General Information of Drug Transporter (DT)
DT ID DTD0367 Transporter Info
Gene Name SLC44A5
Transporter Name Choline transporter-like protein 5
Gene ID
204962
UniProt ID
Q8NCS7
Post-Translational Modification of This DT
Overview ofSLC44A5 Modification Sites with Functional and Structural Information
Sequence
PTM type
X-N-glycosylation X-Phosphorylation X-Phosphorylation X: Amino Acid

N-glycosylation

  Asparagine

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

  PTM Phenomenon1

Have the potential to influence SLC44A5 [1]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

88

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLC44A5 Asparagine 88 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SLC44A5 [1]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

190

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLC44A5 Asparagine 190 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SLC44A5 [1]

Role of PTM

Potential impacts

Modified Residue

Asparagine

Modified Location

314

Experimental Method

Co-Immunoprecipitation

Detailed Description

N-linked Glycosylation at SLC44A5 Asparagine 314 has the potential to affect its expression or activity.

Phosphorylation

  Serine

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

  PTM Phenomenon1

Have the potential to influence SLC44A5 [2]

Role of PTM

Potential impacts

Modified Residue

Serine

Modified Location

12

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Serine 12 has the potential to affect its expression or activity.

  Threonine

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

  PTM Phenomenon1

Have the potential to influence SLC44A5 [2]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

10

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Threonine 10 has the potential to affect its expression or activity.

  PTM Phenomenon2

Have the potential to influence SLC44A5 [3]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

127

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Threonine 127 has the potential to affect its expression or activity.

  PTM Phenomenon3

Have the potential to influence SLC44A5 [4]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

194

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Threonine 194 has the potential to affect its expression or activity.

  PTM Phenomenon4

. [5]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

513

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Threonine 513 has the potential to affect its expression or activity.

  PTM Phenomenon5

. [5]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

513

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Threonine 513 has the potential to affect its expression or activity.

  PTM Phenomenon6

. [5]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

513

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Threonine 513 has the potential to affect its expression or activity.

  PTM Phenomenon7

. [5]

Role of PTM

Potential impacts

Modified Residue

Threonine

Modified Location

513

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Threonine 513 has the potential to affect its expression or activity.

  Tyrosine

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

  PTM Phenomenon1

Have the potential to influence SLC44A5 [3]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

128

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Tyrosine 128 has the potential to affect its expression or activity.

  PTM Phenomenon2

. [5]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

511

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Tyrosine 511 has the potential to affect its expression or activity.

  PTM Phenomenon3

. [5]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

511

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Tyrosine 511 has the potential to affect its expression or activity.

  PTM Phenomenon4

. [5]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

511

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Tyrosine 511 has the potential to affect its expression or activity.

  PTM Phenomenon5

. [5]

Role of PTM

Potential impacts

Modified Residue

Tyrosine

Modified Location

511

Experimental Method

Co-Immunoprecipitation

Detailed Description

Phosphorylation at SLC44A5 Tyrosine 511 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: CTL5_HUMAN)
2 Quantitative phosphoproteomics analysis reveals a key role of insulin growth factor 1 receptor (IGF1R) tyrosine kinase in human sperm capacitation. Mol Cell Proteomics. 2015 Apr;14(4):1104-12.
3 Phosphoproteomics identifies driver tyrosine kinases in sarcoma cell lines and tumors. Cancer Res. 2012 May 15;72(10):2501-11.
4 A strategy for large-scale phosphoproteomics and SRM-based validation of human breast cancer tissue samples. J Proteome Res. 2012 Nov 2;11(11):5311-22.
5 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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