KCND3_HUMAN - dbPTM
KCND3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCND3_HUMAN
UniProt AC Q9UK17
Protein Name Potassium voltage-gated channel subfamily D member 3
Gene Name KCND3
Organism Homo sapiens (Human).
Sequence Length 655
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cell membrane, sarcolemma
Multi-pass membrane protein . Cell projection, dendrite . Interaction with palmitoylated KCNIP2 and KCNIP3 enhances cell surface expression.
Protein Description Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits..
Protein Sequence MAAGVAAWLPFARAAAIGWMPVANCPMPLAPADKNKRQDELIVLNVSGRRFQTWRTTLERYPDTLLGSTEKEFFFNEDTKEYFFDRDPEVFRCVLNFYRTGKLHYPRYECISAYDDELAFYGILPEIIGDCCYEEYKDRKRENAERLMDDNDSENNQESMPSLSFRQTMWRAFENPHTSTLALVFYYVTGFFIAVSVITNVVETVPCGTVPGSKELPCGERYSVAFFCLDTACVMIFTVEYLLRLFAAPSRYRFIRSVMSIIDVVAIMPYYIGLVMTNNEDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGSSASKFTSIPASFWYTIVTMTTLGYGDMVPKTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQKKARLARIRVAKTGSSNAYLHSKRNGLLNEALELTGTPEEEHMGKTTSLIESQHHHLLHCLEKTTGLSYLVDDPLLSVRTSTIKNHEFIDEQMFEQNCMESSMQNYPSTRSPSLSSHPGLTTTCCSRRSKKTTHLPNSNLPATRLRSMQELSTIHIQGSEQPSLTTSRSSLNLKADDGLRPNCKTSQITTAIISIPTPPALTPEGESRPPPASPGPNTNIPSIASNVVKVSAL
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
108PhosphorylationGKLHYPRYECISAYD
CCCCCCCHHHCEECC		15.62-
136PhosphorylationGDCCYEEYKDRKREN
CHHCHHHHHHHHHHH		13.27-
153PhosphorylationRLMDDNDSENNQESM
HHCCCCCCCCCCCCC		48.7729038488
159PhosphorylationDSENNQESMPSLSFR
CCCCCCCCCCCCHHH		26.6527251275
162PhosphorylationNNQESMPSLSFRQTM
CCCCCCCCCHHHHHH		28.1829978859
164PhosphorylationQESMPSLSFRQTMWR
CCCCCCCHHHHHHHH		23.7924719451
288PhosphorylationDVSGAFVTLRVFRVF
CCCCCCHHHHHHHHH		11.46-
435PhosphorylationARIRVAKTGSSNAYL
HHHEECCCCCCCHHH		32.3422817900
437PhosphorylationIRVAKTGSSNAYLHS
HEECCCCCCCHHHHH		26.1728509920
438PhosphorylationRVAKTGSSNAYLHSK
EECCCCCCCHHHHHH		27.1628509920
441PhosphorylationKTGSSNAYLHSKRNG
CCCCCCHHHHHHHCC		14.8129116813
444PhosphorylationSSNAYLHSKRNGLLN
CCCHHHHHHHCCHHH		30.6228509920
459PhosphorylationEALELTGTPEEEHMG
HHHHHHCCCHHHHCC		23.45-
486PhosphorylationLLHCLEKTTGLSYLV
HHHHHHHCCCCHHHC		19.40-
499PhosphorylationLVDDPLLSVRTSTIK
HCCCCCEEEECCCCC		19.75-
504PhosphorylationLLSVRTSTIKNHEFI
CEEEECCCCCCCCCC		35.04-
533PhosphorylationQNYPSTRSPSLSSHP
HHCCCCCCCCCCCCC		20.9430631047
535PhosphorylationYPSTRSPSLSSHPGL
CCCCCCCCCCCCCCC		41.9727251275
537PhosphorylationSTRSPSLSSHPGLTT
CCCCCCCCCCCCCCC		30.8230631047
538PhosphorylationTRSPSLSSHPGLTTT
CCCCCCCCCCCCCCC		38.7130631047
555PhosphorylationSRRSKKTTHLPNSNL
CCCCCCCCCCCCCCC		30.2323836654
565PhosphorylationPNSNLPATRLRSMQE
CCCCCCHHHHHHHHH		28.44-
