dbPTM

KCJ10_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCJ10_MOUSE
UniProt AC	Q9JM63
Protein Name	ATP-sensitive inward rectifier potassium channel 10
Gene Name	Kcnj10
Organism	Mus musculus (Mouse).
Sequence Length	379
Subcellular Localization	Membrane Multi-pass membrane protein . Basolateral cell membrane . In kidney distal convoluted tubules, located in the basolateral membrane where it colocalizes with KCNJ16.
Protein Description	May be responsible for potassium buffering action of glial cells in the brain. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules (By similarity)..
Protein Sequence	MTSVAKVYYSQTTQTESRPLVAPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELGPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	Reference
6	Ubiquitination	--MTSVAKVYYSQTT --CCCEEEEEEEECC	-
8	Phosphorylation	MTSVAKVYYSQTTQT CCCEEEEEEEECCCC	29899451
17	Phosphorylation	SQTTQTESRPLVAPG EECCCCCCCCCCCCC	29899451
206	Phosphorylation	RVANMRKSLLIGCQV EEECCCHHHHEECEE	25521595
224	Ubiquitination	LLQTHQTKEGENIRL HHHEECCCCCCCEEE	-
335	Ubiquitination	SLFDQVVKVASPSGL HHCCEEEECCCCCCC	-
338	Phosphorylation	DQVVKVASPSGLRDS CEEEECCCCCCCCCC	25521595
340	Phosphorylation	VVKVASPSGLRDSTV EEECCCCCCCCCCCC	29899451
345	Phosphorylation	SPSGLRDSTVRYGDP CCCCCCCCCCCCCCH	25521595
346	Phosphorylation	PSGLRDSTVRYGDPE CCCCCCCCCCCCCHH	25521595
354	Ubiquitination	VRYGDPEKLKLEESL CCCCCHHHCCHHHHH	-
356	Ubiquitination	YGDPEKLKLEESLRE CCCHHHCCHHHHHHH	-
367	Ubiquitination	SLREQAEKEGSALSV HHHHHHHHHCCCEEE	-
370	Phosphorylation	EQAEKEGSALSVRIS HHHHHHCCCEEEEEE	22324799
373	Phosphorylation	EKEGSALSVRISNV- HHHCCCEEEEEECC-	22324799
377	Phosphorylation	SALSVRISNV----- CCEEEEEECC-----	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
Oops, there are no upstream regulatory protein records of KCJ10_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KCJ10_MOUSE !!

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 KCJ10_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
IL16_MOUSE	Il16	physical	10479680

Drug and Disease Associations

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

Regulatory Network of KCJ10_MOUSE

Related Literatures of Post-Translational Modification