Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0031 Transporter Info
Gene Name	SLCO2B1
Transporter Name	Organic anion transporting polypeptide 2B1
Gene ID	11309
UniProt ID	O94956

Post-Translational Modification of This DT
Overview ofSLCO2B1 Modification Sites with Functional and Structural Information
Sequence	M G P R I G P A G E V P Q V P D K E T K A T M G T E N T P G G K A S P D P Q D V R P S V F H N I K L F V L C H S L L Q L A Q L M I S G Y L K S S I S T V E K R F G L S S Q T S G L L A S F N E V G N T A L I V F V S Y F G S R V H R P R M I G Y G A I L V A L A G L L M T L P H F I S E P Y R Y D N T S P E D M P Q D F K A S L C L P T T S A P A S A P S N G N C S S Y T E T Q H L S V V G I M F V A Q T L L G V G G V P I Q P F G I S Y I D D F A H N S N S P L Y L G I L F A V T M M G P G L A F G L G S L M L R L Y V D I N Q M P E G G I S L T I K D P R W V G A W W L G F L I A A G A V A L A A I P Y F F F P K E M P K E K R E L Q F R R K V L A V T D S P A R K G K D S P S K Q S P G E S T K K Q D G L V Q I A P N L T V I Q F I K V F P R V L L Q T L R H P I F L L V V L S Q V C L S S M A A G M A I F L P K F L E R Q F S I T A S Y A N L L I G C L S F P S V I V G I V V G G V L V K R L H L G P V G C G A L C L L G M L L C L F F S L P L F F I G C S S H Q I A G I T H Q T S A H P G L E L S P S C M E A C S C P L D G F N P V C D P S T R V E Y I T P C H A G C S S W V V Q D A L D N S Q V F Y T N C S C V V E G N P V L A G S C D S T C S H L V V P F L L L V S L G S A L A C L T H T P S F M L I L R G V K K E D K T L A V G I Q F M F L R I L A W M P S P V I H G S A I D T T C V H W A L S C G R R A V C R Y Y N N D L L R N R F I G L Q F F F K T G S V I C F A L V L A V L R Q Q D K E A R T K E S R S S P A V E Q Q L L V S G P G K K P E D S R V
PTM type	X-N-glycosylation X-N-linked glycosylation X-Phosphorylation X-Phosphorylation 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 SLCO2B1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	176
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLCO2B1 Asparagine 176 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO2B1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	538
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLCO2B1 Asparagine 538 has the potential to affect its expression or activity.
Cysteine	10 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Impairing the function of SLCO2B1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Cysteine	Modified Location	489
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 489 (i.e. Cysteine to Alanine mutation) have been reported to impaire its transport function.
PTM Phenomenon2	Impairing the function of SLCO2B1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Cysteine	Modified Location	495
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 495 (i.e. Cysteine to Alanine mutation) have been reported to impaire its transport function.
PTM Phenomenon3	Impairing the function of SLCO2B1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Cysteine	Modified Location	504
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 504 (i.e. Cysteine to Alanine mutation) have been reported to impaire its transport function.
PTM Phenomenon4	Impairing the function of SLCO2B1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Cysteine	Modified Location	516
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 516 (i.e. Cysteine to Alanine mutation) have been reported to impaire its transport function.
PTM Phenomenon5	Impairing the function of SLCO2B1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Cysteine	Modified Location	520
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 520 (i.e. Cysteine to Alanine mutation) have been reported to impaire its transport function.
PTM Phenomenon6	Impairing the function of SLCO2B1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Cysteine	Modified Location	539
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 539 (i.e. Cysteine to Alanine mutation) have been reported to impaire its transport function.
PTM Phenomenon7	Impairing the function of SLCO2B1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Cysteine	Modified Location	541
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 541 (i.e. Cysteine to Alanine mutation) have been reported to impaire its transport function.
PTM Phenomenon8	Impairing the function of SLCO2B1			[2]
Role of PTM	Protein Activity Modulation
Modified Residue	Cysteine	Modified Location	553
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 553 (i.e. Cysteine to Alanine mutation) have been reported to impaire its transport function.
PTM Phenomenon9	Decreasing the membrane localization and transport function of the SLCO2B1			[2]
Role of PTM	Trafficking to Plasma Membrane
Affected Drug/Substrate	Estrone-3-sulfate and Dehydroepiandrosterone sulfate	Results for Drug	Decreasing the transport of estrone-3-sulfate and dehydroepiandrosterone sulfate
Modified Residue	Cysteine	Modified Location	493
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 493 (i.e. Cysteine to Alanine mutation) have been reported to decrease its membrane localization and transport function.
