General Information of Drug Transporter (DT)
DT ID DTD0165 Transporter Info
Gene Name SLC24A4
Transporter Name Sodium/potassium/calcium exchanger 4
Gene ID
123041
UniProt ID
Q8NFF2
Post-Translational Modification of This DT
Overview ofSLC24A4 Modification Sites with Functional and Structural Information
Sequence
PTM type
X-N-glycosylation X-Phosphorylation X-Phosphorylation X-Ubiquitination X: Amino Acid

N-glycosylation

  Asparagine

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

  PTM Phenomenon1

Have the potential to influence SLC24A4 [1]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

69

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLC24A4 Asparagine 69 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SLC24A4 [1]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

76

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLC24A4 Asparagine 76 has the potential to affect its expression or activity.

Phosphorylation

  Serine

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

  PTM Phenomenon1

Have the potential to influence SLC24A4 [2]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

362

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC24A4 Serine 362 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SLC24A4 [2], [3]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

363

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC24A4 Serine 363 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 SLC24A4 [4]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

6

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC24A4 Threonine 6 has the potential to affect its expression or activity.

  PTM Phenomenon2

. [5]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

143

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC24A4 Threonine 143 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

. [6]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

75

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC24A4 Lysine 75 has the potential to affect its expression or activity.

  PTM Phenomenon2

. [6]

Role of PTM

Potential impacts

Modified Residue

Lysine

Modified Location

75

Experimental Method

Co-Immunoprecipitation

Detailed Description

Ubiquitination at SLC24A4 Lysine 75 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: NCKX4_HUMAN)
2 Comparative phosphoproteomic analysis reveals signaling networks regulating monopolar and bipolar cytokinesis. Sci Rep. 2018 Feb 2;8(1):2269.
3 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.
4 Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
5 15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
6 ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.

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