Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0342 Transporter Info
Gene Name	SLC39A14
Transporter Name	Zinc transporter ZIP14
Gene ID	23516
UniProt ID	Q15043

Post-Translational Modification of This DT
Overview ofSLC39A14 Modification Sites with Functional and Structural Information
Sequence	M K L L L L H P A F Q S C L L L T L L G L W R T T P E A H A S S L G A P A I S A A S F L Q D L I H R Y G E G D S L T L Q Q L K A L L N H L D V G V G R G N V T Q H V Q G H R N L S T C F S S G D L F T A H N F S E Q S R I G S S E L Q E F C P T I L Q Q L D S R A C T S E N Q E N E E N E Q T E E G R P S A V E V W G Y G L L C V T V I S L C S L L G A S V V P F M K K T F Y K R L L L Y F I A L A I G T L Y S N A L F Q L I P E A F G F N P L E D Y Y V S K S A V V F G G F Y L F F F T E K I L K I L L K Q K N E H H H G H S H Y A S E S L P S K K D Q E E G V M E K L Q N G D L D H M I P Q H C S S E L D G K A P M V D E K V I V G S L S V Q D L Q A S Q S A C Y W L K G V R Y S D I G T L A W M I T L S D G L H N F I D G L A I G A S F T V S V F Q G I S T S V A I L C E E F P H E L G D F V I L L N A G M S I Q Q A L F F N F L S A C C C Y L G L A F G I L A G S H F S A N W I F A L A G G M F L Y I S L A D M F P E M N E V C Q E D E R K G S I L I P F I I Q N L G L L T G F T I M V V L T M Y S G Q I Q I G
PTM type	X-Acetylation X-N-glycosylation X-Phosphorylation X-Phosphorylation X-S-palmitoylation X-Ubiquitination X-Ubiquitination X: Amino Acid

Acetylation
Lysine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC39A14			[1]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	326
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at SLC39A14 Lysine 326 has the potential to affect its expression or activity.
N-glycosylation
Asparagine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Critically important for determining membrane extraction and the iron sensitivity of SLC39A14			[2]
Role of PTM	On/Off Switch
Modified Residue	Asparagine	Modified Location	102
Experimental Material(s)	Human embryonic kidney 293 (HEK293) cells
Experimental Method	Co-Immunoprecipitation
Detailed Description	Glycosylation at SLC39A14 Asparagine 102 have been reported to be critically important for determining its membrane extraction and the iron sensitivity.
PTM Phenomenon2	Have the potential to influence SLC39A14			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	77
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC39A14 Asparagine 77 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC39A14			[2]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	87
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at SLC39A14 Asparagine 87 has the potential to affect its expression or activity.
Phosphorylation
Serine	10 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC39A14			[3], [4]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	256
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 256 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC39A14			[3], [5]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	260
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 260 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence SLC39A14			[6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	262
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 262 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence SLC39A14			[3], [6]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	265
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 265 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence SLC39A14			[7], [8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	291
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 291 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence SLC39A14			[9], [10]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	292
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 292 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence SLC39A14			[11], [12]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	309
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 309 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence SLC39A14			[11], [13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	311
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 311 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence SLC39A14			[11], [14]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	318
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 318 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence SLC39A14			[11], [14]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	320
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Serine 320 has the potential to affect its expression or activity.
Threonine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[15]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	99
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Threonine 99 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 SLC39A14			[3]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	258
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at SLC39A14 Tyrosine 258 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 SLC39A14			[16]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	322
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-palmitoylation at SLC39A14 Cystine 322 has the potential to affect its expression or activity.
Ubiquitination
Lysine	4 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence SLC39A14			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	63
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC39A14 Lysine 63 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence SLC39A14			[17]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	267
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC39A14 Lysine 267 has the potential to affect its expression or activity.
PTM Phenomenon3	.			[18]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	297
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC39A14 Lysine 297 has the potential to affect its expression or activity.
PTM Phenomenon4	.			[18]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	304
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at SLC39A14 Lysine 304 has the potential to affect its expression or activity.

References
1	Regulation of cellular metabolism by protein lysine acetylation. Science. 2010 Feb 19;327(5968):1000-4.
2	An iron-regulated and glycosylation-dependent proteasomal degradation pathway for the plasma membrane metal transporter ZIP14. Proc Natl Acad Sci U S A. 2014 Jun 24;111(25):9175-80.
3	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.
4	Defeating Major Contaminants in Fe3+- Immobilized Metal Ion Affinity Chromatography (IMAC) Phosphopeptide Enrichment. Mol Cell Proteomics. 2018 May;17(5):1028-1034.
5	An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62.
6	Integrated analysis of global proteome, phosphoproteome, and glycoproteome enables complementary interpretation of disease-related protein networks. Sci Rep. 2015 Dec 11;5:18189.
7	Proteogenomic integration reveals therapeutic targets in breast cancer xenografts. Nat Commun. 2017 Mar 28;8:14864.
8	Identification of Mediator Kinase Substrates in Human Cells using Cortistatin A and Quantitative Phosphoproteomics. Cell Rep. 2016 Apr 12;15(2):436-50.
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	Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1. EMBO J. 2015 Nov 12;34(22):2840-61.
11	A Methodological Assessment and Characterization of Genetically-Driven Variation in Three Human Phosphoproteomes. Sci Rep. 2018 Aug 14;8(1):12106.
12	Highly reproducible improved label-free quantitative analysis of cellular phosphoproteome by optimization of LC-MS/MS gradient and analytical column construction. J Proteomics. 2017 Aug 8;165:69-74.
13	Capillary Zone Electrophoresis-Tandem Mass Spectrometry for Large-Scale Phosphoproteomics with the Production of over 11,000 Phosphopeptides from the Colon Carcinoma HCT116 Cell Line. Anal Chem. 2019 Feb 5;91(3):2201-2208.
14	Temporal proteomic analysis of HIV infection reveals remodelling of the host phosphoproteome by lentiviral Vif variants. Elife. 2016 Sep 30;5:e18296.
15	15 years of PhosphoSitePlus?: integrating post-translationally modified sites, disease variants and isoforms. Nucleic Acids Res. 2019;47(D1):D433-D441.
16	Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites. J Proteome Res. 2018 May 4;17(5):1907-1922.
17	Systematic and quantitative assessment of the ubiquitin-modified proteome. Mol Cell. 2011 Oct 21;44(2):325-40.
18	ActiveDriverDB: human disease mutations and genome variation in post-translational modification sites of proteins. Nucleic Acids Res. 2018;46(D1):D901-D910.

If you find any error in data or bug in web service, please kindly report it to Dr. Li and Dr. Fu.

Detail Information of Post-Translational Modifications

Visitor Map

Correspondence