KCJ10_HUMAN - dbPTM
KCJ10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCJ10_HUMAN
UniProt AC P78508
Protein Name ATP-sensitive inward rectifier potassium channel 10
Gene Name KCNJ10
Organism Homo sapiens (Human).
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..
Protein Sequence MTSVAKVYYSQTTQTESRPLMGPGIRRRRVLTKDGRSNVRMEHIADKRFLYLKDLWTTFIDMQWRYKLLLFSATFAGTWFLFGVVWYLVAVAHGDLLELDPPANHTPCVVQVHTLTGAFLFSLESQTTIGYGFRYISEECPLAIVLLIAQLVLTTILEIFITGTFLAKIARPKKRAETIRFSQHAVVASHNGKPCLMIRVANMRKSLLIGCQVTGKLLQTHQTKEGENIRLNQVNVTFQVDTASDSPFLILPLTFYHVVDETSPLKDLPLRSGEGDFELVLILSGTVESTSATCQVRTSYLPEEILWGYEFTPAISLSASGKYIADFSLFDQVVKVASPSGLRDSTVRYGDPEKLKLEESLREQAEKEGSALSVRISNV
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 Orthologous
Protein Cluster
6Ubiquitination--MTSVAKVYYSQTT
--CCCEEEEEEEECC
30230243
8PhosphorylationMTSVAKVYYSQTTQT
CCCEEEEEEEECCCC
-
9PhosphorylationTSVAKVYYSQTTQTE
CCEEEEEEEECCCCC
-
32PhosphorylationIRRRRVLTKDGRSNV
CEEEEEECCCCCCCC
-
57PhosphorylationLYLKDLWTTFIDMQW
EEEHHHHHHHHCHHH
26657352
66PhosphorylationFIDMQWRYKLLLFSA
HHCHHHHHHHHHHCC
26657352
154PhosphorylationLIAQLVLTTILEIFI
HHHHHHHHHHHHHHH
22210691
155PhosphorylationIAQLVLTTILEIFIT
HHHHHHHHHHHHHHH
22210691
182PhosphorylationRAETIRFSQHAVVAS
HHCEEEECCCEEEEC
25338102
189PhosphorylationSQHAVVASHNGKPCL
CCCEEEECCCCEEEE
25338102
205UbiquitinationIRVANMRKSLLIGCQ
EEEECCCHHHHEECE
30230243
224UbiquitinationLLQTHQTKEGENIRL
HHHEECCCCCCCEEE
30230243
263PhosphorylationYHVVDETSPLKDLPL
EEECCCCCCCCCCCC
24719451
323PhosphorylationSLSASGKYIADFSLF
EECCCCCEEECHHHC
22210691
335UbiquitinationSLFDQVVKVASPSGL
HHCCEEEECCCCCCC
30230243
338PhosphorylationDQVVKVASPSGLRDS
CEEEECCCCCCCCCC
22210691
340PhosphorylationVVKVASPSGLRDSTV
EEECCCCCCCCCCCC
22210691
345PhosphorylationSPSGLRDSTVRYGDP
CCCCCCCCCCCCCCH
28857561
354UbiquitinationVRYGDPEKLKLEESL
CCCCCHHHCCHHHHH
-
356UbiquitinationYGDPEKLKLEESLRE
CCCHHHCCHHHHHHH
-
367UbiquitinationSLREQAEKEGSALSV
HHHHHHHHHCCCEEE
-

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCJ10_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SIAH1_HUMANSIAH1physical
25416956
HSP7C_HUMANHSPA8physical
26186194
COPB2_HUMANCOPB2physical
26186194
SC24B_HUMANSEC24Bphysical
26186194
COPG1_HUMANCOPG1physical
26186194
SC23B_HUMANSEC23Bphysical
26186194
TTC1_HUMANTTC1physical
26186194
YTHD1_HUMANYTHDF1physical
26186194
TMED8_HUMANTMED8physical
26186194
DYL1_HUMANDYNLL1physical
26186194
SC24A_HUMANSEC24Aphysical
26186194
BAG1_HUMANBAG1physical
26186194
AEDO_HUMANADOphysical
26186194
TMED8_HUMANTMED8physical
28514442
COPG1_HUMANCOPG1physical
28514442
HSP7C_HUMANHSPA8physical
28514442
BAG1_HUMANBAG1physical
28514442
YTHD1_HUMANYTHDF1physical
28514442
AEDO_HUMANADOphysical
28514442
HSP74_HUMANHSPA4physical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCJ10_HUMAN

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Related Literatures of Post-Translational Modification

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