General Information of Drug Transporter (DT)
DT ID DTD0137 Transporter Info
Gene Name SLC20A2
Transporter Name Sodium-dependent phosphate transporter 2
Gene ID
6575
UniProt ID
Q08357
Post-Translational Modification of This DT
Overview ofSLC20A2 Modification Sites with Functional and Structural Information
Sequence
PTM type
X-N-glycosylation X-Phosphorylation X-Phosphorylation X-Ubiquitination X-Ubiquitination 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 SLC20A2 [1]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

81

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLC20A2 Asparagine 81 has the potential to affect its expression or activity.

Phosphorylation

  Serine

        24 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SLC20A2 [2]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

106

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 106 has the potential to affect its expression or activity.

  PTM Phenomenon2

. [3]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

197

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 197 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SLC20A2 [4], [5]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

253

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 253 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SLC20A2 [6], [7]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

256

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 256 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SLC20A2 [6], [7]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

259

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 259 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SLC20A2 [7], [8]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

261

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 261 has the potential to affect its expression or activity.

  PTM Phenomenon7

Have the potential to influence SLC20A2 [6], [9]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

268

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 268 has the potential to affect its expression or activity.

  PTM Phenomenon8

Have the potential to influence SLC20A2 [10]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

283

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 283 has the potential to affect its expression or activity.

  PTM Phenomenon9

Have the potential to influence SLC20A2 [10]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

305

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 305 has the potential to affect its expression or activity.

  PTM Phenomenon10

Have the potential to influence SLC20A2 [6], [11]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

316

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 316 has the potential to affect its expression or activity.

  PTM Phenomenon11

Have the potential to influence SLC20A2 [6], [12]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

321

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 321 has the potential to affect its expression or activity.

  PTM Phenomenon12

Have the potential to influence SLC20A2 [6], [13]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

324

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 324 has the potential to affect its expression or activity.

  PTM Phenomenon13

Have the potential to influence SLC20A2 [6], [13]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

327

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 327 has the potential to affect its expression or activity.

  PTM Phenomenon14

Have the potential to influence SLC20A2 [10], [14]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

351

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 351 has the potential to affect its expression or activity.

  PTM Phenomenon15

Have the potential to influence SLC20A2 [13], [15]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

375

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 375 has the potential to affect its expression or activity.

  PTM Phenomenon16

Have the potential to influence SLC20A2 [6], [9]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

385

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 385 has the potential to affect its expression or activity.

  PTM Phenomenon17

Have the potential to influence SLC20A2 [13], [16]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

413

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 413 has the potential to affect its expression or activity.

  PTM Phenomenon18

Have the potential to influence SLC20A2 [8], [9]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

422

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 422 has the potential to affect its expression or activity.

  PTM Phenomenon19

Have the potential to influence SLC20A2 [8], [13]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

424

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 424 has the potential to affect its expression or activity.

  PTM Phenomenon20

Have the potential to influence SLC20A2 [17], [18]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

432

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 432 has the potential to affect its expression or activity.

  PTM Phenomenon21

Have the potential to influence SLC20A2 [17], [18]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

434

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 434 has the potential to affect its expression or activity.

  PTM Phenomenon22

Have the potential to influence SLC20A2 [17], [19]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

435

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 435 has the potential to affect its expression or activity.

  PTM Phenomenon23

Have the potential to influence SLC20A2 [8], [20]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

458

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 458 has the potential to affect its expression or activity.

  PTM Phenomenon24

Have the potential to influence SLC20A2 [2]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

637

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Serine 637 has the potential to affect its expression or activity.

  Threonine

        11 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SLC20A2 [16]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

69

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 69 has the potential to affect its expression or activity.

  PTM Phenomenon2

. [3]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

190

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 190 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SLC20A2 [21]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

243

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 243 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SLC20A2 [10]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

284

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 284 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SLC20A2 [6], [12]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

318

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 318 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SLC20A2 [13], [17]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

330

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 330 has the potential to affect its expression or activity.

  PTM Phenomenon7

Have the potential to influence SLC20A2 [13], [16]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

337

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 337 has the potential to affect its expression or activity.

  PTM Phenomenon8

Have the potential to influence SLC20A2 [22], [23]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

346

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 346 has the potential to affect its expression or activity.

  PTM Phenomenon9

Have the potential to influence SLC20A2 [9], [12]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

387

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 387 has the potential to affect its expression or activity.

  PTM Phenomenon10

Have the potential to influence SLC20A2 [12], [14]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

390

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 390 has the potential to affect its expression or activity.

  PTM Phenomenon11

Have the potential to influence SLC20A2 [8], [9]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

420

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Threonine 420 has the potential to affect its expression or activity.

  Tyrosine

        11 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

. [3]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

187

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 187 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SLC20A2 [22], [23]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

344

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 344 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SLC20A2 [13], [23]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

354

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 354 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SLC20A2 [13], [24]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

377

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 377 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SLC20A2 [9], [12]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

386

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 386 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SLC20A2 [9], [12]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

389

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 389 has the potential to affect its expression or activity.

