dbPTM

KCNB1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCNB1_RAT
UniProt AC	P15387
Protein Name	Potassium voltage-gated channel subfamily B member 1 {ECO:0000250\|UniProtKB:Q14721}
Gene Name	Kcnb1 {ECO:0000312\|RGD:2954}
Organism	Rattus norvegicus (Rat).
Sequence Length	857
Subcellular Localization	Cell membrane . Perikaryon . Cell projection, dendrite . Cell projection, axon . Cell junction, synapse, postsynaptic cell membrane . Cell junction, synapse . Cell junction, synapse, synaptosome . Membrane Multi-pass membrane protein. Lateral cell membr
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: 10024359]
Protein Sequence	MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLQVCDDYSLEDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGESIAKKDKVQDNHLSPNKWKWTKRALSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYSKMAKTQSQPILNTKEMAPQSKPPEELEMSSMPSPVAPLPARTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLASLSSKAGSSTAPEVGWRGALGASGGRLTETNPIPETSRSGFFVESPRSSMKTNNPLKLRALKVNFVEGDPTPLLPSLGLYHDPLRNRGGAAAAVAGLECASLLDKPVLSPESSIYTTASARTPPRSPEKHTAIAFNFEAGVHHYIDTDTDDEGQLLYSVDSSPPKSLHGSTSPKFSTGARTEKNHFESSPLPTSPKFLRPNCVYSSEGLTGKGPGAQEKCKLENHTPPDVHMLPGGGAHGSTRDQSI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	MTKHGSRSTSSLPPE CCCCCCCCCCCCCCC	34.05	22006306
14	Phosphorylation	KHGSRSTSSLPPEPM CCCCCCCCCCCCCCH	30.99	25403869
15	Phosphorylation	HGSRSTSSLPPEPME CCCCCCCCCCCCCHH	45.01	16917065
128	Phosphorylation	YWGIDEIYLESCCQA CCCCCHHHHHHHHHH	11.45	12615930
253	Acetylation	LRFLSSPKKWKFFKG HHHHHCCCCCCCCCC	73.54	22902405
428	Acetylation	KEQKRQEKAIKRREA HHHHHHHHHHHHHHH	47.26	22902405
444	Phosphorylation	ERAKRNGSIVSMNMK HHHHHHCCEEECCHH	24.30	27097102
447	Phosphorylation	KRNGSIVSMNMKDAF HHHCCEEECCHHHHH	11.63	27097102
457	Phosphorylation	MKDAFARSIEMMDIV HHHHHHHHHHHHHEE	21.33	16917065
474	Sumoylation	KNGESIAKKDKVQDN ECCCCHHCCCCCCCC	60.89	21518833
474	Sumoylation	KNGESIAKKDKVQDN ECCCCHHCCCCCCCC	60.89	-
484	Phosphorylation	KVQDNHLSPNKWKWT CCCCCCCCCCHHHHH	20.90	16917065
496	Phosphorylation	KWTKRALSETSSSKS HHHHHHHHHCCCCCC	37.53	16917065
498	Phosphorylation	TKRALSETSSSKSFE HHHHHHHCCCCCCCC	30.45	22006306
499	Phosphorylation	KRALSETSSSKSFET HHHHHHCCCCCCCCC	28.67	22006306
500	Phosphorylation	RALSETSSSKSFETK HHHHHCCCCCCCCCC	49.56	22006306
501	Phosphorylation	ALSETSSSKSFETKE HHHHCCCCCCCCCCC	31.89	28432305
503	Phosphorylation	SETSSSKSFETKEQG HHCCCCCCCCCCCCC	30.20	16917065
511	Phosphorylation	FETKEQGSPEKARSS CCCCCCCCHHHHHCC	29.58	22006306
517	Phosphorylation	GSPEKARSSSSPQHL CCHHHHHCCCCCCCC	39.16	27097102
518	Phosphorylation	SPEKARSSSSPQHLN CHHHHHCCCCCCCCC	29.31	27097102
519	Phosphorylation	PEKARSSSSPQHLNV HHHHHCCCCCCCCCH	47.48	27097102
520	Phosphorylation	EKARSSSSPQHLNVQ HHHHCCCCCCCCCHH	30.44	27097102
539	Phosphorylation	MYSKMAKTQSQPILN HHHHHHHCCCCCCCC	24.74	27097102
541	Phosphorylation	SKMAKTQSQPILNTK HHHHHCCCCCCCCCC	43.06	16917065
567	Phosphorylation	LEMSSMPSPVAPLPA HCCCCCCCCCCCCCC	24.30	16917065
584	Phosphorylation	EGVIDMRSMSSIDSF CCEECCCCHHHHHHH	19.17	22006306
586	Phosphorylation	VIDMRSMSSIDSFIS EECCCCHHHHHHHHH	25.95	22006306
587	Phosphorylation	IDMRSMSSIDSFISC ECCCCHHHHHHHHHH	23.05	22006306
590	Phosphorylation	RSMSSIDSFISCATD CCHHHHHHHHHHCCC	23.86	16917065
593	Phosphorylation	SSIDSFISCATDFPE HHHHHHHHHCCCCCH	8.83	22006306
605	Phosphorylation	FPEATRFSHSPLASL CCHHHCCCCCCHHHH	21.55	28432305
607	Phosphorylation	EATRFSHSPLASLSS HHHCCCCCCHHHHHC	22.02	16917065
611	Phosphorylation	FSHSPLASLSSKAGS CCCCCHHHHHCCCCC	36.15	22006306
613	Phosphorylation	HSPLASLSSKAGSST CCCHHHHHCCCCCCC	27.57	22006306
618	Phosphorylation	SLSSKAGSSTAPEVG HHHCCCCCCCCCCCC	29.40	22006306
620	Phosphorylation	SSKAGSSTAPEVGWR HCCCCCCCCCCCCCC	48.18	22006306
649	Phosphorylation	PIPETSRSGFFVESP CCCCCCCCCCEEECC	39.45	22006306
655	Phosphorylation	RSGFFVESPRSSMKT CCCCEEECCCHHCCC	21.95	27097102
690	Phosphorylation	LLPSLGLYHDPLRNR CCHHHCCCCCCCCCC	11.46	22106938
719	Phosphorylation	LLDKPVLSPESSIYT HCCCCCCCCCCCCEE	27.19	16917065
732	Phosphorylation	YTTASARTPPRSPEK EECCCCCCCCCCCCC	37.04	25403869
736	Phosphorylation	SARTPPRSPEKHTAI CCCCCCCCCCCCEEE	43.09	25403869
771	Phosphorylation	QLLYSVDSSPPKSLH CEEEEECCCCCCCCC	42.46	16917065
781	Phosphorylation	PKSLHGSTSPKFSTG CCCCCCCCCCCCCCC	54.35	25403869
782	Phosphorylation	KSLHGSTSPKFSTGA CCCCCCCCCCCCCCC	27.99	25403869
798	Phosphorylation	TEKNHFESSPLPTSP CCCCCCCCCCCCCCC	35.99	27097102
799	Phosphorylation	EKNHFESSPLPTSPK CCCCCCCCCCCCCCC	24.21	27097102
803	Phosphorylation	FESSPLPTSPKFLRP CCCCCCCCCCCCCCC	66.40	27097102
804	Phosphorylation	ESSPLPTSPKFLRPN CCCCCCCCCCCCCCC	24.93	16917065
814	Phosphorylation	FLRPNCVYSSEGLTG CCCCCCEEECCCCCC	14.53	22106938
815	Phosphorylation	LRPNCVYSSEGLTGK CCCCCEEECCCCCCC	11.08	22006306
816	Phosphorylation	RPNCVYSSEGLTGKG CCCCEEECCCCCCCC	20.28	22006306
836	Phosphorylation	KCKLENHTPPDVHML HCCCCCCCCCCCCCC	48.36	10719893

