Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0258 Transporter Info
Gene Name	SLC2A3
Transporter Name	Glucose transporter type 3, brain
Gene ID	6515
UniProt ID	P11169

Post-Translational Modification of This DT
Overview ofSLC2A3 Modification Sites with Functional and Structural Information
Sequence	M G T Q K V T P A L I F A I T V A T I G S F Q F G Y N T G V I N A P E K I I K E F I N K T L T D K G N A P P S E V L L T S L W S L S V A I F S V G G M I G S F S V G L F V N R F G R R N S M L I V N L L A V T G G C F M G L C K V A K S V E M L I L G R L V I G L F C G L C T G F V P M Y I G E I S P T A L R G A F G T L N Q L G I V V G I L V A Q I F G L E F I L G S E E L W P L L L G F T I L P A I L Q S A A L P F C P E S P R F L L I N R K E E E N A K Q I L Q R L W G T Q D V S Q D I Q E M K D E S A R M S Q E K Q V T V L E L F R V S S Y R Q P I I I S I V L Q L S Q Q L S G I N A V F Y Y S T G I F K D A G V Q E P I Y A T I G A G V V N T I F T V V S L F L V E R A G R R T L H M I G L G G M A F C S T L M T V S L L L K D N Y N G M S F V C I G A I L V F V A F F E I G P G P I P W F I V A E L F S Q G P R P A A M A V A G C S N W T S N F L V G L L F P S A A H Y L G A Y V F I I F T G F L I T F L A F T F F K V P E T R G R T F E D I T R A F E G Q A H G A D R S G K D G V M E M N S I E P A K E T T T N V
PTM type	X-N-glycosylation X-Phosphorylation X-Phosphorylation X-Ubiquitination X: Amino Acid

N-glycosylation
Asparagine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC2A3			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	43
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC2A3 Asparagine 43 has the potential to affect its expression or activity.
Phosphorylation
Serine	7 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC2A3			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	236
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Serine 236 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC2A3			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	246
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Serine 246 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC2A3			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	250
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Serine 250 has the potential to affect its expression or activity.
PTM Phenomenon4	.			[7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	352
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Serine 352 has the potential to affect its expression or activity.
PTM Phenomenon5	.			[7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	352
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Serine 352 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC2A3			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	475
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Serine 475 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC2A3			[3], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	485
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Serine 485 has the potential to affect its expression or activity.
Threonine	5 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC2A3			[3], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	232
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Threonine 232 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[7]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	333
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Threonine 333 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC2A3			[8], [12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	492
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Threonine 492 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC2A3			[8], [12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	493
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Threonine 493 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC2A3			[8], [12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	494
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A3 Threonine 494 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 SLC2A3			[6], [13]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	217
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC2A3 Lysine 217 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC2A3			[14], [15]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	223
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC2A3 Lysine 223 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC2A3			[6], [14]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	243
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC2A3 Lysine 243 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC2A3			[6], [13]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	253
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC2A3 Lysine 253 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC2A3			[16], [17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	477
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC2A3 Lysine 477 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC2A3			[14], [16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	490
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC2A3 Lysine 490 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: GTR3_HUMAN)
2	Phosphoproteins in extracellular vesicles as candidate markers for breast cancer. Proc Natl Acad Sci U S A. 2017 Mar 21;114(12):3175-3180.
3	Phosphoproteomic and Functional Analyses Reveal Sperm-specific Protein Changes Downstream of Kappa Opioid Receptor in Human Spermatozoa. Mol Cell Proteomics. 2019 Mar 15;18(Suppl 1):S118-S131.
4	Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res. 2013 Jun 7;12(6):2414-21.
5	System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3.
6	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
7	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
8	Temporal quantitative phosphoproteomics of ADP stimulation reveals novel central nodes in platelet activation and inhibition. Blood. 2017 Jan 12;129(2):e1-e12.
9	Global Analyses of Selective Insulin Resistance in Hepatocytes Caused by Palmitate Lipotoxicity. Mol Cell Proteomics. 2018 May;17(5):836-849.
10	Actionable Cytopathogenic Host Responses of Human Alveolar Type 2 Cells to SARS-CoV-2. Mol Cell. 2020 Dec 17;80(6):1104-1122.e9.
11	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
12	Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71.
13	Global identification of modular cullin-RING ligase substrates. Cell. 2011 Oct 14;147(2):459-74.
14	UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nat Struct Mol Biol. 2018 Jul;25(7):631-640.
15	Integrative Analysis of Proteome and Ubiquitylome Reveals Unique Features of Lysosomal and Endocytic Pathways in Gefitinib-Resistant Non-Small Cell Lung Cancer Cells. Proteomics. 2018 Aug;18(15):e1700388.
16	Global Landscape and Dynamics of Parkin and USP30-Dependent Ubiquitylomes in iNeurons during Mitophagic Signaling. Mol Cell. 2020 Mar 5;77(5):1124-1142.e10.
17	Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV. Nature. 2021 Jun;594(7862):246-252.

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Detail Information of Post-Translational Modifications

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