KCNH7_HUMAN - dbPTM
KCNH7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCNH7_HUMAN
UniProt AC Q9NS40
Protein Name Potassium voltage-gated channel subfamily H member 7
Gene Name KCNH7
Organism Homo sapiens (Human).
Sequence Length 1196
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Pore-forming (alpha) subunit of voltage-gated potassium channel. Channel properties may be modulated by cAMP and subunit assembly..
Protein Sequence MPVRRGHVAPQNTFLGTIIRKFEGQNKKFIIANARVQNCAIIYCNDGFCEMTGFSRPDVMQKPCTCDFLHGPETKRHDIAQIAQALLGSEERKVEVTYYHKNGSTFICNTHIIPVKNQEGVAMMFIINFEYVTDNENAATPERVNPILPIKTVNRKFFGFKFPGLRVLTYRKQSLPQEDPDVVVIDSSKHSDDSVAMKHFKSPTKESCSPSEADDTKALIQPSKCSPLVNISGPLDHSSPKRQWDRLYPDMLQSSSQLSHSRSRESLCSIRRASSVHDIEGFGVHPKNIFRDRHASEDNGRNVKGPFNHIKSSLLGSTSDSNLNKYSTINKIPQLTLNFSEVKTEKKNSSPPSSDKTIIAPKVKDRTHNVTEKVTQVLSLGADVLPEYKLQTPRINKFTILHYSPFKAVWDWLILLLVIYTAIFTPYSAAFLLNDREEQKRRECGYSCSPLNVVDLIVDIMFIIDILINFRTTYVNQNEEVVSDPAKIAIHYFKGWFLIDMVAAIPFDLLIFGSGSDETTTLIGLLKTARLLRLVRVARKLDRYSEYGAAVLMLLMCIFALIAHWLACIWYAIGNVERPYLTDKIGWLDSLGQQIGKRYNDSDSSSGPSIKDKYVTALYFTFSSLTSVGFGNVSPNTNSEKIFSICVMLIGSLMYASIFGNVSAIIQRLYSGTARYHMQMLRVKEFIRFHQIPNPLRQRLEEYFQHAWTYTNGIDMNMVLKGFPECLQADICLHLNQTLLQNCKAFRGASKGCLRALAMKFKTTHAPPGDTLVHCGDVLTALYFLSRGSIEILKDDIVVAILGKNDIFGEMVHLYAKPGKSNADVRALTYCDLHKIQREDLLEVLDMYPEFSDHFLTNLELTFNLRHESAKADLLRSQSMNDSEGDNCKLRRRKLSFESEGEKENSTNDPEDSADTIRHYQSSKRHFEEKKSRSSSFISSIDDEQKPLFSGIVDSSPGIGKASGLDFEETVPTSGRMHIDKRSHSCKDITDMRSWERENAHPQPEDSSPSALQRAAWGISETESDLTYGEVEQRLDLLQEQLNRLESQMTTDIQTILQLLQKQTTVVPPAYSMVTAGSEYQRPIIQLMRTSQPEASIKTDRSFSPSSQCPEFLDLEKSKLKSKESLSSGVHLNTASEDNLTSLLKQDSDLSLELHLRQRKTYVHPIRHPSLPDSSLSTVGIVGLHRHVSDPGLPGK
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
97PhosphorylationEERKVEVTYYHKNGS
CCCEEEEEEEECCCC		12.5929759185
98PhosphorylationERKVEVTYYHKNGST
CCEEEEEEEECCCCE		14.5629759185
99PhosphorylationRKVEVTYYHKNGSTF
CEEEEEEEECCCCEE		9.2829759185
174PhosphorylationVLTYRKQSLPQEDPD
EEEECCCCCCCCCCC		45.0830243723
226PhosphorylationLIQPSKCSPLVNISG
HCCHHHCCCCEECCC		25.63-
238PhosphorylationISGPLDHSSPKRQWD
CCCCCCCCCCHHHHH		48.26-
248PhosphorylationKRQWDRLYPDMLQSS
HHHHHHHCHHHHHCC		9.7029759185
261PhosphorylationSSSQLSHSRSRESLC
CCHHHCCCCCHHHHH		28.6829759185
269PhosphorylationRSRESLCSIRRASSV
CCHHHHHHHHCCCCC		25.1519664994
274PhosphorylationLCSIRRASSVHDIEG
HHHHHCCCCCCCCCC		30.95-
275PhosphorylationCSIRRASSVHDIEGF
HHHHCCCCCCCCCCC		23.6124275748
312PhosphorylationGPFNHIKSSLLGSTS
CCCHHHHHHHCCCCC		26.1432142685
317PhosphorylationIKSSLLGSTSDSNLN
HHHHHCCCCCCCCCC		25.3822468782
318PhosphorylationKSSLLGSTSDSNLNK
HHHHCCCCCCCCCCH		34.4530576142