569PhosphorylationLPATRLRSMQELSTI
CCHHHHHHHHHHEEE		29.43-
585PhosphorylationIQGSEQPSLTTSRSS
ECCCCCCCCCCCCHH		37.73-
591PhosphorylationPSLTTSRSSLNLKAD
CCCCCCCHHCCCCCC		38.6627251275
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
108YPhosphorylationKinaseSRCP12931
PSP
136YPhosphorylationKinaseEGFRP00533
PSP
535SPhosphorylationKinaseRSK-SUBFAMILY-GPS
569SPhosphorylationKinaseCAMK2DQ13557
Uniprot
569SPhosphorylationKinaseRSK-SUBFAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
569SPhosphorylation

-
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 KCND3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRC_HUMANSRCphysical
18620005
DPP10_HUMANDPP10physical
22387313
AUP1_HUMANAUP1physical
17725712
CDK1_HUMANCDK1physical
17725712
CNBP_HUMANCNBPphysical
17725712
CUX1_HUMANCUX1physical
17725712
CASP_HUMANCUX1physical
17725712
DDB1_HUMANDDB1physical
17725712
EMD_HUMANEMDphysical
17725712
EWS_HUMANEWSR1physical
17725712
G3BP1_HUMANG3BP1physical
17725712
GRP78_HUMANHSPA5physical
17725712
HNRPF_HUMANHNRNPFphysical
17725712
HSP7C_HUMANHSPA8physical
17725712
XRCC6_HUMANXRCC6physical
17725712
XRCC5_HUMANXRCC5physical
17725712
LBR_HUMANLBRphysical
17725712
NONO_HUMANNONOphysical
17725712
NP1L1_HUMANNAP1L1physical
17725712
NDUS2_HUMANNDUFS2physical
17725712
P5CR2_HUMANPYCR2physical
17725712
RCN2_HUMANRCN2physical
17725712
RPGF5_HUMANRAPGEF5physical
17725712
RUVB1_HUMANRUVBL1physical
17725712
TBA1B_HUMANTUBA1Bphysical
17725712
TBB2A_HUMANTUBB2Aphysical
17725712
QCR2_HUMANUQCRC2physical
17725712
VPS4A_HUMANVPS4Aphysical
17725712
KCIP1_RATKcnip1physical
17725712
KCIP2_RATKcnip2physical
17725712
RPGF5_RATRapgef5physical
17725712
RPGF3_RATRapgef3physical
17725712
SEM3A_HUMANSEMA3Aphysical
24963029
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607346Spinocerebellar ataxia 19 (SCA19)
616399Brugada syndrome 9 (BRGDA9)
Kegg Drug
D00631 Bepridil hydrochloride hydrate (JAN); Bepridil hydrochloride (USAN); Vascor (TN)
D00636 Amiodarone hydrochloride (JP16/USAN); Ancaron (TN); Cordarone (TN)
D00638 Flecainide acetate (JP16/USP); Tambocor (TN)
D01856 Nifekalant hydrochloride (JAN); MS 551; Shinbit (TN)
D02537 Dronedarone (INN)
D02910 Amiodarone (USAN/INN)
D03547 Clofilium phosphate (USAN/INN)
D03914 Dronedarone hydrochloride (USAN); Multaq (TN)
D06652 Tedisamil (USAN)
D06653 Tedisamil sesquifumarate (USAN)
D07520 Bepridil (INN); Bepadin (TN)
D07962 Flecainide (INN)
DrugBank
DB00321Amitriptyline
DB06637Dalfampridine
DB00280Disopyramide
DB00458Imipramine
Regulatory Network of KCND3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-435 AND TYR-441, ANDMASS SPECTROMETRY.

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