KCNQ5_HUMAN - dbPTM
KCNQ5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCNQ5_HUMAN
UniProt AC Q9NR82
Protein Name Potassium voltage-gated channel subfamily KQT member 5
Gene Name KCNQ5
Organism Homo sapiens (Human).
Sequence Length 932
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. Therefore, it is important in the regulation of neuronal excitability. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. As the native M-channel, the potassium channel composed of KCNQ3 and KCNQ5 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1..
Protein Sequence MPRHHAGGEEGGAAGLWVKSGAAAAAAGGGRLGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAATLGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGTDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQITSDKKSREKITAEHETTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALALASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLSRSTSANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPISQSDGSAVAATNTIANQINTAPKPAAPTTLQIPPPLPAIKHLPRPETLHPNPAGLQESISDVTTCLVASKENVQVAQSNLTKDRSMRKSFDMGGETLLSVCPMVPKDLGKSLSVQNLIRSTEELNIQLSGSESSGSRGSQDFYPKWRESKLFITDEEVGPEETETDTFDAAPQPAREAAFASDSLRTGRSRSSQSICKAGESTDALSLPHVKLK
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
67PhosphorylationLLGTRAATLGGGGGG
EEECCEECCCCCCCC		25.5829449344
78PhosphorylationGGGGLRESRRGKQGA
CCCCHHHHHCCCCCC		22.3523401153
78 (in isoform 6)Phosphorylation-22.3524719451
88PhosphorylationGKQGARMSLLGKPLS
CCCCCCHHHCCCCCC		18.19-
96PhosphorylationLLGKPLSYTSSQSCR
HCCCCCCCCCCHHHH		20.5125884760
181PhosphorylationEFIIRIWSAGCCCRY
HHHHHHHHCCCCHHH		16.6523898821
233PhosphorylationFATSALRSLRFLQIL
HHHHHHHHHHHHHHH		25.4226670566
251PhosphorylationRMDRRGGTWKLLGSV
HCCCCCCCCHHHEEH		23.4216319223
263PhosphorylationGSVVYAHSKELITAW
EEHHHHCCHHHHHHH		21.47-
318PhosphorylationTIGYGDKTPLTWLGR
ECCCCCCCCCHHHHH		28.4222210691
321PhosphorylationYGDKTPLTWLGRLLS
CCCCCCCHHHHHHHH		21.6122210691
337PhosphorylationGFALLGISFFALPAG
HHHHHCHHHHCCCHH		16.7122210691
348PhosphorylationLPAGILGSGFALKVQ
CCHHHHHCCHHHHHH		27.5622210691
402 (in isoform 2)Phosphorylation-18.6129514088
402PhosphorylationPHLKALHTCSPTKKE
CHHHHHHHCCCCHHH		18.6127732954
404 (in isoform 2)Phosphorylation-36.4429514088
404PhosphorylationLKALHTCSPTKKEQG
HHHHHHCCCCHHHCC		36.4427732954
406PhosphorylationALHTCSPTKKEQGEA
HHHHCCCCHHHCCCC		38.1527732954
406 (in isoform 2)Phosphorylation-38.1529514088
411 (in isoform 3)Phosphorylation-33.26-
411 (in isoform 2)Phosphorylation-33.2628450419
414PhosphorylationKKEQGEASSSQKLSF
HHHCCCCCCCCCCCH		26.6429978859
414 (in isoform 6)Phosphorylation-26.6429083192
415PhosphorylationKEQGEASSSQKLSFK
HHCCCCCCCCCCCHH		43.7829978859
415 (in isoform 6)Phosphorylation-43.7829083192
416 (in isoform 6)Phosphorylation-28.9229083192
416PhosphorylationEQGEASSSQKLSFKE
HCCCCCCCCCCCHHH		28.9229978859
420 (in isoform 3)Phosphorylation-41.1128270605
420 (in isoform 6)Phosphorylation-41.1129083192
420PhosphorylationASSSQKLSFKERVRM
CCCCCCCCHHHHHHH		41.1124719451
421 (in isoform 3)Phosphorylation-16.0728270605
