Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0513 Transporter Info
Gene Name	KCNQ1
Transporter Name	Voltage-gated potassium channel Kv7.1
Gene ID	3784
UniProt ID	P51787

Post-Translational Modification of This DT
Overview ofKCNQ1 Modification Sites with Functional and Structural Information
Sequence	M A A A S S P P R A E R K R W G W G R L P G A R R G S A G L A K K C P F S L E L A E G G P A G G A L Y A P I A P G A P G P A P P A S P A A P A A P P V A S D L G P R P P V S L D P R V S I Y S T R R P V L A R T H V Q G R V Y N F L E R P T G W K C F V Y H F A V F L I V L V C L I F S V L S T I E Q Y A A L A T G T L F W M E I V L V V F F G T E Y V V R L W S A G C R S K Y V G L W G R L R F A R K P I S I I D L I V V V A S M V V L C V G S K G Q V F A T S A I R G I R F L Q I L R M L H V D R Q G G T W R L L G S V V F I H R Q E L I T T L Y I G F L G L I F S S Y F V Y L A E K D A V N E S G R V E F G S Y A D A L W W G V V T V T T I G Y G D K V P Q T W V G K T I A S C F S V F A I S F F A L P A G I L G S G F A L K V Q Q K Q R Q K H F N R Q I P A A A S L I Q T A W R C Y A A E N P D S S T W K I Y I R K A P R S H T L L S P S P K P K K S V V V K K K K F K L D K D N G V T P G E K M L T V P H I T C D P P E E R R L D H F S V D G Y D S S V R K S P T L L E V S M P H F M R T N S F A E D L D L E G E T L L T P I T H I S Q L R E H H R A T I K V I R R M Q Y F V A K K K F Q Q A R K P Y D V R D V I E Q Y S Q G H L N L M V R I K E L Q R R L D Q S I G K P S L F I S V S E K S K D R G S N T I G A R L N R V E D K V T Q L D Q R L A L I T D M L H Q L L S L H G G S T P G S G G P P R E G G A H I T Q P C G S G G S V D P E L F L P S N T L P T Y E Q L T V P R R G P D E G S
PTM type	X-N-glycosylation X-Phosphorylation X-Phosphorylation X-S-nitrosylation X-Ubiquitination X-Ubiquitination X: Amino Acid

