Detail Information of Post-Translational Modifications

General Information of Drug Transporter (DT)
DT ID	DTD0004 Transporter Info
Gene Name	ABCG2
Transporter Name	Breast cancer resistance protein
Gene ID	9429
UniProt ID	Q9UNQ0

Post-Translational Modification of This DT
Overview ofABCG2 Modification Sites with Functional and Structural Information
Sequence	M S S S N V E V F I P V S Q G N T N G F P A T A S N D L K A F T E G A V L S F H N I C Y R V K L K S G F L P C R K P V E K E I L S N I N G I M K P G L N A I L G P T G G G K S S L L D V L A A R K D P S G L S G D V L I N G A P R P A N F K C N S G Y V V Q D D V V M G T L T V R E N L Q F S A A L R L A T T M T N H E K N E R I N R V I Q E L G L D K V A D S K V G T Q F I R G V S G G E R K R T S I G M E L I T D P S I L F L D E P T T G L D S S T A N A V L L L L K R M S K Q G R T I I F S I H Q P R Y S I F K L F D S L T L L A S G R L M F H G P A Q E A L G Y F E S A G Y H C E A Y N N P A D F F L D I I N G D S T A V A L N R E E D F K A T E I I E P S K Q D K P L I E K L A E I Y V N S S F Y K E T K A E L H Q L S G G E K K K K I T V F K E I S Y T T S F C H Q L R W V S K R S F K N L L G N P Q A S I A Q I I V T V V L G L V I G A I Y F G L K N D S T G I Q N R A G V L F F L T T N Q C F S S V S A V E L F V V E K K L F I H E Y I S G Y Y R V S S Y F L G K L L S D L L P M R M L P S I I F T C I V Y F M L G L K P K A D A F F V M M F T L M M V A Y S A S S M A L A I A A G Q S V V S V A T L L M T I C F V F M M I F S G L L V N L T T I A S W L S W L Q Y F S I P R Y G F T A L Q H N E F L G Q N F C P G L N A T G N N P C N Y A T C T G E E Y L V K Q G I D L S P W G L W K N H V A L A C M I V I F L T I A Y L K L L F L K K Y S
PTM type	X-Acetylation X-Disulfide bond X-Methylation X-Methylation X-N-glycosylation X-Phosphorylation X-S-nitrosylation X-Ubiquitination X: Amino Acid

Acetylation
Lysine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence ABCG2			[1]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	171
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at ABCG2 Lysine 171 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence ABCG2			[2]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	172
Experimental Method	Co-Immunoprecipitation
Detailed Description	Acetylation at ABCG2 Lysine 172 has the potential to affect its expression or activity.
Disulfide bond
Cystine	3 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence ABCG2			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	592
Experimental Method	Co-Immunoprecipitation
Detailed Description	Disulfide bond (-SSR) at ABCG2 Cystine 592 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence ABCG2			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	603
Experimental Method	Co-Immunoprecipitation
Detailed Description	Disulfide bond (-SSR) at ABCG2 Cystine 603 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence ABCG2			[3]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	608
Experimental Method	Co-Immunoprecipitation
Detailed Description	Disulfide bond (-SSR) at ABCG2 Cystine 608 has the potential to affect its expression or activity.
Methylation
Alanine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Strongly altering the high affinity for the transporter			[4]
Role of PTM	Protein Activity Modulation
Affected Drug/Substrate	Mitoxantrone	Results for Drug	Decreasing efflux of mitoxantrone
Modified Residue	Alanine
Studied Phenotype	Breast cancer [ICD11: 2C60-2C6Z]
Experimental Method	Co-Immunoprecipitation
Detailed Description	Methylation at ABCG2 Alanine have been reported to strongly alter its high transport affinity.
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	.			[4]
Role of PTM	Influencing the Disease Progression
Experimental Method	Co-Immunoprecipitation
Detailed Description	Methylation at ABCG2 has been reported to influence its interaction with chromone derivatives, potentially affecting drug resistance in breast cancer.
N-glycosylation
Asparagine	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence ABCG2			[5], [6]
Role of PTM	Potential impacts
Modified Residue	Asparagine	Modified Location	596
Experimental Method	Co-Immunoprecipitation
Detailed Description	N-linked Glycosylation at ABCG2 Asparagine 596 has the potential to affect its expression or activity.
Unclear Residue	1 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Increasing the membrane localization and transport function of ABCG2			[7]
Role of PTM	Trafficking to Plasma Membrane
Experimental Method	Co-Immunoprecipitation
Detailed Description	Glycosylation at ABCG2 have been reported to increase its membrane localization and transport function.
Phosphorylation
Serine	15 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	2
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 2 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	3
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 3 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	4
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 4 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	13
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 13 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	25
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 25 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence ABCG2			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	50
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 50 has the potential to affect its expression or activity.
PTM Phenomenon7	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	65
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 65 has the potential to affect its expression or activity.
PTM Phenomenon8	Have the potential to influence ABCG2			[10], [11]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	100
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 100 has the potential to affect its expression or activity.
PTM Phenomenon9	Have the potential to influence ABCG2			[10], [12]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	103
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 103 has the potential to affect its expression or activity.
PTM Phenomenon10	Have the potential to influence ABCG2			[9]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	143
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 143 has the potential to affect its expression or activity.
PTM Phenomenon11	Have the potential to influence ABCG2			[13]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	187
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 187 has the potential to affect its expression or activity.
PTM Phenomenon12	Have the potential to influence ABCG2			[14]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	195
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 195 has the potential to affect its expression or activity.
PTM Phenomenon13	Have the potential to influence ABCG2			[15]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	248
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 248 has the potential to affect its expression or activity.
PTM Phenomenon14	Have the potential to influence ABCG2			[16]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	261
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 261 has the potential to affect its expression or activity.
PTM Phenomenon15	Have the potential to influence ABCG2			[17]
Role of PTM	Potential impacts
Modified Residue	Serine	Modified Location	353
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Serine 353 has the potential to affect its expression or activity.
Threonine	6 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Increasing the expression of ABCG2			[18]
Role of PTM	Surface Expression Modulation
Affected Drug/Substrate	Mitoxantrone and Docetaxel	Results for Drug	Increasing efflux of mitoxantrone and docetaxel
Modified Residue	Threonine	Modified Location	362
Related Enzyme	Serine/threonine-protein kinase pim-1 (PIM1)
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Threonine 362 have been reported to increase its expression.
PTM Phenomenon2	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	17
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Threonine 17 has the potential to affect its expression or activity.
PTM Phenomenon3	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	23
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Threonine 23 has the potential to affect its expression or activity.
PTM Phenomenon4	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	82
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Threonine 82 has the potential to affect its expression or activity.
PTM Phenomenon5	Have the potential to influence ABCG2			[8]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	153
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Threonine 153 has the potential to affect its expression or activity.
PTM Phenomenon6	Have the potential to influence ABCG2			[19]
Role of PTM	Potential impacts
Modified Residue	Threonine	Modified Location	194
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Threonine 194 has the potential to affect its expression or activity.
Tyrosine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence ABCG2			[16]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	247
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Tyrosine 247 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence ABCG2			[9]
Role of PTM	Potential impacts
Modified Residue	Tyrosine	Modified Location	464
Experimental Method	Co-Immunoprecipitation
Detailed Description	Phosphorylation at ABCG2 Tyrosine 464 has the potential to affect its expression or activity.
S-nitrosylation
Cystine	2 PTM Phenomena Related to This Residue		Click to Show/Hide the Full List
PTM Phenomenon1	Have the potential to influence ABCG2			[20]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	55
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation (-SNO) at ABCG2 Cystine 55 has the potential to affect its expression or activity.
PTM Phenomenon2	Have the potential to influence ABCG2			[20]
Role of PTM	Potential impacts
Modified Residue	Cystine	Modified Location	119
Experimental Method	Co-Immunoprecipitation
Detailed Description	S-nitrosylation (-SNO) at ABCG2 Cystine 119 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	.			[21]
Role of PTM	Potential impacts
Modified Residue	Lysine	Modified Location	357
Experimental Method	Co-Immunoprecipitation
Detailed Description	Ubiquitination at ABCG2 Lysine 357 has the potential to affect its expression or activity.