319PhosphorylationSSLLGSTSDSNLNKY
HHHCCCCCCCCCCHH		40.5124076635
321PhosphorylationLLGSTSDSNLNKYST
HCCCCCCCCCCHHCC		42.8822468782
326PhosphorylationSDSNLNKYSTINKIP
CCCCCCHHCCCCCCC		15.2427642862
336PhosphorylationINKIPQLTLNFSEVK
CCCCCCEEECHHHHC		17.8926074081
340PhosphorylationPQLTLNFSEVKTEKK
CCEEECHHHHCCCCC		40.1726074081
344PhosphorylationLNFSEVKTEKKNSSP
ECHHHHCCCCCCCCC		59.2126074081
349PhosphorylationVKTEKKNSSPPSSDK
HCCCCCCCCCCCCCC		53.7717924679
350PhosphorylationKTEKKNSSPPSSDKT
CCCCCCCCCCCCCCC		50.6617924679
353PhosphorylationKKNSSPPSSDKTIIA
CCCCCCCCCCCCEEE		55.3317924679
354PhosphorylationKNSSPPSSDKTIIAP
CCCCCCCCCCCEEEC		49.23-
357PhosphorylationSPPSSDKTIIAPKVK
CCCCCCCCEEECCCC		23.70-
388PhosphorylationGADVLPEYKLQTPRI
CCCCCCCCCCCCCCC		18.3025884760
599PhosphorylationGQQIGKRYNDSDSSS
HHHHHHHCCCCCCCC		27.14-
600N-linked_GlycosylationQQIGKRYNDSDSSSG
HHHHHHCCCCCCCCC		46.47UniProtKB CARBOHYD
604PhosphorylationKRYNDSDSSSGPSIK
HHCCCCCCCCCCCHH		30.29-
614PhosphorylationGPSIKDKYVTALYFT
CCCHHHCCEEEEEEE		17.11-
626PhosphorylationYFTFSSLTSVGFGNV
EEEHHCCCCCCCCCC		24.2626074081
627PhosphorylationFTFSSLTSVGFGNVS
EEHHCCCCCCCCCCC		26.0726074081
830PhosphorylationADVRALTYCDLHKIQ
HHHHHHHHHCHHHCC		5.7025884760
869PhosphorylationTFNLRHESAKADLLR
EEECCCHHHHHHHHH		29.01-
877PhosphorylationAKADLLRSQSMNDSE
HHHHHHHCCCCCCCC		26.95-
879PhosphorylationADLLRSQSMNDSEGD
HHHHHCCCCCCCCCC		22.3124719451
896PhosphorylationKLRRRKLSFESEGEK
HHHHHHCCCCCCCCC		29.9725884760
899PhosphorylationRRKLSFESEGEKENS
HHHCCCCCCCCCCCC		49.22-
1064PhosphorylationLQLLQKQTTVVPPAY
HHHHHHCCCCCCCCH		28.7022210691
1065PhosphorylationQLLQKQTTVVPPAYS
HHHHHCCCCCCCCHH		19.6022210691
1107PhosphorylationDRSFSPSSQCPEFLD
CCCCCCHHHCCHHHH		38.9032142685
1142PhosphorylationASEDNLTSLLKQDSD
CCCCCHHHHHHCCCC		34.5724719451
1170PhosphorylationVHPIRHPSLPDSSLS
ECCCCCCCCCCCCCC		46.54-
1189PhosphorylationVGLHRHVSDPGLPGK
EEECCCCCCCCCCCC		31.7827732954
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 KCNH7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCNH7_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 KCNH7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of KCNH7_HUMAN !!
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
D00638 Flecainide acetate (JP16/USP); Tambocor (TN)
D07962 Flecainide (INN)
DrugBank
DB00590Doxazosin
DB00308Ibutilide
DB01110Miconazole
DB00457Prazosin
DB01162Terazosin
Regulatory Network of KCNH7_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-350 ANDSER-353, AND MASS SPECTROMETRY.

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