Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0025 Transporter Info
Gene Name	SLC22A8
Transporter Name	Organic anion transporter 3
Gene ID	9376
UniProt ID	Q8TCC7

Post-Translational Modification of This DT
Overview ofSLC22A8 Modification Sites with Functional and Structural Information
Sequence	M T F S E I L D R V G S M G H F Q F L H V A I L G L P I L N M A N H N L L Q I F T A A T P V H H C R P P H N A S T G P W V L P M G P N G K P E R C L R F V H P P N A S L P N D T Q R A M E P C L D G W V Y N S T K D S I V T E W D L V C N S N K L K E M A Q S I F M A G I L I G G L V L G D L S D R F G R R P I L T C S Y L L L A A S G S G A A F S P T F P I Y M V F R F L C G F G I S G I T L S T V I L N V E W V P T R M R A I M S T A L G Y C Y T F G Q F I L P G L A Y A I P Q W R W L Q L T V S I P F F V F F L S S W W T P E S I R W L V L S G K S S K A L K I L R R V A V F N G K K E E G E R L S L E E L K L N L Q K E I S L A K A K Y T A S D L F R I P M L R R M T F C L S L A W F A T G F A Y Y S L A M G V E E F G V N L Y I L Q I I F G G V D V P A K F I T I L S L S Y L G R H T T Q A A A L L L A G G A I L A L T F V P L D L Q T V R T V L A V F G K G C L S S S F S C L F L Y T S E L Y P T V I R Q T G M G V S N L W T R V G S M V S P L V K I T G E V Q P F I P N I I Y G I T A L L G G S A A L F L P E T L N Q P L P E T I E D L E N W S L R A K K P K Q E P E V E K A S Q R I P L Q P H G P G L G S S
PTM type	X-N-glycosylation X-Phosphorylation X-SUMOylation X: Amino Acid

N-glycosylation
Asparagine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC22A8			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	86
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC22A8 Asparagine 86 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC22A8			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	102
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC22A8 Asparagine 102 has the potential to affect its expression or activity.
Phosphorylation
Serine	8 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Decreasing the activity of SLC22A8			[2]
Role of PTM	Protein Activity Modulation
Affected Drug/Substrate	Para-aminohippuric acid (PAH)	Results for Drug	Decreasing uptake of para-aminohippuric acid (PAH)
Modified Residue	Serine
Related Enzyme	Protein phosphatase 1 regulatory subunit 1A (PPP1R1A)
Experimental Material(s)	Pig kidney epithelial (LLC-PK1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Serine have been reported to decrease its transport activity.
PTM Phenomenon2	Have the potential to influence SLC22A8			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	4
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Serine 4 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC22A8			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	293
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Serine 293 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC22A8			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	315
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Serine 315 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC22A8			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	460
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Serine 460 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC22A8			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	511
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Serine 511 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC22A8			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	541
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Serine 541 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC22A8			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	542
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Serine 542 has the potential to affect its expression or activity.
Threonine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC22A8			[3]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	2
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Threonine 2 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC22A8			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	313
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Threonine 313 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC22A8			[7]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	373
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Threonine 373 has the potential to affect its expression or activity.
Tyrosine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC22A8			[5]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	312
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 Tyrosine 312 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	Enhancing the expression and transport activity SLC22A8			[8]
Role of PTM	Protein Activity Modulation
Related Enzyme	cAMP-dependent protein kinase catalytic subunit alpha (PRKACA)
Experimental Material(s)	African green monkey kidney fibroblast-like (COS-7) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22A8 have been reported to enhance its expression and transport activity.
SUMOylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Enhancing the recycling rate and transport activity SLC22A8			[9]
Role of PTM	Protein Activity Modulation
Modified Residue	Lysine
Related Enzyme	Small ubiquitin-related modifier 2 (SUMO2) Small ubiquitin-related modifier 3 (SUMO3)
Experimental Material(s)	African green monkey kidney fibroblast-like (COS-7) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	SUMOylation at SLC22A8 Lysine have been reported to enhance its recycling rate and 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: S22A8_HUMAN)
2	Regulation of mOAT-mediated organic anion transport by okadaic acid and protein kinase C in LLC-PK(1) cells. J Biol Chem. 2000 Apr 7;275(14):10278-84.
3	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
4	TiO2 with Tandem Fractionation (TAFT): An Approach for Rapid, Deep, Reproducible, and High-Throughput Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):710-721.
5	Displacement of N/Q-rich peptides on TiO2 beads enhances the depth and coverage of yeast phosphoproteome analyses. J Proteome Res. 2013 Jun 7;12(6):2905-13.
6	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.
7	Phosphoproteomics study on the activated PKC-induced cell death. J Proteome Res. 2013 Oct 4;12(10):4280-301.
8	Insulin-like growth factor 1 modulates the phosphorylation, expression, and activity of organic anion transporter 3 through protein kinase A signaling pathway. Acta Pharm Sin B. 2020 Jan;10(1):186-194.
9	Activation of Protein Kinase A Stimulates SUMOylation, Expression, and Transport Activity of Organic Anion Transporter 3. AAPS J. 2019 Feb 13;21(2):30.

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Detail Information of Post-Translational Modifications

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