References
1	Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Cell Rep. 2012 Aug 30;2(2):419-31.
2	Quantitative Proteomic Atlas of Ubiquitination and Acetylation in the DNA Damage Response. Mol Cell. 2015 Sep 3;59(5):867-81.
3	iCysMod: an integrative database for protein cysteine modifications in eukaryotes. Brief Bioinform. 2021 Sep 2;22(5):bbaa400. (ID: Q9UNQ0)
4	Structure-activity relationships of chromone derivatives toward the mechanism of interaction with and inhibition of breast cancer resistance protein ABCG2. J Med Chem. 2013 Dec 27;56(24):9849-60.
5	Structure of the human multidrug transporter ABCG2. Nature. 2017 Jun 22;546(7659):504-509.
6	N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane. Biochemistry. 2005 Apr 12;44(14):5420-9.
7	Impaired N-linked glycosylation of uptake and efflux transporters in human non-alcoholic fatty liver disease. Liver Int. 2017 Jul;37(7):1074-1081.
8	Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3.
9	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: ABCG2_HUMAN)
10	Systematic functional prioritization of protein posttranslational modifications. Cell. 2012 Jul 20;150(2):413-25.
11	Innovation of Imine Metal Chelates as Corrosion Inhibitors at Different Media: A Collective Study. Int J Mol Sci. 2022 Aug 19;23(16):9360.
12	The Omnipresence of DYRK1A in Human Diseases. Int J Mol Sci. 2022 Aug 19;23(16):9355.
13	Regulation of cell proliferation and growth by angiotensin II. Prog Growth Factor Res. 1994;5(2):177-94.
14	Regulation of the actin cytoskeleton in living cells. Semin Cell Biol. 1994 Jun;5(3):193-9.
15	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.
16	iTRAQ labeling is superior to mTRAQ for quantitative global proteomics and phosphoproteomics. Mol Cell Proteomics. 2012 Jun;11(6):M111.014423.
17	Protein kinase C-alpha interaction with F0F1-ATPase promotes F0F1-ATPase activity and reduces energy deficits in injured renal cells. J Biol Chem. 2015 Mar 13;290(11):7054-66.
18	The 44-kDa Pim-1 kinase phosphorylates BCRP/ABCG2 and thereby promotes its multimerization and drug-resistant activity in human prostate cancer cells. J Biol Chem. 2008 Feb 8;283(6):3349-3356.
19	Effect of position on oxygenation in neonates after weaning from mechanical ventilation. Zhongguo Dang Dai Er Ke Za Zhi. 2008 Apr;10(2):121-4.
20	Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique. Nat Commun. 2019 May 16;10(1):2195.
21	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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