Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0231 Transporter Info
Gene Name	SLC26A3
Transporter Name	Chloride anion exchanger
Gene ID	1811
UniProt ID	P40879

Post-Translational Modification of This DT
Overview ofSLC26A3 Modification Sites with Functional and Structural Information
Sequence	M I E P F G N Q Y I V A R P V Y S T N A F E E N H K K T G R H H K T F L D H L K V C C S C S P Q K A K R I V L S L F P I A S W L P A Y R L K E W L L S D I V S G I S T G I V A V L Q G L A F A L L V D I P P V Y G L Y A S F F P A I I Y L F F G T S R H I S V G P F P I L S M M V G L A V S G A V S K A V P D R N A T T L G L P N N S N N S S L L D D E R V R V A A A A S V T V L S G I I Q L A F G I L R I G F V V I Y L S E S L I S G F T T A A A V H V L V S Q L K F I F Q L T V P S H T D P V S I F K V L Y S V F S Q I E K T N I A D L V T A L I V L L V V S I V K E I N Q R F K D K L P V P I P I E F I M T V I A A G V S Y G C D F K N R F K V A V V G D M N P G F Q P P I T P D V E T F Q N T V G D C F G I A M V A F A V A F S V A S V Y S L K Y D Y P L D G N Q E L I A L G L G N I V C G V F R G F A G S T A L S R S A V Q E S T G G K T Q I A G L I G A I I V L I V V L A I G F L L A P L Q K S V L A A L A L G N L K G M L M Q F A E I G R L W R K D K Y D C L I W I M T F I F T I V L G L G L G L A A S V A F Q L L T I V F R T Q F P K C S T L A N I G R T N I Y K N K K D Y Y D M Y E P E G V K I F R C P S P I Y F A N I G F F R R K L I D A V G F S P L R I L R K R N K A L R K I R K L Q K Q G L L Q V T P K G F I C T V D T I K D S D E E L D N N Q I E V L D Q P I N T T D L P F H I D W N D D L P L N I E V P K I S L H S L I L D F S A V S F L D V S S V R G L K S I L Q E F I R I K V D V Y I V G T D D D F I E K L N R Y E F F D G E V K S S I F F L T I H D A V L H I L M K K D Y S T S K F N P S Q E K D G K I D F T I N T N G G L R N R V Y E V P V E T K F
PTM type	X-N-glycosylation X-Phosphorylation X-Phosphorylation X: Amino Acid

N-glycosylation
Asparagine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Critically important for effective cell surface expression of SLC26A3 and protects it from degradation by proteases			[1]
Role of PTM	Degradation via Proteosome
Modified Residue	Asparagine	Modified Location	165
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-glycosylation at SLC26A3 Asparagine 165 have been reported to be critically important for its effective cell surface expression and protects it from degradation by proteases.
PTM Phenomenon2	Increasing the cell surface expression of SLC26A3			[1]
Role of PTM	Surface Expression Modulation
Modified Residue	Asparagine	Modified Location	153
Experimental Material(s)	Chinese hamster ovary (CHO) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-glycosylation at SLC26A3 Asparagine 153 have been reported to increase its cell surface expression.
PTM Phenomenon3	Increasing the cell surface expression of SLC26A3			[1]
Role of PTM	Surface Expression Modulation
Modified Residue	Asparagine	Modified Location	161
Experimental Material(s)	Chinese hamster ovary (CHO) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-glycosylation at SLC26A3 Asparagine 161 have been reported to increase its cell surface expression.
Phosphorylation
Serine	7 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC26A3			[2]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	242
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Serine 242 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC26A3			[2]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	362
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Serine 362 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC26A3			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	509
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Serine 509 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC26A3			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	563
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Serine 563 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC26A3			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	727
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Serine 727 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC26A3			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	729
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Serine 729 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC26A3			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	734
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Serine 734 has the potential to affect its expression or activity.
Threonine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC26A3			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	503
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Threonine 503 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC26A3			[5]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	728
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Threonine 728 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC26A3			[6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	744
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Threonine 744 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC26A3			[6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	747
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Threonine 747 has the potential to affect its expression or activity.
Tyrosine	5 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC26A3			[7]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	9
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Tyrosine 9 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC26A3			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	520
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Tyrosine 520 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[8]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	526
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Tyrosine 526 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC26A3			[5]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	726
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Tyrosine 726 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC26A3			[9]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	756
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A3 Tyrosine 756 has the potential to affect its expression or activity.

References
1	Role of N-glycosylation in cell surface expression and protection against proteolysis of the intestinal anion exchanger SLC26A3. Am J Physiol Cell Physiol. 2012 Mar 1;302(5):C781-95.
2	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.
3	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
4	ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6.
5	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.
6	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
7	Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder. Nat Chem Biol. 2016 Nov;12(11):959-966.
8	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
9	Phosphotyrosine-based-phosphoproteomics scaled-down to biopsy level for analysis of individual tumor biology and treatment selection. J Proteomics. 2017 Jun 6;162:99-107.

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Detail Information of Post-Translational Modifications

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