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	SRC64	-	PhosphoELM
128	Y	Phosphorylation	Kinase	SRC	Q9WUD9	Uniprot
128	Y	Phosphorylation	Kinase	SRC	P12931	PSP
128	Y	Phosphorylation	Kinase	SRC	P00523	PSP
444	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
444	S	Phosphorylation	Kinase	PRKAA2	P54646	GPS
520	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
520	S	Phosphorylation	Kinase	CDK5	Q03114	Uniprot
541	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
541	S	Phosphorylation	Kinase	PRKAA2	P54646	GPS
607	S	Phosphorylation	Kinase	CDK5	Q03114	Uniprot
607	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
655	S	Phosphorylation	Kinase	CDK5	Q03114	Uniprot
655	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
690	Y	Phosphorylation	Kinase	SRC	P12931	PSP
799	S	Phosphorylation	Kinase	P38A	Q16539	PSP
804	S	Phosphorylation	Kinase	CDK5	Q03114	Uniprot
804	S	Phosphorylation	Kinase	P38A	Q16539	PSP
804	S	Phosphorylation	Kinase	P38A	P70618	PSP
804	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
814	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
15	S	Phosphorylation	16917065
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.
457	S	Phosphorylation	17192433
In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated.
457	S	Phosphorylation	17192433
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.
474	K	Sumoylation	21518833
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	16917065
Phosphorylated on Ser-520, Ser-607, Ser-655 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation.
541	S	Phosphorylation	16917065
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.
567	S	Phosphorylation	17192433
In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated.
567	S	Phosphorylation	17192433
In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced.
567	S	Phosphorylation	17192433
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.
567	S	Phosphorylation	17192433
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.
607	S	Phosphorylation	17192433
In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated.
607	S	Phosphorylation	17192433
The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS).
607	S	Phosphorylation	17192433
Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities.
607	S	Phosphorylation	17192433
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.
607	S	Phosphorylation	17192433
Phosphorylated on Ser-520, Ser-607, Ser-655 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation.
607	S	Phosphorylation	17192433
In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced.
607	S	Phosphorylation	17192433
Dephosphorylated at Ser-607 by protein phosphatase PPP1CA.
607	S	Phosphorylation	17192433
CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity.
655	S	Phosphorylation	16917065
Phosphorylated on Ser-520, Ser-607, Ser-655 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation.
655	S	Phosphorylation	16917065
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.
719	S	Phosphorylation	17192433
In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719 are less dephosphorylated.
719	S	Phosphorylation	17192433
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.
804	S	Phosphorylation	16917065
Phosphorylated on Ser-520, Ser-607, Ser-655 and Ser-804 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation.
804	S	Phosphorylation	16917065
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.

