dbPTM

KCNA2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCNA2_MOUSE
UniProt AC	P63141
Protein Name	Potassium voltage-gated channel subfamily A member 2
Gene Name	Kcna2
Organism	Mus musculus (Mouse).
Sequence Length	499
Subcellular Localization	Cell membrane Multi-pass membrane protein . Membrane . Cell projection, axon . Cell junction, synapse . Endoplasmic reticulum membrane . Cell projection, lamellipodium membrane . Cell junction, synapse, synaptosome . Cell junction, synapse, presynaptic
Protein Description	Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. 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: 12527813]
Protein Sequence	MTVATGDPVDEAAALPGHPQDTYDPEADHECCERVVINISGLRFETQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFSEEIRFYELGEEAMEMFREDEGYIKEEERPLPENEFQRQVWLLFEYPESSGPARIIAIVSVMVILISIVSFCLETLPIFRDENEDMHGGGVTFHTYSNSTIGYQQSTSFTDPFFIVETLCIIWFSFEFLVRFFACPSKAGFFTNIMNIIDIVAIIPYFITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEADERDSQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPDLKKSRSASTISKSDYMEIQEGVNNSNEDFREENLKTANCTLANTNYVNITKMLTDV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	LPGHPQDTYDPEADH CCCCCCCCCCCCCCH	25.28	-
49	Ubiquitination	LRFETQLKTLAQFPE CCHHHHHHHHHHCCH	31.51	-
49	Ubiquitination	LRFETQLKTLAQFPE CCHHHHHHHHHHCCH	31.51	22790023
63	Ubiquitination	ETLLGDPKKRMRYFD HHHHCCHHHCCCCCC	58.72	27667366
63	Ubiquitination	ETLLGDPKKRMRYFD HHHHCCHHHCCCCCC	58.72	22790023
207	N-linked_Glycosylation	VTFHTYSNSTIGYQQ EEEEEECCCCEEEEC	32.53	-
244	S-palmitoylation	FLVRFFACPSKAGFF HHHHHHCCCCCCCCC	3.10	-
415	Phosphorylation	VIVSNFNYFYHRETE EEEECCCEEEECCCC	11.02	-
421	Phosphorylation	NYFYHRETEGEEQAQ CEEEECCCCCHHHHH	49.61	17114649
429	Phosphorylation	EGEEQAQYLQVTSCP CCHHHHHEEEEECCC	11.34	29899451
433	Phosphorylation	QAQYLQVTSCPKIPS HHHEEEEECCCCCCC	16.20	24925903
434	Phosphorylation	AQYLQVTSCPKIPSS HHEEEEECCCCCCCC	29.57	25521595
440	Phosphorylation	TSCPKIPSSPDLKKS ECCCCCCCCCCHHCC	58.96	25521595
441	O-linked_Glycosylation	SCPKIPSSPDLKKSR CCCCCCCCCCHHCCC	19.65	30059200
441	Phosphorylation	SCPKIPSSPDLKKSR CCCCCCCCCCHHCCC	19.65	25521595
447	Phosphorylation	SSPDLKKSRSASTIS CCCCHHCCCCCCCCC	29.85	22817900
449	Phosphorylation	PDLKKSRSASTISKS CCHHCCCCCCCCCHH	33.39	29899451
451	Phosphorylation	LKKSRSASTISKSDY HHCCCCCCCCCHHHH	27.76	29899451
452	Phosphorylation	KKSRSASTISKSDYM HCCCCCCCCCHHHHH	29.05	29899451
454	Phosphorylation	SRSASTISKSDYMEI CCCCCCCCHHHHHHH	26.62	29899451
456	Phosphorylation	SASTISKSDYMEIQE CCCCCCHHHHHHHHH	27.47	25521595
458	Phosphorylation	STISKSDYMEIQEGV CCCCHHHHHHHHHHC	12.07	25521595
468	Phosphorylation	IQEGVNNSNEDFREE HHHHCCCCCHHHHHH	36.07	25521595
482	S-nitrosylation	ENLKTANCTLANTNY HHHHHCCCEECCCCC	2.82	24895380
489	Phosphorylation	CTLANTNYVNITKML CEECCCCCEEHHEEE	7.88	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
Oops, there are no upstream regulatory protein records of KCNA2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCNA2_MOUSE !!

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 KCNA2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
KCAB2_MOUSE	Kcnab2	physical	21106837

Drug and Disease Associations

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

Regulatory Network of KCNA2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-421 AND THR-433, ANDMASS SPECTROMETRY.	17114649 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-429, AND MASSSPECTROMETRY.	18034455 [Abstract]