Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0395 Transporter Info
Gene Name	SLC52A3
Transporter Name	Riboflavin transporter 2
Gene ID	113278
UniProt ID	Q9NQ40

Post-Translational Modification of This DT
Overview ofSLC52A3 Modification Sites with Functional and Structural Information
Sequence	M A F L M H L L V C V F G M G S W V T I N G L W V E L P L L V M E L P E G W Y L P S Y L T V V I Q L A N I G P L L V T L L H H F R P S C L S E V P I I F T L L G V G T V T C I I F A F L W N M T S W V L D G H H S I A F L V L T F F L A L V D C T S S V T F L P F M S R L P T Y Y L T T F F V G E G L S G L L P A L V A L A Q G S G L T T C V N V T E I S D S V P S P V P T R E T D I A Q G V P R A L V S A L P G M E A P L S H L E S R Y L P A H F S P L V F F L L L S I M M A C C L V A F F V L Q R Q P R C W E A S V E D L L N D Q V T L H S I R P R E E N D L G P A G T V D S S Q G Q G Y L E E K A A P C C P A H L A F I Y T L V A F V N A L T N G M L P S V Q T Y S C L S Y G P V A Y H L A A T L S I V A N P L A S L V S M F L P N R S L L F L G V L S V L G T C F G G Y N M A M A V M S P C P L L Q G H W G G E V L I V A S W V L F S G C L S Y V K V M L G V V L R D L S R S A L L W C G A A V Q L G S L L G A L L M F P L V N V L R L F S S A D F C N L H C P A
PTM type	X-Disulfide bond X-N-glycosylation X-Phosphorylation X-Phosphorylation X: Amino Acid

Disulfide bond
Cystine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC52A3			[1]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	386
Experimental Method	Co-Immunoprecipitation
Detailed Description	Disulfide bond (-SSR) at SLC52A3 Cystine 386 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC52A3			[1]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	463
Experimental Method	Co-Immunoprecipitation
Detailed Description	Disulfide bond (-SSR) at SLC52A3 Cystine 463 has the potential to affect its expression or activity.
N-glycosylation
Asparagine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC52A3			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	94
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC52A3 Asparagine 94 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC52A3			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	168
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC52A3 Asparagine 168 has the potential to affect its expression or activity.
Phosphorylation
Serine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC52A3			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	251
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC52A3 Serine 251 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	264
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC52A3 Serine 264 has the potential to affect its expression or activity.
Threonine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[5]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	261
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC52A3 Threonine 261 has the potential to affect its expression or activity.

References
1	iCysMod: an integrative database for protein cysteine modifications in eukaryotes. Brief Bioinform. 2021 Sep 2;22(5):bbaa400. (ID: Q9NQ40)
2	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: S52A3_HUMAN)
3	Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
4	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
5	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.

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Detail Information of Post-Translational Modifications

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