Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0544 Transporter Info
Gene Name	KCNA5
Transporter Name	Voltage-gated potassium channel subunit Kv1.5
Gene ID	3741
UniProt ID	P22460

Post-Translational Modification of This DT
Overview ofKCNA5 Modification Sites with Functional and Structural Information
Sequence	M E I A L V P L E N G G A M T V R G G D E A R A G C G Q A T G G E L Q C P P T A G L S D G P K E P A P K G R G A Q R D A D S G V R P L P P L P D P G V R P L P P L P E E L P R P R R P P P E D E E E E G D P G L G T V E D Q A L G T A S L H H Q R V H I N I S G L R F E T Q L G T L A Q F P N T L L G D P A K R L R Y F D P L R N E Y F F D R N R P S F D G I L Y Y Y Q S G G R L R R P V N V S L D V F A D E I R F Y Q L G D E A M E R F R E D E G F I K E E E K P L P R N E F Q R Q V W L I F E Y P E S S G S A R A I A I V S V L V I L I S I I T F C L E T L P E F R D E R E L L R H P P A P H Q P P A P A P G A N G S G V M A P P S G P T V A P L L P R T L A D P F F I V E T T C V I W F T F E L L V R F F A C P S K A G F S R N I M N I I D V V A I F P Y F I T L G T E L A E Q Q P G G G G G G Q N G Q Q A M S L A I L R V I R L V R V F R I F K L S R H S K G L Q I L G K T L Q A S M R E L G L L I F F L F I G V I L F S S A V Y F A E A D N Q G T H F S S I P D A F W W A V V T M T T V G Y G D M R P I T V G G K I V G S L C A I A G V L T I A L P V P V I V S N F N Y F Y H R E T D H E E P A V L K E E Q G T Q S Q G P G L D R G V Q R K V S G S R G S F C K A G G T L E N A D S A R R G S C P L E K C N V K A K S N V D L R R S L Y A L C L D T S R E T D L
PTM type	X-Acetylation X-Phosphorylation X-Phosphorylation X-S-nitrosylation X-S-palmitoylation X-SUMOylation X: Amino Acid

Acetylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence KCNA5			[1]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	412
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at KCNA5 Lysine 412 has the potential to affect its expression or activity.
Phosphorylation
Serine	11 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence KCNA5			[2]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	62
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 62 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence KCNA5			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	127
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 127 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence KCNA5			[1], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	414
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 414 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence KCNA5			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	417
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 417 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence KCNA5			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	430
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 430 has the potential to affect its expression or activity.
PTM Phenomenon6	.			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	559
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 559 has the potential to affect its expression or activity.
PTM Phenomenon7	.			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	559
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 559 has the potential to affect its expression or activity.
PTM Phenomenon8	.			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	592
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 592 has the potential to affect its expression or activity.
PTM Phenomenon9	.			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	592
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 592 has the potential to affect its expression or activity.
PTM Phenomenon10	.			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	592
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 592 has the potential to affect its expression or activity.
PTM Phenomenon11	.			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	592
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Serine 592 has the potential to affect its expression or activity.
Threonine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence KCNA5			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	15
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Threonine 15 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence KCNA5			[4]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	426
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at KCNA5 Threonine 426 has the potential to affect its expression or activity.
S-nitrosylation
Cystine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence KCNA5			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	331
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation at KCNA5 Cystine 331 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence KCNA5			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	346
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation at KCNA5 Cystine 346 has the potential to affect its expression or activity.
S-palmitoylation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence KCNA5			[10]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	604
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at KCNA5 Cystine 604 has the potential to affect its expression or activity.
SUMOylation
Lysine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Regulating the biophysical properties of the transporter			[11]
Role of PTM	Properties Modulation
Modified Residue	Lysine	Modified Location	221
Related Enzyme	Small ubiquitin-related modifier 3 (SUMO3)
Experimental Method	Co-Immunoprecipitation
Detailed Description	SUMOylation at KCNA5 Lysine 221 have been reported to regulate its biophysical properties, thereby affecting its expression or activity.
PTM Phenomenon2	Regulating the biophysical properties of the transporter			[11]
Role of PTM	Properties Modulation
Modified Residue	Lysine	Modified Location	536
Related Enzyme	Small ubiquitin-related modifier 3 (SUMO3)
Experimental Method	Co-Immunoprecipitation
Detailed Description	SUMOylation at KCNA5 Lysine 536 have been reported to regulate its biophysical properties, thereby affecting its expression or activity.

References
1	Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501.
2	Global detection of protein kinase D-dependent phosphorylation events in nocodazole-treated human cells. Mol Cell Proteomics. 2012 May;11(5):160-70.
3	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.
4	An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas. Cell Rep. 2015 Jun 23;11(11):1834-43.
5	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
6	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
7	A specific N-terminal residue in Kv1.5 is required for upregulation of the channel by SAP97. Biochem Biophys Res Commun. 2006 Mar 31;342(1):1-8.
8	Predict and analyze S-nitrosylation modification sites with the mRMR and IFS approaches. J Proteomics. 2012 Feb 16;75(5):1654-65.
9	Nitric oxide blocks hKv1.5 channels by S-nitrosylation and by a cyclic GMP-dependent mechanism. Cardiovasc Res. 2006 Oct 1;72(1):80-9.
10	Posttranslational modification of voltage-dependent potassium channel Kv1.5: COOH-terminal palmitoylation modulates its biological properties. Am J Physiol Heart Circ Physiol. 2008 May;294(5):H2012-21.
11	SUMO modification regulates inactivation of the voltage-gated potassium channel Kv1.5. Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1805-10.

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Detail Information of Post-Translational Modifications

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