Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0155 Transporter Info
Gene Name	SLC22B3
Transporter Name	Synaptic vesicle glycoprotein 2C
Gene ID	22987
UniProt ID	Q496J9

Post-Translational Modification of This DT
Overview ofSLC22B3 Modification Sites with Functional and Structural Information
Sequence	M E D S Y K D R T S L M K G A K D I A R E V K K Q T V K K V N Q A V D R A Q D E Y T Q R S Y S R F Q D E E D D D D Y Y P A G E T Y N G E A N D D E G S S E A T E G H D E D D E I Y E G E Y Q G I P S M N Q A K D S I V S V G Q P K G D E Y K D R R E L E S E R R A D E E E L A Q Q Y E L I I Q E C G H G R F Q W A L F F V L G M A L M A D G V E V F V V G F V L P S A E T D L C I P N S G S G W L G S I V Y L G M M V G A F F W G G L A D K V G R K Q S L L I C M S V N G F F A F L S S F V Q G Y G F F L F C R L L S G F G I G G A I P T V F S Y F A E V L A R E K R G E H L S W L C M F W M I G G I Y A S A M A W A I I P H Y G W S F S M G S A Y Q F H S W R V F V I V C A L P C V S S V V A L T F M P E S P R F L L E V G K H D E A W M I L K L I H D T N M R A R G Q P E K V F T V N K I K T P K Q I D E L I E I E S D T G T W Y R R C F V R I R T E L Y G I W L T F M R C F N Y P V R D N T I K L T I V W F T L S F G Y Y G L S V W F P D V I K P L Q S D E Y A L L T R N V E R D K Y A N F T I N F T M E N Q I H T G M E Y D N G R F I G V K F K S V T F K D S V F K S C T F E D V T S V N T Y F K N C T F I D T V F D N T D F E P Y K F I D S E F K N C S F F H N K T G C Q I T F D D D Y S A Y W I Y F V N F L G T L A V L P G N I V S A L L M D R I G R L T M L G G S M V L S G I S C F F L W F G T S E S M M I G M L C L Y N G L T I S A W N S L D V V T V E L Y P T D R R A T G F G F L N A L C K A A A V L G N L I F G S L V S I T K S I P I L L A S T V L V C G G L V G L C L P D T R T Q V L M
PTM type	X-N-glycosylation X-Oxidation X-Phosphorylation X: Amino Acid

N-glycosylation
Asparagine	5 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Increasing the affinity of SLC22B3			[1]
Role of PTM	Protein Activity Modulation
Modified Residue	Asparagine	Modified Location	559
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-glycosylation at SLC22B3 Asparagine 559 have been reported to increase its transport affinity.
PTM Phenomenon2	No significant impaired transporter			[1]
Role of PTM	No Significant Effect
Modified Residue	Asparagine	Modified Location	534
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-glycosylation at SLC22B3 Asparagine 534 have been reported to have no significant effect on its expression or subcellular localisation, nor did it affect the rate of drug transport.
PTM Phenomenon3	No significant impaired transporter			[1]
Role of PTM	No Significant Effect
Modified Residue	Asparagine	Modified Location	565
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-glycosylation at SLC22B3 Asparagine 565 have been reported to have no significant effect on its expression or subcellular localisation, nor did it affect the rate of drug transport.
PTM Phenomenon4	Have the potential to influence SLC22B3			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	480
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC22B3 Asparagine 480 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC22B3			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	484
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC22B3 Asparagine 484 has the potential to affect its expression or activity.
Oxidation
Cystine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SV2C			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	145
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SV2C Cystine 145 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SV2C			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	424
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SV2C Cystine 424 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SV2C			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	678
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SV2C Cystine 678 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 SLC22B3			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	108
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22B3 Serine 108 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC22B3			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	515
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22B3 Serine 515 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 SLC22B3			[6]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	41
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC22B3 Tyrosine 41 has the potential to affect its expression or activity.

References
1	Only the complex N559-glycan in the synaptic vesicle glycoprotein 2C mediates high affinity binding to botulinum neurotoxin serotype A1. Biochem J. 2016 Sep 1;473(17):2645-54.
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: SV2C_HUMAN)
3	A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging. Cell. 2020 Mar 5;180(5):968-983.e24.
4	Phosphoproteome Integration Reveals Patient-Specific Networks in Prostate Cancer. Cell. 2016 Aug 11;166(4):1041-1054.
5	iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
6	Neuroblastoma tyrosine kinase signaling networks involve FYN and LYN in endosomes and lipid rafts. PLoS Comput Biol. 2015 Apr 17;11(4):e1004130.

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Detail Information of Post-Translational Modifications

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