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 KCNB1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUMO2_RAT	Sumo2	physical	21518833
SUMO3_RAT	Sumo3	physical	21518833
SUMO1_RAT	Sumo1	physical	21518833
UBC9_RAT	Ube2i	physical	21518833
STX1A_RAT	Stx1a	physical	22411134

Drug and Disease Associations

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

Regulatory Network of KCNB1_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Proteomic analyses of K(v)2.1 channel phosphorylation sitesdetermining cell background specific differences in function."; Park K.S., Mohapatra D.P., Trimmer J.S.; Channels 1:59-61(2007). Cited for: PHOSPHORYLATION AT SER-15; SER-457; SER-541; SER-607; SER-655;SER-719; SER-799; SER-804 AND THR-836, AND MASS SPECTROMETRY.	18690023 [Abstract]
"Graded regulation of the Kv2.1 potassium channel by variablephosphorylation."; Park K.-S., Mohapatra D.P., Misonou H., Trimmer J.S.; Science 313:976-979(2006). Cited for: PHOSPHORYLATION AT SER-15; SER-457; SER-484; SER-496; SER-503;SER-520; SER-541; SER-567; SER-590; SER-607; SER-655; SER-719;SER-771; SER-799; SER-804 AND THR-836, FUNCTION, MASS SPECTROMETRY,AND MUTAGENESIS OF SER-15; SER-457; SER-484; SER-541; SER-567;SER-607; SER-655; SER-719; SER-771 AND SER-804.	16917065 [Abstract]
"Bidirectional activity-dependent regulation of neuronal ion channelphosphorylation."; Misonou H., Menegola M., Mohapatra D.P., Guy L.K., Park K.-S.,Trimmer J.S.; J. Neurosci. 26:13505-13514(2006). Cited for: PHOSPHORYLATION AT SER-457; SER-567; SER-607 AND SER-719,DEVELOPMENTAL STAGE, AND FUNCTION.	17192433 [Abstract]
"Phosphorylation-dependent regulation of Kv2.1 Channel activity attyrosine 124 by Src and by protein-tyrosine phosphatase epsilon."; Tiran Z., Peretz A., Attali B., Elson A.; J. Biol. Chem. 278:17509-17514(2003). Cited for: PHOSPHORYLATION AT TYR-128, FUNCTION, AND MUTAGENESIS OF TYR-128.	12615930 [Abstract]

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