Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0099 Transporter Info
Gene Name	SLC15A4
Transporter Name	Peptide transporter 4
Gene ID	121260
UniProt ID	Q8N697

Post-Translational Modification of This DT
Overview ofSLC15A4 Modification Sites with Functional and Structural Information
Sequence	M E G S G G G A G E R A P L L G A R R A A A A A A A A G A F A G R R A A C G A V L L T E L L E R A A F Y G I T S N L V L F L N G A P F C W E G A Q A S E A L L L F M G L T Y L G S P F G G W L A D A R L G R A R A I L L S L A L Y L L G M L A F P L L A A P A T R A A L C G S A R L L N C T A P G P D A A A R C C S P A T F A G L V L V G L G V A T V K A N I T P F G A D Q V K D R G P E A T R R F F N W F Y W S I N L G A I L S L G G I A Y I Q Q N V S F V T G Y A I P T V C V G L A F V V F L C G Q S V F I T K P P D G S A F T D M F K I L T Y S C C S Q K R S G E R Q S N G E G I G V F Q Q S S K Q S L F D S C K M S H G G P F T E E K V E D V K A L V K I V P V F L A L I P Y W T V Y F Q M Q T T Y V L Q S L H L R I P E I S N I T T T P H T L P A A W L T M F D A V L I L L L I P L K D K L V D P I L R R H G L L P S S L K R I A V G M F F V M C S A F A A G I L E S K R L N L V K E K T I N Q T I G N V V Y H A A D L S L W W Q V P Q Y L L I G I S E I F A S I A G L E F A Y S A A P K S M Q S A I M G L F F F F S G V G S F V G S G L L A L V S I K A I G W M S S H T D F G N I N G C Y L N Y Y F F L L A A I Q G A T L L L F L I I S V K Y D H H R D H Q R S R A N G V P T S R R A
PTM type	X-Phosphorylation X-S-nitrosylation X-Ubiquitination X: Amino Acid

Phosphorylation
Serine	9 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC15A4			[1], [2]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	4
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 4 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC15A4			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	274
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 274 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC15A4			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	279
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 279 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC15A4			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	290
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 290 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC15A4			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	291
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 291 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC15A4			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	294
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 294 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC15A4			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	298
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 298 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC15A4			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	302
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 302 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC15A4			[11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	346
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Serine 346 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 SLC15A4			[12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	142
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Threonine 142 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC15A4			[11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	340
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Threonine 340 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC15A4			[11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	341
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Threonine 341 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 SLC15A4			[11]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	342
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC15A4 Tyrosine 342 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 SLC15A4			[13]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	37
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation (-SNO) at SLC15A4 Cystine 37 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 SLC15A4			[14]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	184
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC15A4 Lysine 184 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC15A4			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	272
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC15A4 Lysine 272 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC15A4			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	292
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC15A4 Lysine 292 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC15A4			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	300
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC15A4 Lysine 300 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC15A4			[14], [17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	311
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC15A4 Lysine 311 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC15A4			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	316
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC15A4 Lysine 316 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 SLC15A4			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	342
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC15A4 Tyrosine 342 has the potential to affect its expression or activity.
Valine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC15A4			[20], [21]
Role of PTM	Potential impacts
Modified Residue	Valine	Modified Location	322
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC15A4 Valine 322 has the potential to affect its expression or activity.

References
1	p38-MK2 signaling axis regulates RNA metabolism after UV-light-induced DNA damage. Nat Commun. 2018 Mar 9;9(1):1017.
2	CEP128 Localizes to the Subdistal Appendages of the Mother Centriole and Regulates TGF-beta/BMP Signaling at the Primary Cilium. Cell Rep. 2018 Mar 6;22(10):2584-2592.
3	Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1. EMBO J. 2015 Nov 12;34(22):2840-61.
4	Global phosphoproteome analysis of human bone marrow reveals predictive phosphorylation markers for the treatment of acute myeloid leukemia with quizartinib. Leukemia. 2014 Mar;28(3):716-9.
5	Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
6	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
7	Global quantitative phosphoproteome analysis of human tumor xenografts treated with a CD44 antagonist. Cancer Res. 2012 Sep 1;72(17):4329-39.
8	iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
9	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
10	Quantitative phosphoproteomic analysis identifies novel functional pathways of tumor suppressor DLC1 in estrogen receptor positive breast cancer. PLoS One. 2018 Oct 2;13(10):e0204658.
11	Characterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics. Mol Cell Proteomics. 2013 Dec;12(12):3851-73.
12	Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics. Nat Commun. 2019 Jan 10;10(1):104.
13	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.
14	Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV. Nature. 2021 Jun;594(7862):246-252.
15	A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284.
16	Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 2011 Oct 21;44(2):325-40.
17	UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nat Struct Mol Biol. 2018 Jul;25(7):631-640.
18	Highly Multiplexed Quantitative Mass Spectrometry Analysis of Ubiquitylomes. Cell Syst. 2016 Oct 26;3(4):395-403.e4.
19	Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature. 2013 Apr 18;496(7445):372-6.
20	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
21	Global identification of modular cullin-RING ligase substrates. Cell. 2011 Oct 14;147(2):459-74.

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Detail Information of Post-Translational Modifications

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