Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0119 Transporter Info
Gene Name	SLC17A6
Transporter Name	Vesicular glutamate transporter 2
Gene ID	57084
UniProt ID	Q9P2U8

Post-Translational Modification of This DT
Overview ofSLC17A6 Modification Sites with Functional and Structural Information
Sequence	M E S V K Q R I L A P G K E G L K N F A G K S L G Q I Y R V L E K K Q D T G E T I E L T E D G K P L E V P E R K A P L C D C T C F G L P R R Y I I A I M S G L G F C I S F G I R C N L G V A I V D M V N N S T I H R G G K V I K E K A K F N W D P E T V G M I H G S F F W G Y I I T Q I P G G Y I A S R L A A N R V F G A A I L L T S T L N M L I P S A A R V H Y G C V I F V R I L Q G L V E G V T Y P A C H G I W S K W A P P L E R S R L A T T S F C G S Y A G A V I A M P L A G I L V Q Y T G W S S V F Y V Y G S F G M V W Y M F W L L V S Y E S P A K H P T I T D E E R R Y I E E S I G E S A N L L G A M E K F K T P W R K F F T S M P V Y A I I V A N F C R S W T F Y L L L I S Q P A Y F E E V F G F E I S K V G M L S A V P H L V M T I I V P I G G Q I A D F L R S K Q I L S T T T V R K I M N C G G F G M E A T L L L V V G Y S H T R G V A I S F L V L A V G F S G F A I S G F N V N H L D I A P R Y A S I L M G I S N G V G T L S G M V C P I I V G A M T K N K S R E E W Q Y V F L I A A L V H Y G G V I F Y A I F A S G E K Q P W A D P E E T S E E K C G F I H E D E L D E E T G D I T Q N Y I N Y G T T K S Y G A T T Q A N G G W P S G W E K K E E F V Q G E V Q D S H S Y K D R V D Y S
PTM type	X-N-glycosylation X-Oxidation X-Phosphorylation X-S-nitrosylation X-Ubiquitination X: Amino Acid

N-glycosylation
Asparagine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC17A6			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	100
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC17A6 Asparagine 100 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC17A6			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	101
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC17A6 Asparagine 101 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC17A6			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	470
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC17A6 Asparagine 470 has the potential to affect its expression or activity.
Oxidation
Cystine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC17A6			[2]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	179
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC17A6 Cystine 179 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC17A6			[2]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	198
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC17A6 Cystine 198 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC17A6			[2]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	516
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC17A6 Cystine 516 has the potential to affect its expression or activity.
Phosphorylation
Serine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC17A6			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	163
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC17A6 Serine 163 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC17A6			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	171
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC17A6 Serine 171 has the potential to affect its expression or activity.
Threonine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC17A6			[3]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	162
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC17A6 Threonine 162 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC17A6			[3]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	164
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC17A6 Threonine 164 has the potential to affect its expression or activity.
Tyrosine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC17A6			[4]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	177
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC17A6 Tyrosine 177 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC17A6			[5]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	281
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC17A6 Tyrosine 281 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC17A6			[6]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	405
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC17A6 Tyrosine 405 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 SLC17A6			[7]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	179
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation (-SNO) at SLC17A6 Cystine 179 has the potential to affect its expression or activity.
Ubiquitination
Lysine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[8]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	109
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC17A6 Lysine 109 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[8]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	109
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC17A6 Lysine 109 has the potential to affect its expression or activity.

References
1	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: VGLU2_HUMAN)
2	A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging. Cell. 2020 Mar 5;180(5):968-983.e24.
3	Quantitative analysis of a phosphoproteome readily altered by the protein kinase CK2 inhibitor quinalizarin in HEK-293T cells. Biochim Biophys Acta. 2015 Jun;1854(6):609-23.
4	Quantitative analysis of signaling networks across differentially embedded tumors highlights interpatient heterogeneity in human glioblastoma. J Proteome Res. 2014 Nov 7;13(11):4581-93.
5	Phospho-proteomic analysis of mantle cell lymphoma cells suggests a pro-survival role of B-cell receptor signaling. Cell Oncol (Dordr). 2011 Apr;34(2):141-53.
6	iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
7	MDD-SOH: exploiting maximal dependence decomposition to identify S-sulfenylation sites with substrate motifs. Bioinformatics. 2016 Jan 15;32(2):165-72.
8	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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