Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0329 Transporter Info
Gene Name	SLC38A2
Transporter Name	Sodium-coupled neutral amino acid transporter 2
Gene ID	54407
UniProt ID	Q96QD8

Post-Translational Modification of This DT
Overview ofSLC38A2 Modification Sites with Functional and Structural Information
Sequence	M K K A E M G R F S I S P D E D S S S Y S S N S D F N Y S Y P T K Q A A L K S H Y A D V D P E N Q N F L L E S N L G K K K Y E T E F H P G T T S F G M S V F N L S N A I V G S G I L G L S Y A M A N T G I A L F I I L L T F V S I F S L Y S V H L L L K T A N E G G S L L Y E Q L G Y K A F G L V G K L A A S G S I T M Q N I G A M S S Y L F I V K Y E L P L V I Q A L T N I E D K T G L W Y L N G N Y L V L L V S L V V I L P L S L F R N L G Y L G Y T S G L S L L C M V F F L I V V I C K K F Q V P C P V E A A L I I N E T I N T T L T Q P T A L V P A L S H N V T E N D S C R P H Y F I F N S Q T V Y A V P I L I F S F V C H P A V L P I Y E E L K D R S R R R M M N V S K I S F F A M F L M Y L L A A L F G Y L T F Y E H V E S E L L H T Y S S I L G T D I L L L I V R L A V L M A V T L T V P V V I F P I R S S V T H L L C A S K D F S W W R H S L I T V S I L A F T N L L V I F V P T I R D I F G F I G A S A A S M L I F I L P S A F Y I K L V K K E P M K S V Q K I G A L F F L L S G V L V M T G S M A L I V L D W V H N A P G G G H
PTM type	X-Methylation X-N-glycosylation X-Phosphorylation X-Polyubiquitination X-S-palmitoylation X-Sulfoxidation X-Ubiquitination X-Ubiquitination X: Amino Acid

Methylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC38A2			[1]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	38
Experimental Method	Co-Immunoprecipitation
Detailed Description	Methylation at SLC38A2 Lysine 38 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 SLC38A2			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	258
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC38A2 Asparagine 258 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC38A2			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	274
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC38A2 Asparagine 274 has the potential to affect its expression or activity.
Phosphorylation
Serine	15 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC38A2			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	10
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 10 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC38A2			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	12
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 12 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC38A2			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	17
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 17 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC38A2			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	18
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 18 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC38A2			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	19
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 19 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC38A2			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	21
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 21 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC38A2			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	22
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 22 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC38A2			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	24
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 24 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC38A2			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	29
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 29 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC38A2			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	39
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 39 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLC38A2			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	55
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 55 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence SLC38A2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	210
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 210 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence SLC38A2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	320
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 320 has the potential to affect its expression or activity.
PTM Phenomenon14	Have the potential to influence SLC38A2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	328
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 328 has the potential to affect its expression or activity.
PTM Phenomenon15	Have the potential to influence SLC38A2			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	469
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Serine 469 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	Have the potential to influence SLC38A2			[3], [10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	32
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Threonine 32 has the potential to affect its expression or activity.
Tyrosine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC38A2			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	20
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Tyrosine 20 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC38A2			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	28
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Tyrosine 28 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC38A2			[5], [10]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	30
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Tyrosine 30 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC38A2			[3], [11]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	41
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC38A2 Tyrosine 41 has the potential to affect its expression or activity.
Polyubiquitination
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Regulating the degradation and activity of the transporter			[12]
Role of PTM	Degradation via Proteosome
Related Enzyme	E3 ubiquitin-protein ligase NEDD4-like (NEDD4L)
Experimental Method	Co-Immunoprecipitation
Detailed Description	Polyubiquitination at SLC38A2 have been reported to regulate its degradation and transport activity.
S-palmitoylation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC38A2			[13], [14]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	403
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at SLC38A2 Cystine 403 has the potential to affect its expression or activity.
Sulfoxidation
Methionine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC38A2			[15]
Role of PTM	Potential impacts
Modified Residue	Methionine	Modified Location	324
Experimental Method	Co-Immunoprecipitation
Detailed Description	Sulfoxidation at SLC38A2 Methionine 324 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC38A2			[15]
Role of PTM	Potential impacts
Modified Residue	Methionine	Modified Location	325
Experimental Method	Co-Immunoprecipitation
Detailed Description	Sulfoxidation at SLC38A2 Methionine 325 has the potential to affect its expression or activity.
Ubiquitination
Lysine	9 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Decreasing cell surface expression of SLC38A2			[16]
Role of PTM	Surface Expression Modulation
Modified Residue	Lysine	Modified Location	60
Studied Phenotype	Hepatoblastoma [ICD11: 2C12.01]
Experimental Material(s)	Human hepatoblastoma (HepG2.2.15) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 60 have been reported to decrease its cell surface expression.
PTM Phenomenon2	.			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	2
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 2 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	2
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 2 has the potential to affect its expression or activity.
PTM Phenomenon4	.			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	2
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 2 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC38A2			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	3
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 3 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC38A2			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	33
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 33 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC38A2			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	38
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 38 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC38A2			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	59
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 59 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC38A2			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	140
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 Lysine 140 has the potential to affect its expression or activity.
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Decreasing the plasma membrane expression of SLC38A2			[20]
Role of PTM	Surface Expression Modulation
Affected Drug/Substrate	Amino acid	Results for Drug	Decreasing uptake of cellular amino acid
Related Enzyme	E3 ubiquitin-protein ligase NEDD4-like (NEDD4L)
Experimental Material(s)	Primary human trophoblast (PHT) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC38A2 have been reported to decrease its plasma membrane expression.

References
1	A strong tradition of dentistry. J Ir Dent Assoc. 2013;59(6):285-6.
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: S38A2_HUMAN)
3	Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
4	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
5	An orthogonal proteomic survey uncovers novel Zika virus host factors. Nature. 2018 Sep;561(7722):253-257.
6	Synthesizing Signaling Pathways from Temporal Phosphoproteomic Data. Cell Rep. 2018 Sep 25;24(13):3607-3618.
7	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.
8	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.
9	A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7.
10	An integrated strategy for highly sensitive phosphoproteome analysis from low micrograms of protein samples. Analyst. 2018 Jul 23;143(15):3693-3701.
11	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.
12	Increased ubiquitination and reduced plasma membrane trafficking of placental amino acid transporter SNAT-2 in human IUGR. Clin Sci (Lond). 2015 Dec;129(12):1131-41.
13	Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites. J Proteome Res. 2018 May 4;17(5):1907-1922.
14	Site-specific analysis of protein S-acylation by resin-assisted capture. J Lipid Res. 2011 Feb;52(2):393-8.
15	Global analysis of methionine oxidation provides a census of folding stabilities for the human proteome. Proc Natl Acad Sci U S A. 2019 Mar 26;116(13):6081-6090.
16	Global analysis of HBV-mediated host proteome and ubiquitylome change in HepG2.2.15 human hepatoblastoma cell line. Cell Biosci. 2021 Apr 17;11(1):75.
17	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
18	A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284.
19	Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 2011 Oct 21;44(2):325-40.
20	Regulation of amino acid transporter trafficking by mTORC1 in primary human trophoblast cells is mediated by the ubiquitin ligase Nedd4-2. Clin Sci (Lond). 2016 Apr 1;130(7):499-512.

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Detail Information of Post-Translational Modifications

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