Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0100 Transporter Info
Gene Name	SLC16A1
Transporter Name	Monocarboxylate transporter 1
Gene ID	6566
UniProt ID	P53985

Post-Translational Modification of This DT
Overview ofSLC16A1 Modification Sites with Functional and Structural Information
Sequence	M P P A V G G P V G Y T P P D G G W G W A V V I G A F I S I G F S Y A F P K S I T V F F K E I E G I F H A T T S E V S W I S S I M L A V M Y G G G P I S S I L V N K Y G S R I V M I V G G C L S G C G L I A A S F C N T V Q Q L Y V C I G V I G G L G L A F N L N P A L T M I G K Y F Y K R R P L A N G L A M A G S P V F L C T L A P L N Q V F F G I F G W R G S F L I L G G L L L N C C V A G A L M R P I G P K P T K A G K D K S K A S L E K A G K S G V K K D L H D A N T D L I G R H P K Q E K R S V F Q T I N Q F L D L T L F T H R G F L L Y L S G N V I M F F G L F A P L V F L S S Y G K S Q H Y S S E K S A F L L S I L A F V D M V A R P S M G L V A N T K P I R P R I Q Y F F A A S V V A N G V C H M L A P L S T T Y V G F C V Y A G F F G F A F G W L S S V L F E T L M D L V G P Q R F S S A V G L V T I V E C C P V L L G P P L L G R L N D M Y G D Y K Y T Y W A C G V V L I I S G I Y L F I G M G I N Y R L L A K E Q K A N E Q K K E S K E E E T S I D V A G K P N E V T K A A E S P D Q K D T D G G P K E E E S P V
PTM type	X-Acetylation X-Methylation X-Phosphorylation X-Phosphorylation 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 SLC16A1			[1], [2]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	462
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC16A1 Lysine 462 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC16A1			[1]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	473
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC16A1 Lysine 473 has the potential to affect its expression or activity.
Methylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC16A1			[3]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	494
Experimental Method	Co-Immunoprecipitation
Detailed Description	Methylation at SLC16A1 Lysine 494 has the potential to affect its expression or activity.
Phosphorylation
Serine	12 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	33
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 33 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	33
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 33 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	33
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 33 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC16A1			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	210
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 210 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC16A1			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	213
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 213 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC16A1			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	220
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 220 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC16A1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	244
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 244 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC16A1			[11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	315
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 315 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC16A1			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	461
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 461 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC16A1			[14], [15]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	467
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 467 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLC16A1			[7], [16]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	483
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 483 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence SLC16A1			[12], [16]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	498
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Serine 498 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 SLC16A1			[17]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	41
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Threonine 41 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC16A1			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	231
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Threonine 231 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC16A1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	248
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Threonine 248 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC16A1			[10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	256
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Threonine 256 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC16A1			[10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	259
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Threonine 259 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC16A1			[14], [15]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	466
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Threonine 466 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC16A1			[20], [21]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	478
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Threonine 478 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC16A1			[5], [20]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	489
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Threonine 489 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 SLC16A1			[17]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	11
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Tyrosine 11 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[4]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	34
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Tyrosine 34 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[4]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	34
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Tyrosine 34 has the potential to affect its expression or activity.
PTM Phenomenon4	.			[4]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	34
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A1 Tyrosine 34 has the potential to affect its expression or activity.
Ubiquitination
Lysine	9 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[22]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	204
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 204 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC16A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	216
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 216 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC16A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	224
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 224 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC16A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	459
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 459 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC16A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	462
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 462 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC16A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	473
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 473 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC16A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	479
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 479 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC16A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	487
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 487 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC16A1			[23], [24]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	494
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A1 Lysine 494 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	Large-scale global identification of protein lysine methylation in vivo. Epigenetics. 2013 May;8(5):477-85.
4	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
5	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
6	An orthogonal proteomic survey uncovers novel Zika virus host factors. Nature. 2018 Sep;561(7722):253-257.
7	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
8	An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas. Cell Rep. 2015 Jun 23;11(11):1834-43.
9	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
10	System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3.
11	The Plk1-dependent phosphoproteome of the early mitotic spindle. Mol Cell Proteomics. 2011 Jan;10(1):M110.004457.
12	Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
13	Quantitative Phosphoproteome Analysis of Clostridioides difficile Toxin B Treated Human Epithelial Cells. Front Microbiol. 2018 Dec 17;9:3083.
14	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.
15	Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics. Nat Commun. 2019 Jan 10;10(1):104.
16	The Global Phosphorylation Landscape of SARS-CoV-2 Infection. Cell. 2020 Aug 6;182(3):685-712.e19.
17	Inhibition of DDR1-BCR signalling by nilotinib as a new therapeutic strategy for metastatic colorectal cancer. EMBO Mol Med. 2018 Apr;10(4):e7918.
18	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.
19	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
20	Comparative phosphoproteomic analysis reveals signaling networks regulating monopolar and bipolar cytokinesis. Sci Rep. 2018 Feb 2;8(1):2269.
21	Phosphoproteins in extracellular vesicles as candidate markers for breast cancer. Proc Natl Acad Sci U S A. 2017 Mar 21;114(12):3175-3180.
22	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
23	Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 2011 Oct 21;44(2):325-40.
24	Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin. J Proteome Res. 2012 Feb 3;11(2):796-807.

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Detail Information of Post-Translational Modifications

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