Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0502 Transporter Info
Gene Name	SLCO4A1
Transporter Name	Organic anion transporting polypeptide 4A1
Gene ID	28231
UniProt ID	Q96BD0

Post-Translational Modification of This DT
Overview ofSLCO4A1 Modification Sites with Functional and Structural Information
Sequence	M P L H Q L G D K P L T F P S P N S A M E N G L D H T P P S R R A S P G T P L S P G S L R S A A H S P L D T S K Q P L C Q L W A E K H G A R G T H E V R Y V S A G Q S V A C G W W A F A P P C L Q V L N T P K G I L F F L C A A A F L Q G M T V N G F I N T V I T S L E R R Y D L H S Y Q S G L I A S S Y D I A A C L C L T F V S Y F G G S G H K P R W L G W G V L L M G T G S L V F A L P H F T A G R Y E V E L D A G V R T C P A N P G A V C A D S T S G L S R Y Q L V F M L G Q F L H G V G A T P L Y T L G V T Y L D E N V K S S C S P V Y I A I F Y T A A I L G P A A G Y L I G G A L L N I Y T E M G R R T E L T T E S P L W V G A W W V G F L G S G A A A F F T A V P I L G Y P R Q L P G S Q R Y A V M R A A E M H Q L K D S S R G E A S N P D F G K T I R D L P L S I W L L L K N P T F I L L C L A G A T E A T L I T G M S T F S P K F L E S Q F S L S A S E A A T L F G Y L V V P A G G G G T F L G G F F V N K L R L R G S A V I K F C L F C T V V S L L G I L V F S L H C P S V P M A G V T A S Y G G S L L P E G H L N L T A P C N A A C S C Q P E H Y S P V C G S D G L M Y F S L C H A G C P A A T E T N V D G Q K V Y R D C S C I P Q N L S S G F G H A T A G K C T S T C Q R K P L L L V F I F V V I F F T F L S S I P A L T A T L R C V R D P Q R S F A L G I Q W I V V R I L G G I P G P I A F G W V I D K A C L L W Q D Q C G Q Q G S C L V Y Q N S A M S R Y I L I M G L L Y K V L G V L F F A I A C F L Y K P L S E S S D G L E T C L P S Q S S A P D S A T D S Q L Q S S V
PTM type	X-N-glycosylation X-Phosphorylation X-S-nitrosylation X-Ubiquitination 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 SLCO4A1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	499
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLCO4A1 Asparagine 499 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO4A1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	557
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLCO4A1 Asparagine 557 has the potential to affect its expression or activity.
Phosphorylation
Serine	13 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLCO4A1			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	15
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 15 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO4A1			[2], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	18
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 18 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLCO4A1			[2], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	30
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 30 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLCO4A1			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	34
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 34 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLCO4A1			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	40
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 40 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLCO4A1			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	43
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 43 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLCO4A1			[5], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	46
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 46 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLCO4A1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	50
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 50 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLCO4A1			[4], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	55
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 55 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLCO4A1			[11], [12]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	355
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 355 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLCO4A1			[13], [14]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	356
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 356 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence SLCO4A1			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	361
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 361 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence SLCO4A1			[17]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	406
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Serine 406 has the potential to affect its expression or activity.
Threonine	5 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLCO4A1			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	12
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Threonine 12 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO4A1			[2], [4]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	27
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Threonine 27 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLCO4A1			[7], [9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	37
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Threonine 37 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLCO4A1			[2], [20]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	54
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Threonine 54 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLCO4A1			[21]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	300
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Threonine 300 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 SLCO4A1			[22]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	666
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Tyrosine 666 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO4A1			[22]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	674
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLCO4A1 Tyrosine 674 has the potential to affect its expression or activity.
S-nitrosylation
Cystine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLCO4A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	60
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation (-SNO) at SLCO4A1 Cystine 60 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO4A1			[23]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	216
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation (-SNO) at SLCO4A1 Cystine 216 has the potential to affect its expression or activity.
Ubiquitination
Lysine	6 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLCO4A1			[25]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	9
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLCO4A1 Lysine 9 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLCO4A1			[25], [26]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	56
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLCO4A1 Lysine 56 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLCO4A1			[27]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	66
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLCO4A1 Lysine 66 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLCO4A1			[28]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	353
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLCO4A1 Lysine 353 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLCO4A1			[28]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	367
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLCO4A1 Lysine 367 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLCO4A1			[27]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	569
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLCO4A1 Lysine 569 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: SO4A1_HUMAN)
2	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
3	Dataset from the global phosphoproteomic mapping of early mitotic exit in human cells. Data Brief. 2015 Aug 24;5:45-52.
4	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
5	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
6	Combined inhibition of receptor tyrosine and p21-activated kinases as a therapeutic strategy in childhood ALL. Blood Adv. 2018 Oct 9;2(19):2554-2567.
7	Capillary Zone Electrophoresis-Tandem Mass Spectrometry for Large-Scale Phosphoproteomics with the Production of over 11,000 Phosphopeptides from the Colon Carcinoma HCT116 Cell Line. Anal Chem. 2019 Feb 5;91(3):2201-2208.
8	Quantitative Phosphoproteome Analysis of Clostridioides difficile Toxin B Treated Human Epithelial Cells. Front Microbiol. 2018 Dec 17;9:3083.
9	Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
10	The Global Phosphorylation Landscape of SARS-CoV-2 Infection. Cell. 2020 Aug 6;182(3):685-712.e19.
11	Offline pentafluorophenyl (PFP)-RP prefractionation as an alternative to high-pH RP for comprehensive LC-MS/MS proteomics and phosphoproteomics. Anal Bioanal Chem. 2017 Jul;409(19):4615-4625.
12	Identification of Candidate Casein Kinase 2 Substrates in Mitosis by Quantitative Phosphoproteomics. Front Cell Dev Biol. 2017 Nov 22;5:97.
13	Protein kinase C-alpha interaction with F0F1-ATPase promotes F0F1-ATPase activity and reduces energy deficits in injured renal cells. J Biol Chem. 2015 Mar 13;290(11):7054-66.
14	Ultradeep human phosphoproteome reveals a distinct regulatory nature of Tyr and Ser/Thr-based signaling. Cell Rep. 2014 Sep 11;8(5):1583-94.
15	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
16	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
17	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.
18	Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res. 2013 Jun 7;12(6):2414-21.
19	Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71.
20	Comparative phosphoproteomic analysis reveals signaling networks regulating monopolar and bipolar cytokinesis. Sci Rep. 2018 Feb 2;8(1):2269.
21	iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
22	In situ sample processing approach (iSPA) for comprehensive quantitative phosphoproteome analysis. J Proteome Res. 2014 Sep 5;13(9):3896-904.
23	Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique. Nat Commun. 2019 May 16;10(1):2195.
24	MDD-SOH: exploiting maximal dependence decomposition to identify S-sulfenylation sites with substrate motifs. Bioinformatics. 2016 Jan 15;32(2):165-72.
25	UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nat Struct Mol Biol. 2018 Jul;25(7):631-640.
26	Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition. Mol Cell Proteomics. 2012 May;11(5):148-59.
27	Global identification of modular cullin-RING ligase substrates. Cell. 2011 Oct 14;147(2):459-74.
28	Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 2011 Oct 21;44(2):325-40.

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Detail Information of Post-Translational Modifications

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