Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0255 Transporter Info
Gene Name	SLC2A13
Transporter Name	Proton myo-inositol cotransporter
Gene ID	114134
UniProt ID	Q96QE2

Post-Translational Modification of This DT
Overview ofSLC2A13 Modification Sites with Functional and Structural Information
Sequence	M S R K A S E N V E Y T L R S L S S L M G E R R R K Q P E P D A A S A A G E C S L L A A A E S S T S L Q S A G A G G G G V G D L E R A A R R Q F Q Q D E T P A F V Y V V A V F S A L G G F L F G Y D T G V V S G A M L L L K R Q L S L D A L W Q E L L V S S T V G A A A V S A L A G G A L N G V F G R R A A I L L A S A L F T A G S A V L A A A N N K E T L L A G R L V V G L G I G I A S M T V P V Y I A E V S P P N L R G R L V T I N T L F I T G G Q F F A S V V D G A F S Y L Q K D G W R Y M L G L A A V P A V I Q F F G F L F L P E S P R W L I Q K G Q T Q K A R R I L S Q M R G N Q T I D E E Y D S I K N N I E E E E K E V G S A G P V I C R M L S Y P P T R R A L I V G C G L Q M F Q Q L S G I N T I M Y Y S A T I L Q M S G V E D D R L A I W L A S V T A F T N F I F T L V G V W L V E K V G R R K L T F G S L A G T T V A L I I L A L G F V L S A Q V S P R I T F K P I A P S G Q N A T C T R Y S Y C N E C M L D P D C G F C Y K M N K S T V I D S S C V P V N K A S T N E A A W G R C E N E T K F K T E D I F W A Y N F C P T P Y S W T A L L G L I L Y L V F F A P G M G P M P W T V N S E I Y P L W A R S T G N A C S S G I N W I F N V L V S L T F L H T A E Y L T Y Y G A F F L Y A G F A A V G L L F I Y G C L P E T K G K K L E E I E S L F D N R L C T C G T S D S D E G R Y I E Y I R V K G S N Y H L S D N D A S D V E
PTM type	X-N-glycosylation X-Phosphorylation X-S-palmitoylation 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 SLC2A13			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	433
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC2A13 Asparagine 433 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC2A13			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	458
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC2A13 Asparagine 458 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC2A13			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	485
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC2A13 Asparagine 485 has the potential to affect its expression or activity.
Phosphorylation
Serine	16 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC2A13			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	6
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 6 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC2A13			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	15
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 15 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC2A13			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	17
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 17 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC2A13			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	18
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 18 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC2A13			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	34
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 34 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC2A13			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	40
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 40 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC2A13			[6], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	47
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 47 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC2A13			[6], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	48
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 48 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC2A13			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	50
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 50 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC2A13			[6], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	53
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 53 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLC2A13			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	294
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 294 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence SLC2A13			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	607
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 607 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence SLC2A13			[4], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	621
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 621 has the potential to affect its expression or activity.
PTM Phenomenon14	Have the potential to influence SLC2A13			[12], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	635
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 635 has the potential to affect its expression or activity.
PTM Phenomenon15	Have the potential to influence SLC2A13			[14], [15]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	640
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 640 has the potential to affect its expression or activity.
PTM Phenomenon16	Have the potential to influence SLC2A13			[14], [15]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	645
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Serine 645 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 SLC2A13			[16]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	12
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Threonine 12 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC2A13			[6], [8]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	49
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Threonine 49 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 SLC2A13			[17], [18]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	11
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Tyrosine 11 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC2A13			[4], [17]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	626
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Tyrosine 626 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC2A13			[4]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	629
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Tyrosine 629 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC2A13			[4], [14]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	637
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC2A13 Tyrosine 637 has the potential to affect its expression or activity.
S-palmitoylation
Cystine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC2A13			[19]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	614
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at SLC2A13 Cystine 614 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC2A13			[19]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	616
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at SLC2A13 Cystine 616 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 SLC2A13			[20]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	296
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC2A13 Lysine 296 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC2A13			[21]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	633
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC2A13 Lysine 633 has the potential to affect its expression or activity.

References
1	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: MYCT_HUMAN)
2	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
3	A Methodological Assessment and Characterization of Genetically-Driven Variation in Three Human Phosphoproteomes. Sci Rep. 2018 Aug 14;8(1):12106.
4	An integrated strategy for highly sensitive phosphoproteome analysis from low micrograms of protein samples. Analyst. 2018 Jul 23;143(15):3693-3701.
5	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
6	Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1. EMBO J. 2015 Nov 12;34(22):2840-61.
7	Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells. Sci Signal. 2011 Jun 28;4(179):rs5.
8	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
9	Phosphoproteome dynamics in onset and maintenance of oncogene-induced senescence. Mol Cell Proteomics. 2014 Aug;13(8):2089-100.
10	Feasibility of large-scale phosphoproteomics with higher energy collisional dissociation fragmentation. J Proteome Res. 2010 Dec 3;9(12):6786-94.
11	Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48.
12	Actionable Cytopathogenic Host Responses of Human Alveolar Type 2 Cells to SARS-CoV-2. Mol Cell. 2020 Dec 17;80(6):1104-1122.e9.
13	An orthogonal proteomic survey uncovers novel Zika virus host factors. Nature. 2018 Sep;561(7722):253-257.
14	Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
15	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
16	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.
17	Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder. Nat Chem Biol. 2016 Nov;12(11):959-966.
18	Isoelectric point-based fractionation by HiRIEF coupled to LC-MS allows for in-depth quantitative analysis of the phosphoproteome. Sci Rep. 2017 Jul 3;7(1):4513.
19	Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites. J Proteome Res. 2018 May 4;17(5):1907-1922.
20	UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nat Struct Mol Biol. 2018 Jul;25(7):631-640.
21	Global Landscape and Dynamics of Parkin and USP30-Dependent Ubiquitylomes in iNeurons during Mitophagic Signaling. Mol Cell. 2020 Mar 5;77(5):1124-1142.e10.

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Detail Information of Post-Translational Modifications

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