Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0008 Transporter Info
Gene Name	SLCO1B1
Transporter Name	Organic anion transporting polypeptide 1B1
Gene ID	10599
UniProt ID	Q9Y6L6

Post-Translational Modification of This DT
Overview ofSLCO1B1 Modification Sites with Functional and Structural Information
Sequence	M D Q N Q H L N K T A E A Q P S E N K K T R Y C N G L K M F L A A L S L S F I A K T L G A I I M K S S I I H I E R R F E I S S S L V G F I D G S F E I G N L L V I V F V S Y F G S K L H R P K L I G I G C F I M G I G G V L T A L P H F F M G Y Y R Y S K E T N I N S S E N S T S T L S T C L I N Q I L S L N R A S P E I V G K G C L K E S G S Y M W I Y V F M G N M L R G I G E T P I V P L G L S Y I D D F A K E G H S S L Y L G I L N A I A M I G P I I G F T L G S L F S K M Y V D I G Y V D L S T I R I T P T D S R W V G A W W L N F L V S G L F S I I S S I P F F F L P Q T P N K P Q K E R K A S L S L H V L E T N D E K D Q T A N L T N Q G K N I T K N V T G F F Q S F K S I L T N P L Y V M F V L L T L L Q V S S Y I G A F T Y V F K Y V E Q Q Y G Q P S S K A N I L L G V I T I P I F A S G M F L G G Y I I K K F K L N T V G I A K F S C F T A V M S L S F Y L L Y F F I L C E N K S V A G L T M T Y D G N N P V T S H R D V P L S Y C N S D C N C D E S Q W E P V C G N N G I T Y I S P C L A G C K S S S G N K K P I V F Y N C S C L E V T G L Q N R N Y S A H L G E C P R D D A C T R K F Y F F V A I Q V L N L F F S A L G G T S H V M L I V K I V Q P E L K S L A L G F H S M V I R A L G G I L A P I Y F G A L I D T T C I K W S T N N C G T R G S C R T Y N S T S F S R V Y L G L S S M L R V S S L V L Y I I L I Y A M K K K Y Q E K D I N A S E N G S V M D E A N L E S L N K N K H F V P S A G A D S E T H C
PTM type	X-N-glycosylation X-N-linked glycosylation X-Phosphorylation X-Ubiquitination X: Amino Acid

