KCNB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCNB2_MOUSE
• UniProt AC: A6H8H5
• Protein Name: Potassium voltage-gated channel subfamily B member 2 {ECO:0000312|MGI:MGI:99632}
• Gene Name: Kcnb2 {ECO:0000312|MGI:MGI:99632}
• Organism: Mus musculus (Mouse).
• Sequence Length: 907
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein . Perikaryon . Cell projection, dendrite . Localized uniformly throughout cell bodies and dendrites. Colocalizes with KCNB1 to high-density somatodendritic clusters on cortical pyramidal neurons.
• Protein Description: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells..
• Protein Sequence: MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPEKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQENDEFGQPSDNRKLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANTKDSVDDNHLSPSRWKWARKALSETSSNKSYENKYQEVSQNDSHEHLNNTSSSSPQHLSAQKLEMLYNEITKTQPHSHPNPDCQEQPERPCVYEEEIEMEEVICPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGTDEHQRARAPPFLTLSRDKGPAAREAAVDYAPIDITVNLDAGASHGPLQPDSASDSPKSSLKGSNPLKSRSLKVNFQENRASAPQTPPSTARPLPVTTADFPLTTPQHMSTILLEEALPQGQPPLLEADDSAHCQGPSKGFSPRFPKQKLFPFSSRERRSFTEIDTGEDEDFLDLQRSRPDKQADPSPNCLADKPGDARDSLREEGCVGSSSPQNTDHNCRQDIYQAVGEVKKDSSQEGYKMENHLFAPEIHSNPGDTGHCPTRETSM

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
13	Phosphorylation	PPGLNRKTSRSTLSL CCCCCCCCCCCCCCC	26.57	29899451
16	Phosphorylation	LNRKTSRSTLSLPPE CCCCCCCCCCCCCCC	33.20	29899451
17	Phosphorylation	NRKTSRSTLSLPPEP CCCCCCCCCCCCCCC	21.18	29899451
19	Phosphorylation	KTSRSTLSLPPEPVD CCCCCCCCCCCCCCC	38.63	21183079
171	S-palmitoylation	GEEFDNTCCPEKRKK CCCCCCCCCHHHHHH	4.58	28680068
172	S-palmitoylation	EEFDNTCCPEKRKKL CCCCCCCCHHHHHHH	4.61	28680068
287	N-linked_Glycosylation	TIFLTESNKSVLQFQ EEEECCCCCHHHHHH	34.10	-
448	Phosphorylation	ERAKRNGSIVSMNLK HHHHHHCCEEECCHH	24.30	22324799
451	Phosphorylation	KRNGSIVSMNLKDAF HHHCCEEECCHHHHH	10.57	22324799
461	Phosphorylation	LKDAFARSMELIDVA HHHHHHHHHHHHHHH	17.12	29899451
475	Phosphorylation	AVEKAGESANTKDSV HHHHHCCCCCCCCCC	26.38	20415495
478	Phosphorylation	KAGESANTKDSVDDN HHCCCCCCCCCCCCC	35.63	20415495
481	Phosphorylation	ESANTKDSVDDNHLS CCCCCCCCCCCCCCC	29.06	20415495
488	Phosphorylation	SVDDNHLSPSRWKWA CCCCCCCCHHHHHHH	17.18	22324799
490	Phosphorylation	DDNHLSPSRWKWARK CCCCCCHHHHHHHHH	47.61	29899451
500	Phosphorylation	KWARKALSETSSNKS HHHHHHHHHCCCCHH	43.62	20415495
502	Phosphorylation	ARKALSETSSNKSYE HHHHHHHCCCCHHHH	33.79	20415495
503	Phosphorylation	RKALSETSSNKSYEN HHHHHHCCCCHHHHH	28.06	20415495
504	Phosphorylation	KALSETSSNKSYENK HHHHHCCCCHHHHHH	56.55	29899451
507	Phosphorylation	SETSSNKSYENKYQE HHCCCCHHHHHHHHH	41.76	20415495
508	Phosphorylation	ETSSNKSYENKYQEV HCCCCHHHHHHHHHH	25.73	20415495
520	Phosphorylation	QEVSQNDSHEHLNNT HHHHCCCCCHHHCCC	38.02	29899451
527	Phosphorylation	SHEHLNNTSSSSPQH CCHHHCCCCCCCHHH	28.98	29899451
528	Phosphorylation	HEHLNNTSSSSPQHL CHHHCCCCCCCHHHH	30.28	20415495
529	Phosphorylation	EHLNNTSSSSPQHLS HHHCCCCCCCHHHHC	32.56	20415495
530	Phosphorylation	HLNNTSSSSPQHLSA HHCCCCCCCHHHHCH	45.89	20415495
531	Phosphorylation	LNNTSSSSPQHLSAQ HCCCCCCCHHHHCHH	30.44	20415495
599	Phosphorylation	EVIVDMKSTSSIDSF EEEEECCCCCCCCCC	27.21	29899451
600	Phosphorylation	VIVDMKSTSSIDSFT EEEECCCCCCCCCCC	22.45	29899451
601	Phosphorylation	IVDMKSTSSIDSFTS EEECCCCCCCCCCCC	32.18	29899451
602	Phosphorylation	VDMKSTSSIDSFTSC EECCCCCCCCCCCCC	30.42	21183079
605	Phosphorylation	KSTSSIDSFTSCATD CCCCCCCCCCCCCCC	28.84	19060867
640	Phosphorylation	FPTDLPGTDEHQRAR CCCCCCCCCHHHHHH	35.95	29899451
701	Acetylation	DSPKSSLKGSNPLKS CCCCHHCCCCCCCCC	63.34	15614151
799	Phosphorylation	FSSRERRSFTEIDTG CCCCCCCCCEECCCC	42.62	24759943
801	Phosphorylation	SRERRSFTEIDTGED CCCCCCCEECCCCCC	33.02	29899451
805	Phosphorylation	RSFTEIDTGEDEDFL CCCEECCCCCCCCHH	48.40	29899451
849	Phosphorylation	REEGCVGSSSPQNTD HHCCCCCCCCCCCCC	13.77	29899451
850	Phosphorylation	EEGCVGSSSPQNTDH HCCCCCCCCCCCCCC	39.86	25521595
851	Phosphorylation	EGCVGSSSPQNTDHN CCCCCCCCCCCCCCC	32.00	29899451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of KCNB2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KCNB2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of KCNB2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of KCNB2_MOUSE !!

Drug and Disease Associations

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