Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0362 Transporter Info
Gene Name	SLC43A3
Transporter Name	Equilibrative nucleobase transporter 1
Gene ID	29015
UniProt ID	Q8NBI5

Post-Translational Modification of This DT
Overview ofSLC43A3 Modification Sites with Functional and Structural Information
Sequence	M A G Q G L P L H V A T L L T G L L E C L G F A G V L F G W P S L V F V F K N E D Y F K D L C G P D A G P I G N A T G Q A D C K A Q D E R F S L I F T L G S F M N N F M T F P T G Y I F D R F K T T V A R L I A I F F Y T T A T L I I A F T S A G S A V L L F L A M P M L T I G G I L F L I T N L Q I G N L F G Q H R S T I I T L Y N G A F D S S S A V F L I I K L L Y E K G I S L R A S F I F I S V C S T W H V A R T F L L M P R G H I P Y P L P P N Y S Y G L C P G N G T T K E E K E T A E H E N R E L Q S K E F L S A K E E T P G A G Q K Q E L R S F W S Y A F S R R F A W H L V W L S V I Q L W H Y L F I G T L N S L L T N M A G G D M A R V S T Y T N A F A F T Q F G V L C A P W N G L L M D R L K Q K Y Q K E A R K T G S S T L A V A L C S T V P S L A L T S L L C L G F A L C A S V P I L P L Q Y L T F I L Q V I S R S F L Y G S N A A F L T L A F P S E H F G K L F G L V M A L S A V V S L L Q F P I F T L I K G S L Q N D P F Y V N V M F M L A I L L T F F H P F L V Y R E C R T W K E S P S A I A
PTM type	X-Acetylation X-N-glycosylation X-O-glycosylation X-Phosphorylation X-S-nitrosylation X-S-palmitoylation X-Ubiquitination X-Ubiquitination X: Amino Acid

Acetylation
Lysine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC43A3			[1], [2]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	255
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC43A3 Lysine 255 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC43A3			[3]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	264
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC43A3 Lysine 264 has the potential to affect its expression or activity.
N-glycosylation
Asparagine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC43A3			[4]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	56
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC43A3 Asparagine 56 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC43A3			[4]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	220
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC43A3 Asparagine 220 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC43A3			[4]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	229
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC43A3 Asparagine 229 has the potential to affect its expression or activity.
O-glycosylation
Serine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC43A3			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	419
Experimental Method	Co-Immunoprecipitation
Detailed Description	O-linked Glycosylation at SLC43A3 Serine 419 has the potential to affect its expression or activity.
Phosphorylation
Serine	6 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC43A3			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	71
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Serine 71 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC43A3			[7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	222
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Serine 222 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC43A3			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	248
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Serine 248 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC43A3			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	253
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Serine 253 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC43A3			[11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	486
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Serine 486 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC43A3			[11], [12]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	488
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Serine 488 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 SLC43A3			[7]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	232
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Threonine 232 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC43A3			[10], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	258
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Threonine 258 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC43A3			[11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	482
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Threonine 482 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 SLC43A3			[7]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	223
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC43A3 Tyrosine 223 has the potential to affect its expression or activity.
S-nitrosylation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC43A3			[13], [14]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	226
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation at SLC43A3 Cystine 226 has the potential to affect its expression or activity.
S-palmitoylation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC43A3			[15]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	226
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at SLC43A3 Cystine 226 has the potential to affect its expression or activity.
Ubiquitination
Lysine	8 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	177
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC43A3 Lysine 177 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	236
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC43A3 Lysine 236 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC43A3			[17], [18]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	249
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC43A3 Lysine 249 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC43A3			[17], [18]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	255
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC43A3 Lysine 255 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC43A3			[17], [18]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	264
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC43A3 Lysine 264 has the potential to affect its expression or activity.
PTM Phenomenon6	.			[16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	484
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC43A3 Lysine 484 has the potential to affect its expression or activity.
PTM Phenomenon7	.			[16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	484
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC43A3 Lysine 484 has the potential to affect its expression or activity.
PTM Phenomenon8	.			[16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	484
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC43A3 Lysine 484 has the potential to affect its expression or activity.

References
1	Quantitative Proteomic Atlas of Ubiquitination and Acetylation in the DNA Damage Response. Mol Cell. 2015 Sep 3;59(5):867-81.
2	Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3. PLoS One. 2012;7(12):e50545.
3	Quantitative Analysis of Global Proteome and Lysine Acetylome Reveal the Differential Impacts of VPA and SAHA on HL60 Cells. Sci Rep. 2016 Jan 29;6:19926.
4	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: S43A3_HUMAN)
5	Mapping and Quantification of Over 2000 O-linked Glycopeptides in Activated Human T Cells with Isotope-Targeted Glycoproteomics (Isotag). Mol Cell Proteomics. 2018 Apr;17(4):764-775.
6	Targeting BMK1 Impairs the Drug Resistance to Combined Inhibition of BRAF and MEK1/2 in Melanoma. Sci Rep. 2017 Apr 7;7:46244.
7	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.
8	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.
9	Phosphoproteomic screening identifies physiological substrates of the CDKL5 kinase. EMBO J. 2018 Dec 14;37(24):e99559.
10	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
11	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
12	Phosphoproteome Characterization of Human Colorectal Cancer SW620 Cell-Derived Exosomes and New Phosphosite Discovery for C-HPP. J Proteome Res. 2016 Nov 4;15(11):4060-4072.
13	Predict and analyze S-nitrosylation modification sites with the mRMR and IFS approaches. J Proteomics. 2012 Feb 16;75(5):1654-65.
14	Detergent-free biotin switch combined with liquid chromatography/tandem mass spectrometry in the analysis of S-nitrosylated proteins. Rapid Commun Mass Spectrom. 2008 Apr;22(8):1137-45.
15	Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites. J Proteome Res. 2018 May 4;17(5):1907-1922.
16	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
17	A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284.
18	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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