Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID DTD0517 Transporter Info
Gene Name ATP5E
Transporter Name ATP synthase subunit epsilon
Gene ID
514
UniProt ID
P56381
Post-Translational Modification of This DT
Overview ofATP5E Modification Sites with Functional and Structural Information
Sequence
PTM type
X-Acetylation X-Malonylation X-Oxidation X-Phosphorylation X-S-nitrosylation X-S-sulfhydration X-Succinylation X-Ubiquitination X: Amino Acid

Acetylation

  Lysine

           5 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5E [1]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 21

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Acetylation at ATP5E Lysine 21 has the potential to affect its expression or activity.

  PTM Phenomenon2

 Have the potential to influence ATP5E [2]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 28

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Acetylation at ATP5E Lysine 28 has the potential to affect its expression or activity.

  PTM Phenomenon3

 Have the potential to influence ATP5E [2]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 32

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Acetylation at ATP5E Lysine 32 has the potential to affect its expression or activity.

  PTM Phenomenon4

 Have the potential to influence ATP5E [2]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 37

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Acetylation at ATP5E Lysine 37 has the potential to affect its expression or activity.

  PTM Phenomenon5

 Have the potential to influence ATP5E [3]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 44

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Acetylation at ATP5E Lysine 44 has the potential to affect its expression or activity.

Malonylation

  Lysine

           1 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5E [4]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 21

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Malonylation at ATP5E Lysine 21 has the potential to affect its expression or activity.

Oxidation

  Cystine

           1 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5F1E [5]

Role of PTM

 Potential impacts

Modified Residue

 Cystine

Modified Location

 19

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Oxidation at ATP5F1E Cystine 19 has the potential to affect its expression or activity.

Phosphorylation

  Serine

           2 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5E [6]

Role of PTM

 Potential impacts

Modified Residue

 Serine

Modified Location

 11

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Phosphorylation at ATP5E Serine 11 has the potential to affect its expression or activity.

  PTM Phenomenon2

 Have the potential to influence ATP5E [6]

Role of PTM

 Potential impacts

Modified Residue

 Serine

Modified Location

 16

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Phosphorylation at ATP5E Serine 16 has the potential to affect its expression or activity.

  Threonine

           1 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5E [7], [8]

Role of PTM

 Potential impacts

Modified Residue

 Threonine

Modified Location

 29

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Phosphorylation at ATP5E Threonine 29 has the potential to affect its expression or activity.

  Tyrosine

           2 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5E [6]

Role of PTM

 Potential impacts

Modified Residue

 Tyrosine

Modified Location

 12

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Phosphorylation at ATP5E Tyrosine 12 has the potential to affect its expression or activity.

  PTM Phenomenon2

 Have the potential to influence ATP5E [6]

Role of PTM

 Potential impacts

Modified Residue

 Tyrosine

Modified Location

 15

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Phosphorylation at ATP5E Tyrosine 15 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 ATP5F1E [9]

Role of PTM

 Potential impacts

Modified Residue

 Cystine

Modified Location

 19

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 S-nitrosylation (-SNO) at ATP5F1E Cystine 19 has the potential to affect its expression or activity.

S-sulfhydration

  Cystine

           1 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5F1E [10]

Role of PTM

 Potential impacts

Modified Residue

 Cystine

Modified Location

 19

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 S-sulfhydration (-SSH) at ATP5F1E Cystine 19 has the potential to affect its expression or activity.

Succinylation

  Lysine

           3 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5E [11]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 28

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Succinylation at ATP5E Lysine 28 has the potential to affect its expression or activity.

  PTM Phenomenon2

 Have the potential to influence ATP5E [11], [12]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 32

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Succinylation at ATP5E Lysine 32 has the potential to affect its expression or activity.

  PTM Phenomenon3

 Have the potential to influence ATP5E [11]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 44

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Succinylation at ATP5E Lysine 44 has the potential to affect its expression or activity.

Ubiquitination

  Lysine

           3 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

 Have the potential to influence ATP5E [13], [14]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 21

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Ubiquitination at ATP5E Lysine 21 has the potential to affect its expression or activity.

  PTM Phenomenon2

 Have the potential to influence ATP5E [15]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 28

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Ubiquitination at ATP5E Lysine 28 has the potential to affect its expression or activity.

  PTM Phenomenon3

 Have the potential to influence ATP5E [15]

Role of PTM

 Potential impacts

Modified Residue

 Lysine

Modified Location

 44

Experimental Method

 Co-Immunoprecipitation

Detailed Description

 Ubiquitination at ATP5E Lysine 44 has the potential to affect its expression or activity.
References
1 Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40.
2 Deep, Quantitative Coverage of the Lysine Acetylome Using Novel Anti-acetyl-lysine Antibodies and an Optimized Proteomic Workflow. Mol Cell Proteomics. 2015 Sep;14(9):2429-40.
3 Integrated proteomic analysis of post-translational modifications by serial enrichment. Nat Methods. 2013 Jul;10(7):634-7.
4 Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. Mol Cell Proteomics. 2015 Nov;14(11):3056-71.
5 Identifying Functional Cysteine Residues in the Mitochondria. ACS Chem Biol. 2017 Apr 21;12(4):947-957.
6 Deep Phosphotyrosine Proteomics by Optimization of Phosphotyrosine Enrichment and MS/MS Parameters. J Proteome Res. 2017 Feb 3;16(2):1077-1086.
7 Global Phosphoproteomic Analysis of Human Skeletal Muscle Reveals a Network of Exercise-Regulated Kinases and AMPK Substrates. Cell Metab. 2015 Nov 3;22(5):922-35.
8 Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes. Mol Cell Proteomics. 2011 Jan;10(1):M110.000299.
9 Endogenous NO upon estradiol-17beta stimulation and NO donor differentially regulate mitochondrial S-nitrosylation in endothelial cells. Endocrinology. 2014 Aug;155(8):3005-16.
10 Direct Proteomic Mapping of Cysteine Persulfidation. Antioxid Redox Signal. 2020 Nov 20;33(15):1061-1076.
11 Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep. 2013 Aug 29;4(4):842-51.
12 Lysine Acetylation and Succinylation in HeLa Cells and their Essential Roles in Response to UV-induced Stress. Sci Rep. 2016 Jul 25;6:30212.
13 Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
14 A COFRADIC protocol to study protein ubiquitination. J Proteome Res. 2014 Jun 6;13(6):3107-13.
15 UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nat Struct Mol Biol. 2018 Jul;25(7):631-640.

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