Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0364 Transporter Info
Gene Name	SLC44A2
Transporter Name	Choline transporter-like protein 2
Gene ID	57153
UniProt ID	Q8IWA5

Post-Translational Modification of This DT
Overview ofSLC44A2 Modification Sites with Functional and Structural Information
Sequence	M G D E R P H Y Y G K H G T P Q K Y D P T F K G P I Y N R G C T D I I C C V F L L L A I V G Y V A V G I I A W T H G D P R K V I Y P T D S R G E F C G Q K G T K N E N K P Y L F Y F N I V K C A S P L V L L E F Q C P T P Q I C V E K C P D R Y L T Y L N A R S S R D F E Y Y K Q F C V P G F K N N K G V A E V L Q D G D C P A V L I P S K P L A R R C F P A I H A Y K G V L M V G N E T T Y E D G H G S R K N I T D L V E G A K K A N G V L E A R Q L A M R I F E D Y T V S W Y W I I I G L V I A M A M S L L F I I L L R F L A G I M V W V M I I M V I L V L G Y G I F H C Y M E Y S R L R G E A G S D V S L V D L G F Q T D F R V Y L H L R Q T W L A F M I I L S I L E V I I I L L L I F L R K R I L I A I A L I K E A S R A V G Y V M C S L L Y P L V T F F L L C L C I A Y W A S T A V F L S T S N E A V Y K I F D D S P C P F T A K T C N P E T F P S S N E S R Q C P N A R C Q F A F Y G G E S G Y H R A L L G L Q I F N A F M F F W L A N F V L A L G Q V T L A G A F A S Y Y W A L R K P D D L P A F P L F S A F G R A L R Y H T G S L A F G A L I L A I V Q I I R V I L E Y L D Q R L K A A E N K F A K C L M T C L K C C F W C L E K F I K F L N R N A Y I M I A I Y G T N F C T S A R N A F F L L M R N I I R V A V L D K V T D F L F L L G K L L I V G S V G I L A F F F F T H R I R I V Q D T A P P L N Y Y W V P I L T V I V G S Y L I A H G F F S V Y G M C V D T L F L C F L E D L E R N D G S A E R P Y F M S S T L K K L L N K T N K K A A E S
PTM type	X-Acetylation X-N-glycosylation X-Oxidation X-Phosphorylation X-Phosphorylation X-Ubiquitination X-Ubiquitination X: Amino Acid

Acetylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC44A2			[1]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	115
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC44A2 Lysine 115 has the potential to affect its expression or activity.
N-glycosylation
Asparagine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC44A2			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	187
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC44A2 Asparagine 187 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC44A2			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	200
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC44A2 Asparagine 200 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC44A2			[3]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	417
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC44A2 Asparagine 417 has the potential to affect its expression or activity.
Oxidation
Cystine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC44A2			[4]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	74
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC44A2 Cystine 74 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC44A2			[5]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	550
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC44A2 Cystine 550 has the potential to affect its expression or activity.
Phosphorylation
Serine	5 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC44A2			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	165
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Serine 165 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC44A2			[7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	504
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Serine 504 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC44A2			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	681
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Serine 681 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC44A2			[7], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	689
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Serine 689 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC44A2			[7], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	690
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Serine 690 has the potential to affect its expression or activity.
Threonine	5 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC44A2			[11], [12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	14
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Threonine 14 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC44A2			[13], [14]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	21
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Threonine 21 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[15]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	303
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Threonine 303 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC44A2			[7]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	502
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Threonine 502 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC44A2			[7], [10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	691
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Threonine 691 has the potential to affect its expression or activity.
Tyrosine	5 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC44A2			[13], [16]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	8
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Tyrosine 8 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC44A2			[13], [17]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	9
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Tyrosine 9 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC44A2			[18], [19]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	18
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Tyrosine 18 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC44A2			[7]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	500
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Tyrosine 500 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC44A2			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	686
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC44A2 Tyrosine 686 has the potential to affect its expression or activity.
Ubiquitination
Lysine	7 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC44A2			[20]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	17
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC44A2 Lysine 17 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[15]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	199
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC44A2 Lysine 199 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[15]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	199
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC44A2 Lysine 199 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC44A2			[20]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	209
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC44A2 Lysine 209 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC44A2			[20]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	406
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC44A2 Lysine 406 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC44A2			[20]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	481
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC44A2 Lysine 481 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC44A2			[20]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	693
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC44A2 Lysine 693 has the potential to affect its expression or activity.

References
1	Response of fibroblast cultures from ataxia-telangiectasia patients to reactive oxygen species generated during inflammatory reactions. Environ Mol Mutagen. 1994;24(2):103-11.
2	Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86.
3	Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes. Mol Cell Proteomics. 2007 Nov;6(11):1933-41.
4	A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging. Cell. 2020 Mar 5;180(5):968-983.e24.
5	Identifying Functional Cysteine Residues in the Mitochondria. ACS Chem Biol. 2017 Apr 21;12(4):947-957.
6	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.
7	Phosphoproteins in extracellular vesicles as candidate markers for breast cancer. Proc Natl Acad Sci U S A. 2017 Mar 21;114(12):3175-3180.
8	Temporal quantitative phosphoproteomics of ADP stimulation reveals novel central nodes in platelet activation and inhibition. Blood. 2017 Jan 12;129(2):e1-e12.
9	Quantitative phosphoproteomics reveals extensive cellular reprogramming during HIV-1 entry. Cell Host Microbe. 2013 May 15;13(5):613-623.
10	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
11	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
12	Phosphoproteomic analysis reveals PAK2 as a therapeutic target for lapatinib resistance in HER2-positive breast cancer cells. Biochem Biophys Res Commun. 2018 Oct 20;505(1):187-193.
13	Deep Phosphotyrosine Proteomics by Optimization of Phosphotyrosine Enrichment and MS/MS Parameters. J Proteome Res. 2017 Feb 3;16(2):1077-1086.
14	Quantitative phosphoproteomic analysis reveals system-wide signaling pathways regulated by site-specific phosphorylation of Keratin-8 in skin squamous cell carcinoma derived cell line. Proteomics. 2017 Apr;17(7).
15	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
16	A fast sample processing strategy for large-scale profiling of human urine phosphoproteome by mass spectrometry. Talanta. 2018 Aug 1;185:166-173.
17	Deep Coverage of Global Protein Expression and Phosphorylation in Breast Tumor Cell Lines Using TMT 10-plex Isobaric Labeling. J Proteome Res. 2017 Mar 3;16(3):1121-1132.
18	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
19	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
20	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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