Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0412 Transporter Info
Gene Name	SLC57A5
Transporter Name	NIPA-like protein 3
Gene ID	57185
UniProt ID	Q6P499

Post-Translational Modification of This DT
Overview ofSLC57A5 Modification Sites with Functional and Structural Information
Sequence	M D G S H S A A L K L Q Q L P P T S S S S A V S E A S F S Y K E N L I G A L L A I F G H L V V S I A L N L Q K Y C H I R L A G S K D P R A Y F K T K T W W L G L F L M L L G E L G V F A S Y A F A P L S L I V P L S A V S V I A S A I I G I I F I K E K W K P K D F L R R Y V L S F V G C G L A V V G T Y L L V T F A P N S H E K M T G E N V T R H L V S W P F L L Y M L V E I I L F C L L L Y F Y K E K N A N N I V V I L L L V A L L G S M T V V T V K A V A G M L V L S I Q G N L Q L D Y P I F Y V M F V C M V A T A V Y Q A A F L S Q A S Q M Y D S S L I A S V G Y I L S T T I A I T A G A I F Y L D F I G E D V L H I C M F A L G C L I A F L G V F L I T R N R K K P I P F E P Y I S M D A M P G M Q N M H D K G M T V Q P E L K A S F S Y G A L E N N D N I S E I Y A P A T L P V M Q E E H G S R S A S G V P Y R V L E H T K K E
PTM type	X-N-glycosylation X-Phosphorylation X: Amino Acid

N-glycosylation
Asparagine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC57A5			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	166
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC57A5 Asparagine 166 has the potential to affect its expression or activity.
Phosphorylation
Serine	6 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC57A5			[2]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	24
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Serine 24 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC57A5			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	335
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Serine 335 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC57A5			[4], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	359
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Serine 359 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC57A5			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	361
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Serine 361 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC57A5			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	372
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Serine 372 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC57A5			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	391
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Serine 391 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 SLC57A5			[10], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	379
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Threonine 379 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC57A5			[12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	403
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Threonine 403 has the potential to affect its expression or activity.
Tyrosine	6 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC57A5			[13]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	30
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Tyrosine 30 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC57A5			[14]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	70
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Tyrosine 70 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC57A5			[3], [15]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	333
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Tyrosine 333 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC57A5			[16], [17]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	362
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Tyrosine 362 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC57A5			[9], [11]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	375
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Tyrosine 375 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC57A5			[12], [18]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	397
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC57A5 Tyrosine 397 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: NPAL3_HUMAN)
2	A fast sample processing strategy for large-scale profiling of human urine phosphoproteome by mass spectrometry. Talanta. 2018 Aug 1;185:166-173.
3	Sensitive, Robust, and Cost-Effective Approach for Tyrosine Phosphoproteome Analysis. Anal Chem. 2017 Sep 5;89(17):9307-9314.
4	Quantitative proteomic and phosphoproteomic comparison of human colon cancer DLD-1 cells differing in ploidy and chromosome stability. Mol Biol Cell. 2018 May 1;29(9):1031-1047.
5	A Methodological Assessment and Characterization of Genetically-Driven Variation in Three Human Phosphoproteomes. Sci Rep. 2018 Aug 14;8(1):12106.
6	Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
7	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
8	Targeting CDK2 overcomes melanoma resistance against BRAF and Hsp90 inhibitors. Mol Syst Biol. 2018 Mar 5;14(3):e7858.
9	Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
10	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
11	HIV-1 Activates T Cell Signaling Independently of Antigen to Drive Viral Spread. Cell Rep. 2017 Jan 24;18(4):1062-1074.
12	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.
13	iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
14	Kinase-substrate enrichment analysis provides insights into the heterogeneity of signaling pathway activation in leukemia cells. Sci Signal. 2013 Mar 26;6(268):rs6.
15	Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder. Nat Chem Biol. 2016 Nov;12(11):959-966.
16	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
17	Phosphoproteome Analysis Reveals Differential Mode of Action of Sorafenib in Wildtype and Mutated FLT3 Acute Myeloid Leukemia (AML) Cells. Mol Cell Proteomics. 2017 Jul;16(7):1365-1376.
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.

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