCEEEEECCCCC
15.1226437602
552PhosphorylationAKRKFKETLRPYDVK
HHHHHHHCCCCCCHH
28.7622817900
565PhosphorylationVKDVIEQYSAGHLDM
HHHHHHHHCHHCHHH
6.4128111955
566PhosphorylationKDVIEQYSAGHLDML
HHHHHHHCHHCHHHH
27.7128111955
678PhosphorylationPVDHEDISVSAQTLS
CCCHHHCCEEEEEEE
23.49-
685PhosphorylationSVSAQTLSISRSVST
CEEEEEEEEEECCCC
23.1624719451

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 KCNQ4_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCNQ4_HUMAN !!

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 KCNQ4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS90A_HUMANHSP90AA1physical
23431407
ENPL_HUMANHSP90B1physical
23431407
DNJA1_HUMANDNAJA1physical
23431407
HSP7C_HUMANHSPA8physical
23431407
STIP1_HUMANSTIP1physical
23431407
CHIP_HUMANSTUB1physical
23431407

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCNQ4_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP