Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0429 Transporter Info
Gene Name	SLC5A9
Transporter Name	Sodium/glucose cotransporter 4
Gene ID	200010
UniProt ID	Q2M3M2

Post-Translational Modification of This DT
Overview ofSLC5A9 Modification Sites with Functional and Structural Information
Sequence	M S K E L A A M G P G A S G D G V R T E T A P H I A L D S R V G L H A Y D I S V V V I Y F V F V I A V G I W S S I R A S R G T I G G Y F L A G R S M S W W P I G A S L M S S N V G S G L F I G L A G T G A A G G L A V G G F E W N A T W L L L A L G W V F V P V Y I A A G V V T M P Q Y L K K R F G G Q R I Q V Y M S V L S L I L Y I F T K I S T D I F S G A L F I Q M A L G W N L Y L S T G I L L V V T A V Y T I A G G L M A V I Y T D A L Q T V I M V G G A L V L M F L G F Q D V G W Y P G L E Q R Y R Q A I P N V T V P N T T C H L P R P D A F H I L R D P V S G D I P W P G L I F G L T V L A T W C W C T D Q V I V Q R S L S A K S L S H A K G G S V L G G Y L K I L P M F F I V M P G M I S R A L F P D E V G C V D P D V C Q R I C G A R V G C S N I A Y P K L V M A L M P V G L R G L M I A V I M A A L M S S L T S I F N S S S T L F T I D V W Q R F R R K S T E Q E L M V V G R V F V V F L V V I S I L W I P I I Q S S N S G Q L F D Y I Q A V T S Y L A P P I T A L F L L A I F C K R V T E P G A F W G L V F G L G V G L L R M I L E F S Y P A P A C G E V D R R P A V L K D F H Y L Y F A I L L C G L T A I V I V I V S L C T T P I P E E Q L T R L T W W T R N C P L S E L E K E A H E S T P E I S E R P A G E C P A G G G A A E N S S L G Q E Q P E A P S R S W G K L L W S W F C G L S G T P E Q A L S P A E K A A L E Q K L T S I E E E P L W R H V C N I N A V L L L A I N I F L W G Y F A
PTM type	X-N-glycosylation X-Oxidation X-Phosphorylation 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 SLC5A9			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	251
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC5A9 Asparagine 251 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 SLC5A9			[2]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	365
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC5A9 Cystine 365 has the potential to affect its expression or activity.
Phosphorylation
Serine	6 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC5A9			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	2
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Serine 2 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC5A9			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	13
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Serine 13 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC5A9			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	582
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Serine 582 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC5A9			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	587
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Serine 587 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC5A9			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	604
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Serine 604 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC5A9			[6], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	605
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Serine 605 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 SLC5A9			[3]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	21
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Threonine 21 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC5A9			[9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	253
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Threonine 253 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC5A9			[9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	257
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Threonine 257 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC5A9			[9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	258
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Threonine 258 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC5A9			[5]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	583
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC5A9 Threonine 583 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: SC5A9_HUMAN)
2	A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging. Cell. 2020 Mar 5;180(5):968-983.e24.
3	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.
4	A large-scale quantitative proteomic approach to identifying sulfur mustard-induced protein phosphorylation cascades. Chem Res Toxicol. 2010 Jan;23(1):20-5.
5	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
6	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
7	TiO2 with Tandem Fractionation (TAFT): An Approach for Rapid, Deep, Reproducible, and High-Throughput Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):710-721.
8	A fast sample processing strategy for large-scale profiling of human urine phosphoproteome by mass spectrometry. Talanta. 2018 Aug 1;185:166-173.
9	Phosphoproteomics reveals ALK promote cell progress via RAS/ JNK pathway in neuroblastoma. Oncotarget. 2016 Nov 15;7(46):75968-75980.

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Detail Information of Post-Translational Modifications

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