Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0282 Transporter Info
Gene Name	SLC33A1
Transporter Name	Acetyl-coenzyme A transporter 1
Gene ID	9197
UniProt ID	O00400

Post-Translational Modification of This DT
Overview ofSLC33A1 Modification Sites with Functional and Structural Information
Sequence	M S P T I S H K D S S R Q R R P G N F S H S L D M K S G P L P P G G W D D S H L D S A G R E G D R E A L L G D T G T G D F L K A P Q S F R A E L S S I L L L L F L Y V L Q G I P L G L A G S I P L I L Q S K N V S Y T D Q A F F S F V F W P F S L K L L W A P L V D A V Y V K N F G R R K S W L V P T Q Y I L G L F M I Y L S T Q V D R L L G N T D D R T P D V I A L T V A F F L F E F L A A T Q D I A V D G W A L T M L S R E N V G Y A S T C N S V G Q T A G Y F L G N V L F L A L E S A D F C N K Y L R F Q P Q P R G I V T L S D F L F F W G T V F L I T T T L V A L L K K E N E V S V V K E E T Q G I T D T Y K L L F A I I K M P A V L T F C L L I L T A K I G F S A A D A V T G L K L V E E G V P K E H L A L L A V P M V P L Q I I L P L I I S K Y T A G P Q P L N T F Y K A M P Y R L L L G L E Y A L L V W W T P K V E H Q G G F P I Y Y Y I V V L L S Y A L H Q V T V Y S M Y V S I M A F N A K V S D P L I G G T Y M T L L N T V S N L G G N W P S T V A L W L V D P L T V K E C V G A S N Q N C R T P D A V E L C K K L G G S C V T A L D G Y Y V E S I I C V F I G F G W W F F L G P K F K K L Q D E G S S S W K C K R N N
PTM type	X-N-glycosylation X-Oxidation X-Phosphorylation X-Phosphorylation X-S-palmitoylation 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 SLC33A1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	103
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC33A1 Asparagine 103 has the potential to affect its expression or activity.
Oxidation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC33A1			[2]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	487
Experimental Method	Co-Immunoprecipitation
Detailed Description	Oxidation at SLC33A1 Cystine 487 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 SLC33A1			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	2
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Serine 2 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC33A1			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	6
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Serine 6 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC33A1			[6], [7]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	20
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Serine 20 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC33A1			[6], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	22
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Serine 22 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC33A1			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	38
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Serine 38 has the potential to affect its expression or activity.
PTM Phenomenon6	.			[10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	42
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Serine 42 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 SLC33A1			[3], [11]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	4
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Threonine 4 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC33A1			[12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	367
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Threonine 367 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC33A1			[12]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	375
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Threonine 375 has the potential to affect its expression or activity.
Tyrosine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC33A1			[12]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	366
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Tyrosine 366 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC33A1			[12]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	377
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Tyrosine 377 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC33A1			[12]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	382
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC33A1 Tyrosine 382 has the potential to affect its expression or activity.
S-palmitoylation
Cystine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC33A1			[13]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	496
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at SLC33A1 Cystine 496 has the potential to affect its expression or activity.
Ubiquitination
Lysine	6 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC33A1			[14], [15]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	63
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC33A1 Lysine 63 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC33A1			[15], [16]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	135
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC33A1 Lysine 135 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC33A1			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	288
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC33A1 Lysine 288 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC33A1			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	497
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC33A1 Lysine 497 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC33A1			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	534
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC33A1 Lysine 534 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC33A1			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	544
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC33A1 Lysine 544 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: ACATN_HUMAN)
2	Identifying Functional Cysteine Residues in the Mitochondria. ACS Chem Biol. 2017 Apr 21;12(4):947-957.
3	CEP128 Localizes to the Subdistal Appendages of the Mother Centriole and Regulates TGF-beta/BMP Signaling at the Primary Cilium. Cell Rep. 2018 Mar 6;22(10):2584-2592.
4	Specificity of Phosphorylation Responses to Mitogen Activated Protein (MAP) Kinase Pathway Inhibitors in Melanoma Cells. Mol Cell Proteomics. 2018 Apr;17(4):550-564.
5	Identifying novel targets of oncogenic EGF receptor signaling in lung cancer through global phosphoproteomics. Proteomics. 2015 Jan;15(2-3):340-55.
6	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
7	Phosphoproteome Profiling Reveals Molecular Mechanisms of Growth-Factor-Mediated Kinase Inhibitor Resistance in EGFR-Overexpressing Cancer Cells. J Proteome Res. 2016 Dec 2;15(12):4490-4504.
8	UniProt: a worldwide hub of protein knowledge. Nucleic Acids Res. 2019 Jan 8;47(D1):D506-D515.
9	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.
10	BioMuta and BioXpress: mutation and expression knowledgebases for cancer biomarker discovery. Nucleic Acids Res. 2018;46(D1):D1128-D1136.
11	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
12	Citric acid-assisted two-step enrichment with TiO2 enhances the separation of multi- and monophosphorylated peptides and increases phosphoprotein profiling. J Proteome Res. 2013 Jun 7;12(6):2467-76.
13	Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites. J Proteome Res. 2018 May 4;17(5):1907-1922.
14	Highly Multiplexed Quantitative Mass Spectrometry Analysis of Ubiquitylomes. Cell Syst. 2016 Oct 26;3(4):395-403.e4.
15	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
16	Global identification of modular cullin-RING ligase substrates. Cell. 2011 Oct 14;147(2):459-74.
17	UbiSite approach for comprehensive mapping of lysine and N-terminal ubiquitination sites. Nat Struct Mol Biol. 2018 Jul;25(7):631-640.

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Detail Information of Post-Translational Modifications

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