Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0110 Transporter Info
Gene Name	SLC16A6
Transporter Name	Monocarboxylate transporter 7
Gene ID	9120
UniProt ID	O15403

Post-Translational Modification of This DT
Overview ofSLC16A6 Modification Sites with Functional and Structural Information
Sequence	M T Q N K L K L C S K A N V Y T E V P D G G W G W A V A V S F F F V E V F T Y G I I K T F G V F F N D L M D S F N E S N S R I S W I I S I C V F V L T F S A P L A T V L S N R F G H R L V V M L G G L L V S T G M V A A S F S Q E V S H M Y V A I G I I S G L G Y C F S F L P T V T I L S Q Y F G K R R S I V T A V A S T G E C F A V F A F A P A I M A L K E R I G W R Y S L L F V G L L Q L N I V I F G A L L R P I F I R G P A S P K I V I Q E N R K E A Q Y M L E N E K T R T S I D S I D S G V E L T T S P K N V P T H T N L E L E P K A D M Q Q V L V K T S P R P S E K K A P L L D F S I L K E K S F I C Y A L F G L F A T L G F F A P S L Y I I P L G I S L G I D Q D R A A F L L S T M A I A E V F G R I G A G F V L N R E P I R K I Y I E L I C V I L L T V S L F A F T F A T E F W G L M S C S I F F G F M V G T I G G T H I P L L A E D D V V G I E K M S S A A G V Y I F I Q S I A G L A G P P L A G L L V D Q S K I Y S R A F Y S C A A G M A L A A V C L A L V R P C K M G L C Q H H H S G E T K V V S H R G K T L Q D I P E D F L E M D L A K N E H R V H V Q M E P V
PTM type	X-Acetylation X-Phosphorylation X-Ubiquitination X: Amino Acid

Acetylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC16A6			[1]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	220
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC16A6 Lysine 220 has the potential to affect its expression or activity.
Phosphorylation
Serine	10 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC16A6			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	234
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 234 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC16A6			[2], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	237
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 237 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC16A6			[2], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	240
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 240 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC16A6			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	247
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 247 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC16A6			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	273
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 273 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC16A6			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	277
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 277 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC16A6			[7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	287
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 287 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC16A6			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	312
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 312 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC16A6			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	451
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 451 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC16A6			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	456
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Serine 456 has the potential to affect its expression or activity.
Threonine	7 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC16A6			[3], [9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	231
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Threonine 231 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC16A6			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	233
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Threonine 233 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC16A6			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	245
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Threonine 245 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC16A6			[9], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	246
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Threonine 246 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC16A6			[9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	253
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Threonine 253 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC16A6			[9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	255
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Threonine 255 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC16A6			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	272
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Threonine 272 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 SLC16A6			[11], [12]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	224
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Tyrosine 224 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC16A6			[8]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	314
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Tyrosine 314 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC16A6			[8]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	450
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Tyrosine 450 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC16A6			[8]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	455
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC16A6 Tyrosine 455 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	.			[13]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	212
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A6 Lysine 212 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[13]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	230
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A6 Lysine 230 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[13]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	249
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A6 Lysine 249 has the potential to affect its expression or activity.
PTM Phenomenon4	.			[13]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	511
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC16A6 Lysine 511 has the potential to affect its expression or activity.

References
1	Monoclonal antibody cocktail as an enrichment tool for acetylome analysis. Anal Chem. 2011 May 15;83(10):3623-6.
2	Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
3	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
4	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
5	Identification of Candidate Casein Kinase 2 Substrates in Mitosis by Quantitative Phosphoproteomics. Front Cell Dev Biol. 2017 Nov 22;5:97.
6	Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells. Sci Signal. 2011 Jun 28;4(179):rs5.
7	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.
8	An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas. Cell Rep. 2015 Jun 23;11(11):1834-43.
9	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
10	Feasibility of label-free phosphoproteomics and application to base-line signaling of colorectal cancer cell lines. J Proteomics. 2015 Sep 8;127(Pt B):247-58.
11	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.
12	Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder. Nat Chem Biol. 2016 Nov;12(11):959-966.
13	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.

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Detail Information of Post-Translational Modifications

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