422 (in isoform 3)Phosphorylation-41.0328270605
426 (in isoform 3)Phosphorylation-22.5928270605
429 (in isoform 6)Phosphorylation-13.0428270605
430 (in isoform 6)Phosphorylation-34.5828270605
431 (in isoform 6)Phosphorylation-53.9728270605
435 (in isoform 6)Phosphorylation-3.4528270605
439 (in isoform 6)Phosphorylation-45.1124719451
441PhosphorylationSIKSRQASVGDRRSP
CHHHCCCCCCCCCCC		20.4929523821
447PhosphorylationASVGDRRSPSTDITA
CCCCCCCCCCCCCEE		24.8930266825
449PhosphorylationVGDRRSPSTDITAEG
CCCCCCCCCCCEECC		39.7029255136
450PhosphorylationGDRRSPSTDITAEGS
CCCCCCCCCCEECCC		34.5030266825
453PhosphorylationRSPSTDITAEGSPTK
CCCCCCCEECCCCCE		22.8229255136
457PhosphorylationTDITAEGSPTKVQKS
CCCEECCCCCEEEEE		22.3930266825
459PhosphorylationITAEGSPTKVQKSWS
CEECCCCCEEEEEEC		45.6130266825
464PhosphorylationSPTKVQKSWSFNDRT
CCCEEEEEECCCCCC		15.7430266825
466PhosphorylationTKVQKSWSFNDRTRF
CEEEEEECCCCCCCC		22.6623401153
476 (in isoform 6)Phosphorylation-23.1224719451
485 (in isoform 6)Phosphorylation-44.2624719451
500PhosphorylationALGTDDVYDEKGCQC
CCCCCCCCCCCCCCC		25.9425884760
540PhosphorylationAKRKFKETLRPYDVK
HHHHHHHHCCCCCHH		28.76-
581PhosphorylationILGKGQITSDKKSRE
HHCCCCCCCCHHHHH		24.00-
615PhosphorylationKVEKQVQSIESKLDC
HHHHHHHHHHHHHHH		29.4822210691
618PhosphorylationKQVQSIESKLDCLLD
HHHHHHHHHHHHHHH		36.5322210691
619UbiquitinationQVQSIESKLDCLLDI
HHHHHHHHHHHHHHH		35.24-
657PhosphorylationECEQTSDYQSPVDSK
CCCCCCCCCCCCCCC		15.62-
673PhosphorylationLSGSAQNSGCLSRST
CCCCCCCCCCCCCCC		20.8525262027
677PhosphorylationAQNSGCLSRSTSANI
CCCCCCCCCCCCCCC		28.4128450419
679PhosphorylationNSGCLSRSTSANISR
CCCCCCCCCCCCCCC		24.2828102081
680PhosphorylationSGCLSRSTSANISRG
CCCCCCCCCCCCCCC		30.6528102081
681PhosphorylationGCLSRSTSANISRGL
CCCCCCCCCCCCCCC		22.1428102081
685PhosphorylationRSTSANISRGLQFIL
CCCCCCCCCCCEEEE		21.8028102081
807PhosphorylationKDRSMRKSFDMGGET
CCHHHHHHHCCCCCC		19.0022777824
826 (in isoform 6)Phosphorylation-13.3727251275
829PhosphorylationVPKDLGKSLSVQNLI
CCHHHCCCCCHHHHH		24.8729978859
831PhosphorylationKDLGKSLSVQNLIRS
HHHCCCCCHHHHHHC		28.8422617229
850 (in isoform 6)Phosphorylation-53.0727251275
861PhosphorylationSRGSQDFYPKWRESK
CCCCCCCCHHHHCCC		16.5225884760
863AcetylationGSQDFYPKWRESKLF
CCCCCCHHHHCCCEE		47.7219821663
900PhosphorylationAREAAFASDSLRTGR
HHHHHHHCCCHHCCC		22.6825850435
902PhosphorylationEAAFASDSLRTGRSR
HHHHHCCCHHCCCCC		19.7725850435
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
88SPhosphorylationKinasePKACAP17612
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCNQ5_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 KCNQ5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCNQ3_HUMANKCNQ3physical
12890507
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D04741 Linopirdine (USAN/INN)
D09569 Ezogabine (USAN); Retigabine (INN); Potiga (TN)
DrugBank
DB04953Ezogabine
Regulatory Network of KCNQ5_HUMAN

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Related Literatures of Post-Translational Modification

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