KCNRG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCNRG_HUMAN
• UniProt AC: Q8N5I3
• Protein Name: Potassium channel regulatory protein
• Gene Name: KCNRG
• Organism: Homo sapiens (Human).
• Sequence Length: 272
• Subcellular Localization: Endoplasmic reticulum .
• Protein Description: Inhibits potassium fluxes in cells. May regulate Kv1 family channel proteins by retaining a fraction of channels in endomembranes..
• Protein Sequence: MSSQELVTLNVGGKIFTTRFSTIKQFPASRLARMLDGRDQEFKMVGGQIFVDRDGDLFSFILDFLRTHQLLLPTEFSDYLRLQREALFYELRSLVDLLNPYLLQPRPALVEVHFLSRNTQAFFRVFGSCSKTIEMLTGRITVFTEQPSAPTWNGNFFPPQMTLLPLPPQRPSYHDLVFQCGSDSTTDNQTGVRYVSIKPDNRKLANGTNVLGLLIDTLLKEGFHLVSTRTVSSEDKTECYSFERIKSPEVLITNETPKPETIIIPEQSQIKK

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
22	Phosphorylation	IFTTRFSTIKQFPAS EEEECHHHHHHCCHH	29.49	-
29	Phosphorylation	TIKQFPASRLARMLD HHHHCCHHHHHHHHC	28.23	22817900
208	Phosphorylation	NRKLANGTNVLGLLI CCCCCCCCCHHHHHH	23.20	19413330
211 (in isoform 2)	Phosphorylation	-	4.31	27251275
212 (in isoform 2)	Phosphorylation	-	17.72	27251275
214 (in isoform 2)	Phosphorylation	-	2.94	27251275
217 (in isoform 2)	Phosphorylation	-	27.31	27251275
219 (in isoform 2)	Phosphorylation	-	5.29	27251275
225 (in isoform 2)	Phosphorylation	-	2.80	27251275

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KCNRG_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 KCNRG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KCNRG_HUMAN	KCNRG	physical	16189514
KCNRG_HUMAN	KCNRG	physical	19968958
KCNRG_HUMAN	KCNRG	physical	19447967
KCNRG_HUMAN	KCNRG	physical	25416956

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208, AND MASSSPECTROMETRY.
PubMed: 19413330