Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0469 Transporter Info
Gene Name	SLC7A3
Transporter Name	Cationic amino acid transporter 3
Gene ID	84889
UniProt ID	Q8WY07

Post-Translational Modification of This DT
Overview ofSLC7A3 Modification Sites with Functional and Structural Information
Sequence	M P W Q A F R R F G Q K L V R R R T L E S G M A E T R L A R C L S T L D L V A L G V G S T L G A G V Y V L A G E V A K D K A G P S I V I C F L V A A L S S V L A G L C Y A E F G A R V P R S G S A Y L Y S Y V T V G E L W A F T T G W N L I L S Y V I G T A S V A R A W S S A F D N L I G N H I S K T L Q G S I A L H V P H V L A E Y P D F F A L G L V L L L T G L L A L G A S E S A L V T K V F T G V N L L V L G F V M I S G F V K G D V H N W K L T E E D Y E L A M A E L N D T Y S L G P L G S G G F V P F G F E G I L R G A A T C F Y A F V G F D C I A T T G E E A Q N P Q R S I P M G I V I S L S V C F L A Y F A V S S A L T L M M P Y Y Q L Q P E S P L P E A F L Y I G W A P A R Y V V A V G S L C A L S T S L L G S M F P M P R V I Y A M A E D G L L F R V L A R I H T G T R T P I I A T V V S G I I A A F M A F L F K L T D L V D L M S I G T L L A Y S L V S I C V L I L R Y Q P D Q E T K T G E E V E L Q E E A I T T E S E K L T L W G L F F P L N S I P T P L S G Q I V Y V C S S L L A V L L T A L C L V L A Q W S V P L L S G D L L W T A V V V L L L L L I I G I I V V I W R Q P Q S S T P L H F K V P A L P L L P L M S I F V N I Y L M M Q M T A G T W A R F G V W M L I G F A I Y F G Y G I Q H S L E E I K S N Q P S R K S R A K T V D L D P G T L Y V H S V
PTM type	X-N-glycosylation 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 SLC7A3			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	232
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC7A3 Asparagine 232 has the potential to affect its expression or activity.
Phosphorylation
Serine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC7A3			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	618
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC7A3 Serine 618 has the potential to affect its expression or activity.
Threonine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC7A3			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	18
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC7A3 Threonine 18 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC7A3			[2], [6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	606
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC7A3 Threonine 606 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC7A3			[3]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	613
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC7A3 Threonine 613 has the potential to affect its expression or activity.
Tyrosine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC7A3			[3]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	615
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC7A3 Tyrosine 615 has the potential to affect its expression or activity.
Ubiquitination
Lysine	8 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[7]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	601
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC7A3 Lysine 601 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[8]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	605
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC7A3 Lysine 605 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[8]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	605
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC7A3 Lysine 605 has the potential to affect its expression or activity.
PTM Phenomenon4	.			[8]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	605
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC7A3 Lysine 605 has the potential to affect its expression or activity.
PTM Phenomenon5	.			[8]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	605
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC7A3 Lysine 605 has the potential to affect its expression or activity.
PTM Phenomenon6	.			[7]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	605
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC7A3 Lysine 605 has the potential to affect its expression or activity.
PTM Phenomenon7	.			[8]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	605
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC7A3 Lysine 605 has the potential to affect its expression or activity.
PTM Phenomenon8	.			[8]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	605
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC7A3 Lysine 605 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: CTR3_HUMAN)
2	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
3	An integrated strategy for highly sensitive phosphoproteome analysis from low micrograms of protein samples. Analyst. 2018 Jul 23;143(15):3693-3701.
4	Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1. EMBO J. 2015 Nov 12;34(22):2840-61.
5	Comprehensive quantitative comparison of the membrane proteome, phosphoproteome, and sialiome of human embryonic and neural stem cells. Mol Cell Proteomics. 2014 Jan;13(1):311-28.
6	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
7	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
8	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.

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Detail Information of Post-Translational Modifications

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