Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0238 Transporter Info
Gene Name	SLC27A1
Transporter Name	Fatty acid transport protein 1
Gene ID	376497
UniProt ID	Q6PCB7

Post-Translational Modification of This DT
Overview ofSLC27A1 Modification Sites with Functional and Structural Information
Sequence	M R A P G A G A A S V V S L A L L W L L G L P W T W S A A A A L G V Y V G S G G W R F L R I V C K T A R R D L F G L S V L I R V R L E L R R H Q R A G H T I P R I F Q A V V Q R Q P E R L A L V D A G T G E C W T F A Q L D A Y S N A V A N L F R Q L G F A P G D V V A I F L E G R P E F V G L W L G L A K A G M E A A L L N V N L R R E P L A F C L G T S G A K A L I F G G E M V A A V A E V S G H L G K S L I K F C S G D L G P E G I L P D T H L L D P L L K E A S T A P L A Q I P S K G M D D R L F Y I Y T S G T T G L P K A A I V V H S R Y Y R M A A F G H H A Y R M Q A A D V L Y D C L P L Y H S A G N I I G V G Q C L I Y G L T V V L R K K F S A S R F W D D C I K Y N C T V V Q Y I G E I C R Y L L K Q P V R E A E R R H R V R L A V G N G L R P A I W E E F T E R F G V R Q I G E F Y G A T E C N C S I A N M D G K V G S C G F N S R I L P H V Y P I R L V K V N E D T M E L L R D A Q G L C I P C Q A G E P G L L V G Q I N Q Q D P L R R F D G Y V S E S A T S K K I A H S V F S K G D S A Y L S G D V L V M D E L G Y M Y F R D R S G D T F R W R G E N V S T T E V E G V L S R L L G Q T D V A V Y G V A V P G V E G K A G M A A V A D P H S L L D P N A I Y Q E L Q K V L A P Y A R P I F L R L L P Q V D T T G T F K I Q K T R L Q R E G F D P R Q T S D R L F F L D L K Q G H Y L P L N E A V Y T R I C S G A F A L
PTM type	X-Acetylation X-Malonylation X-Oxidation X-Phosphorylation X-Phosphorylation 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 SLC27A1			[1]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	238
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC27A1 Lysine 238 has the potential to affect its expression or activity.
Malonylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC27A1			[2]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	346
Experimental Method	Co-Immunoprecipitation
Detailed Description	Malonylation at SLC27A1 Lysine 346 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 SLC27A1			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	326
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC27A1 Cystine 326 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC27A1			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	406
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC27A1 Cystine 406 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 SLC27A1			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	10
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Serine 10 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC27A1			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	13
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Serine 13 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC27A1			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	199
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Serine 199 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC27A1			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	228
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Serine 228 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC27A1			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	237
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Serine 237 has the potential to affect its expression or activity.
PTM Phenomenon6	.			[7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	468
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Serine 468 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC27A1			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	529
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Serine 529 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 SLC27A1			[6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	229
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Threonine 229 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC27A1			[8]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	428
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Threonine 428 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC27A1			[9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	593
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Threonine 593 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC27A1			[9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	594
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Threonine 594 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC27A1			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	596
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Threonine 596 has the potential to affect its expression or activity.
Tyrosine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC27A1			[11]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	417
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Tyrosine 417 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC27A1			[12]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	501
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Tyrosine 501 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC27A1			[13]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	569
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC27A1 Tyrosine 569 has the potential to affect its expression or activity.
Ubiquitination
Lysine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC27A1			[14]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	202
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC27A1 Lysine 202 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC27A1			[14]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	225
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC27A1 Lysine 225 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC27A1			[14], [15]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	474
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC27A1 Lysine 474 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC27A1			[14]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	475
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC27A1 Lysine 475 has the potential to affect its expression or activity.

References
1	Use of antihypertensive medication after ischemic stroke in young adults and its association with long-term outcome. Ann Med. 2019 Feb;51(1):68-77.
2	Proteomic and Biochemical Studies of Lysine Malonylation Suggest Its Malonic Aciduria-associated Regulatory Role in Mitochondrial Function and Fatty Acid Oxidation. Mol Cell Proteomics. 2015 Nov;14(11):3056-71.
3	A Quantitative Tissue-Specific Landscape of Protein Redox Regulation during Aging. Cell. 2020 Mar 5;180(5):968-983.e24.
4	An Augmented Multiple-Protease-Based Human Phosphopeptide Atlas. Cell Rep. 2015 Jun 23;11(11):1834-43.
5	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.
6	A Phosphoproteomic Comparison of B-RAFV600E and MKK1/2 Inhibitors in Melanoma Cells. Mol Cell Proteomics. 2015 Jun;14(6):1599-615.
7	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
8	Quantitative global phosphoproteomics of human umbilical vein endothelial cells after activation of the Rap signaling pathway. Mol Biosyst. 2013 Apr 5;9(4):732-49.
9	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
10	Nuclear Phosphoproteomic Screen Uncovers ACLY as Mediator of IL-2-induced Proliferation of CD4+ T lymphocytes. Mol Cell Proteomics. 2016 Jun;15(6):2076-92.
11	Citric acid-assisted two-step enrichment with TiO2 enhances the separation of multi- and monophosphorylated peptides and increases phosphoprotein profiling. J Proteome Res. 2013 Jun 7;12(6):2467-76.
12	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
13	Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder. Nat Chem Biol. 2016 Nov;12(11):959-966.
14	UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nat Struct Mol Biol. 2018 Jul;25(7):631-640.
15	Quantitative Analysis of the Brain Ubiquitylome in Alzheimer's Disease. Proteomics. 2018 Oct;18(20):e1800108.

If you find any error in data or bug in web service, please kindly report it to Dr. Li and Dr. Fu.

Detail Information of Post-Translational Modifications

Visitor Map

Correspondence