KCNB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCNB2_HUMAN
• UniProt AC: Q92953
• Protein Name: Potassium voltage-gated channel subfamily B member 2 {ECO:0000312|HGNC:HGNC:6232}
• Gene Name: KCNB2 {ECO:0000312|HGNC:HGNC:6232}
• Organism: Homo sapiens (Human).
• Sequence Length: 911
• 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: MAEKAPPGLNRKTSRSTLSLPPEPVDIIRSKTCSRRVKINVGGLNHEVLWRTLDRLPRTRLGKLRDCNTHESLLEVCDDYNLNENEYFFDRHPGAFTSILNFYRTGKLHMMEEMCALSFGQELDYWGIDEIYLESCCQARYHQKKEQMNEELRREAETMREREGEEFDNTCCPDKRKKLWDLLEKPNSSVAAKILAIVSILFIVLSTIALSLNTLPELQETDEFGQLNDNRQLAHVEAVCIAWFTMEYLLRFLSSPNKWKFFKGPLNVIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDATKFTSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNLKDAFARSMELIDVAVEKAGESANTKDSADDNHLSPSRWKWARKALSETSSNKSFENKYQEVSQKDSHEQLNNTSSSSPQHLSAQKLEMLYNEITKTQPHSHPNPDCQEKPERPSAYEEEIEMEEVVCPQEQLAVAQTEVIVDMKSTSSIDSFTSCATDFTETERSPLPPPSASHLQMKFPTDLPGTEEHQRARGPPFLTLSREKGPAARDGTLEYAPVDITVNLDASGSQCGLHSPLQSDNATDSPKSSLKGSNPLKSRSLKVNFKENRGSAPQTPPSTARPLPVTTADFSLTTPQHISTILLEETPSQGDRPLLGTEVSAPCQGPSKGLSPRFPKQKLFPFSSRERRSFTEIDTGDDEDFLELPGAREEKQVDSSPNCFADKPSDGRDPLREEGSVGSSSPQDTGHNCRQDIYHAVSEVKKDSSQEGCKMENHLFAPEIHSNPGDTGYCPTRETSM

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
4	Ubiquitination	----MAEKAPPGLNR ----CCCCCCCCCCC	57.57	-
19	Phosphorylation	KTSRSTLSLPPEPVD CCCCCCCCCCCCCCC	38.63	32142685
97	Phosphorylation	DRHPGAFTSILNFYR CCCCCHHHHHHHHHH	17.83	-
103	Phosphorylation	FTSILNFYRTGKLHM HHHHHHHHHHCCCCH	13.24	-
105	Phosphorylation	SILNFYRTGKLHMME HHHHHHHHCCCCHHH	27.56	-
132	Phosphorylation	YWGIDEIYLESCCQA CCCCCHHHHHHHHHH	11.45	12615930
287	N-linked_Glycosylation	TIFLTESNKSVLQFQ EEEECCCCCHHHHHH	34.10	UniProtKB CARBOHYD
327	Phosphorylation	GLQSLGFTLRRSYNE CHHHHCHHHHCCHHH	19.98	24719451
378	Phosphorylation	SFWWATITMTTVGYG HHHEEEEEEEECCCC	12.24	-
384	Phosphorylation	ITMTTVGYGDIYPKT EEEEECCCCCCCCHH	13.80	22817900
388	Phosphorylation	TVGYGDIYPKTLLGK ECCCCCCCCHHHHHH	11.92	-
448	Phosphorylation	ERAKRNGSIVSMNLK HHHHHHCCEEECCHH	24.30	26471730
451	Phosphorylation	KRNGSIVSMNLKDAF HHHCCEEECCHHHHH	10.57	32142685
455	Ubiquitination	SIVSMNLKDAFARSM CEEECCHHHHHHHHH	41.84	32142685
461	Phosphorylation	LKDAFARSMELIDVA HHHHHHHHHHHHHHH	17.12	29449344
479	Ubiquitination	AGESANTKDSADDNH HCCCCCCCCCCCCCC	49.87	32142685
488	Phosphorylation	SADDNHLSPSRWKWA CCCCCCCCHHHHHHH	17.18	29691806
490	Phosphorylation	DDNHLSPSRWKWARK CCCCCCHHHHHHHHH	47.61	29691806
503	Phosphorylation	RKALSETSSNKSFEN HHHHHHCCCCHHHHH	28.06	26471730
504	Phosphorylation	KALSETSSNKSFENK HHHHHCCCCHHHHHH	56.55	26471730
506	Ubiquitination	LSETSSNKSFENKYQ HHHCCCCHHHHHHHH	59.47	32142685
507	Phosphorylation	SETSSNKSFENKYQE HHCCCCHHHHHHHHH	41.88	26471730
511	Ubiquitination	SNKSFENKYQEVSQK CCHHHHHHHHHHHHH	40.90	32142685
527	Phosphorylation	SHEQLNNTSSSSPQH CHHHHHCCCCCCHHH	28.98	22496350
528	Phosphorylation	HEQLNNTSSSSPQHL HHHHHCCCCCCHHHH	30.28	25002506
529	Phosphorylation	EQLNNTSSSSPQHLS HHHHCCCCCCHHHHC	32.56	25002506
530	Phosphorylation	QLNNTSSSSPQHLSA HHHCCCCCCHHHHCH	45.89	25002506
531	Phosphorylation	LNNTSSSSPQHLSAQ HHCCCCCCHHHHCHH	30.44	22496350
536	Phosphorylation	SSSPQHLSAQKLEML CCCHHHHCHHHHHHH	26.91	25002506
544	Phosphorylation	AQKLEMLYNEITKTQ HHHHHHHHHHHHCCC	14.94	29978859
599	Phosphorylation	EVIVDMKSTSSIDSF EEEEECCCCCCCCCC	27.21	26471730
600	Phosphorylation	VIVDMKSTSSIDSFT EEEECCCCCCCCCCC	22.45	26471730
601	Phosphorylation	IVDMKSTSSIDSFTS EEECCCCCCCCCCCC	32.18	26471730
602	Phosphorylation	VDMKSTSSIDSFTSC EECCCCCCCCCCCCC	30.42	26471730
653	Phosphorylation	ARGPPFLTLSREKGP HHCCCCEEEECCCCC	24.06	24719451
705	Ubiquitination	DSPKSSLKGSNPLKS CCCCHHCCCCCCCCC	63.34	29967540
714	Phosphorylation	SNPLKSRSLKVNFKE CCCCCCCEEEEECCC	39.37	-
732	Phosphorylation	SAPQTPPSTARPLPV CCCCCCCCCCCCCCC	35.58	-
733	Phosphorylation	APQTPPSTARPLPVT CCCCCCCCCCCCCCC	32.24	-
803	Phosphorylation	FSSRERRSFTEIDTG CCCCCCCCCEECCCC	42.62	32142685
805	Phosphorylation	SRERRSFTEIDTGDD CCCCCCCEECCCCCC	33.02	24626860
868	Phosphorylation	HNCRQDIYHAVSEVK CCHHHHHHHHHHHHC	7.63	27642862
872	Phosphorylation	QDIYHAVSEVKKDSS HHHHHHHHHHCCCCC	37.14	27642862

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

Oops, there are no upstream regulatory protein records of KCNB2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KCNB2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCNB1_HUMAN	KCNB1	physical	19074135
KCNB2_HUMAN	KCNB2	physical	19074135
KCNG3_HUMAN	KCNG3	physical	19074135
KCNG4_HUMAN	KCNG4	physical	19074135

Drug and Disease Associations

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