dbPTM

KCNC4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCNC4_HUMAN
UniProt AC	Q03721
Protein Name	Potassium voltage-gated channel subfamily C member 4
Gene Name	KCNC4 {ECO:0000312\|HGNC:HGNC:6236}
Organism	Homo sapiens (Human).
Sequence Length	635
Subcellular Localization	Membrane Multi-pass membrane protein.
Protein Description	This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient..
Protein Sequence	MISSVCVSSYRGRKSGNKPPSKTCLKEEMAKGEASEKIIINVGGTRHETYRSTLRTLPGTRLAWLADPDGGGRPETDGGGVGSSGSSGGGGCEFFFDRHPGVFAYVLNYYRTGKLHCPADVCGPLFEEELTFWGIDETDVEPCCWMTYRQHRDAEEALDIFESPDGGGSGAGPSDEAGDDERELALQRLGPHEGGAGHGAGSGGCRGWQPRMWALFEDPYSSRAARVVAFASLFFILVSITTFCLETHEAFNIDRNVTEILRVGNITSVHFRREVETEPILTYIEGVCVLWFTLEFLVRIVCCPDTLDFVKNLLNIIDFVAILPFYLEVGLSGLSSKAARDVLGFLRVVRFVRILRIFKLTRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYYAERIGARPSDPRGNDHTDFKNIPIGFWWAVVTMTTLGYGDMYPKTWSGMLVGALCALAGVLTIAMPVPVIVNNFGMYYSLAMAKQKLPKKRKKHVPRPAQLESPMYCKSEETSPRDSTCSDTSPPAREEGMIERKRADSKQNGDANAVLSDEEGAGLTQPLASSPTPEERRALRRSTTRDRNKKAAACFLLSTGDYACADGSVRKGTFVLRDLPLQHSPEAACPPTAGTLFLPH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MISSVCVSSYR ----CCCEEEECCCC	14.49	30631047
8	Phosphorylation	MISSVCVSSYRGRKS CCCEEEECCCCCCCC	19.27	9649584
9	Phosphorylation	ISSVCVSSYRGRKSG CCEEEECCCCCCCCC	9.84	9649584
15	Phosphorylation	SSYRGRKSGNKPPSK CCCCCCCCCCCCCCC	46.36	9649584
21	Phosphorylation	KSGNKPPSKTCLKEE CCCCCCCCCHHHHHH	49.47	9649584
49	Phosphorylation	VGGTRHETYRSTLRT ECCCCCHHHHHHHHC	20.36	-
50	Phosphorylation	GGTRHETYRSTLRTL CCCCCHHHHHHHHCC	10.28	-
256	N-linked_Glycosylation	EAFNIDRNVTEILRV HHHCCCCCHHHHEEE	41.12	UniProtKB CARBOHYD
265	N-linked_Glycosylation	TEILRVGNITSVHFR HHHEEECCEEEEEEE	31.35	UniProtKB CARBOHYD
332	Phosphorylation	FYLEVGLSGLSSKAA HHHHHCCCCCCHHHH	31.59	-
504	Phosphorylation	PRPAQLESPMYCKSE CCCHHCCCCCCCCCC	24.45	22210691
513	Phosphorylation	MYCKSEETSPRDSTC CCCCCCCCCCCCCCC	39.72	22210691
514	Phosphorylation	YCKSEETSPRDSTCS CCCCCCCCCCCCCCC	22.63	22210691
567	Phosphorylation	QPLASSPTPEERRAL CCCCCCCCHHHHHHH	45.33	22210691
577	Phosphorylation	ERRALRRSTTRDRNK HHHHHHHHCCCHHHH	27.91	30576142
578	Phosphorylation	RRALRRSTTRDRNKK HHHHHHHCCCHHHHH	24.84	30576142
597	Phosphorylation	FLLSTGDYACADGSV EEHHCCCCCCCCCCC	12.62	-
608 (in isoform 3)	Phosphorylation	-	17.38	24114839
617 (in isoform 3)	Phosphorylation	-	32.83	24114839
626 (in isoform 3)	Phosphorylation	-	34.46	24114839

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
8	S	Phosphorylation	Kinase	KPCA	P17252	PhosphoELM
8	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
8	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
8	S	Phosphorylation	Kinase	PRKCG	P05129	GPS
9	S	Phosphorylation	Kinase	KPCA	P17252	PhosphoELM
9	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
9	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
9	S	Phosphorylation	Kinase	PRKCG	P05129	GPS
15	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
15	S	Phosphorylation	Kinase	PKCA	P05696	PSP
15	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
15	S	Phosphorylation	Kinase	PRKCG	P05129	GPS
21	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
21	S	Phosphorylation	Kinase	PKCA	P05696	PSP
21	S	Phosphorylation	Kinase	PRKCB	P05771	GPS
21	S	Phosphorylation	Kinase	PRKCG	P05129	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCNC4_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 KCNC4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCNC3_HUMAN	KCNC3	physical	28514442
KCNC1_HUMAN	KCNC1	physical	28514442
DNJB5_HUMAN	DNAJB5	physical	28514442
S2551_HUMAN	SLC25A51	physical	28514442
PLD6_HUMAN	PLD6	physical	28514442
NSMA_HUMAN	SMPD2	physical	28514442
DNJB4_HUMAN	DNAJB4	physical	28514442
RHBL4_HUMAN	RHBDD1	physical	28514442
RN215_HUMAN	RNF215	physical	28514442
TYW1_HUMAN	TYW1	physical	28514442
AMFR_HUMAN	AMFR	physical	28514442
ABCBA_HUMAN	ABCB10	physical	28514442
DNJB1_HUMAN	DNAJB1	physical	28514442
PDZD8_HUMAN	PDZD8	physical	28514442
BAG5_HUMAN	BAG5	physical	28514442
NGBR_HUMAN	NUS1	physical	28514442
HERC3_HUMAN	HERC3	physical	28514442
PDE3B_HUMAN	PDE3B	physical	28514442
LEMD2_HUMAN	LEMD2	physical	28514442
ESYT1_HUMAN	ESYT1	physical	28514442
GXLT2_HUMAN	GXYLT2	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442
NPL4_HUMAN	NPLOC4	physical	28514442
BRAF_HUMAN	BRAF	physical	28514442
B3GA3_HUMAN	B3GAT3	physical	28514442
NAT14_HUMAN	NAT14	physical	28514442

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
There are no disease associations of PTM sites.

Regulatory Network of KCNC4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Interactions between multiple phosphorylation sites in theinactivation particle of a K+ channel. Insights into the molecularmechanism of protein kinase C action."; Beck E.J., Sorensen R.G., Slater S.J., Covarrubias M.; J. Gen. Physiol. 112:71-84(1998). Cited for: PHOSPHORYLATION AT SER-8 AND SER-9, AND MUTAGENESIS OF SER-8; SER-9;SER-15 AND SER-21.	9649584 [Abstract]
"Elimination of rapid potassium channel inactivation byphosphorylation of the inactivation gate."; Covarrubias M., Wei A., Salkoff L., Vyas T.B.; Neuron 13:1403-1412(1994). Cited for: PHOSPHORYLATION AT SER-15 AND SER-21, AND MUTAGENESIS OF SER-15 ANDSER-21.	7993631 [Abstract]