General Information of Drug Transporter (DT)
DT ID DTD0029 Transporter Info
Gene Name SLCO1A2
Transporter Name Organic anion transporting polypeptide 1A2
Gene ID
6579
UniProt ID
P46721
Post-Translational Modification of This DT
Overview ofSLCO1A2 Modification Sites with Functional and Structural Information
Sequence
PTM type
X-Acetylation X-N-glycosylation X-Oxidation X-Phosphorylation 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 SLCO1A2 [1]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

33

Experimental Method

Co-Immunoprecipitation

Detailed Description

Acetylation at SLCO1A2 Lysine 33 has the potential to affect its expression or activity.

N-glycosylation

  Asparagine

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

  PTM Phenomenon1

Decreasing the membrane localization and transport function of the SLCO1A2 [2]

Role of PTM

Trafficking to Plasma Membrane

Affected Drug/Substrate

Taurocholate

Results for Drug

Decreasing the transport of taurocholate

Modified Residue

Asparagine

Modified Location

62

Modified State

Asparagine to Aspartate substitution

Experimental Method

Co-Immunoprecipitation

Detailed Description

Removal of the N-glycosylation at SLCO1A2 Asparagine 62 (i.e. Asparagine to Aspartate substitution) have been reported to decrease its membrane localization and transport function.

  PTM Phenomenon2

Decreasing the membrane localization and transport function of the SLCO1A2 [2]

Role of PTM

Trafficking to Plasma Membrane

Affected Drug/Substrate

Taurocholate

Results for Drug

Decreasing the transport of taurocholate

Modified Residue

Asparagine

Modified Location

124

Modified State

Asparagine to Aspartate substitution

Experimental Method

Co-Immunoprecipitation

Detailed Description

Removal of the N-glycosylation at SLCO1A2 Asparagine 124 (i.e. Asparagine to Aspartate substitution) have been reported to decrease its membrane localization and transport function.

  PTM Phenomenon3

Decreasing the membrane localization and transport function of the SLCO1A2 [2]

Role of PTM

Trafficking to Plasma Membrane

Affected Drug/Substrate

Taurocholate

Results for Drug

Decreasing the transport of taurocholate

Modified Residue

Asparagine

Modified Location

135

Modified State

Asparagine to Aspartate substitution

Experimental Method

Co-Immunoprecipitation

Detailed Description

Removal of the N-glycosylation at SLCO1A2 Asparagine 135 (i.e. Asparagine to Aspartate substitution) have been reported to decrease its membrane localization and transport function.

  PTM Phenomenon4

Decreasing the membrane localization and transport function of the SLCO1A2 [2]

Role of PTM

Trafficking to Plasma Membrane

Affected Drug/Substrate

Taurocholate

Results for Drug

Decreasing the transport of taurocholate

Modified Residue

Asparagine

Modified Location

492

Modified State

Asparagine to Aspartate substitution

Experimental Method

Co-Immunoprecipitation

Detailed Description

Removal of the N-glycosylation at SLCO1A2 Asparagine 492 (i.e. Asparagine to Aspartate substitution) have been reported to decrease its membrane localization and transport function.

  PTM Phenomenon5

Have the potential to influence SLCO1A2 [3]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

412

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLCO1A2 Asparagine 412 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SLCO1A2 [3]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

419

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLCO1A2 Asparagine 419 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 SLCO1A2 [4]

Role of PTM

Potential impacts

Modified Residue

Cystine

Modified Location

500

Experimental Method

Co-Immunoprecipitation

Detailed Description

Oxidation at SLCO1A2 Cystine 500 has the potential to affect its expression or activity.

Phosphorylation

  Serine

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

  PTM Phenomenon1

Have the potential to influence SLCO1A2 [5]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

337

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLCO1A2 Serine 337 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 SLCO1A2 [6]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

422

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLCO1A2 Tyrosine 422 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SLCO1A2 [6]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

430

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLCO1A2 Tyrosine 430 has the potential to affect its expression or activity.
References
1 Peripheral autonomic changes accompanying learning and reaction time performance in older people. J Gerontol. 1980 Jan;35(1):57-65.
2 N-glycosylation controls functional activity of Oatp1, an organic anion transporter. Am J Physiol Gastrointest Liver Physiol. 2003 Aug;285(2):G371-81.
3 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: SO1A2_HUMAN)
4 Identifying Functional Cysteine Residues in the Mitochondria. ACS Chem Biol. 2017 Apr 21;12(4):947-957.
5 iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
6 An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62.

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