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 SLCO1B1			[1]
Role of PTM	Protein Activity Modulation
Modified Residue	Asparagine	Modified Location	134
Modified State	Asparagine to Glutamine substitution
Experimental Material(s)	Human embryonic kidney 293 (HEK293) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the N-glycosylation at SLCO1B1 Asparagine134 (i.e. Asparagine to Glutamine substitution) have been reported to decrease its membrane localization and transport function.
PTM Phenomenon2	Decreasing the membrane localization and transport function of the SLCO1B1			[1]
Role of PTM	Protein Activity Modulation
Modified Residue	Asparagine	Modified Location	503
Modified State	Asparagine to Glutamine substitution
Experimental Material(s)	Human embryonic kidney 293 (HEK293) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the N-glycosylation at SLCO1B1 Asparagine503 (i.e. Asparagine to Glutamine substitution) have been reported to decrease its membrane localization and transport function.
PTM Phenomenon3	Decreasing the membrane localization and transport function of the SLCO1B1			[1]
Role of PTM	Protein Activity Modulation
Modified Residue	Asparagine	Modified Location	516
Modified State	Asparagine to Glutamine substitution
Experimental Material(s)	Human embryonic kidney 293 (HEK293) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the N-glycosylation at SLCO1B1 Asparagine516 (i.e. Asparagine to Glutamine substitution) have been reported to decrease its membrane localization and transport function.
PTM Phenomenon4	Have the potential to influence SLCO1B1			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	130
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLCO1B1 Asparagine 130 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLCO1B1			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	432
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLCO1B1 Asparagine 432 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLCO1B1			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	617
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLCO1B1 Asparagine 617 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	Decreasing the membrane expression and lower substrate transport of the SLCO1B1			[3]
Role of PTM	Surface Expression Modulation
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-glycosylation at SLCO1B1 have been reported to decrease its membrane expression and lower substrate transport.
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 SLCO1B1 has been reported to altered drug disposition in humans NASH.
Phosphorylation
Serine	14 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLCO1B1			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	37
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 37 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO1B1			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	231
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 231 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLCO1B1			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	293
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 293 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLCO1B1			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	295
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 295 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLCO1B1			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	328
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 328 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLCO1B1			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	420
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 420 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLCO1B1			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	618
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 618 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLCO1B1			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	620
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 620 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLCO1B1			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	622
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 622 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLCO1B1			[6], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	659
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 659 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLCO1B1			[6], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	663
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 663 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence SLCO1B1			[5], [12]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	672
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 672 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence SLCO1B1			[5], [12]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	682
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 682 has the potential to affect its expression or activity.
PTM Phenomenon14	Have the potential to influence SLCO1B1			[13], [14]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	687
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Serine 687 has the potential to affect its expression or activity.
Threonine	8 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLCO1B1			[13], [15]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	301
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Threonine 301 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO1B1			[13]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	308
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Threonine 308 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLCO1B1			[13]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	312
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Threonine 312 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLCO1B1			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	319
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Threonine 319 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLCO1B1			[8]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	323
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Threonine 323 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLCO1B1			[10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	615
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Threonine 615 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLCO1B1			[10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	619
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Threonine 619 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLCO1B1			[13]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	689
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Threonine 689 has the potential to affect its expression or activity.
Tyrosine	7 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Potentially affecting the transporter			[16]
Role of PTM	On/Off Switch
Modified Residue	Tyrosine
Modified State	Tyrosine kinase inhibitors
Experimental Method	Co-Immunoprecipitation
Detailed Description	Removal of the Phosphorylation at SLCO1B1 Tyrosine (i.e. Tyrosine kinase inhibitors) have been reported to have the potential to affect the transporter.
PTM Phenomenon2	Have the potential to influence SLCO1B1			[9]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	422
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Tyrosine 422 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLCO1B1			[9]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	425
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Tyrosine 425 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLCO1B1			[10]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	616
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Tyrosine 616 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLCO1B1			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	625
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Tyrosine 625 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLCO1B1			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	645
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Tyrosine 645 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLCO1B1			[6]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	651
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 Tyrosine 651 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	Decreasing the function of the SLCO1B1 by affecting internalization and recycling of the transporter protein			[17]
Role of PTM	Protein Activity Modulation
Affected Drug/Substrate	Estrone-3-sulfate	Results for Drug	Decreasing uptake of estron-3-sulfate
Related Enzyme	Protein kinase C alpha type (PRKCA)
Experimental Material(s)	Human embryonic kidney 293 (HEK293) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO1B1 have been reported to decrease its function by affecting internalization and recycling of the transporter protein.
Ubiquitination
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Significantly decreased the maximal transport velocity (Vmax) of transporter			[18]
Role of PTM	Protein Activity Modulation
Affected Drug/Substrate	[3H]CCK-8	Results for Drug	Decreasing the transport of [3H]CCK-8
Experimental Material(s)	Human embryonic kidney 293 (HEK293) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLCO1B1 have been reported to significantly decrease its maximal transport velocity (Vmax).

References
1	N-Glycosylation dictates proper processing of organic anion transporting polypeptide 1B1. PLoS One. 2012;7(12):e52563.
2	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: SO1B1_HUMAN)
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	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.
5	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
6	Non-alcoholic fatty liver disease phosphoproteomics: A functional piece of the precision puzzle. Hepatol Res. 2017 Dec;47(13):1469-1483.
7	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
8	Identification of tyrosine-phosphorylated proteins associated with metastasis and functional analysis of FER in human hepatocellular carcinoma cells. BMC Cancer. 2009 Oct 16;9:366.
9	Phosphoproteomics identifies driver tyrosine kinases in sarcoma cell lines and tumors. Cancer Res. 2012 May 15;72(10):2501-11.
10	Unique signalling connectivity of FGFR3-TACC3 oncoprotein revealed by quantitative phosphoproteomics and differential network analysis. Oncotarget. 2017 Oct 25;8(61):102898-102911.
11	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.
12	An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62.
13	In situ sample processing approach (iSPA) for comprehensive quantitative phosphoproteome analysis. J Proteome Res. 2014 Sep 5;13(9):3896-904.
14	Systematic analysis of protein phosphorylation networks from phosphoproteomic data. Mol Cell Proteomics. 2012 Oct;11(10):1070-83.
15	Phosphoproteome analysis of human liver tissue by long-gradient nanoflow LC coupled with multiple stage MS analysis. Electrophoresis. 2010 Mar;31(6):1080-9.
16	Post-translational modifications of transporters. Pharmacol Ther. 2018 Dec;192:88-99.
17	Protein kinase C affects the internalization and recycling of organic anion transporting polypeptide 1B1. Biochim Biophys Acta. 2015 Oct;1848(10 Pt A):2022-30.
18	Treatment with proteasome inhibitor bortezomib decreases organic anion transporting polypeptide (OATP) 1B3-mediated transport in a substrate-dependent manner. PLoS One. 2017 Nov 6;12(11):e0186924.

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Detail Information of Post-Translational Modifications

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