  PTM Phenomenon7

Have the potential to influence SLC20A2 [8], [25]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

423

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 423 has the potential to affect its expression or activity.

  PTM Phenomenon8

Have the potential to influence SLC20A2 [17], [19]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

430

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 430 has the potential to affect its expression or activity.

  PTM Phenomenon9

Have the potential to influence SLC20A2 [17], [19]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

433

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 433 has the potential to affect its expression or activity.

  PTM Phenomenon10

Have the potential to influence SLC20A2 [17], [19]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

436

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 436 has the potential to affect its expression or activity.

  PTM Phenomenon11

Have the potential to influence SLC20A2 [2]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

646

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC20A2 Tyrosine 646 has the potential to affect its expression or activity.

Ubiquitination

  Lysine

          8 PTM Phenomena Related to This Residue Click to Show/Hide the Full List

  PTM Phenomenon1

Have the potential to influence SLC20A2 [26]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

262

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC20A2 Lysine 262 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SLC20A2 [27]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

272

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC20A2 Lysine 272 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SLC20A2 [26], [27]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

278

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC20A2 Lysine 278 has the potential to affect its expression or activity.

  PTM Phenomenon4

. [28]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

349

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC20A2 Lysine 349 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SLC20A2 [26], [27]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

360

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC20A2 Lysine 360 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SLC20A2 [26]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

370

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC20A2 Lysine 370 has the potential to affect its expression or activity.

  PTM Phenomenon7

Have the potential to influence SLC20A2 [26]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

415

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC20A2 Lysine 415 has the potential to affect its expression or activity.

  PTM Phenomenon8

Have the potential to influence SLC20A2 [29]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

425

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC20A2 Lysine 425 has the potential to affect its expression or activity.
References
1 Transmembrane topology of PiT-2, a phosphate transporter-retrovirus receptor. J Virol. 2001 Jun;75(12):5584-92.
2 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.
3 15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
4 Modulation of Cl- signaling and ion transport by recruitment of kinases and phosphatases mediated by the regulatory protein IRBIT. Sci Signal. 2018 Oct 30;11(554):eaat5018.
5 Quantitative phosphoproteomic analysis identifies novel functional pathways of tumor suppressor DLC1 in estrogen receptor positive breast cancer. PLoS One. 2018 Oct 2;13(10):e0204658.
6 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.
7 Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics. Nat Commun. 2019 Jan 10;10(1):104.
8 Phosphoproteomic screening identifies physiological substrates of the CDKL5 kinase. EMBO J. 2018 Dec 14;37(24):e99559.
9 Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
10 Offline pentafluorophenyl (PFP)-RP prefractionation as an alternative to high-pH RP for comprehensive LC-MS/MS proteomics and phosphoproteomics. Anal Bioanal Chem. 2017 Jul;409(19):4615-4625.
11 Quantitative Phosphoproteome Analysis of Clostridioides difficile Toxin B Treated Human Epithelial Cells. Front Microbiol. 2018 Dec 17;9:3083.
12 Phosphoproteomic-based kinase profiling early in influenza virus infection identifies GRK2 as antiviral drug target. Nat Commun. 2018 Sep 11;9(1):3679.
13 An integrated strategy for highly sensitive phosphoproteome analysis from low micrograms of protein samples. Analyst. 2018 Jul 23;143(15):3693-3701.
14 Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
15 Resolution of Novel Pancreatic Ductal Adenocarcinoma Subtypes by Global Phosphotyrosine Profiling. Mol Cell Proteomics. 2016 Aug;15(8):2671-85.
16 Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res. 2013 Jun 7;12(6):2414-21.
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 Role of the E3 ubiquitin ligase RNF157 as a novel downstream effector linking PI3K and MAPK signaling pathways to the cell cycle. J Biol Chem. 2017 Sep 1;292(35):14311-14324.
19 Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
20 Protein kinase C-alpha interaction with F0F1-ATPase promotes F0F1-ATPase activity and reduces energy deficits in injured renal cells. J Biol Chem. 2015 Mar 13;290(11):7054-66.
21 Phosphoproteomic and Functional Analyses Reveal Sperm-specific Protein Changes Downstream of Kappa Opioid Receptor in Human Spermatozoa. Mol Cell Proteomics. 2019 Mar 15;18(Suppl 1):S118-S131.
22 Deep Phosphotyrosine Proteomics by Optimization of Phosphotyrosine Enrichment and MS/MS Parameters. J Proteome Res. 2017 Feb 3;16(2):1077-1086.
23 Sensitive, Robust, and Cost-Effective Approach for Tyrosine Phosphoproteome Analysis. Anal Chem. 2017 Sep 5;89(17):9307-9314.
24 Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder. Nat Chem Biol. 2016 Nov;12(11):959-966.
25 Fibroblasts Mobilize Tumor Cell Glycogen to Promote Proliferation and Metastasis. Cell Metab. 2019 Jan 8;29(1):141-155.e9.
26 Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 2011 Oct 21;44(2):325-40.
27 A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics. 2011 Oct;10(10):M111.013284.
28 ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
29 New findings on essential amino acids. Cesk Fysiol. 1990;39(1):13-25.

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