Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0089 Transporter Info
Gene Name	SLC12A8
Transporter Name	Cation-chloride cotransporter 9
Gene ID	84561
UniProt ID	A0AV02

Post-Translational Modification of This DT
Overview ofSLC12A8 Modification Sites with Functional and Structural Information
Sequence	M T Q M S Q V Q E L F H E A A Q Q D A L A Q P Q P W W K T Q L F M W E P V L F G T W D G V F T S C M I N I F G V V L F L R T G W L V G N T G V L L G M F L V S F V I L V A L V T V L S G I G V G E R S S I G S G G V Y S M I S S V L G G Q T G G T I G L L Y V F G Q C V A G A M Y I T G F A E S I S D L L G L G N I W A V R G I S V A V L L A L L G I N L A G V K W I I R L Q L L L L F L L A V S T L D F V V G S F T H L D P E H G F I G Y S P E L L Q N N T L P D Y S P G E S F F T V F G V F F P A A T G V M A G F N M G G D L R E P A A S I P L G S L A A V G I S W F L Y I I F V F L L G A I C T R E A L R Y D F L I A E K V S L M G F L F L L G L Y I S S L A S C M G G L Y G A P R I L Q C I A Q E K V I P A L A C L G Q G K G P N K T P V A A I C L T S L V T M A F V F V G Q V N V L A P I V T I N F M L T Y V A V D Y S Y F S L S M C S C S L T P V P E P V L R E G A E G L H C S E H L L L E K A P S Y G S E G P A Q R V L E G T L L E F T K D M D Q L L Q L T R K L E S S Q P R Q G E G N R T P E S Q K R K S K K A T K Q T L Q D S F L L D L K S P P S F P V E I S D R L P A A S W E G Q E S C W N K Q T S K S E G T Q P E G T Y G E Q L V P E L C N Q S E S S G E D F F L K S R L Q E Q D V W R R S T S F Y T H M C N P W V S L L G A V G S L L I M F V I Q W V Y T L V N M G V A A I V Y F Y I G R A S P G L H L G S A S N F S F F R W M R S L L L P S C R S L R S P Q E Q I I L A P S L A K V D M E M T Q L T Q E N A D F A T R D R Y H H S S L V N R E Q L M P H Y
PTM type	X-N-glycosylation X-Phosphorylation X-Ubiquitination 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 SLC12A8			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	221
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC12A8 Asparagine 221 has the potential to affect its expression or activity.
Phosphorylation
Serine	11 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC12A8			[2]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	411
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 411 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC12A8			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	440
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 440 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC12A8			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	443
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 443 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC12A8			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	504
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 504 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC12A8			[5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	511
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 511 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC12A8			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	647
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 647 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC12A8			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	662
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 662 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC12A8			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	665
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 665 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC12A8			[8], [9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	675
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 675 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC12A8			[2], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	702
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 702 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence SLC12A8			[2], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	703
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Serine 703 has the potential to affect its expression or activity.
Threonine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC12A8			[6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	469
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Threonine 469 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC12A8			[3], [6]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	485
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Threonine 485 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC12A8			[4]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	497
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Threonine 497 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC12A8			[4]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	500
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Threonine 500 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 SLC12A8			[10]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	699
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC12A8 Tyrosine 699 has the potential to affect its expression or activity.
Ubiquitination
Lysine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[12]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	437
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC12A8 Lysine 437 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC12A8			[13]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	471
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC12A8 Lysine 471 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC12A8			[13]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	537
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC12A8 Lysine 537 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: S12A8_HUMAN)
2	Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics. Nat Commun. 2019 Jan 10;10(1):104.
3	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.
4	Tip-Based Fractionation of Batch-Enriched Phosphopeptides Facilitates Easy and Robust Phosphoproteome Analysis. J Proteome Res. 2018 Jan 5;17(1):46-54.
5	Isoelectric point-based fractionation by HiRIEF coupled to LC-MS allows for in-depth quantitative analysis of the phosphoproteome. Sci Rep. 2017 Jul 3;7(1):4513.
6	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.
7	Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
8	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
9	Proteogenomics connects somatic mutations to signalling in breast cancer. Nature. 2016 Jun 2;534(7605):55-62.
10	Identification of missing proteins in the neXtProt database and unregistered phosphopeptides in the PhosphoSitePlus database as part of the Chromosome-centric Human Proteome Project. J Proteome Res. 2013 Jun 7;12(6):2414-21.
11	An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62.
12	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.
13	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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