KCNA4_HUMAN - dbPTM
KCNA4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCNA4_HUMAN
UniProt AC P22459
Protein Name Potassium voltage-gated channel subfamily A member 4
Gene Name KCNA4
Organism Homo sapiens (Human).
Sequence Length 653
Subcellular Localization Cell membrane
Multi-pass membrane protein . Cell projection, axon .
Protein Description Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. [PubMed: 19912772]
Protein Sequence MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGSGGSGGGSHHHHQSRGACTSHDPQSSRGSRRRRRQRSEKKKAHYRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEDDHGDECSYTDLLPQDEGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLVMALSAGGHGGLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCAKEEKCQGKGDDSETDKNNCSNAKAVETDV
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
90PhosphorylationRRRRRQRSEKKKAHY
HHHHHHHHHHHHHHH
45.49-
122PhosphorylationEKILRELSEEEEDEE
HHHHHHHCHHCCCHH
37.90-
219PhosphorylationFDPLRNEYFFDRNRP
CCHHHCCCCCCCCCC
17.07-
227PhosphorylationFFDRNRPSFDAILYY
CCCCCCCCCCEEEEE
32.30-
233PhosphorylationPSFDAILYYYQSGGR
CCCCEEEEEECCCCC
8.26-
352N-linked_GlycosylationGGHGGLLNDTSAPHL
CCCCCCCCCCCCCCH
56.40UniProtKB CARBOHYD
458PhosphorylationVFRIFKLSRHSKGLQ
HHHHHHHCCCCCHHH
28.6526074081
542PhosphorylationVGGKIVGSLCAIAGV
ECCEEHHHHHHHHHH
14.91-
565PhosphorylationVIVSNFNYFYHRETE
EEEECCCEEEECCCC
11.0212151401
571PhosphorylationNYFYHRETENEEQTQ
CEEEECCCCCHHHHH
44.0328270605
577PhosphorylationETENEEQTQLTQNAV
CCCCHHHHHHHHHHH
28.9128270605
580PhosphorylationNEEQTQLTQNAVSCP
CHHHHHHHHHHHCCC
15.2328270605
585PhosphorylationQLTQNAVSCPYLPSN
HHHHHHHCCCCCCHH
13.6328270605
588PhosphorylationQNAVSCPYLPSNLLK
HHHHCCCCCCHHHHH
35.2628270605
591PhosphorylationVSCPYLPSNLLKKFR
HCCCCCCHHHHHHHH
37.2028270605
599PhosphorylationNLLKKFRSSTSSSLG
HHHHHHHHCCCCCCC
40.89-
601PhosphorylationLKKFRSSTSSSLGDK
HHHHHHCCCCCCCCH
33.6015955806

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
90SPhosphorylationKinasePKA-Uniprot
599SPhosphorylationKinasePKA-Uniprot
601TPhosphorylationKinasePRKACAP17612
GPS
-KUbiquitinationE3 ubiquitin ligaseLNX1Q8TBB1
PMID:22889411

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCNA4_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 KCNA4_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG1_HUMANDLG1physical
12860415
DLG4_HUMANDLG4physical
11997254
DLG2_HUMANDLG2physical
11997254
DLG1_HUMANDLG1physical
11997254
KCNA2_HUMANKCNA2physical
10428084
KCNA1_HUMANKCNA1physical
10428084
DLG4_HUMANDLG4physical
9581762
DLG4_HUMANDLG4physical
8938729
DLG1_HUMANDLG1physical
8938729
DLG4_HUMANDLG4physical
8601796
SRC_HUMANSRCphysical
11149959
KCNRG_HUMANKCNRGphysical
19968958
DLG4_HUMANDLG4physical
11723117
DLG4_HUMANDLG4physical
7477295
DLG1_HUMANDLG1physical
7477295
KCAB2_HUMANKCNAB2physical
23390957
SIR1_HUMANSIRT1physical
23390957

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
There are no disease associations of PTM sites.
DrugBank
DB06637Dalfampridine
Regulatory Network of KCNA4_HUMAN

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Related Literatures of Post-Translational Modification

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