Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0126 Transporter Info
Gene Name	SLC19A1
Transporter Name	Folate transporter 1
Gene ID	6573
UniProt ID	P41440

Post-Translational Modification of This DT
Overview ofSLC19A1 Modification Sites with Functional and Structural Information
Sequence	M V P S S P A V E K Q V P V E P G P D P E L R S W R H L V C Y L C F Y G F M A Q I R P G E S F I T P Y L L G P D K N F T R E Q V T N E I T P V L S Y S Y L A V L V P V F L L T D Y L R Y T P V L L L Q G L S F V S V W L L L L L G H S V A H M Q L M E L F Y S V T M A A R I A Y S S Y I F S L V R P A R Y Q R V A G Y S R A A V L L G V F T S S V L G Q L L V T V G R V S F S T L N Y I S L A F L T F S V V L A L F L K R P K R S L F F N R D D R G R C E T S A S E L E R M N P G P G G K L G H A L R V A C G D S V L A R M L R E L G D S L R R P Q L R L W S L W W V F N S A G Y Y L V V Y Y V H I L W N E V D P T T N S A R V Y N G A A D A A S T L L G A I T S F A A G F V K I R W A R W S K L L I A G V T A T Q A G L V F L L A H T R H P S S I W L C Y A A F V L F R G S Y Q F L V P I A T F Q I A S S L S K E L C A L V F G V N T F F A T I V K T I I T F I V S D V R G L G L P V R K Q F Q L Y S V Y F L I L S I I Y F L G A M L D G L R H C Q R G H H P R Q P P A Q G L R S A A E E K A A Q A L S V Q D K G L G G L Q P A Q S P P L S P E D S L G A V G P A S L E Q R Q S D P Y L A Q A P A P Q A A E F L S P V T T P S P C T L C S A Q A S G P E A A D E T C P Q L A V H P P G V S K L G L Q C L P S D G V Q N V N Q
PTM type	X-Acetylation X-N-glycosylation X-Phosphorylation X-S-nitrosylation X-S-palmitoylation X-Ubiquitination X: Amino Acid

Acetylation
Methionine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC19A1			[1]
Role of PTM	Potential impacts
Modified Residue	Methionine	Modified Location	1
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC19A1 Methionine 1 has the potential to affect its expression or activity.
N-glycosylation
Asparagine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC19A1			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	58
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC19A1 Asparagine 58 has the potential to affect its expression or activity.
Phosphorylation
Serine	14 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC19A1			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	4
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 4 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC19A1			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	5
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 5 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC19A1			[4], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	223
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 223 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC19A1			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	225
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 225 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC19A1			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	436
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 436 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC19A1			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	443
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 443 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC19A1			[10], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	474
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 474 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC19A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	485
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 485 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC19A1			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	499
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 499 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC19A1			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	503
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 503 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLC19A1			[5], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	507
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 507 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence SLC19A1			[7], [14]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	515
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 515 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence SLC19A1			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	521
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 521 has the potential to affect its expression or activity.
PTM Phenomenon14	Have the potential to influence SLC19A1			[4], [17]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	583
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Serine 583 has the potential to affect its expression or activity.
Threonine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC19A1			[4], [18]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	222
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Threonine 222 has the potential to affect its expression or activity.
Tyrosine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC19A1			[9]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	435
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Tyrosine 435 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC19A1			[9]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	438
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Tyrosine 438 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC19A1			[9]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	446
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Tyrosine 446 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC19A1			[16], [19]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	524
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC19A1 Tyrosine 524 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 SLC19A1			[20]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	580
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation (-SNO) at SLC19A1 Cystine 580 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 SLC19A1			[21]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	246
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at SLC19A1 Cystine 246 has the potential to affect its expression or activity.
Ubiquitination
Lysine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC19A1			[22], [23]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	10
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC19A1 Lysine 10 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC19A1			[22]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	237
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC19A1 Lysine 237 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC19A1			[22]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	479
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC19A1 Lysine 479 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC19A1			[24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	489
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC19A1 Lysine 489 has the potential to affect its expression or activity.

References
1	N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. Proc Natl Acad Sci U S A. 2012 Jul 31;109(31):12449-54.
2	Analysis of membrane topology of the human reduced folate carrier protein by hemagglutinin epitope insertion and scanning glycosylation insertion mutagenesis. Biochim Biophys Acta. 2002 Aug 31;1564(2):333-42.
3	Effects of the loss of capacity for N-glycosylation on the transport activity and cellular localization of the human reduced folate carrier. Biochim Biophys Acta. 1998 Oct 15;1375(1-2):6-12.
4	A Methodological Assessment and Characterization of Genetically-Driven Variation in Three Human Phosphoproteomes. Sci Rep. 2018 Aug 14;8(1):12106.
5	Modulation of Cl- signaling and ion transport by recruitment of kinases and phosphatases mediated by the regulatory protein IRBIT. Sci Signal. 2018 Oct 30;11(554):eaat5018.
6	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
7	Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
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	Characterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics. Mol Cell Proteomics. 2013 Dec;12(12):3851-73.
10	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.
11	Finding the same needles in the haystack? A comparison of phosphotyrosine peptides enriched by immuno-affinity precipitation and metal-based affinity chromatography. J Proteomics. 2013 Oct 8;91:331-7.
12	Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
13	Improved Method for Determining Absolute Phosphorylation Stoichiometry Using Bayesian Statistics and Isobaric Labeling. J Proteome Res. 2017 Nov 3;16(11):4217-4226.
14	Large-Scale Reanalysis of Publicly Available HeLa Cell Proteomics Data in the Context of the Human Proteome Project. J Proteome Res. 2018 Dec 7;17(12):4160-4170.
15	An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62.
16	An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas. Cell Rep. 2015 Jun 23;11(11):1834-43.
17	An integrated strategy for highly sensitive phosphoproteome analysis from low micrograms of protein samples. Analyst. 2018 Jul 23;143(15):3693-3701.
18	Synthesizing Signaling Pathways from Temporal Phosphoproteomic Data. Cell Rep. 2018 Sep 25;24(13):3607-3618.
19	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
20	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.
21	Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites. J Proteome Res. 2018 May 4;17(5):1907-1922.
22	A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284.
23	Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 2011 Oct 21;44(2):325-40.
24	New findings on essential amino acids. Cesk Fysiol. 1990;39(1):13-25.

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Detail Information of Post-Translational Modifications

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