Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0130 Transporter Info
Gene Name	SLC1A2
Transporter Name	Excitatory amino acid transporter 2
Gene ID	6506
UniProt ID	P43004

Post-Translational Modification of This DT
Overview ofSLC1A2 Modification Sites with Functional and Structural Information
Sequence	M A S T E G A N N M P K Q V E V R M H D S H L G S E E P K H R H L G L R L C D K L G K N L L L T L T V F G V I L G A V C G G L L R L A S P I H P D V V M L I A F P G D I L M R M L K M L I L P L I I S S L I T G L S G L D A K A S G R L G T R A M V Y Y M S T T I I A A V L G V I L V L A I H P G N P K L K K Q L G P G K K N D E V S S L D A F L D L I R N L F P E N L V Q A C F Q Q I Q T V T K K V L V A P P P D E E A N A T S A V V S L L N E T V T E V P E E T K M V I K K G L E F K D G M N V L G L I G F F I A F G I A M G K M G D Q A K L M V D F F N I L N E I V M K L V I M I M W Y S P L G I A C L I C G K I I A I K D L E V V A R Q L G M Y M V T V I I G L I I H G G I F L P L I Y F V V T R K N P F S F F A G I F Q A W I T A L G T A S S A G T L P V T F R C L E E N L G I D K R V T R F V L P V G A T I N M D G T A L Y E A V A A I F I A Q M N G V V L D G G Q I V T V S L T A T L A S V G A A S I P S A G L V T M L L I L T A V G L P T E D I S L L V A V D W L L D R M R T S V N V V G D S F G A G I V Y H L S K S E L D T I D S Q H R V H E D I E M T K T Q S I Y D D M K N H R E S N S N Q C V Y A A H N S V I V D E C K V T L A A N G K S A D C S V E E E P W K R E K
PTM type	X-N-glycosylation X-Oxidation X-Palmitoylation X-Phosphorylation X-Phosphorylation X-SUMOylation X-SUMOylation X-Ubiquitination X: Amino Acid

N-glycosylation
Asparagine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC1A2			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	206
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC1A2 Asparagine 206 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC1A2			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	216
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC1A2 Asparagine 216 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 SLC1A2			[2]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	38
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC1A2 Cystine 38 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC1A2			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	184
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC1A2 Cystine 184 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC1A2			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	563
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC1A2 Cystine 563 has the potential to affect its expression or activity.
Palmitoylation
Cysteine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Critically Important for the uptake activity of SLC1A2			[4]
Role of PTM	On/Off Switch
Modified Residue	Cysteine	Modified Location	38
Experimental Method	Co-Immunoprecipitation
Detailed Description	Palmitoylation at SLC1A2 Cysteine 38 have been reported to be critically Important for its uptake activity.
Phosphorylation
Serine	11 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC1A2			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	3
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 3 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC1A2			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	21
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 21 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC1A2			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	25
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 25 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC1A2			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	99
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 99 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC1A2			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	100
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 100 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC1A2			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	521
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 521 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC1A2			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	532
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 532 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC1A2			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	534
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 534 has the potential to affect its expression or activity.
PTM Phenomenon9	.			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	560
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 560 has the potential to affect its expression or activity.
PTM Phenomenon10	.			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	560
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 560 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLC1A2			[6], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	564
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Serine 564 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 SLC1A2			[5]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	4
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Threonine 4 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC1A2			[12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	103
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Threonine 103 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 SLC1A2			[13], [14]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	494
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Tyrosine 494 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC1A2			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	523
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Tyrosine 523 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC1A2			[6]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	539
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC1A2 Tyrosine 539 has the potential to affect its expression or activity.
SUMOylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	571
Experimental Method	Co-Immunoprecipitation
Detailed Description	SUMOylation at SLC1A2 Lysine 571 has the potential to affect its expression or activity.
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Enhancing the activity of SLC1A2			[18], [19]
Role of PTM	Protein Activity Modulation
Affected Drug/Substrate	Glutamate	Results for Drug	Increasing uptake of glutamate
Experimental Material(s)	Human astrocytes
Experimental Method	Co-Immunoprecipitation
Detailed Description	SUMOylation at SLC1A2 have been reported to enhance its transport activity.
Ubiquitination
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Decreasing the expression and function of SLC1A2			[20]
Role of PTM	Trafficking to Plasma Membrane
Affected Drug/Substrate	Glutamate	Results for Drug	Decreasing uptake of glutamate
Related Enzyme	NEDD4-binding protein 2-like 2 (N4BP2L2)
Studied Phenotype	Parkinson's disease [ICD11:8A00.0]
Experimental Material(s)	Parkinson's disease model mice
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC1A2 have been reported to decrease its expression and transport function.

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: EAA2_HUMAN)
2	Identifying Functional Cysteine Residues in the Mitochondria. ACS Chem Biol. 2017 Apr 21;12(4):947-957.
3	A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging. Cell. 2020 Mar 5;180(5):968-983.e24.
4	UniProt: the Universal Protein Knowledgebase in 2023. Nucleic Acids Res. 2023 Jan 6;51(D1):D523-D531. (ID: P43004)
5	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
6	Quantitative phosphoproteomics of Alzheimer's disease reveals cross-talk between kinases and small heat shock proteins. Proteomics. 2015 Jan;15(2-3):508-519.
7	Refined phosphopeptide enrichment by phosphate additive and the analysis of human brain phosphoproteome. Proteomics. 2015 Jan;15(2-3):500-7.
8	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
9	Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6.
10	BioMuta and BioXpress: mutation and expression knowledgebases for cancer biomarker discovery. Nucleic Acids Res. 2018;46(D1):D1128-D1136.
11	Defective sphingosine 1-phosphate receptor 1 (S1P1) phosphorylation exacerbates TH17-mediated autoimmune neuroinflammation. Nat Immunol. 2013 Nov;14(11):1166-72.
12	Phosphoproteomics study on the activated PKC-induced cell death. J Proteome Res. 2013 Oct 4;12(10):4280-301.
13	Phosphoproteome resource for systems biology research. Methods Mol Biol. 2011;694:307-22.
14	PhosphoPep--a database of protein phosphorylation sites in model organisms. Nat Biotechnol. 2008 Dec;26(12):1339-40.
15	Neuroblastoma tyrosine kinase signaling networks involve FYN and LYN in endosomes and lipid rafts. PLoS Comput Biol. 2015 Apr 17;11(4):e1004130.
16	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.
17	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
18	Sumoylation of the astroglial glutamate transporter EAAT2 governs its intracellular compartmentalization. Glia. 2014 Aug;62(8):1241-53.
19	Motor neuron impairment mediated by a sumoylated fragment of the glial glutamate transporter EAAT2. Glia. 2011 Nov;59(11):1719-31.
20	Regulation of glutamate transporter trafficking by Nedd4-2 in a Parkinson's disease model. Cell Death Dis. 2017 Feb 2;8(2):e2574.

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Detail Information of Post-Translational Modifications

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