Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0284 Transporter Info
Gene Name	SLC34A1
Transporter Name	Sodium-dependent phosphate transport protein 2A
Gene ID	6569
UniProt ID	Q06495

Post-Translational Modification of This DT
Overview ofSLC34A1 Modification Sites with Functional and Structural Information
Sequence	M L S Y G E R L G S P A V S P L P V R G G H V M R G T A F A Y V P S P Q V L H R I P G T S A Y A F P S L G P V A L A E H T C P C G E V L E R H E P L P A K L A L E E E Q K P E S R L V P K L R Q A G A M L L K V P L M L T F L Y L F V C S L D M L S S A F Q L A G G K V A G D I F K D N A I L S N P V A G L V V G I L V T V L V Q S S S T S T S I I V S M V S S G L L E V S S A I P I I M G S N I G T S V T N T I V A L M Q A G D R T D F R R A F A G A T V H D C F N W L S V L V L L P L E A A T G Y L H H I T R L V V A S F N I H G G R D A P D L L K I I T E P F T K L I I Q L D E S V I T S I A T G D E S L R N H S L I Q I W C H P D S L Q A P T S M S R A E A N S S Q T L G N A T M E K C N H I F V D T G L P D L A V G L I L L A G S L V L L C T C L I L L V K M L N S L L K G Q V A K V I Q K V I N T D F P A P F T W V T G Y F A M V V G A S M T F V V Q S S S V F T S A I T P L I G L G V I S I E R A Y P L T L G S N I G T T T T A I L A A L A S P R E K L S S A F Q I A L C H F F F N I S G I L L W Y P V P C T R L P I R M A K A L G K R T A K Y R W F A V L Y L L V C F L L L P S L V F G I S M A G W Q V M V G V G T P F G A L L A F V V L I N V L Q S R S P G H L P K W L Q T W D F L P R W M H S L K P L D H L I T R A T L C C A R P E P R S P P L P P R V F L E E L P P A T P S P R L A L P A H H N A T R L
PTM type	X-N-glycosylation X-Phosphorylation X-Phosphorylation X-Ubiquitination 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 SLC34A1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	298
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC34A1 Asparagine 298 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC34A1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	323
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC34A1 Asparagine 323 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC34A1			[1]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	330
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC34A1 Asparagine 330 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 SLC34A1			[2]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	3
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Serine 3 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC34A1			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	10
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Serine 10 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC34A1			[2], [3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	14
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Serine 14 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC34A1			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	34
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Serine 34 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC34A1			[4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	375
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Serine 375 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC34A1			[3]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	625
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Serine 625 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	.			[5]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	508
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Threonine 508 has the potential to affect its expression or activity.
PTM Phenomenon2	.			[5]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	508
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Threonine 508 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 SLC34A1			[2]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	4
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC34A1 Tyrosine 4 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	.			[6]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	268
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC34A1 Lysine 268 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: NPT2A_HUMAN)
2	Characterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics. Mol Cell Proteomics. 2013 Dec;12(12):3851-73.
3	Identification of Missing Proteins in the Phosphoproteome of Kidney Cancer. J Proteome Res. 2017 Dec 1;16(12):4364-4373.
4	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.
5	BioMuta and BioXpress: mutation and expression knowledgebases for cancer biomarker discovery. Nucleic Acids Res. 2018;46(D1):D1128-D1136.
6	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.

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Detail Information of Post-Translational Modifications

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