Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0349 Transporter Info
Gene Name	SLC39A8
Transporter Name	Zinc transporter ZIP8
Gene ID	64116
UniProt ID	Q9C0K1

Post-Translational Modification of This DT
Overview ofSLC39A8 Modification Sites with Functional and Structural Information
Sequence	M A P G R A V A G L L L L A A A G L G G V A E G P G L A F S E D V L S V F G A N L S L S A A Q L Q H L L E Q M G A A S R V G V P E P G Q L H F N Q C L T A E E I F S L H G F S N A T Q I T S S K F S V I C P A V L Q Q L N F H P C E D R P K H K T R P S H S E V W G Y G F L S V T I I N L A S L L G L I L T P L I K K S Y F P K I L T F F V G L A I G T L F S N A I F Q L I P E A F G F D P K V D S Y V E K A V A V F G G F Y L L F F F E R M L K M L L K T Y G Q N G H T H F G N D N F G P Q E K T H Q P K A L P A I N G V T C Y A N P A V T E A N G H I H F D N V S V V S L Q D G K K E P S S C T C L K G P K L S E I G T I A W M I T L C D A L H N F I D G L A I G A S C T L S L L Q G L S T S I A I L C E E F P H E L G D F V I L L N A G M S T R Q A L L F N F L S A C S C Y V G L A F G I L V G N N F A P N I I F A L A G G M F L Y I S L A D M F P E M N D M L R E K V T G R K T D F T F F M I Q N A G M L T G F T A I L L I T L Y A G E I E L E
PTM type	X-N-glycosylation X-N-linked glycosylation X-Phosphorylation 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 SLC39A8			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	273
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC39A8 Asparagine 273 has the potential to affect its expression or activity.
N-linked glycosylation
Asparagine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[2]
Role of PTM	Influencing the Disease Progression
Modified Residue	Asparagine	Modified Location	40
Experimental Material(s)	ARPE19 cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked glycosylation at SLC39A8 Asparagine 40 have been reported to be essential for the intracellular iron accumulation mediated by ZIP8, which further led to increased lipid peroxidation and RPE death.
PTM Phenomenon2	.			[2]
Role of PTM	Influencing the Disease Progression
Modified Residue	Asparagine	Modified Location	72
Experimental Material(s)	ARPE19 cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked glycosylation at SLC39A8 Asparagine 72 have been reported to be essential for the intracellular iron accumulation mediated by ZIP8, which further led to increased lipid peroxidation and RPE death.
PTM Phenomenon3	.			[2]
Role of PTM	Influencing the Disease Progression
Modified Residue	Asparagine	Modified Location	88
Experimental Material(s)	ARPE19 cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked glycosylation at SLC39A8 Asparagine 88 have been reported to be essential for the intracellular iron accumulation mediated by ZIP8, which further led to increased lipid peroxidation and RPE death.
Phosphorylation
Serine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC39A8			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	275
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Serine 275 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC39A8			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	278
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Serine 278 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC39A8			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	287
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Serine 287 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC39A8			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	288
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Serine 288 has the potential to affect its expression or activity.
Threonine	5 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC39A8			[7]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	150
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Threonine 150 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC39A8			[4]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	255
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Threonine 255 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC39A8			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	263
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Threonine 263 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC39A8			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	290
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Threonine 290 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC39A8			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	424
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Threonine 424 has the potential to affect its expression or activity.
Tyrosine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC39A8			[4]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	257
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A8 Tyrosine 257 has the potential to affect its expression or activity.
Ubiquitination
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[10]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	284
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC39A8 Lysine 284 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: S39A8_HUMAN)
2	Targeting ZIP8 mediated ferroptosis as a novel strategy to protect against the retinal pigment epithelial degeneration. Free Radic Biol Med. 2024;214:42-53.
3	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
4	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
5	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
6	HIV-1 Activates T Cell Signaling Independently of Antigen to Drive Viral Spread. Cell Rep. 2017 Jan 24;18(4):1062-1074.
7	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.
8	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
9	Global phosphoproteome of HT-29 human colon adenocarcinoma cells. J Proteome Res. 2005 Jul-Aug;4(4):1339-46.
10	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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Detail Information of Post-Translational Modifications

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