KCNB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCNB1_MOUSE
• UniProt AC: Q03717
• Protein Name: Potassium voltage-gated channel subfamily B member 1 {ECO:0000250|UniProtKB:Q14721}
• Gene Name: Kcnb1 {ECO:0000312|MGI:MGI:96666}
• Organism: Mus musculus (Mouse).
• Sequence Length: 857
• Subcellular Localization: Cell membrane . Perikaryon . Cell projection, axon . Cell projection, dendrite . Membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane . Cell junction, synapse . Cell junction, synapse, synaptosome . Lateral cell membra
• Protein Description: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain. [PubMed: 14684365]
• Protein Sequence: MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLQVCDDYSLEDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGEGVAKKDKVQDNHLSPNKWKWTKRALSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLQDMYSKMAKTQSQPILNTKEMAPQSQPQEELEMGSMPSPVAPLPTRTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLASLSGKSGGSTAPEVGWRGALGASGGRLMETNPIPEASRSGFFVESPRSSMKTHNPMKLRALKVNFLEGDPTPLLPALGLYHDPLRNRGGAAAAVAGLECASLLDKPVLSPESSIYTTASARTPPRSPEKHTAIAFNFEAGVHQYIDTDTDDEGQLLYSVDSSPPKSLHGSTSPKFSLGARTEKNHFESSPLPTSPKFLRPNCVYASEGLPGKGPGAQEKCKLENHTSPDVHMLPGGGAHGSTRDQSI

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
12	Phosphorylation	MTKHGSRSTSSLPPE CCCCCCCCCCCCCCC	34.05	22817900
13	Phosphorylation	TKHGSRSTSSLPPEP CCCCCCCCCCCCCCC	22.64	25521595
15	Phosphorylation	HGSRSTSSLPPEPME CCCCCCCCCCCCCHH	45.01	25521595
128	Phosphorylation	YWGIDEIYLESCCQA CCCCCHHHHHHHHHH	11.45	-
167	S-palmitoylation	GEEFDNTCCAEKRKK CCCCCCCCHHHHHHH	2.31	28680068
168	S-palmitoylation	EEFDNTCCAEKRKKL CCCCCCCHHHHHHHH	5.29	28680068
444	Phosphorylation	ERAKRNGSIVSMNMK HHHHHHCCEEECCHH	24.30	19060867
447	Phosphorylation	KRNGSIVSMNMKDAF HHHCCEEECCHHHHH	11.63	22817900
451	Ubiquitination	SIVSMNMKDAFARSI CEEECCHHHHHHHHH	40.68	22790023
457	Phosphorylation	MKDAFARSIEMMDIV HHHHHHHHHHHHEEE	21.33	27180971
474	Sumoylation	KNGEGVAKKDKVQDN ECCCCCCCCCCCCCC	60.13	-
484	Phosphorylation	KVQDNHLSPNKWKWT CCCCCCCCCCHHHHH	20.90	25521595
487	Ubiquitination	DNHLSPNKWKWTKRA CCCCCCCHHHHHHHH	54.24	-
491	Phosphorylation	SPNKWKWTKRALSET CCCHHHHHHHHHHHC	13.61	-
492	Ubiquitination	PNKWKWTKRALSETS CCHHHHHHHHHHHCC	34.26	-
496	Phosphorylation	KWTKRALSETSSSKS HHHHHHHHHCCCCCC	37.53	27841257
503	Phosphorylation	SETSSSKSFETKEQG HHCCCCCCCCCCCCC	30.20	-
517	Phosphorylation	GSPEKARSSSSPQHL CCHHHHHCCCCCCCC	39.16	22324799
518	Phosphorylation	SPEKARSSSSPQHLN CHHHHHCCCCCCCCC	29.31	22324799
519	Phosphorylation	PEKARSSSSPQHLNV HHHHHCCCCCCCCCH	47.48	25521595
520	Phosphorylation	EKARSSSSPQHLNVQ HHHHCCCCCCCCCHH	30.44	25521595
533	Phosphorylation	VQQLQDMYSKMAKTQ HHHHHHHHHHHHHCC	17.27	29899451
539	Phosphorylation	MYSKMAKTQSQPILN HHHHHHHCCCCCCCC	24.74	22324799
541	Phosphorylation	SKMAKTQSQPILNTK HHHHHCCCCCCCCHH	43.06	22324799
547	Phosphorylation	QSQPILNTKEMAPQS CCCCCCCHHHCCCCC	25.57	22324799
554	Phosphorylation	TKEMAPQSQPQEELE HHHCCCCCCCHHHHH	42.65	29899451
564	Phosphorylation	QEELEMGSMPSPVAP HHHHHCCCCCCCCCC	26.64	21183079
567	Phosphorylation	LEMGSMPSPVAPLPT HHCCCCCCCCCCCCC	24.30	22817900
574	Phosphorylation	SPVAPLPTRTEGVID CCCCCCCCCCCCEEC	58.88	20415495
586	Phosphorylation	VIDMRSMSSIDSFIS EECCHHHHHHHHHHH	25.95	29899451
587	Phosphorylation	IDMRSMSSIDSFISC ECCHHHHHHHHHHHH	23.05	29899451
590	Phosphorylation	RSMSSIDSFISCATD HHHHHHHHHHHHCCC	23.86	-
593	Phosphorylation	SSIDSFISCATDFPE HHHHHHHHHCCCCCH	8.83	29899451
605	Phosphorylation	FPEATRFSHSPLASL CCHHHCCCCCCCHHH	21.55	28066266
607	Phosphorylation	EATRFSHSPLASLSG HHHCCCCCCCHHHCC	22.02	22817900
611	Phosphorylation	FSHSPLASLSGKSGG CCCCCCHHHCCCCCC	30.65	29899451
613	Phosphorylation	HSPLASLSGKSGGST CCCCHHHCCCCCCCC	41.50	29899451
647	Phosphorylation	TNPIPEASRSGFFVE CCCCCHHHHCCCEEE	25.89	29514104
655	Phosphorylation	RSGFFVESPRSSMKT HCCCEEECCCHHCCC	21.95	21082442
658	Phosphorylation	FFVESPRSSMKTHNP CEEECCCHHCCCCCC	37.86	29899451
719	Phosphorylation	LLDKPVLSPESSIYT HCCCCCCCCCCCCEE	27.19	-
722	Phosphorylation	KPVLSPESSIYTTAS CCCCCCCCCCEECCC	25.97	29899451
723	Phosphorylation	PVLSPESSIYTTASA CCCCCCCCCEECCCC	20.25	29899451
727	Phosphorylation	PESSIYTTASARTPP CCCCCEECCCCCCCC	11.14	29899451
732	Phosphorylation	YTTASARTPPRSPEK EECCCCCCCCCCCCC	37.04	29899451
736	Phosphorylation	SARTPPRSPEKHTAI CCCCCCCCCCCCEEE	43.09	23384938
771	Phosphorylation	QLLYSVDSSPPKSLH CEEEEECCCCCCCCC	42.46	-
776	Phosphorylation	VDSSPPKSLHGSTSP ECCCCCCCCCCCCCC	31.22	20415495
780	Phosphorylation	PPKSLHGSTSPKFSL CCCCCCCCCCCCCCC	18.24	20415495
781	Phosphorylation	PKSLHGSTSPKFSLG CCCCCCCCCCCCCCC	54.35	20415495
782	Phosphorylation	KSLHGSTSPKFSLGA CCCCCCCCCCCCCCC	27.99	20415495
798	Phosphorylation	TEKNHFESSPLPTSP CCCCCCCCCCCCCCC	35.99	28066266
799	Phosphorylation	EKNHFESSPLPTSPK CCCCCCCCCCCCCCC	24.21	28066266
803	Phosphorylation	FESSPLPTSPKFLRP CCCCCCCCCCCCCCC	66.40	25521595
804	Phosphorylation	ESSPLPTSPKFLRPN CCCCCCCCCCCCCCC	24.93	25521595
836	Phosphorylation	KCKLENHTSPDVHML HHCCCCCCCCCCCCC	54.24	-

