Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0248 Transporter Info
Gene Name	SLC29A2
Transporter Name	Equilibrative nucleoside transporter 2
Gene ID	3177
UniProt ID	Q14542

Post-Translational Modification of This DT
Overview ofSLC29A2 Modification Sites with Functional and Structural Information
Sequence	M A R G D A P R D S Y H L V G I S F F I L G L G T L L P W N F F I T A I P Y F Q A R L A G A G N S T A R I L S T N H T G P E D A F N F N N W V T L L S Q L P L L L F T L L N S F L Y Q C V P E T V R I L G S L L A I L L L F A L T A A L V K V D M S P G P F F S I T M A S V C F I N S F S A V L Q G S L F G Q L G T M P S T Y S T L F L S G Q G L A G I F A A L A M L L S M A S G V D A E T S A L G Y F I T P C V G I L M S I V C Y L S L P H L K F A R Y Y L A N K S S Q A Q A Q E L E T K A E L L Q S D E N G I P S S P Q K V A L T L D L D L E K E P E S E P D E P Q K P G K P S V F T V F Q K I W L T A L C L V L V F T V T L S V F P A I T A M V T S S T S P G K W S Q F F N P I C C F L L F N I M D W L G R S L T S Y F L W P D E D S R L L P L L V C L R F L F V P L F M L C H V P Q R S R L P I L F P Q D A Y F I T F M L L F A V S N G Y L V S L T M C L A P R Q V L P H E R E V A G A L M T F F L A L G L S C G A S L S F L F K A L L
PTM type	X-N-glycosylation 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 SLC29A2			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	48
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC29A2 Asparagine 48 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC29A2			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	57
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC29A2 Asparagine 57 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC29A2			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	225
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC29A2 Asparagine 225 has the potential to affect its expression or activity.
Phosphorylation
Serine	7 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC29A2			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	49
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Serine 49 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC29A2			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	244
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Serine 244 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC29A2			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	251
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Serine 251 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC29A2			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	252
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Serine 252 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC29A2			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	346
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Serine 346 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC29A2			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	349
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Serine 349 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC29A2			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	358
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Serine 358 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 SLC29A2			[3]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	50
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Threonine 50 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC29A2			[10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	348
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Threonine 348 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 SLC29A2			[10], [11]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	350
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC29A2 Tyrosine 350 has the potential to affect its expression or activity.
Ubiquitination
Lysine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC29A2			[12]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	226
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC29A2 Lysine 226 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC29A2			[12]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	238
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC29A2 Lysine 238 has the potential to affect its expression or activity.

References
1	Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2. Arch Biochem Biophys. 2003 Mar 1;411(1):19-26.
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: S29A2_HUMAN)
3	Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res. 2013 Jun 7;12(6):2414-21.
4	Comparative phosphoproteomic analysis reveals signaling networks regulating monopolar and bipolar cytokinesis. Sci Rep. 2018 Feb 2;8(1):2269.
5	Large-Scale Reanalysis of Publicly Available HeLa Cell Proteomics Data in the Context of the Human Proteome Project. J Proteome Res. 2018 Dec 7;17(12):4160-4170.
6	Phosphoproteomic screening identifies physiological substrates of the CDKL5 kinase. EMBO J. 2018 Dec 14;37(24):e99559.
7	Modulation of Cl- signaling and ion transport by recruitment of kinases and phosphatases mediated by the regulatory protein IRBIT. Sci Signal. 2018 Oct 30;11(554):eaat5018.
8	Capillary Zone Electrophoresis-Tandem Mass Spectrometry for Large-Scale Phosphoproteomics with the Production of over 11,000 Phosphopeptides from the Colon Carcinoma HCT116 Cell Line. Anal Chem. 2019 Feb 5;91(3):2201-2208.
9	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
10	An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas. Cell Rep. 2015 Jun 23;11(11):1834-43.
11	An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62.
12	Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 2011 Oct 21;44(2):325-40.

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Detail Information of Post-Translational Modifications

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