Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0230 Transporter Info
Gene Name	SLC26A2
Transporter Name	Sulfate transporter
Gene ID	1836
UniProt ID	P50443

Post-Translational Modification of This DT
Overview ofSLC26A2 Modification Sites with Functional and Structural Information
Sequence	M S S E S K E Q H N V S P R D S A E G N D S Y P S G I H L E L Q R E S S T D F K Q F E T N D Q C R P Y H R I L I E R Q E K S D T N F K E F V I K K L Q K N C Q C S P A K A K N M I L G F L P V L Q W L P K Y D L K K N I L G D V M S G L I V G I L L V P Q S I A Y S L L A G Q E P V Y G L Y T S F F A S I I Y F L L G T S R H I S V G I F G V L C L M I G E T V D R E L Q K A G Y D N A H S A P S L G M V S N G S T L L N H T S D R I C D K S C Y A I M V G S T V T F I A G V Y Q V A M G F F Q V G F V S V Y L S D A L L S G F V T G A S F T I L T S Q A K Y L L G L N L P R T N G V G S L I T T W I H V F R N I H K T N L C D L I T S L L C L L V L L P T K E L N E H F K S K L K A P I P I E L V V V V A A T L A S H F G K L H E N Y N S S I A G H I P T G F M P P K V P E W N L I P S V A V D A I A I S I I G F A I T V S L S E M F A K K H G Y T V K A N Q E M Y A I G F C N I I P S F F H C F T T S A A L A K T L V K E S T G C H T Q L S G V V T A L V L L L V L L V I A P L F Y S L Q K S V L G V I T I V N L R G A L R K F R D L P K M W S I S R M D T V I W F V T M L S S A L L S T E I G L L V G V C F S I F C V I L R T Q K P K S S L L G L V E E S E V F E S V S A Y K N L Q I K P G I K I F R F V A P L Y Y I N K E C F K S A L Y K Q T V N P I L I K V A W K K A A K R K I K E K V V T L G G I Q D E M S V Q L S H D P L E L H T I V I D C S A I Q F L D T A G I H T L K E V R R D Y E A I G I Q V L L A Q C N P T V R D S L T N G E Y C K K E E E N L L F Y S V Y E A M A F A E V S K N Q K G V C V P N G L S L S S D
PTM type	X-N-glycosylation X-Oxidation X-Phosphorylation 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 SLC26A2			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	199
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC26A2 Asparagine 199 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC26A2			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	205
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC26A2 Asparagine 205 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC26A2			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	357
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC26A2 Asparagine 357 has the potential to affect its expression or activity.
Oxidation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC26A2			[2]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	212
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC26A2 Cystine 212 has the potential to affect its expression or activity.
Phosphorylation
Serine	14 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC26A2			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	2
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 2 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC26A2			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	3
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 3 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC26A2			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	5
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 5 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC26A2			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	12
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 12 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC26A2			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	16
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 16 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC26A2			[4], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	22
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 22 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC26A2			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	25
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 25 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC26A2			[4], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	35
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 35 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC26A2			[4], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	36
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 36 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC26A2			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	506
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 506 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLC26A2			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	508
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 508 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence SLC26A2			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	735
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 735 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence SLC26A2			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	737
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 737 has the potential to affect its expression or activity.
PTM Phenomenon14	Have the potential to influence SLC26A2			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	738
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Serine 738 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 SLC26A2			[8], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	37
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Threonine 37 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC26A2			[3], [12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	44
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Threonine 44 has the potential to affect its expression or activity.
Tyrosine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC26A2			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	23
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Tyrosine 23 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC26A2			[13], [14]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	51
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC26A2 Tyrosine 51 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 SLC26A2			[15]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	6
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC26A2 Lysine 6 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC26A2			[13], [16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	40
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC26A2 Lysine 40 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC26A2			[16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	67
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC26A2 Lysine 67 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC26A2			[16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	596
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC26A2 Lysine 596 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC26A2			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	601
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC26A2 Lysine 601 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC26A2			[16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	726
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC26A2 Lysine 726 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: S26A2_HUMAN)
2	Identifying Functional Cysteine Residues in the Mitochondria. ACS Chem Biol. 2017 Apr 21;12(4):947-957.
3	Phosphoproteomic analysis identifies the tumor suppressor PDCD4 as a RSK substrate negatively regulated by 14-3-3. Proc Natl Acad Sci U S A. 2014 Jul 22;111(29):E2918-27.
4	Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
5	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
6	Phosphoproteomic-based kinase profiling early in influenza virus infection identifies GRK2 as antiviral drug target. Nat Commun. 2018 Sep 11;9(1):3679.
7	A Methodological Assessment and Characterization of Genetically-Driven Variation in Three Human Phosphoproteomes. Sci Rep. 2018 Aug 14;8(1):12106.
8	Phosphoproteomic screening identifies physiological substrates of the CDKL5 kinase. EMBO J. 2018 Dec 14;37(24):e99559.
9	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.
10	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
11	Integrated Proteomics Reveals Apoptosis-related Mechanisms Associated with Placental Malaria. Mol Cell Proteomics. 2019 Feb;18(2):182-199.
12	Reactive Oxygen Species (ROS)-Activated ATM-Dependent Phosphorylation of Cytoplasmic Substrates Identified by Large-Scale Phosphoproteomics Screen. Mol Cell Proteomics. 2016 Mar;15(3):1032-47.
13	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
14	Akt-RSK-S6 kinase signaling networks activated by oncogenic receptor tyrosine kinases. Sci Signal. 2010 Aug 24;3(136):ra64.
15	Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV. Nature. 2021 Jun;594(7862):246-252.
16	UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nat Struct Mol Biol. 2018 Jul;25(7):631-640.

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Detail Information of Post-Translational Modifications

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