dbPTM

KCND2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCND2_MOUSE
UniProt AC	Q9Z0V2
Protein Name	Potassium voltage-gated channel subfamily D member 2
Gene Name	Kcnd2
Organism	Mus musculus (Mouse).
Sequence Length	630
Subcellular Localization	Cell membrane Multi-pass membrane protein . Cell projection, dendrite . Cell junction, synapse . Perikaryon . Cell junction, synapse, postsynaptic cell membrane . Cell projection, dendritic spine . Cell junction . Membrane, caveola . Cell membrane, sarc
Protein Description	Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in rodent heart. Mediates the major part of the dendritic A-type current I(SA) in brain neurons. [PubMed: 10818150]
Protein Sequence	MAAGVAAWLPFARAAAIGWMPVASGPMPAPPRQERKRTQDALIVLNVSGTRFQTWQDTLERYPDTLLGSSERDFFYHPETQQYFFDRDPDIFRHILNFYRTGKLHYPRHECISAYDEELAFFGLIPEIIGDCCYEEYKDRRRENAERLQDDADTDNTGESALPTMTARQRVWRAFENPHTSTMALVFYYVTGFFIAVSVIANVVETVPCGSSPGHIKELPCGERYAVAFFCLDTACVMIFTVEYLLRLAAAPSRYRFVRSVMSIIDVVAILPYYIGLVMTDNEDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSCASELGFLLFSLTMAIIIFATVMFYAEKGSSASKFTSIPAAFWYTIVTMTTLGYGDMVPKTIAGKIFGSICSLSGVLVIALPVPVIVSNFSRIYHQNQRADKRRAQKKARLARIRAAKSGSANAYMQSKRNGLLSNQLQSSEDEPAFISKSGSSFETQHHHLLHCLEKTTNHEFVDEQVFEESCMEVATVNRPSSHSPSLSSQQGVTSTCCSRRHKKTFRIPNANVSGSHRGSVQELSTIQIRCVERTPLSNSRSSLNAKMEECVKLNCEQPYVTTAIISIPTPPVTTPEGDDRPESPEYSGGNIVRVSAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Phosphorylation	PRQERKRTQDALIVL CHHHCCCCCCEEEEE	33.56	10681507
154	Phosphorylation	RLQDDADTDNTGESA HHHCCCCCCCCCCCC	32.63	22817900
157	Phosphorylation	DDADTDNTGESALPT CCCCCCCCCCCCCHH	45.17	22807455
253	Phosphorylation	LRLAAAPSRYRFVRS HHHHHCCHHHHHHHH	36.90	25619855
255	Phosphorylation	LAAAPSRYRFVRSVM HHHCCHHHHHHHHHH	16.85	25619855
315	Phosphorylation	QGLRILGYTLKSCAS CCCHHHCHHHHHHHH	12.88	22817900
316	Phosphorylation	GLRILGYTLKSCASE CCHHHCHHHHHHHHH	26.38	22817900
437	Ubiquitination	LARIRAAKSGSANAY HHHHHHHHCCCHHHH	55.13	27667366
438	Phosphorylation	ARIRAAKSGSANAYM HHHHHHHCCCHHHHH	33.00	30635358
440	Phosphorylation	IRAAKSGSANAYMQS HHHHHCCCHHHHHHH	25.99	30635358
444	Phosphorylation	KSGSANAYMQSKRNG HCCCHHHHHHHHHCC	8.76	30635358
447	Phosphorylation	SANAYMQSKRNGLLS CHHHHHHHHHCCCCH	19.63	30635358
448	Ubiquitination	ANAYMQSKRNGLLSN HHHHHHHHHCCCCHH	32.75	27667366
459	Phosphorylation	LLSNQLQSSEDEPAF CCHHCCCCCCCCCCE	44.26	29899451
460	Phosphorylation	LSNQLQSSEDEPAFI CHHCCCCCCCCCCEE	35.79	25521595
473	Phosphorylation	FISKSGSSFETQHHH EECCCCCCCHHHHHH	30.54	22817900
520	Phosphorylation	SSHSPSLSSQQGVTS CCCCCCCCCCCCCCC	30.36	-
521	Phosphorylation	SHSPSLSSQQGVTST CCCCCCCCCCCCCCC	31.64	-
546	Phosphorylation	RIPNANVSGSHRGSV ECCCCCCCCCCCCCH	34.09	22817900
548	Phosphorylation	PNANVSGSHRGSVQE CCCCCCCCCCCCHHE	11.51	25521595
552	Phosphorylation	VSGSHRGSVQELSTI CCCCCCCCHHEEEEE	22.15	25521595
557	Phosphorylation	RGSVQELSTIQIRCV CCCHHEEEEEEEEEE	23.78	29899451
567	Phosphorylation	QIRCVERTPLSNSRS EEEEEECCCCCCCCH	18.31	23737553
570	Phosphorylation	CVERTPLSNSRSSLN EEECCCCCCCCHHHH	33.68	22324799
572	Phosphorylation	ERTPLSNSRSSLNAK ECCCCCCCCHHHHHC	30.11	25521595
574	Phosphorylation	TPLSNSRSSLNAKME CCCCCCCHHHHHCHH	38.71	22324799
575	Phosphorylation	PLSNSRSSLNAKMEE CCCCCCHHHHHCHHH	25.24	25521595
588	S-palmitoylation	EECVKLNCEQPYVTT HHHHHCCCCCCCEEE	8.13	28680068
602	Phosphorylation	TAIISIPTPPVTTPE EEEEEECCCCCCCCC	38.26	18045912
606	Phosphorylation	SIPTPPVTTPEGDDR EECCCCCCCCCCCCC	42.27	21183079
607	Phosphorylation	IPTPPVTTPEGDDRP ECCCCCCCCCCCCCC	21.41	18045912
616	Phosphorylation	EGDDRPESPEYSGGN CCCCCCCCCCCCCCC	26.22	18045912
619	Phosphorylation	DRPESPEYSGGNIVR CCCCCCCCCCCCEEE	18.92	29899451
620	Phosphorylation	RPESPEYSGGNIVRV CCCCCCCCCCCEEEE	38.26	21183079

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
38	T	Phosphorylation	Kinase	PRKACA	P05132	GPS
552	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
602	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
607	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
616	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
616	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
616	S	Phosphorylation	Kinase	ERK2	P63085	PSP
616	S	Phosphorylation	Kinase	MAPK3	Q63844	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
438	S	Phosphorylation	18045912
Phosphorylation at Ser-438 in response to MAPK activation is increased in stimulated dendrites.
552	S	Phosphorylation	21183079
Interaction with KCNIP2 and DPP6 propomtes phosphorylation by PKA at Ser-552.
552	S	Phosphorylation	21183079
Phosphorylation at Ser-552 has no effect on interaction with KCNIP3, but is required for the regulation of channel activity by KCNIP3.
552	S	Phosphorylation	21183079
Phosphorylation at Ser-552 leads to KCND2 internalization (By similarity).
616	S	Phosphorylation	18045912
Phosphorylation at Ser-616 is required for the down-regulation of neuronal A-type currents in response to signaling via GRM5.

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 KCND2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KCND2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of KCND2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-548, AND MASSSPECTROMETRY.	17114649 [Abstract]

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