KCNA4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCNA4_MOUSE
• UniProt AC: Q61423
• Protein Name: Potassium voltage-gated channel subfamily A member 4
• Gene Name: Kcna4
• Organism: Mus musculus (Mouse).
• Sequence Length: 654
• 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: 8020965 Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (By similarity Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA4 forms a potassium channel that opens in response to membrane depolarization, followed by rapid spontaneous channel closure]
• Protein Sequence: MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGGPHHHHQTRGAYSSHDPQGSRGSRRRRRQRTEKKKLHHRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEEDHGDGCSYTDLLPQDDGGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVILISIVIFCLETLPEFRDDRDLIMALSAGGHSRLLNDTSAPHLENSGHTIFNDPFFIVETVCIVWFSFEFVVRCFACPSQALFFKNIMNIIDIVSILPYFITLGTDLAQQQGGGNGQQQQAMSFAILRIIRLVRVFRIFKLSRHSKGLQILGHTLRASMRELGLLIFFLFIGVILFSSAVYFAEADEPTTHFQSIPDAFWWAVVTMTTVGYGDMKPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETENEEQTQLTQNAVSCPYLPSNLLKKFRSSTSSSLGDKSEYLEMEEGVKESLCGKEEKCQGKGDESETDKNNCSNAKAVETDV

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
79	Phosphorylation	SSHDPQGSRGSRRRR CCCCCCCCHHHHHHH	28.37	29899451
82	Phosphorylation	DPQGSRGSRRRRRQR CCCCCHHHHHHHHHH	22.85	29899451
100	Phosphorylation	KKLHHRQSSFPHCSD HHHHHCCCCCCCHHH	33.62	29899451
101	Phosphorylation	KLHHRQSSFPHCSDL HHHHCCCCCCCHHHC	34.16	22324799
106	Phosphorylation	QSSFPHCSDLMPSGS CCCCCCHHHCCCCCC	30.64	22324799
111	Phosphorylation	HCSDLMPSGSEEKIL CHHHCCCCCCHHHHH	40.77	29899451
113	Phosphorylation	SDLMPSGSEEKILRE HHCCCCCCHHHHHHH	47.09	29899451
122	Phosphorylation	EKILRELSEEEEDEE HHHHHHHCHHCCCHH	37.90	25521595
142	Phosphorylation	EEEGRFYYSEEDHGD HHHCCCEECCCCCCC	13.59	22807455
154	Phosphorylation	HGDGCSYTDLLPQDD CCCCCCCCCCCCCCC	12.13	22817900
193	Ubiquitination	LRFETQMKTLAQFPE CCEEHHHHHHHHCCH	30.48	22790023
208	Ubiquitination	TLLGDPEKRTQYFDP HHHCCHHHCCCCCCH	67.16	27667366
210	Phosphorylation	LGDPEKRTQYFDPLR HCCHHHCCCCCCHHH	38.39	25159016
212	Phosphorylation	DPEKRTQYFDPLRNE CHHHCCCCCCHHHCC	14.88	25159016
349	Phosphorylation	ALSAGGHSRLLNDTS HHHCCCCHHHCCCCC	28.09	22817900
353	N-linked_Glycosylation	GGHSRLLNDTSAPHL CCCHHHCCCCCCCCH	55.92	-
566	Phosphorylation	VIVSNFNYFYHRETE EEEECCCEEEECCCC	11.02	-
586	Phosphorylation	QLTQNAVSCPYLPSN HHHHHHHCCCCCCHH	13.63	25521595
600	Phosphorylation	NLLKKFRSSTSSSLG HHHHHHHHCCCCCCC	40.89	29899451
601	Phosphorylation	LLKKFRSSTSSSLGD HHHHHHHCCCCCCCC	28.22	29899451
602	Phosphorylation	LKKFRSSTSSSLGDK HHHHHHCCCCCCCCH	33.60	29899451
603	Phosphorylation	KKFRSSTSSSLGDKS HHHHHCCCCCCCCHH	21.63	29899451
604	Phosphorylation	KFRSSTSSSLGDKSE HHHHCCCCCCCCHHH	29.66	29899451
605	Phosphorylation	FRSSTSSSLGDKSEY HHHCCCCCCCCHHHH	35.82	29899451
610	Phosphorylation	SSSLGDKSEYLEMEE CCCCCCHHHHHHHHH	35.89	29899451
612	Phosphorylation	SLGDKSEYLEMEEGV CCCCHHHHHHHHHHH	18.30	29899451

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
600	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KCNA4_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KCNA4_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of KCNA4_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.
PubMed: 17114649