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
128	Y	Phosphorylation	Kinase	SRC	P05480	Uniprot
520	S	Phosphorylation	Kinase	CDK5	P49615	Uniprot
607	S	Phosphorylation	Kinase	CDK5	P49615	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
15	S	Phosphorylation	Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties.	10921884
457	S	Phosphorylation	In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated.	21183079
457	S	Phosphorylation	Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties.	21183079
474	K	Sumoylation	Sumoylated on Lys-474, preferentially with SUMO1; sumoylation induces a positive shift in the voltage-dependence of activation and inhibits channel activity.	-
520	S	Phosphorylation	Phosphorylated on Ser-520, Ser-655, Ser-607 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation.	10921884
541	S	Phosphorylation	Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties.	10921884
567	S	Phosphorylation	In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated.	10921884
567	S	Phosphorylation	In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced (By similarity).	10921884
567	S	Phosphorylation	Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties.	10921884
567	S	Phosphorylation	Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5; levels then increase to reach adult levels by P14.	10921884
607	S	Phosphorylation	In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated.	10921884
607	S	Phosphorylation	The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS).	10921884
607	S	Phosphorylation	Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities.	10921884
607	S	Phosphorylation	Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties.	10921884
607	S	Phosphorylation	Phosphorylated on Ser-520, Ser-655, Ser-607 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation.	10921884
607	S	Phosphorylation	In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced (By similarity).	10921884
607	S	Phosphorylation	Dephosphorylated at Ser-607 by protein phosphatase PPP1CA.	10921884
607	S	Phosphorylation	CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity.	10921884
655	S	Phosphorylation	Phosphorylated on Ser-520, Ser-655, Ser-607 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation.	16452087
655	S	Phosphorylation	Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties.	16452087
719	S	Phosphorylation	In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated.	10921884
719	S	Phosphorylation	Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-719 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties.	10921884
804	S	Phosphorylation	Phosphorylated on Ser-520, Ser-655, Ser-607 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation.	21183079
804	S	Phosphorylation	Phosphorylated on Tyr-128 by Src and on Ser-804 by MAPK14/P38MAPK; phosphorylations are necessary and sufficient for an increase in plasma membrane insertion, apoptotic potassium current surge and completion of the neuronal cell death program.	21183079

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of KCNB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCNA2_MOUSE	Kcna2	physical	16008572
KCND2_MOUSE	Kcnd2	physical	16008572
HS71B_MOUSE	Hspa1b	physical	16008572

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-12 AND SER-655, AND MASSSPECTROMETRY.
PubMed: 17114649

"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND MASSSPECTROMETRY.
PubMed: 16452087