General Information of Drug Transporter (DT)
DT ID DTD0291 Transporter Info
Gene Name SLC35A5
Transporter Name Probable UDP-sugar transporter protein SLC35A5
Gene ID
55032
UniProt ID
Q9BS91
Post-Translational Modification of This DT
Overview ofSLC35A5 Modification Sites with Functional and Structural Information
Sequence
PTM type
X-N-glycosylation X-Phosphorylation 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 SLC35A5 [1]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

204

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLC35A5 Asparagine 204 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 SLC35A5 [2]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

87

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Serine 87 has the potential to affect its expression or activity.

  PTM Phenomenon2

. [3]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

288

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Serine 288 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SLC35A5 [4], [5]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

394

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Serine 394 has the potential to affect its expression or activity.

  PTM Phenomenon4

Have the potential to influence SLC35A5 [6], [7]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

401

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Serine 401 has the potential to affect its expression or activity.

  PTM Phenomenon5

Have the potential to influence SLC35A5 [6], [7]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

402

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Serine 402 has the potential to affect its expression or activity.

  PTM Phenomenon6

Have the potential to influence SLC35A5 [6], [8]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

416

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Serine 416 has the potential to affect its expression or activity.

  PTM Phenomenon7

Have the potential to influence SLC35A5 [8], [9]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

419

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Serine 419 has the potential to affect its expression or activity.

  Threonine

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

  PTM Phenomenon1

Have the potential to influence SLC35A5 [10]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

170

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Threonine 170 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SLC35A5 [11], [12]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

412

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Threonine 412 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SLC35A5 [12], [13]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

423

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC35A5 Threonine 423 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: S35A5_HUMAN)
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 UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
5 An integrated strategy for highly sensitive phosphoproteome analysis from low micrograms of protein samples. Analyst. 2018 Jul 23;143(15):3693-3701.
6 Robust, Reproducible, and Economical Phosphopeptide Enrichment Using Calcium Titanate. J Proteome Res. 2019 Mar 1;18(3):1411-1417.
7 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.
8 Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics. Nat Commun. 2019 Jan 10;10(1):104.
9 Actionable Cytopathogenic Host Responses of Human Alveolar Type 2 Cells to SARS-CoV-2. Mol Cell. 2020 Dec 17;80(6):1104-1122.e9.
10 Protein kinase PKN1 represses Wnt/beta-catenin signaling in human melanoma cells. J Biol Chem. 2013 Nov 29;288(48):34658-70.
11 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.
12 Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
13 Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.

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