N-glycosylation
Asparagine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence KCNQ1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	289
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at KCNQ1 Asparagine 289 has the potential to affect its expression or activity.
Phosphorylation
Serine	18 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Enhancing the activity of KCNQ1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Serine	Modified Location	27
Related Enzyme	cAMP-dependent protein kinase catalytic subunit alpha (PRKACA)
Experimental Material(s)	Chinese hamster ovary (CHO) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 27 have been reported to enhance its transport activity.
PTM Phenomenon2	Have the potential to influence KCNQ1			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	5
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 5 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence KCNQ1			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	6
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 6 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence KCNQ1			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	92
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 92 has the potential to affect its expression or activity.
PTM Phenomenon5	.			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	95
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 95 has the potential to affect its expression or activity.
PTM Phenomenon6	.			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	95
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 95 has the potential to affect its expression or activity.
PTM Phenomenon7	.			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	95
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 95 has the potential to affect its expression or activity.
PTM Phenomenon8	.			[7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	199
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 199 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence KCNQ1			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	402
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 402 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence KCNQ1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	407
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 407 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence KCNQ1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	409
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 409 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence KCNQ1			[11], [12]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	457
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 457 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence KCNQ1			[12]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	463
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 463 has the potential to affect its expression or activity.
PTM Phenomenon14	Have the potential to influence KCNQ1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	464
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 464 has the potential to affect its expression or activity.
PTM Phenomenon15	Have the potential to influence KCNQ1			[11], [14]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	468
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 468 has the potential to affect its expression or activity.
PTM Phenomenon16	Have the potential to influence KCNQ1			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	475
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 475 has the potential to affect its expression or activity.
PTM Phenomenon17	Have the potential to influence KCNQ1			[4], [15]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	484
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 484 has the potential to affect its expression or activity.
PTM Phenomenon18	Have the potential to influence KCNQ1			[13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	577
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Serine 577 has the potential to affect its expression or activity.
Threonine	11 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	96
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 96 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	96
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 96 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	96
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 96 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence KCNQ1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	404
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 404 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence KCNQ1			[12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	439
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 439 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence KCNQ1			[12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	444
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 444 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence KCNQ1			[8], [13]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	470
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 470 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence KCNQ1			[11], [15]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	482
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 482 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence KCNQ1			[13]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	513
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 513 has the potential to affect its expression or activity.
PTM Phenomenon10	.			[7]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	610
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 610 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence KCNQ1			[16]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	666
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Threonine 666 has the potential to affect its expression or activity.
Tyrosine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence KCNQ1			[5], [8]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	94
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Tyrosine 94 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence KCNQ1			[13], [17]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	184
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Tyrosine 184 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[7]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	267
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Tyrosine 267 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence KCNQ1			[12]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	461
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNQ1 Tyrosine 461 has the potential to affect its expression or activity.
S-nitrosylation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence KCNQ1			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	445
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation at KCNQ1 Cystine 445 has the potential to affect its expression or activity.
Ubiquitination
Lysine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[7]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	579
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at KCNQ1 Lysine 579 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[7]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	598
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at KCNQ1 Lysine 598 has the potential to affect its expression or activity.
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Decreasing the activity of KCNQ1			[20]
Role of PTM	Protein Activity Modulation
Affected Drug/Substrate	Potassium	Results for Drug	Affecting the inward transport of potassium
Related Enzyme	E3 ubiquitin-protein ligase NEDD4-like (NEDD4L)
Experimental Material(s)	Cardiomyocytes and Renal epithelial cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at KCNQ1 have been reported to decrease its transport activity.

References
1	dbPTM in 2022: an updated database for exploring regulatory networks and functional associations of protein post-translational modifications. Nucleic Acids Res. 2022 Jan 7;50(D1):D471-D479. (ID: KCNQ1_HUMAN)
2	Requirement of a macromolecular signaling complex for beta adrenergic receptor modulation of the KCNQ1-KCNE1 potassium channel. Science. 2002 Jan 18;295(5554):496-9.
3	Citric acid-assisted two-step enrichment with TiO2 enhances the separation of multi- and monophosphorylated peptides and increases phosphoprotein profiling. J Proteome Res. 2013 Jun 7;12(6):2467-76.
4	Biologic Response of Colorectal Cancer Xenograft Tumors to Sequential Treatment with Panitumumab and Bevacizumab. Neoplasia. 2018 Jul;20(7):668-677.
5	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
6	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
7	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
8	Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res. 2013 Jun 7;12(6):2414-21.
9	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
10	An integrated strategy for highly sensitive phosphoproteome analysis from low micrograms of protein samples. Analyst. 2018 Jul 23;143(15):3693-3701.
11	Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
12	Characterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics. Mol Cell Proteomics. 2013 Dec;12(12):3851-73.
13	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
14	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
15	Phosphoproteome Analysis Reveals Differential Mode of Action of Sorafenib in Wildtype and Mutated FLT3 Acute Myeloid Leukemia (AML) Cells. Mol Cell Proteomics. 2017 Jul;16(7):1365-1376.
16	Ischemia in tumors induces early and sustained phosphorylation changes in stress kinase pathways but does not affect global protein levels. Mol Cell Proteomics. 2014 Jul;13(7):1690-704.
17	Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203.
18	Predict and analyze S-nitrosylation modification sites with the mRMR and IFS approaches. J Proteomics. 2012 Feb 16;75(5):1654-65.
19	Redox- and calmodulin-dependent S-nitrosylation of the KCNQ1 channel. J Biol Chem. 2009 Feb 27;284(9):6014-20.
20	O-glycosylation of the cardiac I(Ks) complex. J Physiol. 2011 Aug 1;589(Pt 15):3721-30.

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Detail Information of Post-Translational Modifications

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