KCNQ2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCNQ2_RAT
• UniProt AC: O88943
• Protein Name: Potassium voltage-gated channel subfamily KQT member 2 {ECO:0000305}
• Gene Name: Kcnq2 {ECO:0000312|RGD:621504}
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 852
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein .
• Protein Description: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2 current is blocked by barium and tetraethylammonium whereas 4-aminopyridine and charybdotoxin have no effect on KCNQ2 current. Tyrosine kinase inhibitors genistein or herbimycin a markedly down-regulate KCNQ2 current. As the native M-channel, the potassium channel composed of KCNQ2 and KCNQ3 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1..
• Protein Sequence: MVQKSRNGGVYPGTSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSVLSKPRTGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMISSQTQTYGASRLIPPLNQLEMLRNLKSKSGLTFRKEPQPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLDDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVEDNKSCNCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPTITDKDRTKGPAETELPEDPSMMGRLGKVEKQVLSMEKKLDFLVSIYTQRMGIPPAETEAYFGAKEPEPAPPYHSPEDSRDHADKHGCIIKIVRSTSSTGQRKYAAPPVMPPAECPPSTSWQQSHQRHGTSPVGDHGSLVRIPPPPAHERSLSAYSGGNRASTEFLRLEGTPACRPSEAALRDSDTSISIPSVDHEELERSFSGFSISQSKENLNALASCYAAVAPCAKVRPYIAEGESDTDSDLCTPCGPPPRSATGEGPFGDVAWAGPRK

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
49	Ubiquitination	IAGSEAPKRGSVLSK EECCCCCCCCCCCCC	76.16	-
52	Phosphorylation	SEAPKRGSVLSKPRT CCCCCCCCCCCCCCC	24.74	30181290
55	Phosphorylation	PKRGSVLSKPRTGGA CCCCCCCCCCCCCCC	38.16	30181290
66	Ubiquitination	TGGAGAGKPPKRNAF CCCCCCCCCCCCCHH	58.58	-
217	Phosphorylation	RMDRRGGTWKLLGSV HCCCCCCHHHHCEEH	23.42	-
226	Nitration	KLLGSVVYAHSKELV HHCEEHHHHCCHHHH	9.10	18165258
226	Nitrated tyrosine	KLLGSVVYAHSKELV HHCEEHHHHCCHHHH	9.10	-
349	Phosphorylation	SAWRFYATNLSRTDL HHHHHHHHCCCCCCC	25.88	22673903
352	Phosphorylation	RFYATNLSRTDLHST HHHHHCCCCCCCHHH	34.89	25403869
439	Phosphorylation	VAAKGKGSPQAQTVR HHCCCCCCCCHHCCC	19.82	25403869
448	Phosphorylation	QAQTVRRSPSADQSL CHHCCCCCCCCCCCC	16.79	30411139
450	Phosphorylation	QTVRRSPSADQSLDD HCCCCCCCCCCCCCC	45.80	30240740
454	Phosphorylation	RSPSADQSLDDSPSK CCCCCCCCCCCCCCC	34.02	28432305
458	Phosphorylation	ADQSLDDSPSKVPKS CCCCCCCCCCCCCCC	30.64	30240740
460	Phosphorylation	QSLDDSPSKVPKSWS CCCCCCCCCCCCCCC	50.68	22673903
465	Phosphorylation	SPSKVPKSWSFGDRS CCCCCCCCCCCCCHH	23.14	28432305
467	Phosphorylation	SKVPKSWSFGDRSRA CCCCCCCCCCCHHHH	26.83	30411139
489	Phosphorylation	GAASRQNSEEASLPG CHHHCCCCCCCCCCC	28.60	25403869
493	Phosphorylation	RQNSEEASLPGEDIV CCCCCCCCCCCHHHC	38.07	25403869
534	Phosphorylation	CVMRFLVSKRKFKES HHHHHHHCCHHHHHH	28.96	-
541	Phosphorylation	SKRKFKESLRPYDVM CCHHHHHHCCCCCHH	30.21	-
577 (in isoform 2)	Phosphorylation	-	30.38	22276854
583 (in isoform 2)	Phosphorylation	-	39.20	22276854
586 (in isoform 2)	Phosphorylation	-	67.31	22276854
589	Ubiquitination	ITDKDRTKGPAETEL CCCCCCCCCCCCCCC	64.88	-
589 (in isoform 7)	Phosphorylation	-	64.88	22276854
595 (in isoform 7)	Phosphorylation	-	54.56	22276854
598 (in isoform 7)	Phosphorylation	-	87.79	22276854
618	Ubiquitination	KQVLSMEKKLDFLVS HHHHHHHHHHHHHHH	50.42	-
653	Phosphorylation	EPEPAPPYHSPEDSR CCCCCCCCCCCCCCC	17.55	28551015
655	Phosphorylation	EPAPPYHSPEDSRDH CCCCCCCCCCCCCCH	24.92	30240740
659	Phosphorylation	PYHSPEDSRDHADKH CCCCCCCCCCHHHHC	37.64	28551015
711	Phosphorylation	SHQRHGTSPVGDHGS HHHHCCCCCCCCCCC	23.37	30411139
781	Phosphorylation	DHEELERSFSGFSIS CHHHHHHHHCCCCHH	17.87	27097102
783	Phosphorylation	EELERSFSGFSISQS HHHHHHHCCCCHHCC	39.93	27097102
786	Phosphorylation	ERSFSGFSISQSKEN HHHHCCCCHHCCHHH	25.51	22673903
835	Phosphorylation	PCGPPPRSATGEGPF CCCCCCCCCCCCCCC	35.64	28432305
837	Phosphorylation	GPPPRSATGEGPFGD CCCCCCCCCCCCCCC	36.69	28432305

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
52	S	Phosphorylation	Kinase	PKA	-	Uniprot
541	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
52	S	Phosphorylation	KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of KCNQ2_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_RAT	Ubc	physical	17322297

Drug and Disease Associations

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