PTM Phenomenon10	Decreasing the membrane localization and transport function of the SLCO2B1			[2]
Role of PTM	Trafficking to Plasma Membrane
Affected Drug/Substrate	Estrone-3-sulfate and Dehydroepiandrosterone sulfate	Results for Drug	Decreasing the transport of estrone-3-sulfate and dehydroepiandrosterone sulfate
Modified Residue	Cysteine	Modified Location	557
Modified State	Cysteine to Alanine mutation
Experimental Material(s)	Chinese hamster ovary subclone (CHO-K1) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Glycosylation at SLCO2B1 Cysteine 557 (i.e. Cysteine to Alanine mutation) have been reported to decrease its membrane localization and transport function.
N-linked glycosylation
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[3]
Role of PTM	Influencing the Disease Progression
Experimental Material(s)	liver tissues
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the N-linked glycosylation at SLCO2B1 has been reported to altered drug disposition in humans NASH.
Phosphorylation
Serine	7 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLCO2B1			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	34
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Serine 34 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	74
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Serine 74 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLCO2B1			[7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	264
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Serine 264 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLCO2B1			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	320
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Serine 320 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLCO2B1			[10], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	333
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Serine 333 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLCO2B1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	687
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Serine 687 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLCO2B1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	688
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Serine 688 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	.			[6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	75
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Threonine 75 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO2B1			[14]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	133
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Threonine 133 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLCO2B1			[8], [15]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	318
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Threonine 318 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 SLCO2B1			[16]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	144
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO2B1 Tyrosine 144 has the potential to affect its expression or 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: SO2B1_HUMAN)
2	Functional analysis of the extracellular cysteine residues in the human organic anion transporting polypeptide, OATP2B1. Mol Pharmacol. 2006 Sep;70(3):806-17.
3	Impaired N-linked glycosylation of uptake and efflux transporters in human non-alcoholic fatty liver disease. Liver Int. 2017 Jul;37(7):1074-1081.
4	Super-SILAC mix coupled with SIM/AIMS assays for targeted verification of phosphopeptides discovered in a large-scale phosphoproteome analysis of hepatocellular carcinoma. J Proteomics. 2017 Mar 22;157:40-51.
5	Integrated analysis of global proteome, phosphoproteome, and glycoproteome enables complementary interpretation of disease-related protein networks. Sci Rep. 2015 Dec 11;5:18189.
6	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
7	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.
8	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
9	Integrating proteomics with electrochemistry for identifying kinase biomarkers. Chem Sci. 2015 Aug 1;6(8):4756-4766.
10	iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
11	Systematic analysis of protein phosphorylation networks from phosphoproteomic data. Mol Cell Proteomics. 2012 Oct;11(10):1070-83.
12	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
13	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
14	FAIMS and Phosphoproteomics of Fibroblast Growth Factor Signaling: Enhanced Identification of Multiply Phosphorylated Peptides. J Proteome Res. 2015 Dec 4;14(12):5077-87.
15	A Methodological Assessment and Characterization of Genetically-Driven Variation in Three Human Phosphoproteomes. Sci Rep. 2018 Aug 14;8(1):12106.
16	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.

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Detail Information of Post-Translational Modifications

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